|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
417-902 |
0e+00 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 1046.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 417 TLQMPYQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLADLM 496
Cdd:cd07140 1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 497 EQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINQARPNRNLTLTKKEPVGVCGIVIPWNYP 576
Cdd:cd07140 81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 577 LMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGK 656
Cdd:cd07140 161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 657 HIMKSCALSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKI 736
Cdd:cd07140 241 HIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 737 GNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFA 816
Cdd:cd07140 321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 817 DGDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIK 896
Cdd:cd07140 401 DGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480
|
....*.
gi 21314994 897 TVTFEY 902
Cdd:cd07140 481 TVTIEY 486
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
419-900 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 817.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 419 QMPYQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLADLMEQ 498
Cdd:cd07091 1 EQPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 499 HQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINqarpNRNLTLTKKEPVGVCGIVIPWNYPLM 578
Cdd:cd07091 81 DRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPID----GNFLAYTRREPIGVCGQIIPWNFPLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 579 MLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHI 658
Cdd:cd07091 157 MLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 659 MKSCALSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGN 738
Cdd:cd07091 237 MEAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 739 PLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdg 818
Cdd:cd07091 317 PFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFK-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 819 DVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:cd07091 395 TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
..
gi 21314994 899 TF 900
Cdd:cd07091 475 TI 476
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
417-899 |
0e+00 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 643.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 417 TLQMPY-QLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENG-LWGKINARDRGRLLYRLAD 494
Cdd:cd07141 1 NPEIKYtKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGsPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 495 LMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINqarpNRNLTLTKKEPVGVCGIVIPWN 574
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMD----GDFFTYTRHEPVGVCGQIIPWN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 575 YPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEV 654
Cdd:cd07141 157 FPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 655 GKHIMKSCALSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKM 734
Cdd:cd07141 237 GKLIQQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 735 KIGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISR 814
Cdd:cd07141 317 VVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 815 FAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLR 894
Cdd:cd07141 397 FK--TIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTE 474
|
....*
gi 21314994 895 IKTVT 899
Cdd:cd07141 475 VKTVT 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
430-898 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 636.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 430 FVDAEGaKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEELATIEAL 509
Cdd:pfam00171 1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKAADLLEERKDELAELETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 510 DAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGATIPINQARpnrnLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLA 589
Cdd:pfam00171 78 ENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGR----LAYTRREPLGVVGAITPWNFPLLLPAWKIAPALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 590 AGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKK 669
Cdd:pfam00171 153 AGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 670 VSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQ 749
Cdd:pfam00171 232 VTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 750 NHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANA 829
Cdd:pfam00171 312 ISKAQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFK--DEEEAIEIAND 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 830 TEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDV-AAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:pfam00171 390 TEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
421-902 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 629.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 421 PYQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQ 500
Cdd:COG1012 5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPA--WAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 501 EELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGATIPInqARPNRnLTLTKKEPVGVCGIVIPWNYPLMML 580
Cdd:COG1012 83 EELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPS--DAPGT-RAYVRREPLGVVGAITPWNFPLALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:COG1012 159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 661 SCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPL 740
Cdd:COG1012 239 AAA-ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 741 DRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPR-PGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgD 819
Cdd:COG1012 318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFD--D 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 820 VDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:COG1012 396 EEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTV 475
|
....
gi 21314994 899 TFEY 902
Cdd:COG1012 476 TIRL 479
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
417-898 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 574.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 417 TLQMPYQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENgLWGKINARDRGRLLYRLADLM 496
Cdd:cd07144 3 SYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLADLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 497 EQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINqarpNRNLTLTKKEPVGVCGIVIPWNYP 576
Cdd:cd07144 82 EKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTS----PNKLAYTLHEPYGVCGQIIPWNYP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 577 LMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGK 656
Cdd:cd07144 158 LAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 657 HIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGK-MK 735
Cdd:cd07144 238 LVMKAAA-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 736 IGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGN---QVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMII 812
Cdd:cd07144 317 VGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEkapEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 813 SRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEY 892
Cdd:cd07144 397 SKFK--TYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETY 474
|
....*.
gi 21314994 893 LRIKTV 898
Cdd:cd07144 475 TQTKAV 480
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
462-900 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 571.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 462 DKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTlALKTHVGMSIQTFRYFAGWCDKIQ 541
Cdd:cd07078 1 DAAVAAARAAFKA--WAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 542 GATIPINqarPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKG 621
Cdd:cd07078 78 GEVIPSP---DPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 622 VVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFF 701
Cdd:cd07078 155 VLNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAA-ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 702 NKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPR 781
Cdd:cd07078 234 NAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 782 -PGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFV 860
Cdd:cd07078 314 gKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWI 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 21314994 861 NTYNK-TDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd07078 392 NDYSVgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
441-900 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 567.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 441 TINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTlALK 520
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIR-ETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 521 THVGMSIQTFRYFAGWCDKIQGATIPINqaRPNRnLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADKIEGAVIPVD--KGDY-LNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 601 VTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPL 680
Cdd:cd07114 157 HTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAA-ENLAPVTLELGGKSPN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVE 760
Cdd:cd07114 236 IVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 761 YCQRGVKEGATLVCGGNQVPRP----GFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGDvDAVlSRANATEFGLAS 836
Cdd:cd07114 316 YVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEE-EAI-ALANDSEYGLAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21314994 837 GVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd07114 394 GIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
437-898 |
0e+00 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 564.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 437 KTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYT 516
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 517 LALKTHVGMSIQTFRYFAGWCDKIQGATIPInqarPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVI 596
Cdd:cd07112 82 DALAVDVPSAANTFRWYAEAIDKVYGEVAPT----GPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 597 KPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCALSNVKKVSLELGG 676
Cdd:cd07112 158 KPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 677 KSPLIIFADC-DLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHL 755
Cdd:cd07112 238 KSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 756 RKLVEYCQRGVKEGATLVCGGNQV--PRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGDvDAVlSRANATEFG 833
Cdd:cd07112 318 DKVLGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEE-EAV-ALANDSVYG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21314994 834 LASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:cd07112 396 LAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
425-898 |
0e+00 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 564.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 425 FIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLADLMEQHQEELA 504
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 505 TIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGATIPinqaRPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKT 584
Cdd:cd07119 81 RLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYD----VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAl 664
Cdd:cd07119 156 APALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 665 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDT 744
Cdd:cd07119 235 GNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 745 NHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRP----GFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGDv 820
Cdd:cd07119 315 EMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE- 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21314994 821 DAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:cd07119 394 EAI-RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
421-898 |
0e+00 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 552.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 421 PYQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLADLMEQHQ 500
Cdd:cd07142 3 HTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 501 EELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINQarPNRNLTLtkKEPVGVCGIVIPWNYPLMML 580
Cdd:cd07142 83 DELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADG--PHHVYTL--HEPIGVVGQIIPWNFPLLMF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07142 159 AWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 661 SCALSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPL 740
Cdd:cd07142 239 LAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 741 DRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDV 820
Cdd:cd07142 319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFK--TV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21314994 821 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
441-898 |
0e+00 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 546.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 441 TINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLALK 520
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 521 THVGMSIQTFRYFAGWCDKIQGATIPInqaRPnRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07115 79 LDVPRAADTFRYYAGWADKIEGEVIPV---RG-PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 601 VTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPL 680
Cdd:cd07115 155 LTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVE 760
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 761 YCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFadGDVDAVLSRANATEFGLASGVFT 840
Cdd:cd07115 314 YVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRF--RDEEEALRIANGTEYGLAAGVWT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 21314994 841 RDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:cd07115 392 RDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
417-898 |
0e+00 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 541.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 417 TLQMPYQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGlWG-KINARDRGRLLYRLADL 495
Cdd:cd07143 2 KYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETD-WGlKVSGSKRGRCLSKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 496 MEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINQARpnrnLTLTKKEPVGVCGIVIPWNY 575
Cdd:cd07143 81 MERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKK----LTYTRHEPIGVCGQIIPWNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 576 PLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVG 655
Cdd:cd07143 157 PLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 656 KHIMKSCALSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMK 735
Cdd:cd07143 237 RKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 736 IGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRF 815
Cdd:cd07143 317 VGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 816 ADGdvDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRI 895
Cdd:cd07143 397 KTE--EEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQI 474
|
...
gi 21314994 896 KTV 898
Cdd:cd07143 475 KAV 477
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
442-900 |
0e+00 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 538.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlKT 521
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFK--TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 522 HVGMSIQTFRYFAGWCDKIQGATIPinQARPNRNLtLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 601
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIP--SPAPGKRI-LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 602 TPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLI 681
Cdd:cd07103 156 TPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 682 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEY 761
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 762 CQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFTR 841
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFD--TEDEVIARANDTPYGLAAYVFTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 21314994 842 DINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd07103 393 DLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
423-898 |
1.72e-179 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 527.85 E-value: 1.72e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 423 QLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLADLMEQHQEE 502
Cdd:PLN02766 22 KLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 503 LATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPInqARPNRNLTLtkKEPVGVCGIVIPWNYPLMMLSW 582
Cdd:PLN02766 102 LAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKM--SRQLQGYTL--KEPIGVVGHIIPWNFPSTMFFM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:PLN02766 178 KVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 663 ALSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDR 742
Cdd:PLN02766 258 ATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 743 DTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDA 822
Cdd:PLN02766 338 RARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFK--TVEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21314994 823 VLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
441-899 |
1.84e-179 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 525.98 E-value: 1.84e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 441 TINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLALK 520
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG--WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 521 THVGMSIQTFRYFAGWCDKIQGATIPinqaRPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07093 79 RDIPRAAANFRFFADYILQLDGESYP----QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 601 VTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPL 680
Cdd:cd07093 155 WTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA-PNLKPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVE 760
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 761 YCQRGVKEGATLVCGGNQVPRP----GFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGdvDAVLSRANATEFGLAS 836
Cdd:cd07093 314 YVELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDE--EEAIELANDTPYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21314994 837 GVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVT 899
Cdd:cd07093 392 YVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
441-898 |
1.50e-176 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 518.40 E-value: 1.50e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 441 TINPTDGSVICQVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlK 520
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK--EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 521 THVGMSIQTFRYFAGWCDKIQGATIPInqarPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07090 78 VDIDSSADCLEYYAGLAPTLSGEHVPL----PGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 601 VTPLTALKFAELTLKAGIPKGVVNILPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPL 680
Cdd:cd07090 154 FTPLTALLLAEILTEAGLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVE 760
Cdd:cd07090 232 IIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 761 YCQRGVKEGATLVCGGNQVP-----RPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLA 835
Cdd:cd07090 312 YIESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFD--TEEEVIRRANDTTYGLA 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21314994 836 SGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:cd07090 390 AGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
423-898 |
1.44e-173 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 513.97 E-value: 1.44e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 423 QLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLADLMEQHQEE 502
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 503 LATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINQarPNRNLTLtkKEPVGVCGIVIPWNYPLMMLSW 582
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADG--PHHVQTL--HEPIGVAGQIIPWNFPLLMFAW 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:PLN02466 215 KVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 663 ALSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDR 742
Cdd:PLN02466 295 AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 743 DTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDA 822
Cdd:PLN02466 375 GVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK--DLDE 452
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21314994 823 VLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:PLN02466 453 VIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
425-896 |
6.11e-168 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 496.64 E-value: 6.11e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 425 FIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFenGLWGKINARDRGRLLYRLADLMEQHQEELA 504
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 505 TIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPInqarPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKT 584
Cdd:TIGR01804 79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPL----GGPSFAYTIREPLGVCVGIGAWNYPLQIASWKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAl 664
Cdd:TIGR01804 155 APALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 665 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDT 744
Cdd:TIGR01804 234 GHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 745 NHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRP----GFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGdv 820
Cdd:TIGR01804 314 EMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVglqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDE-- 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21314994 821 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIK 896
Cdd:TIGR01804 392 DEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
422-898 |
1.82e-167 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 496.33 E-value: 1.82e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 422 YQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQE 501
Cdd:PRK13252 7 QSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK--IWAAMTAMERSRILRRAVDILRERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 502 ELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINQArpnrNLTLTKKEPVGVCGIVIPWNYPLMMLS 581
Cdd:PRK13252 85 ELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGG----SFVYTRREPLGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 662 CALSnVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLD 741
Cdd:PRK13252 240 AAAS-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 742 RDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPR----PGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAD 817
Cdd:PRK13252 319 PATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 818 GdvDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKT 897
Cdd:PRK13252 399 E--DEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKS 476
|
.
gi 21314994 898 V 898
Cdd:PRK13252 477 V 477
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
424-900 |
7.31e-165 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 488.94 E-value: 7.31e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 424 LFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEEL 503
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WSATSVEERAALLERIAEAYEARADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 504 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGwcdkiQGATIPINQARPNrnlTLTKKEPVGVCGIVIPWNYPLMMLSWK 583
Cdd:cd07138 79 AQAITLEMGAPITLARAAQVGLGIGHLRAAAD-----ALKDFEFEERRGN---SLVVREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 584 TAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCA 663
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 664 lSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRD 743
Cdd:cd07138 231 -DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 744 TNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPR---PGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGDv 820
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEgleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDED- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 821 DAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd07138 389 EAI-AIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQG 466
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
442-900 |
4.28e-160 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 475.96 E-value: 4.28e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGlWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlKT 521
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESG-WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 522 HVGMSIQTFRYFAGWCDKIQGATIPINQArpnrNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 601
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPG----YFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 602 TPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLI 681
Cdd:cd07109 156 APLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA-ENVVPVTLELGGKSPQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 682 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDrDTNHGPQNHEAHLRKLVEY 761
Cdd:cd07109 235 VFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 762 CQRGVKEGATLVCGGNQV---PRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFadGDVDAVLSRANATEFGLASGV 838
Cdd:cd07109 314 VARARARGARIVAGGRIAegaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPF--DDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21314994 839 FTRDINKALYVSDKLQAGTVFVNTYNKT-DVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNYGAGgGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
424-900 |
7.48e-159 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 473.60 E-value: 7.48e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 424 LFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLADLMEQHQEEL 503
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 504 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWcdkiqGATIPINQARP--NRNLTLTKKEPVGVCGIVIPWNYPLMMLS 581
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAAL-----ARDFPFEERRPgsGGGHVLVRREPVGVVAAIVPWNAPLFLAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGsGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07139 156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 662 CAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLD 741
Cdd:cd07139 235 CG-ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 742 RDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRP--GFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGD 819
Cdd:cd07139 314 PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLdrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 820 vDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYnKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVT 899
Cdd:cd07139 394 -DAV-RIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIY 470
|
.
gi 21314994 900 F 900
Cdd:cd07139 471 L 471
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
442-900 |
3.98e-158 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 471.05 E-value: 3.98e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlKT 521
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 522 HVGMSIQTFRYFAGWCDKIQGATIpiNQARPNRnLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 601
Cdd:cd07118 81 EIEGAADLWRYAASLARTLHGDSY--NNLGDDM-LGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 602 TPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLI 681
Cdd:cd07118 158 TSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAA-RNLKKVSLELGGKNPQI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 682 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEY 761
Cdd:cd07118 237 VFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 762 CQRGVKEGATLVCGGNQVP-RPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFadGDVDAVLSRANATEFGLASGVFT 840
Cdd:cd07118 317 VDAGRAEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 841 RDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd07118 395 KDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
420-900 |
6.92e-158 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 471.32 E-value: 6.92e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 420 MPYQLFIGGEFVDAEGAkTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQH 499
Cdd:PRK13473 1 MQTKLLINGELVAGEGE-KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 500 QEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGwcdkiqgATipinqarpnRNLT-------------LTKKEPVGV 566
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAG-------AA---------RCLEgkaageyleghtsMIRRDPVGV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 567 CGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNILPGSGSLVGQRLSDHPDVRKI 646
Cdd:PRK13473 142 VASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 647 GFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQK 726
Cdd:PRK13473 221 SLTGSIATGKHVLSAAA-DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 727 VVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEG-ATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEES 805
Cdd:PRK13473 300 LAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 806 FGPIMIISRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLG 885
Cdd:PRK13473 380 FGPVVSVTPFD--DEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMS 457
|
490
....*....|....*
gi 21314994 886 EAALNEYLRIKTVTF 900
Cdd:PRK13473 458 LYGLEDYTVVRHVMV 472
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
442-900 |
1.14e-155 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 464.49 E-value: 1.14e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLALKT 521
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 522 HVGMSIQTFRYFAGWCDKIQGATIpiNQARPNRnLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 601
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLEGPAA--GEYLPGH-TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 602 TPLTALKFAELtLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScALSNVKKVSLELGGKSPLI 681
Cdd:cd07092 157 TPLTTLLLAEL-AAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARA-AADTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 682 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEY 761
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 762 CQRgVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFTR 841
Cdd:cd07092 315 VER-APAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFD--DEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 21314994 842 DINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| FMT_core_FDH_N |
cd08647 |
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
1-203 |
1.32e-154 |
|
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.
Pssm-ID: 187716 [Multi-domain] Cd Length: 203 Bit Score: 451.90 E-value: 1.32e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 1 MKIAVIGQSLFGQEVYCQLRKEGHEVVGVFTIPDKDGKADPLGLEAEKDGVPVFKFPRWRARGQALPEVVAKYQALGAEL 80
Cdd:cd08647 1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVVAKYKALGAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 81 NVLPFCSQFIPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTV 160
Cdd:cd08647 81 NVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21314994 161 STLYNRFLFPEGIKGMVQAVRLIAEGTAPRRPQPEEGATYEGI 203
Cdd:cd08647 161 DTLYNRFLYPEGIKAMVEAVRLIAEGKAPRIPQPEEGATYEGI 203
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
425-898 |
4.65e-154 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 461.33 E-value: 4.65e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 425 FIGGEFVdaEGAKTYSTINPTDGS-VICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEEL 503
Cdd:cd07097 4 YIDGEWV--AGGDGEENRNPSDTSdVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 504 ATIEALDAGAvyTLAL-KTHVGMSIQTFRYFAGWCDKIQGATIPinQARPNRNLTlTKKEPVGVCGIVIPWNYPLMMLSW 582
Cdd:cd07097 80 ARLLTREEGK--TLPEaRGEVTRAGQIFRYYAGEALRLSGETLP--STRPGVEVE-TTREPLGVVGLITPWNFPIAIPAW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:cd07097 155 KIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 663 AlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDR 742
Cdd:cd07097 235 A-ARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 743 DTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRP--GFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDV 820
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVR--DY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 821 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN-TYNKTDVAAPFGGFKQSGFG-KDLGEAALNEYLRIKTV 898
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
422-902 |
4.29e-153 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 459.12 E-value: 4.29e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 422 YQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQE 501
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 502 ELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINQarpnRNLTLTKKEPVGVCGIVIPWNYPLMMLS 581
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDE----DTLSYHFHEPLGVVGQIIPWNFPLLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07559 155 WKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 662 cALSNVKKVSLELGGKSPLIIFAD-----CDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKI 736
Cdd:cd07559 234 -AAENLIPVTLELGGKSPNIFFDDamdadDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 737 GNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRP----GFFFQPTVFTDVEDHMYIAKEESFGPIMII 812
Cdd:cd07559 313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 813 SRFADgdVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEY 892
Cdd:cd07559 393 ITFKD--EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHY 470
|
490
....*....|
gi 21314994 893 LRIKTVTFEY 902
Cdd:cd07559 471 QQTKNILVSY 480
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
442-900 |
1.22e-151 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 454.39 E-value: 1.22e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWgKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLALKT 521
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 522 HVGMSIQTFRYFAGWCDKIQGA-TIPINQARPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEfDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 601 VTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPL 680
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVE 760
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 761 YCQRGVKEGATLVCGGNQVPR--PGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFaDGDVDAVlSRANATEFGLASGV 838
Cdd:cd07089 320 YIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPY-DDDDEAV-RIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21314994 839 FTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
425-898 |
1.49e-151 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 454.42 E-value: 1.49e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 425 FIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEELA 504
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK--AWERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 505 TIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGATIPinQARPNRNLTLTKkEPVGVCGIVIPWNYPLMMLSWKT 584
Cdd:cd07088 79 KLIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIP--SDRPNENIFIFK-VPIGVVAGILPWNFPFFLIARKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAl 664
Cdd:cd07088 155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 665 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDT 744
Cdd:cd07088 234 ENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 745 NHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVP-RPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAV 823
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFS--SLDEA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21314994 824 LSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:cd07088 392 IELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
466-900 |
2.77e-151 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 450.14 E-value: 2.77e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 466 AAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGATI 545
Cdd:cd06534 1 AAARAAFKA--WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 546 PINqarPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNI 625
Cdd:cd06534 78 PSP---DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 626 LPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGE 705
Cdd:cd06534 155 VPGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAA-ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 706 NCIAAGRLFVEDSIHDQFVQKVVeevgkmkignpldrdtnhgpqnheahlrklveycqrgvkegatlvcggnqvprpgff 785
Cdd:cd06534 234 ICTAASRLLVHESIYDEFVEKLV--------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 786 fqpTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNK 865
Cdd:cd06534 257 ---TVLVDVDPDMPIAQEEIFGPVLPVIRFK--DEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSI 331
|
410 420 430
....*....|....*....|....*....|....*.
gi 21314994 866 -TDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd06534 332 gVGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
422-894 |
7.32e-151 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 453.39 E-value: 7.32e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 422 YQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQE 501
Cdd:cd07111 22 FGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 502 ELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGAtipinqarpnrnltLTKKEPVGVCGIVIPWNYPLMMLS 581
Cdd:cd07111 100 LFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTE--------------LAGWKPVGVVGQIVPWNFPLLMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLvGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07111 166 WKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 662 CALSnVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLD 741
Cdd:cd07111 245 TAGT-GKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 742 RDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVD 821
Cdd:cd07111 324 KAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFR--TAK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21314994 822 AVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLR 894
Cdd:cd07111 402 EAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
441-899 |
9.94e-147 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 441.79 E-value: 9.94e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 441 TINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLALk 520
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 521 THVGMSIQTFRYFAGWCDKIQgatipinqARPNRNLTL--------TKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGN 592
Cdd:cd07110 78 WDVDDVAGCFEYYADLAEQLD--------AKAERAVPLpsedfkarVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 593 TVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSL 672
Cdd:cd07110 150 TVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-QDIKPVSL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 673 ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHE 752
Cdd:cd07110 229 ELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 753 AHLRKLVEYCQRGVKEGATLVCGGN--QVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGDvDAVLSrANAT 830
Cdd:cd07110 309 AQYEKVLSFIARGKEEGARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATED-EAIAL-ANDS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21314994 831 EFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVT 899
Cdd:cd07110 387 EYGLAAAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
441-899 |
1.00e-145 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 439.10 E-value: 1.00e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 441 TINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAvytlALK 520
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPE--WAATPARERGKLLARIADALEARSEELARLLALETGN----ALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 521 TH----VGMSIQTFRYFAGWCDKIQGATIPinqARPNRnLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVI 596
Cdd:cd07108 75 TQarpeAAVLADLFRYFGGLAGELKGETLP---FGPDV-LTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 597 KPAQVTPLTALKFAELtLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGG 676
Cdd:cd07108 151 KAAEDAPLAVLLLAEI-LAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA-DRLIPVSLELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 677 KSPLIIFADCDLNKAVQ---MGMSsvFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEA 753
Cdd:cd07108 229 KSPMIVFPDADLDDAVDgaiAGMR--FTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 754 HLRKLVEYCQRGVKE-GATLVCGGNQVP----RPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRAN 828
Cdd:cd07108 307 QFAKVCGYIDLGLSTsGATVLRGGPLPGegplADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWK--DEDEVIAMAN 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21314994 829 ATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLG-EAALNEYLRIKTVT 899
Cdd:cd07108 385 DSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVN 456
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
424-902 |
1.93e-145 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 439.18 E-value: 1.93e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 424 LFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGlWGKINARDRGRLLYRLADLMEQHQEEL 503
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSA-WAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 504 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINQARPN--RNLTLTKKEPVGVCGIVIPWNYPLMMLS 581
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIPSMQgeRYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 662 cALSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLD 741
Cdd:cd07113 240 -AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 742 RDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPT--VFTDVEDHMYiaKEESFGPIMIISRFADGd 819
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTlvLARSADSRLM--REETFGPVVSFVPYEDE- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 820 vDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVT 899
Cdd:cd07113 396 -EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
...
gi 21314994 900 FEY 902
Cdd:cd07113 475 IRY 477
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
423-898 |
1.12e-144 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 437.97 E-value: 1.12e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 423 QLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEE 502
Cdd:PLN02278 26 QGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPS--WSKLTASERSKILRRWYDLIIANKED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 503 LATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGATIPINQarPNRNLtLTKKEPVGVCGIVIPWNYPLMMLSW 582
Cdd:PLN02278 104 LAQLMTLEQGKPLKEAI-GEVAYGASFLEYFAEEAKRVYGDIIPSPF--PDRRL-LVLKQPVGVVGAITPWNFPLAMITR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:PLN02278 180 KVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 663 AlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDR 742
Cdd:PLN02278 260 A-ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 743 DTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADgDVDA 822
Cdd:PLN02278 339 GVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKT-EEEA 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21314994 823 VLSrANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:PLN02278 418 IAI-ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
422-898 |
9.65e-144 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 434.57 E-value: 9.65e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 422 YQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQE 501
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 502 ELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINQarpnRNLTLTKKEPVGVCGIVIPWNYPLMMLS 581
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDE----DTLSIVLREPIGVVGQIIPWNFPFLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07117 155 WKLAPALAAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 662 CAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLD 741
Cdd:cd07117 234 AA-KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 742 RDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRP----GFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAd 817
Cdd:cd07117 313 PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFK- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 818 gDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKT 897
Cdd:cd07117 392 -TEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKN 470
|
.
gi 21314994 898 V 898
Cdd:cd07117 471 I 471
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
442-900 |
2.00e-142 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 430.03 E-value: 2.00e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlKT 521
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 522 HVGMSIQTFRYFAGwcdkiqgATIP---INQARPNRnlTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKP 598
Cdd:cd07106 79 EVGGAVAWLRYTAS-------LDLPdevIEDDDTRR--VELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 599 AQVTPLTALKFAELtLKAGIPKGVVNILPGSGSLvGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKS 678
Cdd:cd07106 150 SPFTPLCTLKLGEL-AQEVLPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGND 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 679 PLIIFADCDLNKAV-QMGMSSvFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRK 757
Cdd:cd07106 227 AAIVLPDVDIDAVApKLFWGA-FINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 758 LVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFadGDVDAVLSRANATEFGLASG 837
Cdd:cd07106 306 VKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKY--SDEDEVIARANDSEYGLGAS 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21314994 838 VFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd07106 384 VWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
425-902 |
1.92e-140 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 426.38 E-value: 1.92e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 425 FIGGEFVDAEGAKTYSTINPTDGS-VICQVSLAQVSDVDKAVAAAKEAFenGLWGKINARDRGRLLYRLADLMEQHQEEL 503
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAF--PEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 504 ATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGATIPinQARPNRNLtLTKKEPVGVCGIVIPWNYPLMMLSWK 583
Cdd:cd07131 80 ARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVP--SELPNKDA-MTRRQPIGVVALITPWNFPVAIPSWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 584 TAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCA 663
Cdd:cd07131 156 IFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 664 LSNvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRD 743
Cdd:cd07131 236 RPN-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 744 TNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPR----PGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFaDGD 819
Cdd:cd07131 315 TDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEV-SSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 820 VDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtyNKT---DVAAPFGGFKQSGFG-KDLGEAALNEYLRI 895
Cdd:cd07131 394 EEAI-EIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN--APTigaEVHLPFGGVKKSGNGhREAGTTALDAFTEW 470
|
....*..
gi 21314994 896 KTVTFEY 902
Cdd:cd07131 471 KAVYVDY 477
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
414-898 |
5.16e-140 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 425.85 E-value: 5.16e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 414 KKLTLQMPYQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLA 493
Cdd:PRK09847 12 KALSLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 494 DLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINqarpNRNLTLTKKEPVGVCGIVIPW 573
Cdd:PRK09847 92 DLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTS----SHELAMIVREPVGVIAAIVPW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 574 NYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTE 653
Cdd:PRK09847 168 NFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 654 VGKHIMKSCALSNVKKVSLELGGKSPLIIFADC-DLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVG 732
Cdd:PRK09847 248 TGKQLLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 733 KMKIGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGaTLVCGGNQVPRPGfFFQPTVFTDVEDHMYIAKEESFGPIMII 812
Cdd:PRK09847 328 NWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 813 SRFAdGDVDAvLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEY 892
Cdd:PRK09847 406 TRFT-SEEQA-LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKF 483
|
....*.
gi 21314994 893 LRIKTV 898
Cdd:PRK09847 484 TELKTI 489
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
441-899 |
1.29e-139 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 423.32 E-value: 1.29e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 441 TINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTlALK 520
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE--WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 521 THVGMSIQTFRYFAGWCDKIQGATIPInqarPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07107 78 GDVMVAAALLDYFAGLVTELKGETIPV----GGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 601 VTPLTALKFAELtLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPL 680
Cdd:cd07107 154 QAPLSALRLAEL-AREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAA-EGIKHVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 681 IIFADCDLNKAVQ---MGMSsvFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRK 757
Cdd:cd07107 232 IVFPDADPEAAADaavAGMN--FTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 758 LVEYCQRGVKEGATLVCGGNQVPRP----GFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADgdVDAVLSRANATEFG 833
Cdd:cd07107 310 VMHYIDSAKREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRD--EAEMVAQANGVEYG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21314994 834 LASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVT 899
Cdd:cd07107 388 LTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVN 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
442-900 |
6.18e-139 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 421.23 E-value: 6.18e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGlwGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLALKt 521
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM--KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 522 HVGMSIQTFRYFAGWCDKIQGATIPINQARPNRN-LTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFDASPGGEGrIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 601 VTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCALsnvKKVSLELGGKSPL 680
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGL---KKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVE 760
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 761 YCQRGVKEGATLVCGGNqvpRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFT 840
Cdd:cd07149 318 WVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFD--TLDEAIAMANDSPYGLQAGVFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21314994 841 RDINKALYVSDKLQAGTVFVN---TYnKTDvAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd07149 393 NDLQKALKAARELEVGGVMINdssTF-RVD-HMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
443-899 |
1.18e-134 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 410.18 E-value: 1.18e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 443 NPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAL-KT 521
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPA--WAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWfET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 522 HVGMSIqtFRYFAGWCDKIQGATIPinQARPNRnLTLTKKEPVGVCGIVIPWNYPLMmLSWKTAA-CLAAGNTVVIKPAQ 600
Cdd:cd07150 83 TFTPEL--LRAAAGECRRVRGETLP--SDSPGT-VSMSVRRPLGVVAGITPFNYPLI-LATKKVAfALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 601 VTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPL 680
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVE 760
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 761 YCQRGVKEGATLVCGGNqvpRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGDvDAvLSRANATEFGLASGVFT 840
Cdd:cd07150 316 QVEDAVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAE-EA-LELANDTEYGLSAAILT 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 841 RDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRIKTVT 899
Cdd:cd07150 391 NDLQRAFKLAERLESGMVHINDPTILDEAhVPFGGVKASGFGREGGEWSMEEFTELKWIT 450
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
423-899 |
1.42e-133 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 409.51 E-value: 1.42e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 423 QLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAF---ENGLWGKINARDRGRLLYRLADLMEQH 499
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnKGKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 500 QEELATIEALDAGAVYTLALKTHVGMSiQTFRYFAGWCDKIQG-ATIPINQARPNRNLTLtKKEPVGVCGIVIPWNYPLM 578
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVA-GCFEYYADLAEALDAkQKAPVSLPMETFKGYV-LKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 579 MLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHI 658
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 659 MKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGN 738
Cdd:PLN02467 247 MTAAA-QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 739 PLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGN--QVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFA 816
Cdd:PLN02467 326 PLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFS 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 817 DGdvDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIK 896
Cdd:PLN02467 406 TE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
...
gi 21314994 897 TVT 899
Cdd:PLN02467 484 QVT 486
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
442-898 |
3.93e-131 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 401.34 E-value: 3.93e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlKT 521
Cdd:cd07145 4 RNPANGEVIDTVPSLSREEVREAIEVAEKAKD--VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS-RV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 522 HVGMSIQTFRYFAGWCDKIQGATIPINQARPNRN-LTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERrIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 601 VTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScALSNVKKVSLELGGKSPL 680
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASK-AGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVE 760
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 761 YCQRGVKEGATLVCGGNQVprPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGDvDAVlSRANATEFGLASGVFT 840
Cdd:cd07145 320 LVNDAVEKGGKILYGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDE-EAV-EIANSTEYGLQASVFT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 841 RDINKALYVSDKLQAGTVFVN--TYNKTDvAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:cd07145 396 NDINRALKVARELEAGGVVINdsTRFRWD-NLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
460-899 |
2.32e-128 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 393.05 E-value: 2.32e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 460 DVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYtlaLKTH--VGMSIQTFRYFAGWC 537
Cdd:cd07104 1 DVDRAYAAAAAAQKA--WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTR---PKAAfeVGAAIAILREAAGLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 538 DKIQGATIPinQARPNRnLTLTKKEPVGVCGIVIPWNYPLMmLSWKTAA-CLAAGNTVVIKPAQVTPLT-ALKFAELTLK 615
Cdd:cd07104 76 RRPEGEILP--SDVPGK-ESMVRRVPLGVVGVISPFNFPLI-LAMRSVApALALGNAVVLKPDSRTPVTgGLLIAEIFEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 616 AGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMG 695
Cdd:cd07104 152 AGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAG-RHLKKVALELGGNNPLIVLDDADLDLAVSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 696 MSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCG 775
Cdd:cd07104 231 AFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 776 GnqvPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADgDVDAVlSRANATEFGLASGVFTRDINKALYVSDKLQA 855
Cdd:cd07104 311 G---TYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDD-DEEAV-ELANDTEYGLSAAVFTRDLERAMAFAERLET 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 21314994 856 GTVFVN--TYNKtDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVT 899
Cdd:cd07104 386 GMVHINdqTVND-EPHVPFGGVKASGGGRFGGPASLEEFTEWQWIT 430
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
441-899 |
5.39e-128 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 393.25 E-value: 5.39e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 441 TINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWgKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlK 520
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 521 THVGMSIQTFRYFAGWCDKIQGATIpinQARPNrNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMI---EPEPG-SFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 601 VTPLTALKFAELTLKA-GIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSP 679
Cdd:cd07120 155 QTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 680 LIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLV 759
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 760 EYCQRGVKEGATLVCGGNQVPR---PGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGDvDAVlSRANATEFGLAS 836
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEA-EAV-ALANDTDYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21314994 837 GVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVT 899
Cdd:cd07120 392 SVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
425-902 |
1.16e-125 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 387.69 E-value: 1.16e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 425 FIGGEFVDAeGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFenGLWGKINARDRGRLLYRLADLMEQHQEELA 504
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEWRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 505 TIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGATIPinQARPNRNLtLTKKEPVGVCGIVIPWNYPLMMLSWKT 584
Cdd:cd07086 79 RLVSLEMGKILPEGL-GEVQEMIDICDYAVGLSRMLYGLTIP--SERPGHRL-MEQWNPLGVVGVITAFNFPVAVPGWNA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKA----GIPKGVVNILPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07086 155 AIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 661 SCALSNvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPL 740
Cdd:cd07086 234 TVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 741 DRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPR--PGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFadG 818
Cdd:cd07086 313 DEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKF--D 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 819 DVDAVLSRANATEFGLASGVFTRDINKAL-YVSDK-LQAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRI 895
Cdd:cd07086 391 SLEEAIAINNDVPQGLSSSIFTEDLREAFrWLGPKgSDCGIVNVNIpTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRR 470
|
....*..
gi 21314994 896 KTVTFEY 902
Cdd:cd07086 471 STCTINY 477
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
423-896 |
3.93e-123 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 381.56 E-value: 3.93e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 423 QLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEE 502
Cdd:PRK11241 12 QALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--AWRALTAKERANILRRWFNLMMEHQDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 503 LATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGATIPINQarPNRNLtLTKKEPVGVCGIVIPWNYPLMMLSW 582
Cdd:PRK11241 90 LARLMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDTIPGHQ--ADKRL-IVIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 663 AlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDR 742
Cdd:PRK11241 246 A-KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 743 DTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFadGDVDA 822
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRF--KDEAD 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21314994 823 VLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIK 896
Cdd:PRK11241 403 VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
461-898 |
2.75e-117 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 364.09 E-value: 2.75e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 461 VDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAgwcDKI 540
Cdd:cd07100 1 IEAALDRAHAAFLA--WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYA---ENA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 541 QG--ATIPINQARPNrnlTLTKKEPVGVCGIVIPWNYPLmmlsWKT----AACLAAGNTVVIKPAQVTPLTALKFAELTL 614
Cdd:cd07100 75 EAflADEPIETDAGK---AYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 615 KAGIPKGVVNILPGSGSLVGQrLSDHPDVRKIGFTGSTEVGKHImKSCALSNVKKVSLELGGKSPLIIFADCDLNKAVQM 694
Cdd:cd07100 148 EAGFPEGVFQNLLIDSDQVEA-IIADPRVRGVTLTGSERAGRAV-AAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 695 GMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVC 774
Cdd:cd07100 226 AVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 775 GGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGDvDAV-LsrANATEFGLASGVFTRDINKALYVSDKL 853
Cdd:cd07100 306 GGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEE-EAIaL--ANDSPFGLGGSVFTTDLERAERVARRL 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 21314994 854 QAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:cd07100 383 EAGMVFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
442-900 |
1.80e-116 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 362.91 E-value: 1.80e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLALKt 521
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 522 HVGMSIQTFRYFAGWCDKIQGATIP--INQARPNRnLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPA 599
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPldATQGSDNR-LAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 600 QVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCALsnvKKVSLELGGKSP 679
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG---KRIALELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 680 LIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLV 759
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 760 EYCQRGVKEGATLVCGGNqvpRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVF 839
Cdd:cd07094 317 RWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYD--DFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21314994 840 TRDINKALYVSDKLQAGTVFVN--TYNKTDvAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNdsSAFRTD-WMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
422-902 |
5.68e-116 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 362.54 E-value: 5.68e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 422 YQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQE 501
Cdd:cd07116 1 YDNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 502 ELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINqarpNRNLTLTKKEPVGVCGIVIPWNYPLMMLS 581
Cdd:cd07116 79 MLAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEID----ENTVAYHFHEPLGVVGQIIPWNFPLLMAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07116 155 WKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 662 cALSNVKKVSLELGGKSPLIIFADCD------LNKAVQmGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMK 735
Cdd:cd07116 234 -ASENIIPVTLELGGKSPNIFFADVMdaddafFDKALE-GFVMFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 736 IGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRP----GFFFQPTVFTDvEDHMYIAKEESFGPIMI 811
Cdd:cd07116 312 QGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGgllgGGYYVPTTFKG-GNKMRIFQEEIFGPVLA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 812 ISRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNE 891
Cdd:cd07116 391 VTTFK--DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDH 468
|
490
....*....|.
gi 21314994 892 YLRIKTVTFEY 902
Cdd:cd07116 469 YQQTKNLLVSY 479
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
422-899 |
2.36e-114 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 359.61 E-value: 2.36e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 422 YQLFIGGEFVDAEGakTYSTINPTDGS-VICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQ 500
Cdd:cd07124 33 YPLVIGGKEVRTEE--KIESRNPADPSeVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLLRAAALLRRRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 501 EELATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGAtiPINQARPNRNLTLTkkEPVGVCGIVIPWNYPLMML 580
Cdd:cd07124 109 FELAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGF--PVEMVPGEDNRYVY--RPLGVGAVISPWNFPLAIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07124 184 AGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 661 SCA-----LSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMK 735
Cdd:cd07124 264 RAAkvqpgQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 736 IGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGaTLVCGGNqVPRP---GFFFQPTVFTDVEDHMYIAKEESFGPIMII 812
Cdd:cd07124 344 VGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGE-VLELaaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAV 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 813 SRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGtvfvNTY-NKTDVAA-----PFGGFKQSGFG-KDLG 885
Cdd:cd07124 422 IKAK--DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVG----NLYaNRKITGAlvgrqPFGGFKMSGTGsKAGG 495
|
490
....*....|....
gi 21314994 886 EAALNEYLRIKTVT 899
Cdd:cd07124 496 PDYLLQFMQPKTVT 509
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
428-899 |
9.04e-112 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 351.22 E-value: 9.04e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 428 GEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIE 507
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKE--WAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 508 ALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGATIPIN-QARPNRnltlTKKEPVGVCGIVIPWNYPLMMLSWKTAA 586
Cdd:cd07151 79 IRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPSDvPGKENR----VYREPLGVVGVISPWNFPLHLSMRSVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 587 CLAAGNTVVIKPAQVTPLTA-LKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlS 665
Cdd:cd07151 154 ALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG-R 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 666 NVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTN 745
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 746 HGPQNHEAHLRKLVEYCQRGVKEGATLVCGGnqvPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFaDGDVDAVlS 825
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKA-DDEEEAL-E 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21314994 826 RANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRIKTVT 899
Cdd:cd07151 388 LANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPhVPFGGEKNSGLGRFNGEWALEEFTTDKWIS 462
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
423-899 |
6.13e-109 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 344.12 E-value: 6.13e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 423 QLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEE 502
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 503 LATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGATIPinQARPNRNlTLTKKEPVGVCGIVIPWNYPLMMLSW 582
Cdd:cd07085 80 LARLITLEHGKTLADA-RGDVLRGLEVVEFACSIPHLLKGEYLE--NVARGID-TYSYRQPLGVVAGITPFNFPAMIPLW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVgQRLSDHPDVRKIGFTGSTEVGKHIMKSc 662
Cdd:cd07085 156 MFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYER- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 663 ALSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDR 742
Cdd:cd07085 234 AAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 743 DTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRP----GFFFQPTVFTDVEDHMYIAKEESFGPIMIISRfADg 818
Cdd:cd07085 314 GADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVR-VD- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 819 DVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtynkTDVAAP-----FGGFKQSGFGkDL---GEAALN 890
Cdd:cd07085 392 TLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSFFG-DLhfyGKDGVR 466
|
....*....
gi 21314994 891 EYLRIKTVT 899
Cdd:cd07085 467 FYTQTKTVT 475
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
442-899 |
1.80e-108 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 341.89 E-value: 1.80e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLALkT 521
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQR--AWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 522 HVGMSIQTFRYFAGWCDKIQGAT-IPINQARPNRNLTLTKkEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07099 78 EVLLALEAIDWAARNAPRVLAPRkVPTGLLMPNKKATVEY-RPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 601 VTPLTALKFAELTLKAGIPKGVVNILPGSGSlVGQRLSDHPdVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPL 680
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGA-TGAALIDAG-VDKVAFTGSVATGRKVMAAAA-ERLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVE 760
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 761 YCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFT 840
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVA--DEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21314994 841 RDINKALYVSDKLQAGTVFVN--TYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVT 899
Cdd:cd07099 392 RDLARAEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
442-896 |
9.55e-108 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 339.99 E-value: 9.55e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlKT 521
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFR--PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA-RG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 522 HVGMSIQTFRYFAGWCDKIQGATIPIN-QARPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPLDiSARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 601 VTPLTALKFAELTLKAGIPKGVVNILPGSGSLvGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlsnVKKVSLELGGKSPL 680
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAG---KKKVVLELGGNAAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVE 760
Cdd:cd07147 237 IVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 761 YCQRGVKEGATLVCGGNqvpRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFT 840
Cdd:cd07147 317 WVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYD--DFDEALAAVNDSKFGLQAGVFT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21314994 841 RDINKALYVSDKLQAGTVFVNtynktDV------AAPFGGFKQSGFGKDLGEAALNEYLRIK 896
Cdd:cd07147 392 RDLEKALRAWDELEVGGVVIN-----DVptfrvdHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
460-900 |
2.77e-104 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 330.31 E-value: 2.77e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 460 DVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDK 539
Cdd:cd07105 1 DADQAVEAAAAAFPA--WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWA-GFNVDLAAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 540 IQGATIPinQARPNRnLTLTKKEPVGVC-GIViPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGI 618
Cdd:cd07105 78 IIGGSIP--SDKPGT-LAMVVKEPVGVVlGIA-PWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 619 PKGVVNIL---PGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMG 695
Cdd:cd07105 154 PKGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAA-KHLKPVLLELGGKAPAIVLEDADLDAAANAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 696 MSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDrdtnhGPQ---NHEAHLRKLVEycqRGVKEGATL 772
Cdd:cd07105 233 LFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLvsaAAADRVKELVD---DALSKGAKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 773 VCGGNQVPRP-GFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSD 851
Cdd:cd07105 305 VVGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVK--DEEEAVRIANDSEYGLSAAVFTRDLARALAVAK 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 21314994 852 KLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd07105 383 RIESGAVHINGMTVHDEPtLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
407-899 |
2.51e-101 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 325.28 E-value: 2.51e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 407 NYVEKAVKKLT-----LQMPYQLFIGGEFVDAEGakTYSTINPTDGS-VICQVSLAQVSDVDKAVAAAKEAFENglWGKI 480
Cdd:TIGR01237 13 ENRQAFFKALAtvkeqLGKTYPLVINGERVETEN--KIVSINPCDKSeVVGTVSKASQEHAEHALQAAAKAFEA--WKKT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 481 NARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGATiPINQARPNRNLTLTk 560
Cdd:TIGR01237 89 DPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEA-DAEVAEAIDFMEYYARQMIELAKGK-PVNSREGETNQYVY- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 561 kEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDH 640
Cdd:TIGR01237 166 -TPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 641 PDVRKIGFTGSTEVGKHIMKSCAL-----SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 715
Cdd:TIGR01237 245 PKTSLITFTGSREVGTRIFERAAKvqpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 716 EDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGaTLVCGGNQVPRPGFFFQPTVFTDVE 795
Cdd:TIGR01237 325 HEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 796 DHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFTRD---INKAlyvSDKLQAGTVFvntYNKTDVAA-- 870
Cdd:TIGR01237 404 RKARLAQEEIFGPVVAFIRAS--DFDEALEIANNTEYGLTGGVISNNrdhINRA---KAEFEVGNLY---FNRNITGAiv 475
|
490 500 510
....*....|....*....|....*....|...
gi 21314994 871 ---PFGGFKQSGFG-KDLGEAALNEYLRIKTVT 899
Cdd:TIGR01237 476 gyqPFGGFKMSGTDsKAGGPDYLALFMQAKTVT 508
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
422-879 |
2.89e-101 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 324.97 E-value: 2.89e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 422 YQLFIGGEFVdaEGAKTYSTINPTDGS-VICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQ 500
Cdd:PRK03137 37 YPLIIGGERI--TTEDKIVSINPANKSeVVGRVSKATKELAEKAMQAALEAFET--WKKWSPEDRARILLRAAAIIRRRK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 501 EELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGAtIPINQaRPNRNLTLtKKEPVGVcGIVI-PWNYPLMM 579
Cdd:PRK03137 113 HEFSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMLKLADG-KPVES-RPGEHNRY-FYIPLGV-GVVIsPWNFPFAI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 580 LSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIM 659
Cdd:PRK03137 188 MAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 660 KSCALSN-----VKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKM 734
Cdd:PRK03137 268 ERAAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKEL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 735 KIGNPLDrDTNHGPQNHEAHLRKLVEYCQRGVKEGaTLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISR 814
Cdd:PRK03137 348 TVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIK 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21314994 815 FAdgDVDAVLSRANATEFGLASGVFTRD---INKA--------LYVSDKLQAGTVFVNtynktdvaaPFGGFKQSG 879
Cdd:PRK03137 426 AK--DFDHALEIANNTEYGLTGAVISNNrehLEKArrefhvgnLYFNRGCTGAIVGYH---------PFGGFNMSG 490
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
489-902 |
1.09e-100 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 320.14 E-value: 1.09e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 489 LYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGATIPINqaRPNRNLTLTKKePVGVCG 568
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSD--RPGENILLFKR-ALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 569 IVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGF 648
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 649 TGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVV 728
Cdd:PRK10090 157 TGSVSAGEKIMAAAA-KNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 729 EEVGKMKIGNPLDRDT-NHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFG 807
Cdd:PRK10090 236 EAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 808 PIMIISRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEA 887
Cdd:PRK10090 316 PVLPVVAFD--TLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKH 393
|
410
....*....|....*
gi 21314994 888 ALNEYLRIKTVTFEY 902
Cdd:PRK10090 394 GLHEYLQTQVVYLQS 408
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
442-899 |
3.14e-99 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 317.71 E-value: 3.14e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLALK- 520
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 521 -THVGMsiqTFRYFAGWCDKI------QGATIPINQARPNRNltltkkePVGVCGIVIPWNYPLMMLSWKTAACLAAGNT 593
Cdd:cd07101 79 vLDVAI---VARYYARRAERLlkprrrRGAIPVLTRTTVNRR-------PKGVVGVISPWNYPLTLAVSDAIPALLAGNA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 594 VVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVrkIGFTGSTEVGKHIMKSCAlSNVKKVSLE 673
Cdd:cd07101 149 VVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAG-RRLIGCSLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 674 LGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEA 753
Cdd:cd07101 226 LGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 754 HLRKLVEYCQRGVKEGATLVCGGNQVPRPG-FFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADgDVDAVlSRANATEF 832
Cdd:cd07101 306 QLDRVTAHVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVAD-DDEAI-ELANDTDY 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21314994 833 GLASGVFTRDINKALYVSDKLQAGTVFVN-----TYNKTDvaAPFGGFKQSGFGKDLGEAALNEYLRIKTVT 899
Cdd:cd07101 384 GLNASVWTRDGARGRRIAARLRAGTVNVNegyaaAWASID--APMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
447-888 |
1.20e-97 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 313.08 E-value: 1.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 447 GSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVytlALKTH--VG 524
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRA--WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSI---RPKAGfeVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 525 MSIQTFRYFAGWCDKIQGATIPINQARpnrnLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPL 604
Cdd:cd07152 76 AAIGELHEAAGLPTQPQGEILPSAPGR----LSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 605 TA-LKFAELTLKAGIPKGVVNILPGsGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIF 683
Cdd:cd07152 152 SGgVVIARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAG-RHLKKVSLELGGKNALIVL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 684 ADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEYCQ 763
Cdd:cd07152 230 DDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 764 RGVKEGATLVCGGNqvpRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGDVDAVLsrANATEFGLASGVFTRDI 843
Cdd:cd07152 310 DSVAAGARLEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVAL--ANDTEYGLSAGIISRDV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 21314994 844 NKALYVSDKLQAGTVFVN--TYNKtDVAAPFGGFKQSGFGKDLGEAA 888
Cdd:cd07152 385 GRAMALADRLRTGMLHINdqTVND-EPHNPFGGMGASGNGSRFGGPA 430
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
422-881 |
1.36e-97 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 314.12 E-value: 1.36e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 422 YQLFIGGEFVDAEGaKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFeNGLWGKINARDRGRLLYRLADLMEQHQE 501
Cdd:cd07082 2 FKYLINGEWKESSG-KTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAG-RGWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 502 ELATIEALDAGAVYTLALKtHVGMSIQTFRYFAGWCDKIQGATIPINQARPNRN-LTLTKKEPVGVCGIVIPWNYPLMML 580
Cdd:cd07082 80 EVANLLMWEIGKTLKDALK-EVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGkIAQVRREPLGVVLAIGPFNYPLNLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07082 159 VSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 661 scaLSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPL 740
Cdd:cd07082 239 ---QHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 741 DRDTNHGP---QNHEAHLRKLVEycqRGVKEGATLVCGGNQvpRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAd 817
Cdd:cd07082 316 DNGVDITPlidPKSADFVEGLID---DAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN- 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21314994 818 gDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNK--TDVaAPFGGFKQSGFG 881
Cdd:cd07082 390 -DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrgPDH-FPFLGRKDSGIG 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
431-899 |
1.74e-97 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 315.28 E-value: 1.74e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 431 VDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALD 510
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRA--WAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 511 AGAVYTLALK--THVGMsiqTFRYFAGWCDKI------QGAtIPI-NQARPNRNltltkkePVGVCGIVIPWNYPLMMLS 581
Cdd:PRK09407 104 TGKARRHAFEevLDVAL---TARYYARRAPKLlaprrrAGA-LPVlTKTTELRQ-------PKGVVGVISPWNYPLTLAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVrkIGFTGSTEVGKHIMKS 661
Cdd:PRK09407 173 SDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNADY--LMFTGSTATGRVLAEQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 662 CAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLD 741
Cdd:PRK09407 251 AG-RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 742 RDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGnqVPRPG---FFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdg 818
Cdd:PRK09407 330 YSADMGSLISEAQLETVSAHVDDAVAKGATVLAGG--KARPDlgpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVA-- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 819 DVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN-----TYNKTDvaAPFGGFKQSGFGKDLGEAALNEYL 893
Cdd:PRK09407 406 DVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVD--APMGGMKDSGLGRRHGAEGLLKYT 483
|
....*.
gi 21314994 894 RIKTVT 899
Cdd:PRK09407 484 ESQTIA 489
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
443-900 |
1.53e-96 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 310.77 E-value: 1.53e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 443 NPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGavytlalKTH 522
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQRE--WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTG-------KTM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 523 VGMS---IQTFryfagwCDKIQ-----GATIPINQARPNRNLTLTKK-----EPVGVCGIVIPWNYPLMMLSWKTAACLA 589
Cdd:cd07098 73 VDASlgeILVT------CEKIRwtlkhGEKALRPESRPGGLLMFYKRarveyEPLGVVGAIVSWNYPFHNLLGPIIAALF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 590 AGNTVVIKPAQVTPLTALKFAELTLKA----GIPKGVVNILPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKsCALS 665
Cdd:cd07098 147 AGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPE-TAEALTSHPVIDHITFIGSPPVGKKVMA-AAAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 666 NVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTN 745
Cdd:cd07098 225 SLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 746 HGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRP----GFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVD 821
Cdd:cd07098 305 VGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKAS--DDE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 822 AVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKT--DVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVT 899
Cdd:cd07098 383 EAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
.
gi 21314994 900 F 900
Cdd:cd07098 463 E 463
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
439-899 |
6.75e-92 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 298.12 E-value: 6.75e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 439 YSTINPTDGSVICQVSLAQVSDVDKAVAAAKeafenGLWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGavytLA 518
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALAA-----SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESG----LC 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 519 LKT---HVGMSIQTFRYFAGWCDKIQGATIPINQARP-NRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTV 594
Cdd:cd07146 72 LKDtryEVGRAADVLRFAAAEALRDDGESFSCDLTANgKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 595 VIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHImksCALSNVKKVSLEL 674
Cdd:cd07146 152 VLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 675 GGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEA- 753
Cdd:cd07146 229 GGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEa 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 754 --HLRKLVEycqRGVKEGATLVCGGNqvpRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATE 831
Cdd:cd07146 309 aiQIENRVE---EAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVK--DLDEAIAISNSTA 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 832 FGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLG-EAALNEYLRIKTVT 899
Cdd:cd07146 381 YGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGGKEGvREAMKEMTNVKTYS 450
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
442-900 |
1.96e-87 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 286.45 E-value: 1.96e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlKT 521
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQK--GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-GG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 522 HVGMSIQTFRYFagwCDKIQGATIPINQARPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 601
Cdd:cd07102 78 EIRGMLERARYM---ISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 602 TPLTALKFAELTLKAGIPKGVVNILPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLI 681
Cdd:cd07102 155 TPLCGERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAA-GRFIKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 682 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGP---QNHEAHLRKL 758
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPvvsARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 759 VeycQRGVKEGATLVCGGNQVPRP---GFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADgDVDAVLsRANATEFGLA 835
Cdd:cd07102 313 I---ADAIAKGARALIDGALFPEDkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKS-DAEAIA-LMNDSEYGLT 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21314994 836 SGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:cd07102 388 ASVWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYHL 452
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
440-898 |
1.59e-85 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 281.24 E-value: 1.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 440 STINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAl 519
Cdd:PRK09406 4 ATINPATGETVKTFTALTDDEVDAAIARAHARFRD--YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 520 KTHVGMSIQTFRYFAGWCDKIQgATIPINQARPNRNLTLTKKEPVGVCGIVIPWNYPLmmlsWKT----AACLAAGNTVV 595
Cdd:PRK09406 81 KAEALKCAKGFRYYAEHAEALL-ADEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 596 IKPAQVTPLTALKFAELTLKAGIPKGV-VNILPGSGSlVGQRLSDhPDVRKIGFTGSTEVGKHImKSCALSNVKKVSLEL 674
Cdd:PRK09406 156 LKHASNVPQTALYLADLFRRAGFPDGCfQTLLVGSGA-VEAILRD-PRVAAATLTGSEPAGRAV-AAIAGDEIKKTVLEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 675 GGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAH 754
Cdd:PRK09406 233 GGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 755 LRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGL 834
Cdd:PRK09406 313 RDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVA--DIDEAIEIANATTFGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21314994 835 ASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:PRK09406 391 GSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
424-881 |
8.02e-83 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 276.00 E-value: 8.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 424 LFIGGEFVDAEGAKTystINPTDG-SVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEE 502
Cdd:cd07125 36 IINGEETETGEGAPV---IDPADHeRTIGEVSLADAEDVDAALAIAAAAFAG--WSATPVEERAEILEKAADLLEANRGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 503 LATIEALDAGAvyTLAlKTHVGMS--IQTFRYFAGWCDKIQGATIPINQARPNRNLTLtkkEPVGVcGIVI-PWNYPLMM 579
Cdd:cd07125 111 LIALAAAEAGK--TLA-DADAEVReaIDFCRYYAAQARELFSDPELPGPTGELNGLEL---HGRGV-FVCIsPWNFPLAI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 580 LSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIM 659
Cdd:cd07125 184 FTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLIN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 660 KSCALSNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIG 737
Cdd:cd07125 264 RALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 738 NPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEgATLVCggnQVPRP---GFFFQPTVFTDV--EDHmyiaKEESFGPIMII 812
Cdd:cd07125 344 DPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIA---PAPLDdgnGYFVAPGIIEIVgiFDL----TTEVFGPILHV 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21314994 813 SRFADGDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGtvfvNTY-NKTDVAA-----PFGGFKQSGFG 881
Cdd:cd07125 416 IRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG----NLYiNRNITGAivgrqPFGGWGLSGTG 486
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
1-308 |
1.68e-82 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 267.74 E-value: 1.68e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 1 MKIAVIGQSLFGQEVYCQLRKEGHEVVGVFTIPDKD---GK---ADPLGLEAEKDGVPVFKFPRWRArgqalPEVVAKYQ 74
Cdd:COG0223 1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPagrGRkltPSPVKELALEHGIPVLQPESLKD-----PEFLEELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 75 ALGAELNVLPFCSQFIPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDV 154
Cdd:COG0223 76 ALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGTAPRRPQPEEGATYEGIQKKETAMINWDQPAEAIHNWIRGNDKVPGAW 234
Cdd:COG0223 156 GPDDTAGSLHDK-LAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAF 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21314994 235 TEACGQKLTFFnstlntsglvaQGEALPIPGAHRPGLVTKAG----LILFGNDdrMLLVKNIQLEDGKMMPASQFFKG 308
Cdd:COG0223 235 TTLDGKRLKIW-----------KARVLEEAGGGAPGTILAVDkdglLVACGDG--ALRLLELQPAGKKRMSAADFLRG 299
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
435-902 |
4.72e-80 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 267.15 E-value: 4.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 435 GAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAV 514
Cdd:cd07130 10 GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE--WRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 515 YTLAL----------KTHVGMSIQtfryfagwcdkIQGATIPinQARPNRNLtLTKKEPVGVCGIVIPWNYPLMMLSWKT 584
Cdd:cd07130 88 LPEGLgevqemidicDFAVGLSRQ-----------LYGLTIP--SERPGHRM-MEQWNPLGVVGVITAFNFPVAVWGWNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 585 AACLAAGNTVVIKPAQVTPLTALK----FAELTLKAGIPKGVVNILPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07130 154 AIALVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 661 SCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQmgmsSVFF----NKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKI 736
Cdd:cd07130 233 AVA-ARFGRSLLELGGNNAIIVMEDADLDLAVR----AVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 737 GNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTdVEDHMYIAKEESFGPIMIISRFA 816
Cdd:cd07130 308 GDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 817 dgDVDAVLSRANATEFGLASGVFTRDINKAL-----YVSDklqAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEAALN 890
Cdd:cd07130 387 --TLEEAIAWNNEVPQGLSSSIFTTDLRNAFrwlgpKGSD---CGIVNVNIgTSGAEIGGAFGGEKETGGGRESGSDAWK 461
|
490
....*....|..
gi 21314994 891 EYLRIKTVTFEY 902
Cdd:cd07130 462 QYMRRSTCTINY 473
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
411-899 |
2.26e-75 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 255.20 E-value: 2.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 411 KAVKKL--TLQMPYQLFIGGEFVDAEGAKTysTINPTD-GSVICQVSLAQVSDVDKAVAAAKEAFenGLWGKINARDRGR 487
Cdd:cd07083 6 EALRRVkeEFGRAYPLVIGGEWVDTKERMV--SVSPFApSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 488 LLYRLADLMEQHQEELATIEALDAGAVYTLALKThVGMSIQTFRYFAGWCDKIQGATIPINQARPNRNLTLTKKEPVGVC 567
Cdd:cd07083 82 LLLKAADLLRRRRRELIATLTYEVGKNWVEAIDD-VAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 568 giVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIG 647
Cdd:cd07083 161 --ISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGIN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 648 FTGSTEVGKHIMKSCA-----LSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQ 722
Cdd:cd07083 239 FTGSLETGKKIYEAAArlapgQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 723 FVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGaTLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAK 802
Cdd:cd07083 319 VLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 803 EESFGPIMIISRFADGDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAA--PFGGFKQSGF 880
Cdd:cd07083 398 EEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGvqPFGGFKLSGT 477
|
490 500
....*....|....*....|
gi 21314994 881 G-KDLGEAALNEYLRIKTVT 899
Cdd:cd07083 478 NaKTGGPHYLRRFLEMKAVA 497
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
1-180 |
4.59e-70 |
|
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.
Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 229.49 E-value: 4.59e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 1 MKIAVI--GQSLFGQEVYCQLRKEGHEVVGVFTIPDKDGKADPLGLEAEKDGVPVFKFPRWRARGQALPEVVAKYQALGA 78
Cdd:pfam00551 1 MKIAVLisGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 79 ELNVLPFCSQFIPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDD 158
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|..
gi 21314994 159 TVSTLYNRFLFPEGiKGMVQAV 180
Cdd:pfam00551 161 TAETLYNRVADLEH-KALPRVL 181
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
441-898 |
1.11e-69 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 238.61 E-value: 1.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 441 TINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlK 520
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 521 THVGMSiqtfryfAGWCDKIQGATIPINQARPN---RNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIK 597
Cdd:PRK13968 88 AEVAKS-------ANLCDWYAEHGPAMLKAEPTlveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 598 PAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDhPDVRKIGFTGSTEVGKHImKSCALSNVKKVSLELGGK 677
Cdd:PRK13968 161 HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAI-GAQAGAALKKCVLELGGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 678 SPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNhEAHLR- 756
Cdd:PRK13968 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMA-RFDLRd 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 757 KLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISrfADGDVDAVLSRANATEFGLAS 836
Cdd:PRK13968 318 ELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAIT--VAKDAEHALELANDSEFGLSA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21314994 837 GVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:PRK13968 396 TIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
442-881 |
8.35e-65 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 224.99 E-value: 8.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 442 INPTDGSVICQVSLAQVSDVDKAVAAAKEAFEN-GLWgkINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLAlK 520
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA-K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 521 THVGMSIQTFRYFAGWCDKIQGATIPIN--QARPNRnLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKP 598
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGREIPMGltPASAGR-IAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 599 AQVTPLTALKFAELTLKAGIPKGVVNILPgSGSLVGQRLSDHPDVRKIGFTGSTEVGKHiMKScALSNVKKVSLELGGKS 678
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWM-LRS-KLAPGTRCALEHGGAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 679 PLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKL 758
Cdd:cd07148 237 PVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 759 VEYCQRGVKEGATLVCGGNQVPRPgfFFQPTVFTDVEDHMYIAKEESFGPIMIIsrFADGDVDAVLSRANATEFGLASGV 838
Cdd:cd07148 317 EEWVNEAVAAGARLLCGGKRLSDT--TYAPTVLLDPPRDAKVSTQEIFGPVVCV--YSYDDLDEAIAQANSLPVAFQAAV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 21314994 839 FTRDINKALYVSDKLQAGTVFVN--TYNKTDvAAPFGGFKQSGFG 881
Cdd:cd07148 393 FTKDLDVALKAVRRLDATAVMVNdhTAFRVD-WMPFAGRRQSGYG 436
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
460-879 |
3.09e-62 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 217.14 E-value: 3.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 460 DVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGA--------VYTLALKthVGMSIQTFR 531
Cdd:cd07095 1 QVDAAVAAARAAFPG--WAALSLEERAAILRRFAELLKANKEELARLISRETGKplweaqteVAAMAGK--IDISIKAYH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 532 YFAGwcdkiqgatiPINQARPNRNLTLTKKePVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAE 611
Cdd:cd07095 77 ERTG----------ERATPMAQGRAVLRHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 612 LTLKAGIPKGVVNILPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCALSNVKKVSLELGGKSPLIIFADCDLNKA 691
Cdd:cd07095 146 LWEEAGLPPGVLNLVQGGRE-TGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 692 VQMGMSSVFFNKGENCIAAGRLFVEDS-IHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGA 770
Cdd:cd07095 225 AYLIVQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 771 TLVCGGNQVPRPGFFFQPTVF--TDVEDHmyiAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFTRDinKALY 848
Cdd:cd07095 305 EPLLAMERLVAGTAFLSPGIIdvTDAADV---PDEEIFGPLLQVYRYD--DFDEAIALANATRFGLSAGLLSDD--EALF 377
|
410 420 430
....*....|....*....|....*....|....
gi 21314994 849 --VSDKLQAGTVFVN-TYNKTDVAAPFGGFKQSG 879
Cdd:cd07095 378 erFLARIRAGIVNWNrPTTGASSTAPFGGVGLSG 411
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
425-881 |
1.48e-59 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 220.46 E-value: 1.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 425 FIGGEFVDAEGAkTYSTINPTDGS-VICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEEL 503
Cdd:PRK11904 551 WQAGPIINGEGE-ARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPA--WSRTPVEERAAILERAADLLEANRAEL 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 504 ATIEALDAGavytlalKT-HVGMS-----IQTFRYFAgwcdkiqgatipiNQARpnRNLTLTKKEP-------------- 563
Cdd:PRK11904 628 IALCVREAG-------KTlQDAIAevreaVDFCRYYA-------------AQAR--RLFGAPEKLPgptgesnelrlhgr 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 564 -VGVCgiVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPD 642
Cdd:PRK11904 686 gVFVC--ISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPR 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 643 VRKIGFTGSTEVGKHIMKSCALSNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIH 720
Cdd:PRK11904 764 IAGVAFTGSTETARIINRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIA 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 721 DqfvqKVVEEV-GKM---KIGNPLDRDTNHGPQNHEAHLRKLVEYCQRgVKEGATLVCggnQVPRP-----GFFFQPTVF 791
Cdd:PRK11904 844 D----RVIEMLkGAMaelKVGDPRLLSTDVGPVIDAEAKANLDAHIER-MKREARLLA---QLPLPagtenGHFVAPTAF 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 792 tdvE-DHMYIAKEESFGPIMIISRFADGDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVntyNKTDVAA 870
Cdd:PRK11904 916 ---EiDSISQLEREVFGPILHVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYV---NRNQIGA 989
|
490
....*....|....*.
gi 21314994 871 -----PFGGFKQSGFG 881
Cdd:PRK11904 990 vvgvqPFGGQGLSGTG 1005
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
464-898 |
1.12e-57 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 204.30 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 464 AVAAAKEAFENGLWGKINARDRgrLLYRLADLMEQHQEELatIEAL--DAGAVYTLALKTHVGMSIQTFRY----FAGWC 537
Cdd:cd07087 3 LVARLRETFLTGKTRSLEWRKA--QLKALKRMLTENEEEI--AAALyaDLGKPPAEAYLTEIAVVLGEIDHalkhLKKWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 538 DKIQGATIPINQarPNRnlTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAg 617
Cdd:cd07087 79 KPRRVSVPLLLQ--PAK--AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 618 IPKGVVNILPGSGSlVGQRLSDHP-DvrKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGM 696
Cdd:cd07087 154 FDPEAVAVVEGGVE-VATALLAEPfD--HIFFTGSPAVGKIVMEAAA-KHLTPVTLELGGKSPCIVDKDANLEVAARRIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 697 SSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVgKMKIGNPLDRDTNHGPQNHEAHLRKLVEYcqrgvKEGATLVCGG 776
Cdd:cd07087 230 WGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAI-KEFYGEDPKESPDYGRIINERHFDRLASL-----LDDGKVVIGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 777 nQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIM-IISRfadGDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQA 855
Cdd:cd07087 304 -QVDKEERYIAPTILDDVSPDSPLMQEEIFGPILpILTY---DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSS 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 21314994 856 GTVFVNtynktDV-------AAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:cd07087 380 GGVCVN-----DVllhaaipNLPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
426-885 |
1.21e-57 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 206.30 E-value: 1.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 426 IGGEFVDAEGAKtySTINPTDGSVIC-QVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEELA 504
Cdd:TIGR01238 42 IGHSYKADGEAQ--PVTNPADRRDIVgQVFHANLAHVQAAIDSAQQAFP--TWNATPAKERAAKLDRLADLLELHMPELM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 505 TIEALDAGAVYTLALkTHVGMSIQTFRYFAgwcdkiqgatipiNQARpnRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKT 584
Cdd:TIGR01238 118 ALCVREAGKTIHNAI-AEVREAVDFCRYYA-------------KQVR--DVLGEFSVESRGVFVCISPWNFPLAIFTGQI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAL 664
Cdd:TIGR01238 182 SAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 665 SNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDR 742
Cdd:TIGR01238 262 REDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 743 DTNHGP-------QNHEAHLRKLveycqRGV-KEGATLVCGGNQVPRPGFFFQPTVFTdvEDHMYIAKEESFGPIMIISR 814
Cdd:TIGR01238 342 TTDVGPvidaeakQNLLAHIEHM-----SQTqKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVR 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21314994 815 FADGDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVntyNKTDVAA-----PFGGFKQSGFGKDLG 885
Cdd:TIGR01238 415 YKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYV---NRNQVGAvvgvqPFGGQGLSGTGPKAG 487
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
426-881 |
2.36e-57 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 214.42 E-value: 2.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 426 IGGEfvdAEGAKTYSTINPTDGS-VICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELA 504
Cdd:COG4230 562 IAGE---AASGEARPVRNPADHSdVVGTVVEATAADVEAALAAAQAAFPA--WSATPVEERAAILERAADLLEAHRAELM 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 505 TIEALDAG------------AVytlalkthvgmsiqTF-RYFAgwcdkiqgatipiNQARpNRNLTLTKKEPVGVCGIVI 571
Cdd:COG4230 637 ALLVREAGktlpdaiaevreAV--------------DFcRYYA-------------AQAR-RLFAAPTVLRGRGVFVCIS 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 572 PWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGS 651
Cdd:COG4230 689 PWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGS 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 652 TEVGKHIMKSCALSNVKKVSL--ELGGKSPLIIfadcD----LNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDqfvq 725
Cdd:COG4230 769 TETARLINRTLAARDGPIVPLiaETGGQNAMIV----DssalPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIAD---- 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 726 KVVEEV-GKM---KIGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVcggnQVPRP-----GFFFQPTVF--TDV 794
Cdd:COG4230 841 RVLEMLkGAMaelRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVH----QLPLPeecanGTFVAPTLIeiDSI 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 795 EDhmyiAKEESFGPIMIISRFADGDVDAVLSRANATEFGLASGVFTRdINK-ALYVSDKLQAGTVFVntyNKTDVAA--- 870
Cdd:COG4230 917 SD----LEREVFGPVLHVVRYKADELDKVIDAINATGYGLTLGVHSR-IDEtIDRVAARARVGNVYV---NRNIIGAvvg 988
|
490
....*....|...
gi 21314994 871 --PFGGFKQSGFG 881
Cdd:COG4230 989 vqPFGGEGLSGTG 1001
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
438-881 |
5.10e-57 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 213.57 E-value: 5.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 438 TYSTINPTD-GSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYT 516
Cdd:PRK11905 568 TRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPE--WSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLA 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 517 LALkTHVGMSIQTFRYFAgwcdkiqgatipiNQARpnRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVI 596
Cdd:PRK11905 646 NAI-AEVREAVDFLRYYA-------------AQAR--RLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLA 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 597 KPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCALSNVKKVSL--EL 674
Cdd:PRK11905 710 KPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaET 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 675 GGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAH 754
Cdd:PRK11905 790 GGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEA 869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 755 LRKLVEYCQRGVKEGATLvcggNQVPRP-----GFFFQPTVFtdvE-DHMYIAKEESFGPIMIISRFADGDVDAVLSRAN 828
Cdd:PRK11905 870 QANIEAHIEAMRAAGRLV----HQLPLPaetekGTFVAPTLI---EiDSISDLEREVFGPVLHVVRFKADELDRVIDDIN 942
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 21314994 829 ATEFGLASGVFTRDINKALYVSDKLQAGTVFVntyNKTDVAA-----PFGGFKQSGFG 881
Cdd:PRK11905 943 ATGYGLTFGLHSRIDETIAHVTSRIRAGNIYV---NRNIIGAvvgvqPFGGEGLSGTG 997
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
422-881 |
7.78e-57 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 203.83 E-value: 7.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 422 YQLFIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAfeNGLWGKINARDRGRLLYRLADLMEQHQE 501
Cdd:PLN00412 16 YKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA--QKAWAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 502 ELAtiEALdagaVYTLA-----LKTHVGMSIQTFRYFA-------GWCDKIQGATIPINQarpnRN-LTLTKKEPVGVCG 568
Cdd:PLN00412 94 PIA--ECL----VKEIAkpakdAVTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNE----RNkYCLTSKIPLGVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 569 IVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGF 648
Cdd:PLN00412 164 AIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 649 TGStEVGKHIMKSCALSNVKkvsLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVV 728
Cdd:PLN00412 244 TGG-DTGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 729 EEVGKMKIGNPLDrDTNHGPQNHEAH---LRKLVEYCQrgvKEGATLVcggNQVPRPGFFFQPTVFTDVEDHMYIAKEES 805
Cdd:PLN00412 320 AKVAKLTVGPPED-DCDITPVVSESSanfIEGLVMDAK---EKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEP 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21314994 806 FGPIMIISRFadGDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTY-NKTDVAAPFGGFKQSGFG 881
Cdd:PLN00412 393 FGPVLPVIRI--NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIG 467
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
562-886 |
1.26e-56 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 201.30 E-value: 1.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 562 EPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVnILPGsGSLVGQRLSDHP 641
Cdd:cd07134 99 EPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEG-DAEVAQALLELP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 642 dVRKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHD 721
Cdd:cd07134 177 -FDHIFFTGSPAVGKIVMAAAA-KHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 722 QFVQKVVEEVGKMKIGNPLDRDT-NHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGnQVPRPGFFFQPTVFTDVEDHMYI 800
Cdd:cd07134 255 AFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG-QFDAAQRYIAPTVLTNVTPDMKI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 801 AKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtynktDVAA-------PFG 873
Cdd:cd07134 334 MQEEIFGPVLPIITYE--DLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN-----DVVLhflnpnlPFG 406
|
330
....*....|...
gi 21314994 874 GFKQSGFGKDLGE 886
Cdd:cd07134 407 GVNNSGIGSYHGV 419
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
419-902 |
4.65e-55 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 201.51 E-value: 4.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 419 QMPYQL--FIGGEFVDAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLM 496
Cdd:PLN02419 109 QMPPRVpnLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP--LWRNTPITTRQRVMLKFQELI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 497 EQHQEELATIEALDAGAVytlaLKTHVGMSIQTFRYFAGWCDKiqgATIPINQARPNRNL---TLTKKEPVGVCGIVIPW 573
Cdd:PLN02419 187 RKNMDKLAMNITTEQGKT----LKDSHGDIFRGLEVVEHACGM---ATLQMGEYLPNVSNgvdTYSIREPLGVCAGICPF 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 574 NYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQrLSDHPDVRKIGFTGSTE 653
Cdd:PLN02419 260 NFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNT 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 654 VGKHIMKSCALSNvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGR-LFVEDSihDQFVQKVVEEVG 732
Cdd:PLN02419 339 AGMHIYARAAAKG-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA--KSWEDKLVERAK 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 733 KMKIGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGF----FFQPTVFTDVEDHMYIAKEESFGP 808
Cdd:PLN02419 416 ALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGP 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 809 IMIISRfaDGDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTynKTDVAAPFGGF--KQSGFGKDL-- 884
Cdd:PLN02419 496 VLVCMQ--ANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPFFSFtgNKASFAGDLnf 571
|
490
....*....|....*....
gi 21314994 885 -GEAALNEYLRIKTVTFEY 902
Cdd:PLN02419 572 yGKAGVDFFTQIKLVTQKQ 590
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
1-310 |
3.27e-54 |
|
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 191.07 E-value: 3.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 1 MKIAVIGQSLFGQEVYCQLRKEGHEVVGVFTIPDKDG------KADPLGLEAEKDGVPVFKFPRwrargQALPEVVAKYQ 74
Cdd:TIGR00460 1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgkklTPPPVKVLAEEKGIPVFQPEK-----QRQLEELPLVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 75 ALGAELNVLPFCSQFIPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDV 154
Cdd:TIGR00460 76 ELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGTAPRRPQPEEGATYEGIQKKETAMINWDQPAEAIHNWIRGNDKVPGAW 234
Cdd:TIGR00460 156 EEEDNSGTLSDK-LSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALNPWPTAW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 235 TEACGQKLTFFNST-LNTSGLvaqgealpipgAHRPGLV---TKAGLILFGNDDRMLLVKNIQLEDGKMMPASQFFKGSA 310
Cdd:TIGR00460 235 LTFEGKNIKIHKAKvIDLSTY-----------KAKPGEIvyhNKKGILVACGKDGILLLLSLQPPGKKVMRAEDFYNGSR 303
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
424-879 |
2.80e-53 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 193.64 E-value: 2.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 424 LFIGGEFVDAEGAkTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEEL 503
Cdd:PRK09457 3 LWINGDWIAGQGE-AFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 504 ATIEALDAGA--------VYTLALKthVGMSIQTFRYFAGwcdkiqgatiPINQARPNRNLTLTKKePVGVCGIVIPWNY 575
Cdd:PRK09457 80 AEVIARETGKplweaateVTAMINK--IAISIQAYHERTG----------EKRSEMADGAAVLRHR-PHGVVAVFGPYNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 576 PLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGsGSLVGQRLSDHPDVRKIGFTGSTEVG 655
Cdd:PRK09457 147 PGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 656 KHIMKSCALSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIH-DQFVQKVVEEVGKM 734
Cdd:PRK09457 226 YLLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 735 KIGNPlDRDTN--HGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVF--TDVEDhmyIAKEESFGPIM 810
Cdd:PRK09457 306 TVGRW-DAEPQpfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIIdvTGVAE---LPDEEYFGPLL 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21314994 811 IISRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVfvnTYNK----TDVAAPFGGFKQSG 879
Cdd:PRK09457 382 QVVRYD--DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIV---NWNKpltgASSAAPFGGVGASG 449
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
3-182 |
2.94e-50 |
|
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.
Pssm-ID: 187712 [Multi-domain] Cd Length: 173 Bit Score: 174.78 E-value: 2.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 3 IAVIGQSLFGQEVYCQLR-KEGHEVVGVFTIPDKDGKADPLGLEAEKDgvpvfkfPRWRARGQALPEVVAKYQALGAELN 81
Cdd:cd08369 1 IVILGSGNIGQRVLKALLsKEGHEIVGVVTHPDSPRGTAQLSLELVGG-------KVYLDSNINTPELLELLKEFAPDLI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 82 VLPFCSQFIPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTVS 161
Cdd:cd08369 74 VSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAG 153
|
170 180
....*....|....*....|.
gi 21314994 162 TLYNRfLFPEGIKGMVQAVRL 182
Cdd:cd08369 154 TLYQR-LIELGPKLLKEALQK 173
|
|
| FDH_Hydrolase_C |
cd08703 |
The C-terminal subdomain of the hydrolase domain on the bi-functional protein ... |
206-306 |
2.32e-49 |
|
The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding.
Pssm-ID: 187731 [Multi-domain] Cd Length: 100 Bit Score: 169.45 E-value: 2.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 206 KETAMINWDQPAEAIHNWIRGNDKVPGAWTEACGQKLTFFNSTLNTSGLVaQGEALPIPGAHRPGLVTKAGLILFGNDDR 285
Cdd:cd08703 1 KELAKINWDQTAEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKP-PGGEVEVEGLERPGIVHKNGLLITGSDGK 79
|
90 100
....*....|....*....|.
gi 21314994 286 MLLVKNIQLEDGKMMPASQFF 306
Cdd:cd08703 80 MVNVKRLQFEDGKMIPASKYG 100
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
560-898 |
2.47e-48 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 179.45 E-value: 2.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 560 KKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNILPGsGSLVGQRLSD 639
Cdd:PTZ00381 106 IPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 640 HP-DVrkIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDS 718
Cdd:PTZ00381 184 EPfDH--IFFTGSPRVGKLVMQAAA-ENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 719 IHDQFVQKVVEEVGKMkIGNPLDRDTNHGPQNHEAHLRKLVEYCQrgvKEGATLVCGGnQVPRPGFFFQPTVFTDVEDHM 798
Cdd:PTZ00381 261 IKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIK---DHGGKVVYGG-EVDIENKYVAPTIIVNPDLDS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 799 YIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN--TYNKTDVAAPFGGFK 876
Cdd:PTZ00381 336 PLMQEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGVG 413
|
330 340
....*....|....*....|..
gi 21314994 877 QSGFGKDLGEAALNEYLRIKTV 898
Cdd:PTZ00381 414 NSGMGAYHGKYGFDTFSHPKPV 435
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
482-881 |
4.28e-48 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 177.29 E-value: 4.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 482 ARDRGRLLYRLADLMEQHQEELAtiEALDA-----GAVYTLALKthVGMSIQTFRY----FAGWCdkiqgatipinqaRP 552
Cdd:cd07133 19 LEERRDRLDRLKALLLDNQDALA--EAISAdfghrSRHETLLAE--ILPSIAGIKHarkhLKKWM-------------KP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 553 NR---NLTLT------KKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVV 623
Cdd:cd07133 82 SRrhvGLLFLpakaevEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 624 NILPGSGslVGQRLS----DHpdvrkIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSV 699
Cdd:cd07133 162 VVTGGAD--VAAAFSslpfDH-----LLFTGSTAVGRHVMRAAA-ENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 700 FFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKM---KIGNPldrdtNHGPQNHEAHLRKLVEYCQRGVKEGATLV-CG 775
Cdd:cd07133 234 LLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIeLN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 776 GNQVPRPGF-FFQPTVFTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQ 854
Cdd:cd07133 309 PAGEDFAATrKLPPTLVLNVTDDMRVMQEEIFGPILPILTYD--SLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTH 386
|
410 420 430
....*....|....*....|....*....|....
gi 21314994 855 AGTVFVNtynktDVA-------APFGGFKQSGFG 881
Cdd:cd07133 387 SGGVTIN-----DTLlhvaqddLPFGGVGASGMG 415
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
425-902 |
6.76e-48 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 178.49 E-value: 6.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 425 FIGGEFvdAEGAKTYSTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEELA 504
Cdd:PLN02315 24 YVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAK--IWMQVPAPKRGEIVRQIGDALRAKLDYLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 505 TIEALDAGAVYTLALKtHVGMSIQTFRYFAGWCDKIQGATIPinQARPNrNLTLTKKEPVGVCGIVIPWNYPLMMLSWKT 584
Cdd:PLN02315 100 RLVSLEMGKILAEGIG-EVQEIIDMCDFAVGLSRQLNGSIIP--SERPN-HMMMEVWNPLGIVGVITAFNFPCAVLGWNA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 585 AACLAAGNTVVIKPAQVTPLTALK----FAELTLKAGIPKGVVNILPGsGSLVGQRLSDHPDVRKIGFTGSTEVGKhIMK 660
Cdd:PLN02315 176 CIALVCGNCVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGL-MVQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 661 SCALSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPL 740
Cdd:PLN02315 254 QTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 741 DRDTNHGPQnHEAHLRKLVEYCQRGVK-EGATLVCGGNQVPRPGFFFQPTVfTDVEDHMYIAKEESFGPIMIISRFAdgD 819
Cdd:PLN02315 334 EKGTLLGPL-HTPESKKNFEKGIEIIKsQGGKILTGGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFK--T 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 820 VDAVLSRANATEFGLASGVFTRD---INKAL--YVSDklqAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEAALNEYL 893
Cdd:PLN02315 410 LEEAIEINNSVPQGLSSSIFTRNpetIFKWIgpLGSD---CGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYM 486
|
....*....
gi 21314994 894 RIKTVTFEY 902
Cdd:PLN02315 487 RRSTCTINY 495
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
560-898 |
1.74e-47 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 175.49 E-value: 1.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 560 KKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNILPG----SGSLVGQ 635
Cdd:cd07135 105 RKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVVQGgvpeTTALLEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 636 RLSdhpdvrKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 715
Cdd:cd07135 184 KFD------KIFYTGSGRVGRIIAEAAA-KHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 716 EDSIHDQFVQ---KVVEEVgkmkIGNPLDRDTNHGPQNHEAHLRKLVEYCQrgvKEGATLVCGG--NQVPRpgfFFQPTV 790
Cdd:cd07135 257 DPSVYDEFVEelkKVLDEF----YPGGANASPDYTRIVNPRHFNRLKSLLD---TTKGKVVIGGemDEATR---FIPPTI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 791 FTDVEDHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN-TYNKTDV- 868
Cdd:cd07135 327 VSDVSWDDSLMSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdTLIHVGVd 404
|
330 340 350
....*....|....*....|....*....|
gi 21314994 869 AAPFGGFKQSGFGKDLGEAALNEYLRIKTV 898
Cdd:cd07135 405 NAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
1-200 |
2.05e-45 |
|
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187715 [Multi-domain] Cd Length: 204 Bit Score: 162.23 E-value: 2.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 1 MKIAVIGQSLFGQEVYCQLRKEGHEVVGVFTIPDKD---GK---ADPLGLEAEKDGVPVFKFPRWRArgqalPEVVAKYQ 74
Cdd:cd08646 1 MRIVFMGTPDFAVPSLEALLKSGHEVVAVVTQPDKPrgrGKkltPSPVKELALELGLPVLQPEKLKD-----EEFLEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 75 ALGAELNVLPFCSQFIPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDV 154
Cdd:cd08646 76 ALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21314994 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGTAPRRPQPEEGATY 200
Cdd:cd08646 156 DPDDTAGELLDK-LAELGADLLLEVLDDIEAGKLNPVPQDESEATY 200
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
426-881 |
3.15e-45 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 177.09 E-value: 3.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 426 IGGEFVDAEGAKTystINPTDGS-VICQVSLAQVSDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEELA 504
Cdd:PRK11809 651 LEDPVAAGEMSPV---INPADPRdIVGYVREATPAEVEQALESAVNAAP--IWFATPPAERAAILERAADLMEAQMQTLM 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 505 TIEALDAGAVYTLALkTHVGMSIQTFRYFAGwcdkiqgatipinQARPN-RNLTLTKKEPVgVCgiVIPWNYPLMMLSWK 583
Cdd:PRK11809 726 GLLVREAGKTFSNAI-AEVREAVDFLRYYAG-------------QVRDDfDNDTHRPLGPV-VC--ISPWNFPLAIFTGQ 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 584 TAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCA 663
Cdd:PRK11809 789 VAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLA 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 664 --LSNV-KKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGN 738
Cdd:PRK11809 869 grLDPQgRPIPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGN 948
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 739 PlDR-DTNHGP-------QNHEAHLrklveycQRGVKEGATLVcggnQVPRP-------GFFFQPTVftdVE-DHMYIAK 802
Cdd:PRK11809 949 P-DRlSTDIGPvidaeakANIERHI-------QAMRAKGRPVF----QAAREnsedwqsGTFVPPTL---IElDSFDELK 1013
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 803 EESFGPIMIISRFADGDVDAVLSRANATEFGLASGVFTR-DINKAlYVSDKLQAGTVFVntyNKTDVAA-----PFGGFK 876
Cdd:PRK11809 1014 REVFGPVLHVVRYNRNQLDELIEQINASGYGLTLGVHTRiDETIA-QVTGSAHVGNLYV---NRNMVGAvvgvqPFGGEG 1089
|
....*
gi 21314994 877 QSGFG 881
Cdd:PRK11809 1090 LSGTG 1094
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
560-881 |
3.15e-45 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 169.22 E-value: 3.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 560 KKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNILPG----SGSLVGQ 635
Cdd:cd07136 97 YYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEGgveeNQELLDQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 636 RLsDHpdvrkIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 715
Cdd:cd07136 176 KF-DY-----IFFTGSVRVGKIVMEAAA-KHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 716 EDSIHDQFVQKVVEEVGKMKIGNPLDRDtNHGPQNHEAHLRKLVEYCqrgvkEGATLVCGGNqVPRPGFFFQPTVFTDVE 795
Cdd:cd07136 249 HESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLL-----DNGKIVFGGN-TDRETLYIEPTILDNVT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 796 DHMYIAKEESFGPIMIISRFAdgDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAG------TV--FVNTYnktd 867
Cdd:cd07136 322 WDDPVMQEEIFGPILPVLTYD--TLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGggcindTImhLANPY---- 395
|
330
....*....|....
gi 21314994 868 vaAPFGGFKQSGFG 881
Cdd:cd07136 396 --LPFGGVGNSGMG 407
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
1-201 |
3.34e-43 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187724 [Multi-domain] Cd Length: 192 Bit Score: 155.31 E-value: 3.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 1 MKIAVIGQSLFGQEVYCQLRKEGHEVVGVFTIPDKDGKAdplgLEAEKDGVPVFKfprwrarGQALPEVVAKYQALGAEL 80
Cdd:cd08822 1 MKIAIAGQKWFGTAVLEALRARGIALLGVAAPEEGDRLA----AAARTAGSRGLP-------RAGVAVLPADAIPPGTDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 81 NVLPFCSQFIPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTV 160
Cdd:cd08822 70 IVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21314994 161 STLYNRFLFPEGIKGMVQAV-RLIAEGTAPRRPQPEEGATYE 201
Cdd:cd08822 150 AELWRRALAPMGVKLLTQVIdALLRGGNLPAQPQDERLATWE 191
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
409-879 |
4.57e-43 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 164.68 E-value: 4.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 409 VEKAVKKL---TLQMPyqLFIGGEFVDAEGAKTysTINPTD-GSVICQVSLAQVSDVDKAVAAAKEAFENglWGKINARD 484
Cdd:cd07123 19 LQEALAELkslTVEIP--LVIGGKEVRTGNTGK--QVMPHDhAHVLATYHYADAALVEKAIEAALEARKE--WARMPFED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 485 RGRLLYRLADLM--EQHQEELAT---------IEA-LDAGAvytlalkthvgMSIQTFRYFAGWCDKIQgATIPINQARP 552
Cdd:cd07123 93 RAAIFLKAADLLsgKYRYELNAAtmlgqgknvWQAeIDAAC-----------ELIDFLRFNVKYAEELY-AQQPLSSPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 553 NRNlTLTKKEPVGVCGIVIPWNY----------PLMMlswktaaclaaGNTVVIKPAQVTPLTALKFAELTLKAGIPKGV 622
Cdd:cd07123 161 VWN-RLEYRPLEGFVYAVSPFNFtaiggnlagaPALM-----------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 623 VNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCA--LSNVK---KVSLELGGKSPLIIFADCDLNKAVQMGMS 697
Cdd:cd07123 229 INFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGenLDRYRtypRIVGETGGKNFHLVHPSADVDSLVTATVR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 698 SVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEYCQRGVKE-GATLVCGG 776
Cdd:cd07123 309 GAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 777 NQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGDVDAVLSRAN-ATEFGLASGVFTRD---INKAlyvSDK 852
Cdd:cd07123 389 KCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDtTSPYALTGAIFAQDrkaIREA---TDA 465
|
490 500 510
....*....|....*....|....*....|.
gi 21314994 853 LQ--AGTVFVNTYNKTDVAA--PFGGFKQSG 879
Cdd:cd07123 466 LRnaAGNFYINDKPTGAVVGqqPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
551-882 |
4.22e-37 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 145.44 E-value: 4.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 551 RPNRNLT------LTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtlkagIPKGVVN 624
Cdd:cd07132 82 PVKKNLAtllddvYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLDK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 625 IL--------PGSGSLVGQRLsDHpdvrkIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGM 696
Cdd:cd07132 157 ECypvvlggvEETTELLKQRF-DY-----IFYTGSTSVGKIVMQAAA-KHLTPVTLELGGKSPCYVDKSCDIDVAARRIA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 697 SSVFFNKGENCIAAGRLFVEDSIHDQFVQKvVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEYCqrgvkEGATLVCGG 776
Cdd:cd07132 230 WGKFINAGQTCIAPDYVLCTPEVQEKFVEA-LKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVAIGG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 777 NQVPRPGfFFQPTVFTDVEDHMYIAKEESFGPIMIIsrFADGDVDAVLSRANATEFGLASGVFTRD---INKALyvsDKL 853
Cdd:cd07132 304 QTDEKER-YIAPTVLTDVKPSDPVMQEEIFGPILPI--VTVNNLDEAIEFINSREKPLALYVFSNNkkvINKIL---SNT 377
|
330 340 350
....*....|....*....|....*....|....*.
gi 21314994 854 QAGTVFVNtynktDV-------AAPFGGFKQSGFGK 882
Cdd:cd07132 378 SSGGVCVN-----DTimhytldSLPFGGVGNSGMGA 408
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
2-166 |
3.31e-32 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187720 [Multi-domain] Cd Length: 180 Bit Score: 123.53 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 2 KIAVIGQSLFGQEVYCQLRKEGHEVVGVFTIPDKDGKADP----LGLEAEKDGVPVFKFPRWRArgqalPEVVAKYQALG 77
Cdd:cd08651 1 RIVFIGCVEFSLIALEAILEAGGEVVGVITLDDSSSNNDSdyldLDSFARKNGIPYYKFTDIND-----EEIIEWIKEAN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 78 AELNvlpFC---SQFIPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDV 154
Cdd:cd08651 76 PDII---FVfgwSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPI 152
|
170
....*....|..
gi 21314994 155 LPDDTVSTLYNR 166
Cdd:cd08651 153 DKDDTANSLYDK 164
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
461-894 |
3.64e-30 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 124.66 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 461 VDKAVAAAKEAfeNGLWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLALKthVGMSIQTFRYFAgwcDKI 540
Cdd:cd07084 1 PERALLAADIS--TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAEN--ICGDQVQLRARA---FVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 541 QGATIPINQA-RPNRNLTLTKKE---PVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKA 616
Cdd:cd07084 74 YSYRIPHEPGnHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 617 GI-PKGVVNILPGSGSLvGQRLSDHPDVRKIGFTGSTEVGKHIMkscALSNVKKVSLELGGKSPLIIFADCDLNKAV--- 692
Cdd:cd07084 154 GLlPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKLA---LDAKQARIYLELAGFNWKVLGPDAQAVDYVawq 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 693 ---QMGMSSvffnkGENCIAAGRLFVEDsihDQFVQKVVEEVgKMKIGNPLDRDTNHGPQNHEAHLRKLVEycqRGVKEG 769
Cdd:cd07084 230 cvqDMTACS-----GQKCTAQSMLFVPE---NWSKTPLVEKL-KALLARRKLEDLLLGPVQTFTTLAMIAH---MENLLG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 770 ATLVCGGNQVPR------PGFFFQPTVF--TDVEDHMYIA-KEESFGPIMIISRFADGDVDAVLSRANATEFGLASGVFT 840
Cdd:cd07084 298 SVLLFSGKELKNhsipsiYGACVASALFvpIDEILKTYELvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYS 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 21314994 841 RDINKALYVSDKLQ-AGTVFVNTYNKTDVAAP---FGGFKQSGFGKDLGEA-ALNEYLR 894
Cdd:cd07084 378 NDPIFLQELIGNLWvAGRTYAILRGRTGVAPNqnhGGGPAADPRGAGIGGPeAIKLVWR 436
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
46-313 |
3.73e-30 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 121.72 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 46 AEKDGVPVFKfprwrARGQALPEVVAKYQALGAELnVLPFCSQF-IPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLI 124
Cdd:PRK06988 51 AAEHGIPVIT-----PADPNDPELRAAVAAAAPDF-IFSFYYRHmIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 125 HGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTVSTLYNrflfpegiKGMVQAVRLIAE-------GTAPRRPQPEEG 197
Cdd:PRK06988 125 NGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFD--------KVTVAAEQTLWRvlpallaGEAPHLPNDLAQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 198 ATYEGIQKKETAMINWDQPAEAIHNWIRG-NDKVPGAWTEACGQKLtffnstlntsgLVAQ----GEALPIPGAHRPGLV 272
Cdd:PRK06988 197 GSYFGGRKPEDGRIDWSKPAAQVYNLIRAvAPPYPGAFTDLGGTRF-----------VVARarlaAPGAAAARDLPPGLH 265
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 21314994 273 TKAGLILFGNDDRMLL----VKNIQLEDGKMMPASQFFKGSASSA 313
Cdd:PRK06988 266 VSDNALFGVCGDGRAVsileLRRQQDGGETVVTPAQFAQFIHSSR 310
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
562-881 |
1.70e-26 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 113.66 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 562 EPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNILPGSGSLVGQRLSDHP 641
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYLDTKAIKVIEGGVPETTALLEQKW 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 642 DvrKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVF-FNKGENCIAAGRLFVEDSIH 720
Cdd:cd07137 179 D--KIFFTGSPRVGRIIMAAAA-KHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 721 DQFVQKVVEEVGKMKIGNP-----LDRDTNhgpQNHEAHLRKLVEYcqrgvKEGATLVCGGNQVPRPGFFFQPTVFTDVE 795
Cdd:cd07137 256 PTLIDALKNTLEKFFGENPkeskdLSRIVN---SHHFQRLSRLLDD-----PSVADKIVHGGERDEKNLYIEPTILLDPP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 796 DHMYIAKEESFGPIM-IIS-RFADGDVDAVLSRANAtefgLASGVFTRdiNKALY--VSDKLQAGTVFVNtynktDVAA- 870
Cdd:cd07137 328 LDSSIMTEEIFGPLLpIITvKKIEESIEIINSRPKP----LAAYVFTK--NKELKrrIVAETSSGGVTFN-----DTVVq 396
|
330
....*....|....*..
gi 21314994 871 ------PFGGFKQSGFG 881
Cdd:cd07137 397 yaidtlPFGGVGESGFG 413
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
562-900 |
2.71e-25 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 110.52 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 562 EPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNILPGSGSLVGQRLSDHP 641
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTETTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 642 DvrKIGFTGSTEVGKHIMKSCAlSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVF-FNKGENCIAAGRLFVEDSIH 720
Cdd:PLN02174 190 D--KIFYTGSSKIGRVIMAAAA-KHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 721 DQFVQKVVEEVGKMKIGNPLD-----RDTNhgpQNHEAHLRKLVEYcqrgvKEGATLVCGGNQVPRPGFFFQPTVFTDVE 795
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPMEskdmsRIVN---STHFDRLSKLLDE-----KEVSDKIVYGGEKDRENLKIAPTILLDVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 796 DHMYIAKEESFGPIMIISRFADGD--VDAVLSRANAtefgLASGVFTRDINKALYVSDKLQAGTVFVNtynktDVAA--- 870
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEesFDVIRSRPKP----LAAYLFTHNKKLKERFAATVSAGGIVVN-----DIAVhla 409
|
330 340 350
....*....|....*....|....*....|....
gi 21314994 871 ----PFGGFKQSGFGKDLGEAALNEYLRIKTVTF 900
Cdd:PLN02174 410 lhtlPFGGVGESGMGAYHGKFSFDAFSHKKAVLY 443
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
562-882 |
3.36e-24 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 107.12 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 562 EPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTAlKFaeltLKAGIPK----GVVNILPGsGSLVGQRL 637
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS-AF----LAANIPKyldsKAVKVIEG-GPAVGEQL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 638 SDHP-DvrKIGFTGSTEVGKHIMkSCALSNVKKVSLELGGKSPLIIfaDC-DLNKAVQMGMSSVFFNK-----GENCIAA 710
Cdd:PLN02203 181 LQHKwD--KIFFTGSPRVGRIIM-TAAAKHLTPVALELGGKCPCIV--DSlSSSRDTKVAVNRIVGGKwgscaGQACIAI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 711 GRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNhEAHLRKLVEYCQ-RGVKegATLVCGGNQVPRpGFFFQPT 789
Cdd:PLN02203 256 DYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILN-KKHFQRLSNLLKdPRVA--ASIVHGGSIDEK-KLFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 790 VFTDVEDHMYIAKEESFGPIM-IISRfadGDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVfvnTYNKTDV 868
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLpIITV---KKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDAII 405
|
330
....*....|....*....
gi 21314994 869 -----AAPFGGFKQSGFGK 882
Cdd:PLN02203 406 qyacdSLPFGGVGESGFGR 424
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
1-202 |
1.44e-23 |
|
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle.
Pssm-ID: 187713 [Multi-domain] Cd Length: 203 Bit Score: 99.34 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 1 MKIAVIGQSLFGQEVYCQLRKEGHEVVGVFTIPDKDGKA---DPLGLEAEKDGVPVF-----KFPRWRARGQAL-PEVVA 71
Cdd:cd08644 1 MKAVVFAYHEVGYRCLEALLAAGFEVVAVFTHTDNPGENiwfGSVAQLAREHGIPVFtpddiNHPEWVERLRALkPDLIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 72 KYqalgaelnvlpFCSQFIPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKE 151
Cdd:cd08644 81 SF-----------YYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21314994 152 CDVLPDDTVSTLYNRFLFPEGIKgMVQAVRLIAEGTAPRRPQPEEGATYEG 202
Cdd:cd08644 150 VPILPDDTAKSLFHKLCVAARRL-LARTLPALKAGKARERPQDETQASYFG 199
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
461-817 |
5.81e-21 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 96.84 E-value: 5.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 461 VDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGavYTLALKT-HVGMSIQTFRYFA----- 534
Cdd:cd07129 1 VDAAAAAAAAAFE--SYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARLQgELGRTTGQLRLFAdlvre 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 535 -GWcdkiQGATI----PINQARPNRNLTLTKKePVGVCGIVIPWNYPLM--MLSWKTAACLAAGNTVVIK--PAQvtPLT 605
Cdd:cd07129 77 gSW----LDARIdpadPDRQPLPRPDLRRMLV-PLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKahPAH--PGT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 606 ALKFAELTLKA----GIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCALSNV-KKVSLELGGKSPL 680
Cdd:cd07129 150 SELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSVNPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 681 IIFADCDLNKAVQMGMS---SVFFNKGENCIAAGRLFVEDSIH-DQFVQKVVEEVGKMKIGNPLdrdtNHGPQNHeahlr 756
Cdd:cd07129 230 FILPGALAERGEAIAQGfvgSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQTML----TPGIAEA----- 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21314994 757 klveYcQRGVKE-----GATLVCGGNQvPRPGFFFQPTVF-TDVEDhmYIAK----EESFGPIMIISRFAD 817
Cdd:cd07129 301 ----Y-RQGVEAlaaapGVRVLAGGAA-AEGGNQAAPTLFkVDAAA--FLADpalqEEVFGPASLVVRYDD 363
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
25-186 |
6.09e-21 |
|
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 91.63 E-value: 6.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 25 EVVGVFTipdkDgKADPLGLE-AEKDGVPVF-----KFPRWRARGQALPEVVAKYQAlgaELNVL---------PFCSQF 89
Cdd:COG0299 30 EIVLVIS----N-RPDAYGLErARAAGIPTFvldhkDFPSREAFDAALLEALDAYGP---DLVVLagfmriltpEFVRAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 90 iPMEVINaprhgsiiYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTVSTLYNRFLf 169
Cdd:COG0299 102 -PGRIIN--------IHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAARIL- 171
|
170
....*....|....*..
gi 21314994 170 PEGIKGMVQAVRLIAEG 186
Cdd:COG0299 172 EQEHRLYPEAIRLLAEG 188
|
|
| Formyl_trans_C |
pfam02911 |
Formyl transferase, C-terminal domain; |
205-308 |
1.33e-20 |
|
Formyl transferase, C-terminal domain;
Pssm-ID: 460744 [Multi-domain] Cd Length: 99 Bit Score: 87.33 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 205 KKETAMINWDQPAEAIHNWIRGNDKVPGAWTEACGQKLTFFNStlntsglvaqgEALPIPGAHRPGLV--TKAGLILFGN 282
Cdd:pfam02911 3 KKEDGRIDWNQPAEEIHRLIRALDPWPGAYTFLNGKRVKLLKA-----------SVLDQESGAAPGTIvtVDKGGLLVAC 71
|
90 100
....*....|....*....|....*.
gi 21314994 283 DDRMLLVKNIQLEDGKMMPASQFFKG 308
Cdd:pfam02911 72 GDGALLILELQLEGKKPMSAEDFLNG 97
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
19-272 |
1.41e-20 |
|
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;
Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 96.98 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 19 LRKEGHEVVGVFTIPDKDGKADPLG----LEAEKdGVPVF-----KFPRWRARGQAL-PEVVAK--YQALGAElnvlpfc 86
Cdd:PRK08125 19 LLAAGYEIAAVFTHTDNPGENHFFGsvarLAAEL-GIPVYapedvNHPLWVERIRELaPDVIFSfyYRNLLSD------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 87 sqfipmEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTVSTLYNR 166
Cdd:PRK08125 91 ------EILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 167 FLFPEGiKGMVQAVRLIAEGTAPRRPQPEEGATYEGIQKKETAMINWDQPAEAIHNWIRG-NDKVPGAWTEACGQKLTff 245
Cdd:PRK08125 165 LCHAAR-QLLEQTLPAIKHGNIPEIPQDESQATYFGRRTPADGLIDWHKPASTLHNLVRAvTDPWPGAFSYVGEQKFT-- 241
|
250 260
....*....|....*....|....*..
gi 21314994 246 nstlntsglVAQGEALPIPGAHRPGLV 272
Cdd:PRK08125 242 ---------VWSSRVLPDASGAQPGTV 259
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
25-233 |
1.17e-17 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 85.13 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 25 EVVGVFTIPDKDGK------ADPLGLEAEKDGVPVFK-FPRWRARGqalPEVVAKYQALGAELNVLPFCSQFIPMEVINA 97
Cdd:PLN02285 37 EVAAVVTQPPARRGrgrklmPSPVAQLALDRGFPPDLiFTPEKAGE---EDFLSALRELQPDLCITAAYGNILPQKFLDI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 98 PRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTVSTLYNRfLFPEGIKGMV 177
Cdd:PLN02285 114 PKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPL-LFELGTKLLL 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21314994 178 QAVRLIAEGTAPRR--PQPEEGATYEGIQKKETAMINWDQPAEAIHNWIRGNDKVPGA 233
Cdd:PLN02285 193 RELPSVLDGSAKDKatPQDDSKATHAPKISPEESWLSFDEEARVLHNKVRAFAGWPGT 250
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
38-174 |
3.13e-17 |
|
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 80.51 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 38 KADPLGLE-AEKDGVPVF-----KFPRWRARGQALPEVVAKYQAlgaELNVL---------PFCSQFiPMEVINaprhgs 102
Cdd:cd08645 36 NPDAYGLErAKKAGIPTFvinrkDFPSREEFDEALLELLKEYKV---DLIVLagfmrilspEFLEAF-PGRIIN------ 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21314994 103 iIyHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTVSTLYNRF------LFPEGIK 174
Cdd:cd08645 106 -I-HPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPETLAERIhalehrLYPEAIK 181
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
67-181 |
1.05e-15 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187721 [Multi-domain] Cd Length: 152 Bit Score: 74.94 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 67 PEVVAKYQALGAELNVLPFCSqFIPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGD-KKGGFTIFWADDGLDTGD 145
Cdd:cd08653 37 PEVVAALRALAPDVVSVYGCG-IIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDpDNVGVTVHLVDAGIDTGD 115
|
90 100 110
....*....|....*....|....*....|....*.
gi 21314994 146 LLLQKECDVLPDDTVSTLYNRfLFPEGIKGMVQAVR 181
Cdd:cd08653 116 VLAQARPPLAAGDTLLSLYLR-LYRAGVELMVEAIA 150
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
425-817 |
2.06e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 80.13 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 425 FIGGEFVDAEGAKTySTINPTDGSVICQVSlAQVSDVDKAVAAAKEAFENGLWGkINARDRGRLLYRLADLMEQHQEELA 504
Cdd:PRK11903 8 YVAGRWQAGSGAGT-PLFDPVTGEELVRVS-ATGLDLAAAFAFAREQGGAALRA-LTYAQRAALLAAIVKVLQANRDAYY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 505 TIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWcdkiqGATIPINQARPNRNLTLTKKEPV-----------GVCGIVIPW 573
Cdd:PRK11903 85 DIATANSGTTRNDS-AVDIDGGIFTLGYYAKL-----GAALGDARLLRDGEAVQLGKDPAfqgqhvlvptrGVALFINAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 574 NYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGI-PKGVVNILPGSGSlvgqRLSDH---PDVrkIGFT 649
Cdd:PRK11903 159 NFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSA----GLLDHlqpFDV--VSFT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 650 GSTEVGKHIMkscALSNVKKVSLELGgkspliIFADcDLNKAV---QMGMSSVFFN-------------KGENCIAAGRL 713
Cdd:PRK11903 233 GSAETAAVLR---SHPAVVQRSVRVN------VEAD-SLNSALlgpDAAPGSEAFDlfvkevvremtvkSGQKCTAIRRI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 714 FVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPQNHEAHLRKLVEYCQRgVKEGATLVCGGNQV------PRPGFFFQ 787
Cdd:PRK11903 303 FVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGFalvdadPAVAACVG 381
|
410 420 430
....*....|....*....|....*....|..
gi 21314994 788 PTVF--TDVEDHMYIAKEESFGPIMIISRFAD 817
Cdd:PRK11903 382 PTLLgaSDPDAATAVHDVEVFGPVATLLPYRD 413
|
|
| Met_tRNA_FMT_C |
cd08704 |
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ... |
207-302 |
1.83e-14 |
|
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding.
Pssm-ID: 187732 [Multi-domain] Cd Length: 87 Bit Score: 69.48 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 207 ETAMINWDQPAEAIHNWIRGNDKVPGAWTEACGQKLTFFnstlntsglvaQGEALPIPGAHRPG---LVTKAGLILFGND 283
Cdd:cd08704 1 EEGRIDWSKSAEEIHNLIRALNPWPGAYTTLNGKRLKIL-----------KAEVLEESGEAAPGtilAVDKKGLLVACGD 69
|
90
....*....|....*....
gi 21314994 284 DrMLLVKNIQLEDGKMMPA 302
Cdd:cd08704 70 G-ALEILELQPEGKKRMSA 87
|
|
| FMT_core_NRPS_like |
cd08649 |
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
18-163 |
3.19e-14 |
|
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.
Pssm-ID: 187718 [Multi-domain] Cd Length: 166 Bit Score: 71.14 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 18 QLRKEGHEVVGVFTipdkdgkADPLgleaekdgvpvfkFPRWrARGQALPeVVAKYQALGAELNVLPFCSQF-------I 90
Cdd:cd08649 17 QLLAAGHRIAAVVS-------TDPA-------------IRAW-AAAEGIA-VLEPGEALEELLSDEPFDWLFsivnlriL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21314994 91 PMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTVSTL 163
Cdd:cd08649 75 PSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
434-863 |
7.35e-14 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 75.22 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 434 EGAKTYSTI-NPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDR----GRLLYRLADLMEQHQeelatIEA 508
Cdd:cd07126 8 KGASNYTTLlDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKNPERyllyGDVSHRVAHELRKPE-----VED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 509 LDAGAVYTLALKTHV---GMSIQTFRYFAGWC-DKIQ----GATIPINQARPNRNLTltkKEPVGVCGIVIPWNYPLMML 580
Cdd:cd07126 83 FFARLIQRVAPKSDAqalGEVVVTRKFLENFAgDQVRflarSFNVPGDHQGQQSSGY---RWPYGPVAIITPFNFPLEIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDhPDVRKIGFTGSTEVGKHImk 660
Cdd:cd07126 160 ALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-ANPRMTLFTGSSKVAERL-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 661 scALSNVKKVSLELGGKSPLIIFADC-DLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQ-FVQKVVEEVGKMKIGN 738
Cdd:cd07126 237 --ALELHGKVKLEDAGFDWKILGPDVsDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAgILDKLKALAEQRKLED 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 739 ----PLDRDTNHGPQNHEAHLRKL----VEYCQRGVKEGATLVCGGNQVPRPgfFFQPTVFTDVEDHMYIAKEESFGPIM 810
Cdd:cd07126 315 ltigPVLTWTTERILDHVDKLLAIpgakVLFGGKPLTNHSIPSIYGAYEPTA--VFVPLEEIAIEENFELVTTEVFGPFQ 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 21314994 811 IISRFADGDVDAVLSRANATEFGLASGVFTRDINkalyVSDKLQAGTVFVNTY 863
Cdd:cd07126 393 VVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIR----FLQEVLANTVNGTTY 441
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
458-889 |
1.33e-13 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 74.44 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 458 VSDVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAGAVYTLALK---THV---GMSIQTFR 531
Cdd:cd07127 83 QCDPDALLAAARAAMPG--WRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQaggPHAqdrGLEAVAYA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 532 YFAgwCDKIQGATIPINQARPNRNLTLTKK---EPVGV-----CGIVIPWN-YPLMMlswktaACLAAGNTVVIKP--AQ 600
Cdd:cd07127 161 WRE--MSRIPPTAEWEKPQGKHDPLAMEKTftvVPRGValvigCSTFPTWNgYPGLF------ASLATGNPVIVKPhpAA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 601 VTPLT-ALKFAELTL-KAGIPKGVVNILPGS-GSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCalsNVKKVSLELGGK 677
Cdd:cd07127 233 ILPLAiTVQVAREVLaEAGFDPNLVTLAADTpEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANA---RQAQVYTEKAGV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 678 SPLIIFADCDLNKAVQ-MGMSSVFFNkGENCIAAGRLFV-EDSI--------HDQFVQKVVEEVGKMkIGNPLDRDTNHG 747
Cdd:cd07127 310 NTVVVDSTDDLKAMLRnLAFSLSLYS-GQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGL-LADPARAAALLG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 748 PQNHEAHLRKLVEYCQRGvkegaTLVCGGNQVPRPGfFFQPTVFT------DVEDH-MYiaKEESFGPIMIISRFADGDV 820
Cdd:cd07127 388 AIQSPDTLARIAEARQLG-----EVLLASEAVAHPE-FPDARVRTplllklDASDEaAY--AEERFGPIAFVVATDSTDH 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 821 DAVLSRANATEFG-LASGVFTRD-------INKALYVSDKLQ---AGTVFVNTynktdvAAPFGGFKQSGfGKDLGEAAL 889
Cdd:cd07127 460 SIELARESVREHGaMTVGVYSTDpevvervQEAALDAGVALSinlTGGVFVNQ------SAAFSDFHGTG-ANPAANAAL 532
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
38-178 |
1.44e-13 |
|
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 70.09 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 38 KADPLGLE-AEKDGVPVFKFPR--WRARGQALPEVVAKYQALGAELNVL---------PFCSQFiPMEVINAprhgsiiy 105
Cdd:TIGR00639 37 KPDAYGLErAAQAGIPTFVLSLkdFPSREAFDQAIIEELRAHEVDLVVLagfmrilgpTFLSRF-AGRILNI-------- 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21314994 106 HPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTVSTLYNRF------LFPEGIKGMVQ 178
Cdd:TIGR00639 108 HPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTEETLEQRIhkqehrIYPLAIAWFAQ 186
|
|
| FMT_core_HypX_N |
cd08650 |
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase ... |
13-180 |
3.80e-11 |
|
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase domain of HypX protein. HypX is involved in the maturation process of active [NiFe] hydrogenase. [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions. [NiFe] hydrogenases consist of a large and a small subunit. The large subunit contains [NiFe] active site, which is synthesized as a precursor without the [NiFe] active site. This precursor then undergoes a complex post-translational maturation process that requires the presence of a number of accessory proteins. HypX has been shown to be involved in this maturation process and have been proposed to participate in the generation and transport of the CO and CN ligands. However, HypX is not present in all hydrogen-metabolizing bacteria. Furthermore, hypX deletion mutants have a reduced but detectable level of hydrogenase activity. Thus, HypX might not be a determining factor in the matur ation process. Members of this group have an N-terminal formyl transferase domain and a C-terminal enoyl-CoA hydratase/isomerase domain.
Pssm-ID: 187719 [Multi-domain] Cd Length: 151 Bit Score: 61.87 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 13 QEVYCQLRKEGHEVVGVFTIPDKdgkadplgleaekdgvpvfkfprwrargqALPEVVAKYQAlgaELNVLPFCSQFIPM 92
Cdd:cd08650 15 QRAFLELRERGHEVSVEYALSDD-----------------------------EMREAVALFAP---DLIICPFLKKRIPE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 93 EVINapRHGSIIYHPSLlPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTVSTLYNRFLFPEG 172
Cdd:cd08650 63 EIWS--NYPCLIVHPGI-VGDRGPSSLDWAILEGEKEWGVTVLQAVEEMDAGPIWATRNFPLRRAATKSSLYRGEVTDAA 139
|
....*...
gi 21314994 173 IKGMVQAV 180
Cdd:cd08650 140 VKAVLEAV 147
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
84-184 |
1.12e-10 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187725 [Multi-domain] Cd Length: 177 Bit Score: 61.31 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 84 PFCSQF---IPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTV 160
Cdd:cd08823 75 VVVFTFpyrIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTY 154
|
90 100
....*....|....*....|....
gi 21314994 161 STLYNRfLFPEGIKGMVQAVRLIA 184
Cdd:cd08823 155 GLLCSR-LAMLAVGLLEELYQNLA 177
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
423-842 |
1.22e-10 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 64.98 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 423 QLFIGGEFVDAEGAKTySTINPTDGSVICQVSlAQVSDVDKAVAAAKEAFENGLwGKINARDRGRLLYRLADLMEQHQEE 502
Cdd:cd07128 2 QSYVAGQWHAGTGDGR-TLHDAVTGEVVARVS-SEGLDFAAAVAYAREKGGPAL-RALTFHERAAMLKALAKYLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 503 LATIeALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDK--------IQGATIPINqarpnRNLT------LTKKEPVGVcg 568
Cdd:cd07128 79 LYAL-SAATGATRRDS-WIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLS-----KDGTfvgqhiLTPRRGVAV-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 569 IVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGI-PKGVVNILPGS-GSLVGQRlsDHPDVrkI 646
Cdd:cd07128 150 HINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSvGDLLDHL--GEQDV--V 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 647 GFTGSTEVGKHIMkscALSNVKKVSLelggksPLIIFADcDLNKAV-----QMGMSSV-FFNK----------GENCIAA 710
Cdd:cd07128 226 AFTGSAATAAKLR---AHPNIVARSI------RFNAEAD-SLNAAIlgpdaTPGTPEFdLFVKevaremtvkaGQKCTAI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 711 GRLFVEDSIHDQFVQKVVEEVGKMKIGNPLDRDTNHGPqnheahlrkLVEYCQR-GVKEG-------ATLVCGGNQVPRP 782
Cdd:cd07128 296 RRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGP---------LVSREQReDVRAAvatllaeAEVVFGGPDRFEV 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21314994 783 -------GFFFQPTVF--------TDVEDHmyiakeESFGPIMIIsrFADGDVDAVLSRANATEFGLASGVFTRD 842
Cdd:cd07128 367 vgadaekGAFFPPTLLlcddpdaaTAVHDV------EAFGPVATL--MPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
461-742 |
2.35e-10 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 63.82 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 461 VDKAVAAAKEAfENGLWGKINARdRGRLLYRLADLMEQHQEELATIEALDAGA--VYTLALKTHVGMsiqtfRYFAG-WC 537
Cdd:cd07081 1 LDDAVAAAKVA-QQGLSCKSQEM-VDLIFRAAAEAAEDARIDLAKLAVSETGMgrVEDKVIKNHFAA-----EYIYNvYK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 538 DKIQGATIpinqARPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKP----AQVTPLTALKFAELT 613
Cdd:cd07081 74 DEKTCGVL----TGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 614 LKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGstevGKHIMKScALSNVKKVSLELGGKSPLIIFADCDLNKAVQ 693
Cdd:cd07081 150 VAAGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKA-AYSSGKPAIGVGAGNTPVVIDETADIKRAVQ 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 21314994 694 MGMSSVFFNKGENCIAAGRLFVEDSIHDQfVQKVVEEVGKMKI-GNPLDR 742
Cdd:cd07081 225 SIVKSKTFDNGVICASEQSVIVVDSVYDE-VMRLFEGQGAYKLtAEELQQ 273
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
492-730 |
9.01e-10 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 61.86 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 492 LADLMEQHQEELATIEALDAGA-VYTLALKTHVGMSIQ---------TFRYFAGWCDKIQGATipinqaRPNRNLTLTKK 561
Cdd:cd07077 25 IANALYDTRQRLASEAVSERGAyIRSLIANWIAMMGCSesklyknidTERGITASVGHIQDVL------LPDNGETYVRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 562 EPVGVCGIVIPWNYPLMMLSwKTAACLAAGNTVVIKPAQVTPLTALKFAELT---LKAGIPKGVVNILPGSGSLVGQRLS 638
Cdd:cd07077 99 FPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFqaaDAAHGPKILVLYVPHPSDELAEELL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 639 DHPDVRKIGFTGSTEVGKHIMKSCALSNVKKVSlelGGKSPLIIFADCDLNKAVQMGMSSVFFNkGENCIAAGRLFVEDS 718
Cdd:cd07077 178 SHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFG---AGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYVVDD 253
|
250
....*....|....*.
gi 21314994 719 IHD----QFVQKVVEE 730
Cdd:cd07077 254 VLDplyeEFKLKLVVE 269
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
460-730 |
7.17e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 59.15 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 460 DVDKAVAAAKEAFENglWGKINARDRGRLLYRLADLMEQHQEELATIEALDAG--------AVYTLALKTHVGMSIQTFR 531
Cdd:PRK15398 37 SVDDAVAAAKVAQQR--YQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedkiAKNVAAAEKTPGVEDLTTE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 532 YFAGwcdkiqgatipinqarpNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKP----AQVTPLTAL 607
Cdd:PRK15398 115 ALTG-----------------DNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgaKKVSLRAIE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 608 KFAELTLKAGIPKGVVNIL--PGSGSLvgQRLSDHPDVRKIGFTGSTEVGKHIMKSCalsnvKKVSLELGGKSPLIIFAD 685
Cdd:PRK15398 178 LLNEAIVAAGGPENLVVTVaePTIETA--QRLMKHPGIALLVVTGGPAVVKAAMKSG-----KKAIGAGAGNPPVVVDET 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 21314994 686 CDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEE 730
Cdd:PRK15398 251 ADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKN 295
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
85-164 |
1.40e-08 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187722 [Multi-domain] Cd Length: 173 Bit Score: 55.14 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 85 FCSQF---IPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTVS 161
Cdd:cd08820 74 ISVQYhwiLPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVI 153
|
...
gi 21314994 162 TLY 164
Cdd:cd08820 154 SLY 156
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
459-730 |
3.19e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 56.86 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 459 SDVDKAVAAAKEAFEngLWGKINARDRGRLLYRLADLMEQHQEELATIEALDA--GAVYTLALKTHVGMsiqtfryfagw 536
Cdd:cd07121 4 ATVDDAVAAAKAAQK--QYRKCTLADREKIIEAIREALLSNAEELAEMAVEETgmGRVEDKIAKNHLAA----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 537 cDKIQGATIPINQARPNRN-LTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKP----AQVTPLTALKFAE 611
Cdd:cd07121 71 -EKTPGTEDLTTTAWSGDNgLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgaKKVSAYAVELINK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 612 LTLKAGIPKGVVNIL--PGSGSLvgQRLSDHPDVRKIGFTGSTEVGKHIMKSCalsnvKKVSLELGGKSPLIIFADCDLN 689
Cdd:cd07121 150 AIAEAGGPDNLVVTVeePTIETT--NELMAHPDINLLVVTGGPAVVKAALSSG-----KKAIGAGAGNPPVVVDETADIE 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 21314994 690 KAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDQFVQKVVEE 730
Cdd:cd07121 223 KAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQRN 263
|
|
| Arna_FMT_C |
cd08702 |
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with ... |
210-305 |
1.36e-07 |
|
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with 4-amino-4-deoxy-l-arabinose; Domain found in ArnA with similarity to the C-terminal domain of Formyltransferase. ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal domain of ArnA is a dehydrogenase domain that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the N-terminal domain is a formyltransferase domain that catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the C-terminal subdomain of the formyltransferase domain, downstream of the N-terminal subdomain containing the catalytic center. ArnA forms a hexameric structure (a dimer of trimers), in which the dehydrogenase domains are arranged at the center with the transformylase domains on the outside of the complex.
Pssm-ID: 187730 Cd Length: 92 Bit Score: 49.93 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 210 MINWDQPAEAIHNWIRG-NDKVPGAWTEACGQKLTFFNSTlntsgLVAQGEALPIPGAH----RPGLVTKAGlilfgndD 284
Cdd:cd08702 4 LIDWRMSAREIYNLVRAvTKPYPGAFTFVGGQKIKIWKAR-----PVDDAFYNGEPGKVlsvdGDPLIVACG-------D 71
|
90 100
....*....|....*....|.
gi 21314994 285 RMLLVKNIQLEDGKMMPASQF 305
Cdd:cd08702 72 GALEILEAELDGGLPLAGEQL 92
|
|
| PRK07579 |
PRK07579 |
dTDP-4-amino-4,6-dideoxyglucose formyltransferase; |
86-171 |
4.07e-07 |
|
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
Pssm-ID: 236058 [Multi-domain] Cd Length: 245 Bit Score: 52.21 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 86 CSQFIPMEVINAPRhgSIIYHPSLLPRHRGASAINWTLIHGDKKGGfTIFWADDGLDTGDLLLQKECDVLPDDTVSTLYN 165
Cdd:PRK07579 74 CKQRFPAKLVNGVR--CINIHPGFNPYNRGWFPQVFSIINGLKIGA-TIHEMDEQLDHGPIIAQREVEIESWDSSGSVYA 150
|
....*.
gi 21314994 166 RFLFPE 171
Cdd:PRK07579 151 RVMDIE 156
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
562-724 |
2.02e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 51.34 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 562 EPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKP---AQVTPLTALKF-AELTLKAGIPKGVVNILPGSGSLVGQRL 637
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAKImREAAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 638 SDHPDVRKIGFTGSTevgkhimkscalSNVK------KVSLELG-GKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAA 710
Cdd:cd07122 174 MKHPDVDLILATGGP------------GMVKaayssgKPAIGVGpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASE 241
|
170
....*....|....
gi 21314994 711 GRLFVEDSIHDQFV 724
Cdd:cd07122 242 QSVIVDDEIYDEVR 255
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
46-171 |
3.30e-06 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 48.92 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 46 AEKDGVPVFKFPRWRARGQALP--EVVAKYQALGAELNVLPFCSQFIPMEVINA-PRhgSII-YHPSLLPRH--RGASAI 119
Cdd:PLN02331 45 ARENGIPVLVYPKTKGEPDGLSpdELVDALRGAGVDFVLLAGYLKLIPVELVRAyPR--SILnIHPALLPAFggKGYYGI 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 21314994 120 NwtlIH------GDKKGGFTIFWADDGLDTGDLLLQKECDVLPDDTVSTLYNRFLFPE 171
Cdd:PLN02331 123 K---VHkaviasGARYSGPTVHFVDEHYDTGRILAQRVVPVLATDTPEELAARVLHEE 177
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
309-399 |
4.08e-03 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 40.12 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21314994 309 SASSALELTEEELATAEAVRSSWMRILP-NVPEVEDSTDFFKSGAASVDVVRLVEEVKElcDGLELENEDVYMATTFGDF 387
Cdd:COG3433 206 LAAASPAPALETALTEEELRADVAELLGvDPEEIDPDDNLFDLGLDSIRLMQLVERWRK--AGLDVSFADLAEHPTLAAW 283
|
90
....*....|..
gi 21314994 388 IQLLVRKLRGED 399
Cdd:COG3433 284 WALLAAAQAAAA 295
|
|
| |
