|
Name |
Accession |
Description |
Interval |
E-value |
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
78-528 |
0e+00 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 815.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 158 LYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA 237
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 238 LALAELASQAGIPSGVYNVIPCSRknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFD 317
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGSR--AKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 318 SANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVN 397
Cdd:TIGR01780 239 DADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKK-LKVGNGLDEGVTQGPLINEKAVEKVEKHIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 398 DAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQ 477
Cdd:TIGR01780 318 DAVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 4507229 478 IWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 528
Cdd:TIGR01780 398 IWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
78-531 |
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: 775.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 158 LYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA 237
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 238 LALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFD 317
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGS---PAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 318 SANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVN 397
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKK-LKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 398 DAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQ 477
Cdd:cd07103 317 DAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 4507229 478 IWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 531
Cdd:cd07103 397 AWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVS 450
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
55-535 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 718.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 55 SAALLRTDSFVGGRWLPA--AATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMI 132
Cdd:PLN02278 19 NAGLLRTQGLIGGKWTDAydGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLII 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 133 QNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMIT 212
Cdd:PLN02278 99 ANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMIT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 213 RKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIpcsRKNAKEVGEAICTDPLVSKISFTGSTTTGKIL 292
Cdd:PLN02278 179 RKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVV---MGDAPEIGDALLASPKVRKITFTGSTAVGKKL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 293 LHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGN 372
Cdd:PLN02278 256 MAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQK-LVVGD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 373 GFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTE 452
Cdd:PLN02278 335 GFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 453 EEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCY 532
Cdd:PLN02278 415 EEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
...
gi 4507229 533 GGL 535
Cdd:PLN02278 495 GNM 497
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
56-533 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 601.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 56 AALLRTDSFVGGRWLPA--AATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQ 133
Cdd:PRK11241 6 STLFRQQALINGEWLDAnnGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMME 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 134 NKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITR 213
Cdd:PRK11241 86 HQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 214 KVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILL 293
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGS---AGAVGGELTSNPLVRKLSFTGSTEIGRQLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 294 HHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNG 373
Cdd:PRK11241 243 EQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSK-LHIGDG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 374 FEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEE 453
Cdd:PRK11241 322 LEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 454 EAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYG 533
Cdd:PRK11241 402 DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIG 481
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
60-531 |
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: 593.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 60 RTDSFVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDD 137
Cdd:COG1012 5 EYPLFIGGEWVAAASgeTFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 138 LARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGA 217
Cdd:COG1012 85 LAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 218 ALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAA 297
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGD---GSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 298 NSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEG 377
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKA-LKVGDPLDPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 378 TTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGK-NFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAI 456
Cdd:COG1012 321 TDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGgYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507229 457 AIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSV-ECPFGGVKQSGLGREGSKYGIDEYLELKYVC 531
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVpQAPFGGVKQSGIGREGGREGLEEYTETKTVT 476
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
69-530 |
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: 535.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 69 WLPAAA-TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESG 147
Cdd:pfam00171 1 WVDSESeTIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 148 KPLKEAHGEILYSAFFLEWFSEEARRVYGDIIhTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVV 227
Cdd:pfam00171 81 KPLAEARGEVDRAIDVLRYYAGLARRLDGETL-PSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 228 KPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMEL 307
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAGLPAGVLNVVTGS---GAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 308 GGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEK 387
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKK-LKVGDPLDPDTDMGPLISKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 388 AVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLA 467
Cdd:pfam00171 316 QLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507229 468 GYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVE-CPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:pfam00171 396 AGVFTSDLERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
109-531 |
1.97e-175 |
|
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: 501.35 E-value: 1.97e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 109 FCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRA 188
Cdd:cd07078 11 FKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGELA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 189 LVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVG 268
Cdd:cd07078 91 IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGD---GDEVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 269 EAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLV 348
Cdd:cd07078 168 AALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 349 QRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGK-NFFEPTLLCN 427
Cdd:cd07078 248 HESIYDEFVERLVERVKA-LKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKgYFVPPTVLTD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 428 VTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLIS-SVECPFGG 506
Cdd:cd07078 327 VDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGaEPSAPFGG 406
|
410 420
....*....|....*....|....*
gi 4507229 507 VKQSGLGREGSKYGIDEYLELKYVC 531
Cdd:cd07078 407 VKQSGIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
64-530 |
2.25e-153 |
|
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: 446.71 E-value: 2.25e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARI 141
Cdd:cd07088 1 YINGEFVPSSsgETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 142 ITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAA 221
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 222 GCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVK 301
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGR---GSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 302 RVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQG 381
Cdd:cd07088 238 KVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKA-VKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 382 PLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGK-NFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIAN 460
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKgYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 461 AADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
112-530 |
8.06e-141 |
|
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: 414.26 E-value: 8.06e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVL 191
Cdd:cd07114 37 WRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPcsrKNAKEVGEAI 271
Cdd:cd07114 117 REPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVT---GFGPETGEAL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 272 CTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRG 351
Cdd:cd07114 194 VEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 352 IHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKN----FFEPTLLCN 427
Cdd:cd07114 274 IYDEFVERLVARARA-IRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSGADLgagyFFEPTILAD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 428 VTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGV 507
Cdd:cd07114 353 VTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGF 432
|
410 420
....*....|....*....|...
gi 4507229 508 KQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07114 433 KDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
78-531 |
3.92e-139 |
|
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: 409.65 E-value: 3.92e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEA-HGE 156
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLArTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 157 ILYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS 236
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDG-GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 237 ALALAELASQAGIPSGVYNVIpcsRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVF 316
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVV---HGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 317 DSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQV 396
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKA-LKVGDPLDPDTEVGPLISKEHLEKVLGYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 397 NDAVSKGATVVTGGKRHQL----GKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYS 472
Cdd:cd07093 316 ELARAEGATILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 4507229 473 QDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 531
Cdd:cd07093 396 RDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
64-530 |
2.78e-135 |
|
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: 400.82 E-value: 2.78e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAF--CRWREVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07091 7 FINNEFVDSVSgkTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFetGWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 140 RIITAESGKPLKE-AHGEILYSAFFLEWFSEEARRVYGDIIHTPaKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAA 218
Cdd:cd07091 87 ALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIPID-GNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 219 LAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAAN 298
Cdd:cd07091 166 LAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGF---GPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 299 S-VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEG 377
Cdd:cd07091 243 SnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEK-RVVGDPFDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 378 TTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIA 457
Cdd:cd07091 322 TFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507229 458 IANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07091 402 RANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
76-530 |
2.89e-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: 397.09 E-value: 2.89e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 76 FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHG 155
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 156 EILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPF 235
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 236 SALALAELASQAGIPSGVYNVIPCSRknaKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIV 315
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGG---AEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 316 FDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQ 395
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASK-LKVGDPRDPDTVIGPLISPRQVERIKRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 396 VNDAVSKGATVVTGGKRHqlgKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDP 475
Cdd:cd07150 317 VEDAVAKGAKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 4507229 476 AQIWRVAEQLEVGMVGVNEGLISS-VECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07150 394 QRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
112-530 |
3.83e-134 |
|
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: 396.13 E-value: 3.83e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVL 191
Cdd:cd07104 16 WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDVPGKESMVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS-ALALAELASQAGIPSGVYNVIPCsrkNAKEVGEA 270
Cdd:cd07104 96 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPG---GGSEIGDA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 271 ICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQR 350
Cdd:cd07104 173 LVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 351 GIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQlgkNFFEPTLLCNVTQ 430
Cdd:cd07104 253 SVYDEFVEKLVAKAKA-LPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEG---LFYQPTVLSDVTP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 431 DMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSvEC--PFGGVK 508
Cdd:cd07104 329 DMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVND-EPhvPFGGVK 407
|
410 420
....*....|....*....|..
gi 4507229 509 QSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07104 408 ASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
76-531 |
8.86e-131 |
|
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: 388.49 E-value: 8.86e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 76 FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHG 155
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 156 EILYSAFFLEWFSEEARRVYGDII----HTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAE 231
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIpfdaSPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 232 DTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAAnsVKRVSMELGGLA 311
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGS---GETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 312 PFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEK 391
Cdd:cd07149 236 AVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKK-LVVGDPLDEDTDVGPMISEAEAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 392 VEKQVNDAVSKGATVVTGGKRHQlgkNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFY 471
Cdd:cd07149 315 IEEWVEEAVEGGARLLTGGKRDG---AILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507229 472 SQDPAQIWRVAEQLEVGMVGVNEglISSVEC---PFGGVKQSGLGREGSKYGIDEYLELKYVC 531
Cdd:cd07149 392 TNDLQKALKAARELEVGGVMIND--SSTFRVdhmPYGGVKESGTGREGPRYAIEEMTEIKLVC 452
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
109-530 |
2.40e-130 |
|
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: 386.43 E-value: 2.40e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 109 FCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGD-IIHTPAKdrR 187
Cdd:cd07100 12 FLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADePIETDAG--K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 188 ALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAkev 267
Cdd:cd07100 90 AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQV--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 268 gEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFL 347
Cdd:cd07100 167 -EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 348 VQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCN 427
Cdd:cd07100 246 VHEDVYDEFLEKFVEAMAA-LKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPTVLTD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 428 VTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGV 507
Cdd:cd07100 325 VTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGV 404
|
410 420
....*....|....*....|...
gi 4507229 508 KQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07100 405 KRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
76-532 |
4.78e-129 |
|
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: 384.01 E-value: 4.78e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 76 FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHG 155
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 156 EILYSAFFLEWFSEEARRVYGDIIHTPAKD----RRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAE 231
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEynerRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 232 DTPFSALALAELASQAGIPSGVYNVIPcsrKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLA 311
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVT---GYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 312 PFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEK 391
Cdd:cd07145 238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKK-LKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 392 VEKQVNDAVSKGATVVTGGKRHQlgKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFY 471
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4507229 472 SQDPAQIWRVAEQLEVGMVGVNE-GLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCY 532
Cdd:cd07145 395 TNDINRALKVARELEAGGVVINDsTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
111-530 |
3.07e-128 |
|
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: 382.07 E-value: 3.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 111 RWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALV 190
Cdd:cd07118 36 PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNLGDDMLGLV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 191 LKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRknaKEVGEA 270
Cdd:cd07118 116 LREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYG---ATVGQA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 271 ICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQR 350
Cdd:cd07118 193 MTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 351 GIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKN-FFEPTLLCNVT 429
Cdd:cd07118 273 SIADAFVAAVVARSRK-VRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGlFYQPTIFTDVT 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 430 QDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQ 509
Cdd:cd07118 352 PDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQ 431
|
410 420
....*....|....*....|.
gi 4507229 510 SGLGREGSKYGIDEYLELKYV 530
Cdd:cd07118 432 SGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
64-528 |
1.87e-127 |
|
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: 380.31 E-value: 1.87e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARI 141
Cdd:cd07138 2 YIDGAWVAPAgtETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 142 ITAESGKPLK---EAH-----GEILYSAFFLEWFSEEARRvygdiihtpakdRRALVLKQPIGVAAVITPWNFPSAMITR 213
Cdd:cd07138 82 ITLEMGAPITlarAAQvglgiGHLRAAADALKDFEFEERR------------GNSLVVREPIGVCGLITPWNWPLNQIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 214 KVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILL 293
Cdd:cd07138 150 KVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGD---GPVVGEALSAHPDVDMVSFTGSTRAGKRVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 294 HHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAfVKAFAEAMKKNLRVGNG 373
Cdd:cd07138 227 EAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAE-AEEIAAAAAEAYVVGDP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 374 FEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGG--KRHQLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFD 450
Cdd:cd07138 306 RDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgRPEGLERGYFvKPTVFADVTPDMTIAREEIFGPVLSIIPYD 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507229 451 TEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSvECPFGGVKQSGLGREGSKYGIDEYLELK 528
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP-GAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
112-531 |
8.51e-127 |
|
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: 375.03 E-value: 8.51e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVL 191
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEAYVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAI 271
Cdd:cd06534 90 REPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG---GDEVGAAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 272 CTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRG 351
Cdd:cd06534 167 LSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHES 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 352 IHDAFVKAFAeamkknlrvgngfeegttqgplinekavekvekqvndavskgatvvtggkrhqlgknffepTLLCNVTQD 431
Cdd:cd06534 247 IYDEFVEKLV-------------------------------------------------------------TVLVDVDPD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 432 MLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI-SSVECPFGGVKQS 510
Cdd:cd06534 266 MPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGVKNS 345
|
410 420
....*....|....*....|.
gi 4507229 511 GLGREGSKYGIDEYLELKYVC 531
Cdd:cd06534 346 GIGREGGPYGLEEYTRTKTVV 366
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
64-530 |
1.54e-126 |
|
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: 378.58 E-value: 1.54e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAF--CRWREVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07119 1 YIDGEWVEAASgkTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 140 RIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAAL 219
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPP-HVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 220 AAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANS 299
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGS---GATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 300 VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTT 379
Cdd:cd07119 237 VKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKK-IKLGNGLDADTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 380 QGPLINEKAVEKVEKQVNDAVSKGATVVTGGKR---HQLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEA 455
Cdd:cd07119 316 MGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRptgDELAKGYFvEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507229 456 IAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07119 396 IRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
74-528 |
5.16e-126 |
|
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: 376.56 E-value: 5.16e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 74 ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAF--CRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLK 151
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFesGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 152 EA-HGEILYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPA 230
Cdd:cd07112 82 DAlAVDVPSAANTFRWYAEAIDKVYGEVAPTGP-DALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 231 EDTPFSALALAELASQAGIPSGVYNVIPcsrKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANS-VKRVSMELGG 309
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVP---GFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 310 LAPFIVF-DSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKA 388
Cdd:cd07112 238 KSPNIVFaDAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAARE-WKPGDPLDPATRMGALVSEAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 389 VEKVEKQVNDAVSKGATVVTGGKRHQL--GKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGL 466
Cdd:cd07112 317 FDKVLGYIESGKAEGARLVAGGKRVLTetGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507229 467 AGYFYSQDPAQIWRVAEQLEVGMVGVN---EGLISSvecPFGGVKQSGLGREGSKYGIDEYLELK 528
Cdd:cd07112 397 AASVWTSDLSRAHRVARRLRAGTVWVNcfdEGDITT---PFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
78-528 |
4.98e-124 |
|
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: 370.71 E-value: 4.98e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 158 LYSAFFLEWFSEEARRVygDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA 237
Cdd:cd07106 81 GGAVAWLRYTASLDLPD--EVIEDDD-TRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 238 LALAELASQAgIPSGVYNVIPcsrkNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFD 317
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVS----GGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 318 SANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFEEGTTQGPLINEKAVEKVEKQVN 397
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAK-AAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 398 DAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQ 477
Cdd:cd07106 312 DAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 4507229 478 IWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 528
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
78-532 |
1.26e-123 |
|
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: 370.42 E-value: 1.26e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRW-REVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHG- 155
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 156 EILYSAFFLEWFSEEARRVYGDIIHTPAKDR----RALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAE 231
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRggpgRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 232 DTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLA 311
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGS---DNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 312 PFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFEEGTTQGPLINEKAVEK 391
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFE-ALPVGDPADPGTVMGPLISAAQRDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 392 VEKQVNDAVSKGATVVTGGKR-HQLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGY 469
Cdd:cd07089 317 VEGYIARGRDEGARLVTGGGRpAGLDKGFYvEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507229 470 FYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCY 532
Cdd:cd07089 397 VWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
63-533 |
1.91e-121 |
|
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: 365.52 E-value: 1.91e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 63 SFVGGRWLPAA--ATFPVQDPASGA-ALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07131 1 NYIGGEWVDSAsgETFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 140 RIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAAL 219
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 220 AAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIpcsRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANS 299
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVV---HGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 300 VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTT 379
Cdd:cd07131 238 NKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKR-LRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 380 QGPLINEKAVEKVEKQVNDAVSKGATVVTGGKR---HQLGK-NFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEA 455
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERltgGGYEKgYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 456 IAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI-SSVECPFGGVKQSGLG-REGSKYGIDEYLELK--YVC 531
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKavYVD 476
|
..
gi 4507229 532 YG 533
Cdd:cd07131 477 YS 478
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
62-530 |
4.92e-120 |
|
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: 361.57 E-value: 4.92e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 62 DSFVGGRWLPAAATFPVQDPAS-GAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLAR 140
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 141 IITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALA 220
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 221 AGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSV 300
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGS---GSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 301 KRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQ 380
Cdd:cd07097 239 ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKA-LKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 381 GPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKN--FFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAI 458
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEgyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507229 459 ANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNE---GLISSVecPFGGVKQSGLG-REGSKYGIDEYLELKYV 530
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLptaGVDYHV--PFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
64-530 |
7.82e-120 |
|
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: 361.12 E-value: 7.82e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR--WREVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07139 2 FIGGRWVAPSgsETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 140 RIITAESGKPLK-EAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAA 218
Cdd:cd07139 82 RLWTAENGMPISwSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 219 LAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRknakEVGEAICTDPLVSKISFTGSTTTGKILLHHAAN 298
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR----EVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 299 SVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGT 378
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAA-LKVGDPLDPAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 379 TQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKR--HQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAI 456
Cdd:cd07139 317 QIGPLASARQRERVEGYIAKGRAEGARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507229 457 AIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNeGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07139 397 RIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
78-531 |
8.05e-118 |
|
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: 355.20 E-value: 8.05e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 158 LYSAFFLEWFSEEARRVYGDIIHTPA----KDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDT 233
Cdd:cd07094 83 DRAIDTLRLAAEEAERIRGEEIPLDAtqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 234 PFSALALAELASQAGIPSGVYNVIPCSRknaKEVGEAICTDPLVSKISFTGSTTTGKILlhHAANSVKRVSMELGGLAPF 313
Cdd:cd07094 163 PLSALELAKILVEAGVPEGVLQVVTGER---EVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 314 IVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVE 393
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKK-LKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 394 KQVNDAVSKGATVVTGGKRHqlgKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQ 473
Cdd:cd07094 317 RWVEEAVEAGARLLCGGERD---GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 4507229 474 DPAQIWRVAEQLEVGMVGVNEGLISSVE-CPFGGVKQSGLGREGSKYGIDEYLELKYVC 531
Cdd:cd07094 394 DLNVAFKAAEKLEVGGVMVNDSSAFRTDwMPFGGVKESGVGREGVPYAMEEMTEEKTVV 452
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
80-531 |
1.19e-117 |
|
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: 354.82 E-value: 1.19e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 80 DPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEA-HGEIL 158
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 159 YSAFFLEWFSEEARRVYGDIIhtPAKDRrAL--VLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS 236
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVI--PVRGP-FLnyTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 237 ALALAELASQAGIPSGVYNVIPcsrKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVF 316
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVT---GFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 317 DSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAeAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQV 396
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFT-SLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 397 NDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPA 476
Cdd:cd07115 316 DVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 4507229 477 QIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 531
Cdd:cd07115 396 RAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVW 450
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
64-530 |
1.33e-117 |
|
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: 355.95 E-value: 1.33e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFC-RWREVSAKERSSLLRKWYNLMIQNKDDLAR 140
Cdd:cd07144 11 FINNEFVKSSDgeTIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFEsWWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 141 IITAESGKPLKE-AHGEILYSAFFLEWFSEEARRVYGD-IIHTPAKdrRALVLKQPIGVAAVITPWNFPSAMITRKVGAA 218
Cdd:cd07144 91 IEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKtIPTSPNK--LAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 219 LAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPcsrKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAAN 298
Cdd:cd07144 169 LAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIP---GYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 299 SVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEEGT 378
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYKVGSPFDDDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 379 TQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRH--QLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEA 455
Cdd:cd07144 326 VVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKApeGLGKGYFiPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507229 456 IAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
78-531 |
4.82e-116 |
|
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: 350.84 E-value: 4.82e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 158 LYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA 237
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPG-GSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 238 LALAELASQAGIPSGVYNVIPcsrkNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFD 317
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQ----GGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 318 SANVDQAVAGAMASKFRNTGQtcVCSN--QFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQ 395
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQ--VCSNgtRVFVQRSIKDEFTERLVERTKK-IRIGDPLDEDTQMGALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 396 VNDAVSKGATVVTGGKRHQL-----GKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYF 470
Cdd:cd07090 313 IESAKQEGAKVLCGGERVVPedgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507229 471 YSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 531
Cdd:cd07090 393 FTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
78-530 |
5.58e-115 |
|
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: 348.07 E-value: 5.58e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 78 VQDPASGAALGMVADCGVREARAAVRAAYEAF-CRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGE 156
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFeSGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 157 ILYSAFFLEWFSEEARRVYGDIIhTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS 236
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETI-PLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 237 ALALAELASQAGIPSGVYNVIPcsrKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVF 316
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVT---GLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 317 DSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGfEEGTTQGPLINEKAVEKVEKQV 396
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRA-LRVGPG-LEDPDLGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 397 NDAVSKGATVVTGGKRHQL---GKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQ 473
Cdd:cd07109 315 ARARARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 4507229 474 DPAQIWRVAEQLEVGMVGVNE-GLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07109 395 DGDRALRVARRLRAGQVFVNNyGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
78-530 |
1.70e-114 |
|
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: 346.65 E-value: 1.70e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 158 LYSAFFLEWFSEEARRV---YGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTP 234
Cdd:cd07110 81 DDVAGCFEYYADLAEQLdakAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 235 FSALALAELASQAGIPSGVYNVIpcsRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFI 314
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVV---TGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 315 VFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMkKNLRVGNGFEEGTTQGPLINEKAVEKVEK 394
Cdd:cd07110 238 VFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAA-EAIRVGDPLEEGVRLGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 395 QVNDAVSKGATVVTGGKRHQ-LGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYS 472
Cdd:cd07110 317 FIARGKEEGARLLCGGRRPAhLEKGYFiAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 4507229 473 QDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
64-530 |
4.60e-112 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 341.12 E-value: 4.60e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLP-AAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARII 142
Cdd:PRK13473 6 LINGELVAgEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 143 TAESGKPLKEA-HGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAA 221
Cdd:PRK13473 86 SLNCGKPLHLAlNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 222 GCTVVVKPAEDTPFSALALAELASQAgIPSGVYNVIpCSRknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVK 301
Cdd:PRK13473 166 GNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVV-TGR--GATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 302 RVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQG 381
Cdd:PRK13473 242 RTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVAT-LKVGDPDDEDTELG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 382 PLINEKAVEKVEKQVNDAVSKG-ATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIAN 460
Cdd:PRK13473 321 PLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWAN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4507229 461 AADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEG--LISsvECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:PRK13473 401 DSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHfmLVS--EMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
124-530 |
2.61e-111 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 337.09 E-value: 2.61e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 124 LRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITP 203
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 204 WNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFT 283
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGR---GETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 284 GSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEA 363
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 364 MkKNLRVGNGFEEGTTQ-GPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGP 442
Cdd:PRK10090 238 M-QAVQFGNPAERNDIAmGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 443 LAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGID 522
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLH 396
|
....*...
gi 4507229 523 EYLELKYV 530
Cdd:PRK10090 397 EYLQTQVV 404
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
61-530 |
1.10e-110 |
|
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: 337.54 E-value: 1.10e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 61 TDSFVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR--WREVSAKERSSLLRKWYNLMIQNKD 136
Cdd:cd07142 4 TKLFINGQFVDAASgkTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 137 DLARIITAESGKPLKEA-HGEILYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKV 215
Cdd:cd07142 84 ELAALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADG-PHHVYTLHEPIGVVGQIIPWNFPLLMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 216 GAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAkevGEAICTDPLVSKISFTGSTTTGKILLHH 295
Cdd:cd07142 163 GPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTA---GAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 296 AANS-VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFV-KAFAEAMKKNlrVGNG 373
Cdd:cd07142 240 AAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVeKAKARALKRV--VGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 374 FEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEE 453
Cdd:cd07142 318 FRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVD 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507229 454 EAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07142 398 EVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
78-530 |
1.44e-110 |
|
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: 336.61 E-value: 1.44e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKE-AHGE 156
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 157 ILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS 236
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 237 ALALAELASQaGIPSGVYNVIpCSRknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVF 316
Cdd:cd07092 161 TLLLAELAAE-VLPPGVVNVV-CGG--GASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 317 DSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQV 396
Cdd:cd07092 237 DDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSA-IRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 397 nDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPA 476
Cdd:cd07092 316 -ERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 4507229 477 QIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07092 395 RAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
76-528 |
3.44e-110 |
|
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: 335.75 E-value: 3.44e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 76 FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHG 155
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 156 EILYSAFFLEWFSEEARRVYGDI----IHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAE 231
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVlpldISARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 232 DTPFSALALAELASQAGIPSGVYNVIPCSRKNAkevgEAICTDPLVSKISFTGSTTTGKILLHHAANsvKRVSMELGGLA 311
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDA----DLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 312 PFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEK 391
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKA-LKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 392 VEKQVNDAVSKGATVVTGGKRHQlgkNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGL-AGYF 470
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGKRDG---ALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLqAGVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507229 471 ySQDPAQIWRVAEQLEVGMVGVNEglISSVEC---PFGGVKQSGLGREGSKYGIDEYLELK 528
Cdd:cd07147 391 -TRDLEKALRAWDELEVGGVVIND--VPTFRVdhmPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
80-530 |
5.46e-109 |
|
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: 332.65 E-value: 5.46e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 80 DPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILY 159
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 160 SAFFLEWFSEEARRVYGD---IIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS 236
Cdd:cd07099 82 ALEAIDWAARNAPRVLAPrkvPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 237 ALALAELASQAGIPSGVYNVIpcsrKNAKEVGEAICtDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVF 316
Cdd:cd07099 162 GELLAEAWAAAGPPQGVLQVV----TGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 317 DSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQV 396
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARA-LRPGADDIGDADIGPMTTARQLDIVRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 397 NDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPA 476
Cdd:cd07099 316 DDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 4507229 477 QIWRVAEQLEVGMVGVNEGLISSV--ECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07099 396 RAEAIARRLEAGAVSINDVLLTAGipALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
64-532 |
1.26e-107 |
|
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: 329.87 E-value: 1.26e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAF-CRW-REVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07143 10 FINGEFVDSVhgGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFeTDWgLKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 140 RIITAESGKP-LKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKdRRALVLKQPIGVAAVITPWNFPSAMITRKVGAA 218
Cdd:cd07143 90 SIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIK-KLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 219 LAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPcsrKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAAN 298
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVS---GYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 299 S-VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEG 377
Cdd:cd07143 246 SnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKK-LKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 378 TTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIA 457
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507229 458 IANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCY 532
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
61-530 |
1.27e-106 |
|
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: 327.38 E-value: 1.27e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 61 TDSFVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR---WREVSAKERSSLLRKWYNLMIQNK 135
Cdd:cd07141 7 TKIFINNEWHDSVSgkTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 136 DDLARIITAESGKPLKEAH-GEILYSAFFLEWFSEEARRVYGDIIhtPAK-DRRALVLKQPIGVAAVITPWNFPSAMITR 213
Cdd:cd07141 87 AYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTI--PMDgDFFTYTRHEPVGVCGQIIPWNFPLLMAAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 214 KVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAkevGEAICTDPLVSKISFTGSTTTGKILL 293
Cdd:cd07141 165 KLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTA---GAAISSHPDIDKVAFTGSTEVGKLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 294 HHAANS-VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNlRVGN 372
Cdd:cd07141 242 QAAGKSnLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKR-VVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 373 GFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTE 452
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507229 453 EEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
64-530 |
2.96e-106 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 327.07 E-value: 2.96e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPA--AATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR-----WREVSAKERSSLLRKWYNLMIQNKD 136
Cdd:PLN02467 11 FIGGEWREPvlGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 137 DLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYG---DIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITR 213
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkqkAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 214 KVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILL 293
Cdd:PLN02467 171 KVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGL---GTEAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 294 HHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMkKNLRVGNG 373
Cdd:PLN02467 248 TAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWA-KNIKISDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 374 FEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKR-HQLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDT 451
Cdd:PLN02467 327 LEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRpEHLKKGFFiEPTIITDVTTSMQIWREEVFGPVLCVKTFST 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4507229 452 EEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:PLN02467 407 EDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
109-530 |
6.88e-106 |
|
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: 323.76 E-value: 6.88e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 109 FCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRA 188
Cdd:cd07105 13 FPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIPSDKPGTLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 189 LVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAKEVG 268
Cdd:cd07105 93 MVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSPEDAPEVV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 269 EAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLV 348
Cdd:cd07105 173 EALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 349 QRGIHDAFVKAFAEAMKKnLRVGngfeeGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGK-RHQLGKNFFEPTLLCN 427
Cdd:cd07105 253 HESIADEFVEKLKAAAEK-LFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLaDESPSGTSMPPTILDN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 428 VTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEgliSSVE----CP 503
Cdd:cd07105 327 VTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHING---MTVHdeptLP 403
|
410 420
....*....|....*....|....*..
gi 4507229 504 FGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07105 404 HGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
80-531 |
2.91e-105 |
|
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: 323.14 E-value: 2.91e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 80 DPASGAALGMVADCGVREARAAVRAAYEAFCR--WReVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 158 LYSAFFLEWFSEEARRVYGDIIhTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA 237
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMI-EPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 238 LALAE-LASQAGIPSGVYNVIPCSRKnakEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVF 316
Cdd:cd07120 161 AAIIRiLAEIPSLPAGVVNLFTESGS---EGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 317 DSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMkKNLRVGNGFEEGTTQGPLINEKAVEKVEKQV 396
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARL-AAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 397 NDAVSKGATVVTGGKRHQLGKN---FFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQ 473
Cdd:cd07120 317 ERAIAAGAEVVLRGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 4507229 474 DPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 531
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
112-530 |
3.97e-105 |
|
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: 323.10 E-value: 3.97e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEIlysAFFLEWFSEEAR---RVYGDII--HTPAKDR 186
Cdd:cd07151 48 WAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEW---GAAMAITREAATfplRMEGRILpsDVPGKEN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 187 RalVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA-LALAELASQAGIPSGVYNVIPcsrKNAK 265
Cdd:cd07151 125 R--VYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVV---GAGS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 266 EVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQ 345
Cdd:cd07151 200 EIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 346 FLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHqlgKNFFEPTLL 425
Cdd:cd07151 280 IIVHEDVYDEFVEKFVERVKA-LPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 426 CNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLIS-SVECPF 504
Cdd:cd07151 356 SDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPF 435
|
410 420
....*....|....*....|....*.
gi 4507229 505 GGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07151 436 GGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
61-530 |
2.27e-104 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 322.16 E-value: 2.27e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 61 TDSFVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAF--CRWREVSAKERSSLLRKWYNLMIQNKD 136
Cdd:PLN02766 21 TKLFINGEFVDAASgkTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFdhGPWPRMSGFERGRIMMKFADLIEEHIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 137 DLARIITAESGK-PLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTpAKDRRALVLKQPIGVAAVITPWNFPSAMITRKV 215
Cdd:PLN02766 101 ELAALDTIDAGKlFALGKAVDIPAAAGLLRYYAGAADKIHGETLKM-SRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 216 GAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAkevGEAICTDPLVSKISFTGSTTTGKILLHH 295
Cdd:PLN02766 180 APALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTA---GAAIASHMDVDKVSFTGSTEVGRKIMQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 296 AANS-VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMkKNLRVGNGF 374
Cdd:PLN02766 257 AATSnLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKA-KDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 375 EEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKrhQLGKN--FFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTE 452
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGK--PCGDKgyYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507229 453 EEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
63-533 |
3.56e-103 |
|
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: 318.35 E-value: 3.56e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 63 SFVGGRWLPAAA-TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARI 141
Cdd:cd07086 1 GVIGGEWVGSGGeTFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 142 ITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAA 221
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 222 GCTVVVKPAEDTPFSALALAELASQA----GIPSGVYNVIPCsrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAA 297
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG----GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 298 NSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEG 377
Cdd:cd07086 237 RRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQ-VRIGDPLDEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 378 TTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKR--HQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEA 455
Cdd:cd07086 316 TLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 456 IAIANAADVGLAGYFYSQDPAQI--WRVAEQLEVGMVGVNEGLI-SSVECPFGGVKQSGLGREGSKYGIDEYLELK--YV 530
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAfrWLGPKGSDCGIVNVNIPTSgAEIGGAFGGEKETGGGRESGSDAWKQYMRRStcTI 475
|
...
gi 4507229 531 CYG 533
Cdd:cd07086 476 NYS 478
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
64-531 |
3.61e-103 |
|
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: 318.23 E-value: 3.61e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAAAT--FPVQDPASGAALGMVADCGVREARAAVRAAYEAF-CRWREVSAKERSSLLRKWYNLMIQNKDDLAR 140
Cdd:cd07113 3 FIDGRPVAGQSEkrLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 141 IITAESGKPLKEAHG-EILYSAFFLEWFSEEARRVYGDIIH----TPAKDR-RALVLKQPIGVAAVITPWNFPSAMITRK 214
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLApsipSMQGERyTAFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 215 VGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIpcsrKNAKEVGEAICTDPLVSKISFTGSTTTGKILLH 294
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVV----NGKGAVGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 295 HAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGF 374
Cdd:cd07113 239 QAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSS-FQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 375 EEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQlGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEE 453
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA-GEGYFvQPTLVLARSADSRLMREETFGPVVSFVPYEDEE 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507229 454 EAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 531
Cdd:cd07113 397 ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
49-526 |
3.80e-101 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 314.51 E-value: 3.80e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 49 GRLAGLSAALLR--TDSFVGGrwlpAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRK 126
Cdd:PRK09407 9 PAPSALTFERLRrlTARVDGA----AGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 127 WYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKD--RRALVLKQPIGVAAVITPW 204
Cdd:PRK09407 85 FHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPKLLAPRRRAGALPvlTKTTELRQPKGVVGVISPW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 205 NFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICtdPLVSKISFTG 284
Cdd:PRK09407 165 NYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGP---GPVVGTALV--DNADYLMFTG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 285 STTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAM 364
Cdd:PRK09407 240 STATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 365 KkNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGK-RHQLGKNFFEPTLLCNVTQDMLCTHEETFGPL 443
Cdd:PRK09407 320 R-AMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKaRPDLGPLFYEPTVLTGVTPDMELAREETFGPV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 444 APVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLIS---SVECPFGGVKQSGLGREGSKYG 520
Cdd:PRK09407 399 VSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAawgSVDAPMGGMKDSGLGRRHGAEG 478
|
....*.
gi 4507229 521 IDEYLE 526
Cdd:PRK09407 479 LLKYTE 484
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
80-526 |
7.58e-101 |
|
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: 311.55 E-value: 7.58e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 80 DPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILY 159
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 160 SAFFLEWFSEEARRVYgdiihTPAKDRRAL-------VLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAED 232
Cdd:cd07101 82 VAIVARYYARRAERLL-----KPRRRRGAIpvltrttVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 233 TPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDplVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAP 312
Cdd:cd07101 157 TALTALWAVELLIEAGLPRDLWQVVTGP---GSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 313 FIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFEEGTTQGPLINEKAVEKV 392
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTR-ALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 393 EKQVNDAVSKGATVVTGGK-RHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFY 471
Cdd:cd07101 311 TAHVDDAVAKGATVLAGGRaRPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVW 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 4507229 472 SQDPAQIWRVAEQLEVGMVGVNEGLIS---SVECPFGGVKQSGLGREGSKYGIDEYLE 526
Cdd:cd07101 391 TRDGARGRRIAARLRAGTVNVNEGYAAawaSIDAPMGGMKDSGLGRRHGAEGLLKYTE 448
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
64-530 |
5.44e-100 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 310.66 E-value: 5.44e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARI 141
Cdd:PRK13252 10 YIDGAYVEATsgETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 142 ITAESGKPLKEAH-GEILYSAFFLEWFSEEARRVYGDIIHTPAKD----RRalvlkQPIGVAAVITPWNFPSAMITRKVG 216
Cdd:PRK13252 90 ETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSfvytRR-----EPLGVCAGIGAWNYPIQIACWKSA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 217 AALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRknakEVGEAICTDPLVSKISFTGSTTTGKILLHHA 296
Cdd:PRK13252 165 PALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG----RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 297 ANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQtcVCSN--QFLVQRGIHDAFVKAFAEAMKKnLRVGNGF 374
Cdd:PRK13252 241 AASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQ--VCTNgtRVFVQKSIKAAFEARLLERVER-IRIGDPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 375 EEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQ---LGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFD 450
Cdd:PRK13252 318 DPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTeggFANGAFvAPTVFTDCTDDMTIVREEIFGPVMSVLTFD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 451 TEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:PRK13252 398 DEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
78-530 |
6.16e-100 |
|
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: 309.29 E-value: 6.16e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLK-EAHGE 156
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 157 ILYSAFFLEWFSEEARRVYGDIIhTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS 236
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETL-PFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 237 ALALAELASQAgIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVF 316
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGY---GEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 317 DSANVDQAVAGAMAS-KFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQ 395
Cdd:cd07108 236 PDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSK-LKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 396 VNDAVS-KGATVVTGG---KRHQLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYF 470
Cdd:cd07108 315 IDLGLStSGATVLRGGplpGEGPLADGFFvQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507229 471 YSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYG-IDEYLELKYV 530
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
116-528 |
7.19e-100 |
|
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: 308.90 E-value: 7.19e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 116 SAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDII----HTPAKDRRALVL 191
Cdd:cd07146 38 TRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRDDGESFscdlTANGKARKIFTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIpcsRKNAKEVGEAI 271
Cdd:cd07146 118 REPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVV---TGEPGEIGDEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 272 CTDPLVSKISFTGSTTTGKILLHHAAnsVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRG 351
Cdd:cd07146 195 ITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHES 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 352 IHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHqlgKNFFEPTLLCNVTQD 431
Cdd:cd07146 273 VADEFVDLLVEKSAA-LVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQRQ---GALYAPTVLDHVPPD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 432 MLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVE-CPFGGVKQS 510
Cdd:cd07146 349 AELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDS 428
|
410
....*....|....*....
gi 4507229 511 GLG-REGSKYGIDEYLELK 528
Cdd:cd07146 429 GLGgKEGVREAMKEMTNVK 447
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
62-532 |
2.75e-99 |
|
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: 308.50 E-value: 2.75e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 62 DSFVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07559 2 DNFINGEWVAPSkgEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 140 RIITAESGKPLKEAHG-EILYSAFFLEWFSEEARRVYGDIiHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAA 218
Cdd:cd07559 82 VAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSL-SEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 219 LAAGCTVVVKPAEDTPFSALALAELASQAgIPSGVYNVIpcsrkNAK--EVGEAICTDPLVSKISFTGSTTTGKILLHHA 296
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVV-----TGFgsEAGKPLASHPRIAKLAFTGSTTVGRLIMQYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 297 ANSVKRVSMELGGLAPFIVFDSA-----NVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVG 371
Cdd:cd07559 235 AENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFE-AIKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 372 NGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKN----FFEPTLLCNVTQDMLCTHEETFGPLAPVI 447
Cdd:cd07559 314 NPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLdkgyFYEPTLIKGGNNDMRIFQEEIFGPVLAVI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 448 KFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLEL 527
Cdd:cd07559 394 TFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQT 473
|
....*..
gi 4507229 528 K--YVCY 532
Cdd:cd07559 474 KniLVSY 480
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
61-530 |
5.17e-98 |
|
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: 305.57 E-value: 5.17e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 61 TDSFVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR--WREVSAKERSSLLRKWYNLMIQNKD 136
Cdd:cd07140 6 HQLFINGEFVDAEGgkTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 137 DLARIITAESGK----PLKEAHG-EILYSAFFLEWfseeARRVYGDIIH-TPAKDRRALVL--KQPIGVAAVITPWNFPS 208
Cdd:cd07140 86 ELATIESLDSGAvytlALKTHVGmSIQTFRYFAGW----CDKIQGKTIPiNQARPNRNLTLtkREPIGVCGIVIPWNYPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 209 AMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNakeVGEAICTDPLVSKISFTGSTTT 288
Cdd:cd07140 162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSL---VGQRLSDHPDVRKLGFTGSTPI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 289 GKILLHHAANS-VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKn 367
Cdd:cd07140 239 GKHIMKSCAVSnLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKK- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 368 LRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVI 447
Cdd:cd07140 318 MKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIIS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 448 KFDTEEEAIAIANAADV--GLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYL 525
Cdd:cd07140 398 KFDDGDVDGVLQRANDTeyGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYL 477
|
....*
gi 4507229 526 ELKYV 530
Cdd:cd07140 478 KTKTV 482
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
61-530 |
1.61e-97 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 305.58 E-value: 1.61e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 61 TDSFVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR--WREVSAKERSSLLRKWYNLMIQNKD 136
Cdd:PLN02466 58 TQLLINGQFVDAASgkTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 137 DLARIITAESGKPLKE-AHGEILYSAFFLEWFSEEARRVYGDIIhtPAKDRRAL-VLKQPIGVAAVITPWNFPSAMITRK 214
Cdd:PLN02466 138 ELAALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHGLTV--PADGPHHVqTLHEPIGVAGQIIPWNFPLLMFAWK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 215 VGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAkevGEAICTDPLVSKISFTGSTTTGKILLH 294
Cdd:PLN02466 216 VGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTA---GAALASHMDVDKLAFTGSTDTGKIVLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 295 HAANS-VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFV-KAFAEAMKKNlrVGN 372
Cdd:PLN02466 293 LAAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVeKAKARALKRV--VGD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 373 GFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTE 452
Cdd:PLN02466 371 PFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDL 450
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507229 453 EEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:PLN02466 451 DEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
112-521 |
1.68e-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: 303.72 E-value: 1.68e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGD----IIHTPAKDRR 187
Cdd:cd07082 55 WPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDslpgDWFPGTKGKI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 188 ALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIpcsRKNAKEV 267
Cdd:cd07082 135 AQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVV---TGRGREI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 268 GEAICTDPLVSKISFTGSTTTGKILLhhAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFL 347
Cdd:cd07082 212 GDPLVTHGRIDVISFTGSTEVGNRLK--KQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 348 VQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRhqLGKNFFEPTLLCN 427
Cdd:cd07082 290 VHESVADELVELLKEEVAK-LKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 428 VTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGlissveC----- 502
Cdd:cd07082 367 VTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSK------Cqrgpd 440
|
410 420
....*....|....*....|.
gi 4507229 503 --PFGGVKQSGLGREGSKYGI 521
Cdd:cd07082 441 hfPFLGRKDSGIGTQGIGDAL 461
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
64-528 |
1.45e-96 |
|
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: 301.30 E-value: 1.45e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARI 141
Cdd:cd07117 4 FINGEWVKGSsgETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 142 ITAESGKPLKEAHG-EILYSAFFLEWF-----SEEARRVYGDiihtpaKDRRALVLKQPIGVAAVITPWNFPSAMITRKV 215
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFagvirAEEGSANMID------EDTLSIVLREPIGVVGQIIPWNFPFLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 216 GAALAAGCTVVVKPAEDTPFSALALAELASQAgIPSGVYNVIPcsrKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHH 295
Cdd:cd07117 158 APALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVT---GKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 296 AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFE 375
Cdd:cd07117 234 AAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFE-NVKVGNPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 376 EGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGK----NFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDT 451
Cdd:cd07117 313 PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGldkgFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKT 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507229 452 EEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 528
Cdd:cd07117 393 EDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMK 469
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
112-530 |
5.39e-96 |
|
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: 298.82 E-value: 5.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVL 191
Cdd:cd07152 29 WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQGEILPSAP-GRLSLAR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA-LALAELASQAGIPSGVYNVIPcsrkNAKEVGEA 270
Cdd:cd07152 108 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLP----GGADAGEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 271 ICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQR 350
Cdd:cd07152 184 LVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 351 GIHDAFVKAFAeAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLgknFFEPTLLCNVTQ 430
Cdd:cd07152 264 SVADAYTAKLA-AKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTYDGL---FYRPTVLSGVKP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 431 DMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSvEC--PFGGVK 508
Cdd:cd07152 340 GMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVND-EPhnPFGGMG 418
|
410 420
....*....|....*....|...
gi 4507229 509 QSGLG-REGSKYGIDEYLELKYV 530
Cdd:cd07152 419 ASGNGsRFGGPANWEEFTQWQWV 441
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
78-530 |
5.80e-92 |
|
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: 288.89 E-value: 5.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 158 LYSAFFLEWFSEEARRVYGDIIHTPAkdrRAL--VLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPF 235
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGG---RNLhyTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 236 SALALAELASQAgIPSGVYNVIPCSRKnakEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIV 315
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGA---TAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 316 FDSANVDQAVAGAMAS-KFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEK 394
Cdd:cd07107 234 FPDADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAA-IKVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 395 QVNDAVSKGATVVTGGKR---HQLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYF 470
Cdd:cd07107 313 YIDSAKREGARLVTGGGRpegPALEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 471 YSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:cd07107 393 WTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
80-533 |
1.19e-91 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 287.79 E-value: 1.19e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 80 DPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILY 159
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 160 SAFFLEWFSEEARRVYGDIIHTPAK--DRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA 237
Cdd:PRK09406 87 CAKGFRYYAEHAEALLADEPADAAAvgASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 238 LALAELASQAGIPSGVYNVIPCSrknAKEVgEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFD 317
Cdd:PRK09406 167 LYLADLFRRAGFPDGCFQTLLVG---SGAV-EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 318 SANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVN 397
Cdd:PRK09406 243 SADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAA-LRVGDPTDPDTDVGPLATEQGRDEVEKQVD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 398 DAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQ 477
Cdd:PRK09406 322 DAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAE 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 4507229 478 IWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYG 533
Cdd:PRK09406 402 QERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
80-521 |
2.88e-88 |
|
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: 279.57 E-value: 2.88e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 80 DPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAH-GEIL 158
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 159 YSAFFLEW--------FSEEARRVYGDIIHtpakdRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPA 230
Cdd:cd07098 82 VTCEKIRWtlkhgekaLRPESRPGGLLMFY-----KRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 231 EDTPFSALALAELASQA----GIPSGVYNVIPCsrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSME 306
Cdd:cd07098 157 EQVAWSSGFFLSIIREClaacGHDPDLVQLVTC----LPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 307 LGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINE 386
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQA-LRQGPPLDGDVDVGAMISP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 387 KAVEKVEKQVNDAVSKGATVVTGGKRHQLGK----NFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAA 462
Cdd:cd07098 312 ARFDRLEELVADAVEKGARLLAGGKRYPHPEypqgHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANST 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507229 463 DVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVEC--PFGGVKQSGLGREGSKYGI 521
Cdd:cd07098 392 EYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGRFAGEEGL 452
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
64-530 |
7.71e-88 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 278.96 E-value: 7.71e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAAA-TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR--W-REVSAKERSslLRKWYNLMIQNKDDLA 139
Cdd:TIGR04284 4 LIDGKLVAGSAgTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDEtdWsRDTALRVRC--LRQLRDALRAHVEELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 140 RIITAESGKPLKEAHGEILYSAFF-LEWFSEEA-----RRVYGDIIHTPAKDRRaLVLKQPIGVAAVITPWNFPSAMITR 213
Cdd:TIGR04284 82 ELTIAEVGAPRMLTAGAQLEGPVDdLGFAADLAesyawTTDLGVASPMGIPTRR-TLRREAVGVVGAITPWNFPHQINLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 214 KVGAALAAGCTVVVKPAEDTPFSALALAEL-ASQAGIPSGVYNVIPCSRknaKEVGEAICTDPLVSKISFTGSTTTGKIL 292
Cdd:TIGR04284 161 KLGPALAAGNTVVLKPAPDTPWCAAVLGELiAEHTDFPPGVVNIVTSSD---HRLGALLAKDPRVDMVSFTGSTATGRAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 293 LHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMkKNLRVGN 372
Cdd:TIGR04284 238 MADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATM-GSIKPGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 373 GFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKR--HQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFD 450
Cdd:TIGR04284 317 PADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGRpaDRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 451 TEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:TIGR04284 397 GDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLI 476
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
112-528 |
1.05e-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: 277.59 E-value: 1.05e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVL 191
Cdd:cd07102 34 WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEALADIRVPEKDGFERYIR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknaKEVGEAI 271
Cdd:cd07102 114 REPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLS----HETSAAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 272 CTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCvCS-NQFLVQR 350
Cdd:cd07102 190 IADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSC-CSiERIYVHE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 351 GIHDAFVKAFAEAMKkNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKR---HQLGKNFFEPTLLCN 427
Cdd:cd07102 269 SIYDAFVEAFVAVVK-GYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALfpeDKAGGAYLAPTVLTN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 428 VTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGV 507
Cdd:cd07102 348 VDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGV 427
|
410 420
....*....|....*....|.
gi 4507229 508 KQSGLGREGSKYGIDEYLELK 528
Cdd:cd07102 428 KDSGRGVTLSRLGYDQLTRPK 448
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
64-527 |
2.11e-87 |
|
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: 278.72 E-value: 2.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAAATFPVQDPA-SGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARII 142
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 143 TAESGKPLKEAHGEILYSAFFLEWFSEEARRvYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAG 222
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLR-LRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 223 CTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANS--- 299
Cdd:cd07124 195 NTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGP---GEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 300 ---VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTC-VCSnQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFE 375
Cdd:cd07124 272 qkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCsACS-RVIVHESVYDEFLERLVERTKA-LKVGDPED 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 376 EGTTQGPLINEKAVEKVEKQVNDAVSKGaTVVTGGKR--HQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEE 453
Cdd:cd07124 350 PEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVleLAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFD 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507229 454 EAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNE---GLISSVEcPFGGVKQSGLgreGSKYGIDEYLEL 527
Cdd:cd07124 429 EALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRkitGALVGRQ-PFGGFKMSGT---GSKAGGPDYLLQ 501
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
36-526 |
1.13e-86 |
|
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: 275.81 E-value: 1.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 36 GPAPGPAqlrcyAGRLAGLSAALLRTDSFVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWR 113
Cdd:cd07111 2 GPAPESA-----ACALAWLDAHDRSFGHFINGKWVKPEnrKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 114 EVSAKERSSLLrkwYNL--MIQNKDDL-ARIITAESGKPLKEAH-GEILYSAFFLEWFSEEARrvygdiihtpaKDRRAL 189
Cdd:cd07111 77 ALPGHVRARHL---YRIarHIQKHQRLfAVLESLDNGKPIRESRdCDIPLVARHFYHHAGWAQ-----------LLDTEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 190 VLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIpcsrKNAKEVGE 269
Cdd:cd07111 143 AGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIV----TGNGSFGS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 270 AICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQ 349
Cdd:cd07111 219 ALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 350 RGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVT 429
Cdd:cd07111 299 ESVAEELIRKLKERMSH-LRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 430 QDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQ 509
Cdd:cd07111 378 PASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRE 457
|
490
....*....|....*..
gi 4507229 510 SGLGREGSKYGIDEYLE 526
Cdd:cd07111 458 SGFGREGGKEGLYEYLR 474
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
59-528 |
1.59e-86 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 276.01 E-value: 1.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 59 LRTDSFVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR--WREVSAKERSSLLRKWYNLMIQN 134
Cdd:PRK09847 18 IENRLFINGEYTAAAenETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 135 KDDLARIITAESGKPLKEA-HGEILYSAFFLEWFSEEARRVYGDIIHTpAKDRRALVLKQPIGVAAVITPWNFPSAMITR 213
Cdd:PRK09847 98 AEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATT-SSHELAMIVREPVGVIAAIVPWNFPLLLTCW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 214 KVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPcsrKNAKEVGEAICTDPLVSKISFTGSTTTGKILL 293
Cdd:PRK09847 177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVT---GFGHEAGQALSRHNDIDAIAFTGSTRTGKQLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 294 HHAANS-VKRVSMELGGLAPFIVF-DSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFaEAMKKNLRVG 371
Cdd:PRK09847 254 KDAGDSnMKRVWLEAGGKSANIVFaDCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALL-KQQAQNWQPG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 372 NGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGgkRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDT 451
Cdd:PRK09847 333 HPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTS 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507229 452 EEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 528
Cdd:PRK09847 411 EEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
61-522 |
1.65e-86 |
|
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: 275.16 E-value: 1.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 61 TDSFVGGRWLPAAAT--FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDL 138
Cdd:cd07085 1 LKLFINGEWVESKTTewLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 139 ARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPsAMITR-KVGA 217
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFP-AMIPLwMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 218 ALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCsrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAA 297
Cdd:cd07085 160 AIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG----GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 298 NSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCV-CSNQFLVQrGIHDAFVKAFAEAMKKnLRVGNGFEE 376
Cdd:cd07085 236 ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMaLSVAVAVG-DEADEWIPKLVERAKK-LKVGAGDDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 377 GTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGK----NFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTE 452
Cdd:cd07085 314 GADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGyengNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTL 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507229 453 EEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVEC-PFGGVKQSGLGrEGSKYGID 522
Cdd:cd07085 394 DEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFfSFGGWKGSFFG-DLHFYGKD 463
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
80-530 |
2.09e-76 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 248.62 E-value: 2.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 80 DPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILY 159
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 160 SAFFLEWFSEearrvygdiiHTPA---------KDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPA 230
Cdd:PRK13968 93 SANLCDWYAE----------HGPAmlkaeptlvENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 231 EDTPFSALALAELASQAGIPSGVYNVIpcsrkNAKEVG-EAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGG 309
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWL-----NADNDGvSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 310 LAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAV 389
Cdd:PRK13968 238 SDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAA-LKMGDPRDEENALGPMARFDLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 390 EKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGY 469
Cdd:PRK13968 317 DELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSAT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507229 470 FYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 530
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
111-523 |
4.52e-73 |
|
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: 239.63 E-value: 4.52e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 111 RWreVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDII---HTPAKD-R 186
Cdd:cd07148 39 NW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIpmgLTPASAgR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 187 RALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRknakE 266
Cdd:cd07148 117 IAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCEN----A 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 267 VGEAICTDPLVSKISFTGSTTTGKILLHHAANSVkRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQF 346
Cdd:cd07148 193 VAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT-RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 347 LVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRhqLGKNFFEPTLLC 426
Cdd:cd07148 272 FVPAEIADDFAQRLAAAAEK-LVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKR--LSDTTYAPTVLL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 427 NVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVE-CPFG 505
Cdd:cd07148 349 DPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFA 428
|
410
....*....|....*...
gi 4507229 506 GVKQSGLGREGSKYGIDE 523
Cdd:cd07148 429 GRRQSGYGTGGIPYTMHD 446
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
109-527 |
7.47e-71 |
|
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: 235.15 E-value: 7.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 109 FCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRA 188
Cdd:TIGR01237 82 FEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 189 LVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVG 268
Cdd:TIGR01237 162 QYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGS---GSEVG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 269 EAICTDPLVSKISFTGSTTTGKILLHHAA------NSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVC 342
Cdd:TIGR01237 239 DYLVDHPKTSLITFTGSREVGTRIFERAAkvqpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 343 SNQFLVQRGIHDAFVKAFAEAmKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGaTVVTGGKRHQLGKNFFEP 422
Cdd:TIGR01237 319 GSRAVVHEKVYDEVVERFVEI-TESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGP 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 423 TLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNE---GLISS 499
Cdd:TIGR01237 397 TIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRnitGAIVG 476
|
410 420
....*....|....*....|....*...
gi 4507229 500 VEcPFGGVKQSGLgreGSKYGIDEYLEL 527
Cdd:TIGR01237 477 YQ-PFGGFKMSGT---DSKAGGPDYLAL 500
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
111-524 |
9.19e-70 |
|
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: 230.19 E-value: 9.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 111 RWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAH-GEILysafflewfseearRVYGDIIHT-------- 181
Cdd:cd07134 13 ALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlTEIL--------------PVLSEINHAikhlkkwm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 182 -PAKDR--------RALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSG 252
Cdd:cd07134 79 kPKRVRtplllfgtKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 253 VynvipcsrknAKEVGEAICTDPLVSK----ISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGA 328
Cdd:cd07134 159 V----------AVFEGDAEVAQALLELpfdhIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 329 MASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLrvgnGFEEGTTQGP----LINEKAVEKVEKQVNDAVSKGA 404
Cdd:cd07134 229 AWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFY----GKDAARKASPdlarIVNDRHFDRLKGLLDDAVAKGA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 405 TVVTGGKrHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQ 484
Cdd:cd07134 305 KVEFGGQ-FDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLAR 383
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 4507229 485 LEVGMVGVNEGLISSVE--CPFGGVKQSGLGREGSKYGIDEY 524
Cdd:cd07134 384 TSSGGVVVNDVVLHFLNpnLPFGGVNNSGIGSYHGVYGFKAF 425
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
109-522 |
1.20e-69 |
|
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: 229.85 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 109 FCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEwFSEEARRVYGDIIHTPAKDRRA 188
Cdd:cd07095 13 FPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKID-ISIKAYHERTGERATPMAQGRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 189 LVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIpcsrKNAKEVG 268
Cdd:cd07095 92 VLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLV----QGGRETG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 269 EAICTDPLVSKISFTGSTTTGKILLHHAANSV-KRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFL 347
Cdd:cd07095 168 EALAAHEGIDGLLFTGSAATGLLLHRQFAGRPgKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 348 VQRG-IHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLL- 425
Cdd:cd07095 248 VPDGaVGDAFLERLVEAAKR-LRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLSPGIId 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 426 ---CNVTQDmlcthEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI-SSVE 501
Cdd:cd07095 327 vtdAADVPD-----EEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTgASST 401
|
410 420
....*....|....*....|.
gi 4507229 502 CPFGGVKQSGLGREGSKYGID 522
Cdd:cd07095 402 APFGGVGLSGNHRPSAYYAAD 422
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
62-528 |
1.25e-68 |
|
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: 228.49 E-value: 1.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 62 DSFVGGRWLPAAAT--FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07116 2 DNFIGGEWVAPVKGeyFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 140 RIITAESGKPLKEAHG-EILYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAA 218
Cdd:cd07116 82 VAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSISEIDE-NTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 219 LAAGCTVVVKPAEDTPFSALALAELASQAgIPSGVYNVIpcsRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAAN 298
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVV---NGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 299 SVKRVSMELGGLAPFIVFDS------ANVDQAVAGAMASKFrNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGN 372
Cdd:cd07116 237 NIIPVTLELGGKSPNIFFADvmdaddAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKA-IKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 373 GFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKN----FFEPTLLCNvTQDMLCTHEETFGPLAPVIK 448
Cdd:cd07116 315 PLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 449 FDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 528
Cdd:cd07116 394 FKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
116-532 |
1.06e-67 |
|
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: 224.33 E-value: 1.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 116 SAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAH--------GEILYSAFFLEWFSEEaRRVYGDIIHTPAKdrr 187
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlteiavvlGEIDHALKHLKKWMKP-RRVSVPLLLQPAK--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 188 ALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAgIPSGVYNVIpcsrKNAKEV 267
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVV----EGGVEV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 268 GEAICTDPLvSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFL 347
Cdd:cd07087 169 ATALLAEPF-DHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 348 VQRGIHDAFVkafaEAMKKNLR--VGNGFEEGTTQGPLINEKAVEKVEKQVNDAvskgaTVVTGGKRHQlGKNFFEPTLL 425
Cdd:cd07087 248 VHESIKDELI----EELKKAIKefYGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGGQVDK-EERYIAPTIL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 426 CNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI--SSVECP 503
Cdd:cd07087 318 DDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLhaAIPNLP 397
|
410 420
....*....|....*....|....*....
gi 4507229 504 FGGVKQSGLGREGSKYGIDEYLELKYVCY 532
Cdd:cd07087 398 FGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
65-527 |
1.33e-67 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 226.74 E-value: 1.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 65 VGGRWLPAAATFPVQDPASGAAL-GMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIIT 143
Cdd:PRK03137 41 IGGERITTEDKIVSINPANKSEVvGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 144 AESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGC 223
Cdd:PRK03137 121 KEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 224 TVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAA------ 297
Cdd:PRK03137 201 TVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGS---GSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAkvqpgq 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 298 NSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGfEEG 377
Cdd:PRK03137 278 IWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKE-LTVGNP-EDN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 378 TTQGPLINEKAVEKVEKQVNDAVSKGaTVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIA 457
Cdd:PRK03137 356 AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALE 434
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507229 458 IANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNE---GLISSVEcPFGGVKQSGlgrEGSKYGIDEYLEL 527
Cdd:PRK03137 435 IANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRgctGAIVGYH-PFGGFNMSG---TDSKAGGPDYLLL 503
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
44-525 |
2.15e-66 |
|
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: 223.61 E-value: 2.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 44 LRCYAGRLAGLSAALLRTDSFVGGRWLPAAATFPVQDPASGAA-LGMVADCGVREARAAVRAAYEAFCRWREVSAKERSS 122
Cdd:cd07125 16 LEALADALKAFDEKEWEAIPIINGEETETGEGAPVIDPADHERtIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 123 LLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVIT 202
Cdd:cd07125 96 ILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCIS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 203 PWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRknaKEVGEAICTDPLVSKISF 282
Cdd:cd07125 176 PWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDG---EEIGEALVAHPRIDGVIF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 283 TGSTTTGKIL---LHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKA 359
Cdd:cd07125 253 TGSTETAKLInraLAERDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 360 FAEAMkKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNdAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLctHEET 439
Cdd:cd07125 333 LKGAM-ASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTE-LMRGEAWLIAPAPLDDGNGYFVAPGIIEIVGIFDL--TTEV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 440 FGPLAPVIKFDTEEEAIAIANAADV--GLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSV--ECPFGGVKQSGLgre 515
Cdd:cd07125 409 FGPILHVIRFKAEDLDEAIEDINATgyGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIvgRQPFGGWGLSGT--- 485
|
490
....*....|
gi 4507229 516 GSKYGIDEYL 525
Cdd:cd07125 486 GPKAGGPNYL 495
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
124-524 |
7.42e-66 |
|
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: 219.78 E-value: 7.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 124 LRKWYNLMIQNKDDLARIITAESGKPLKEA--------HGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRralVLKQPI 195
Cdd:cd07135 33 LKQLYWAVKDNEEAIVEALKKDLGRPPFETlltevsgvKNDILHMLKNLKKWAKDEKVKDGPLAFMFGKPR---IRKEPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 196 GVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAgIPSGVYNVIpcsRKNAKEVGEAIctDP 275
Cdd:cd07135 110 GVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVV---QGGVPETTALL--EQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 276 LVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDA 355
Cdd:cd07135 184 KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 356 FVKAFAEAMKKnlRVGNGFEEGTTQGPLINEKAVEKVEKQVNDavSKGaTVVTGGKRHQlGKNFFEPTLLCNVTQDMLCT 435
Cdd:cd07135 264 FVEELKKVLDE--FYPGGANASPDYTRIVNPRHFNRLKSLLDT--TKG-KVVIGGEMDE-ATRFIPPTIVSDVSWDDSLM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 436 HEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI--SSVECPFGGVKQSGLG 513
Cdd:cd07135 338 SEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPFGGVGDSGYG 417
|
410
....*....|.
gi 4507229 514 REGSKYGIDEY 524
Cdd:cd07135 418 AYHGKYGFDTF 428
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
64-517 |
6.03e-64 |
|
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: 215.92 E-value: 6.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIIT 143
Cdd:cd07130 2 VYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 144 AESGKPLKEAHGEIlysafflewfsEE-----------ARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMIT 212
Cdd:cd07130 82 LEMGKILPEGLGEV-----------QEmidicdfavglSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 213 RKVGAALAAGCTVVVKPAEDTPFSALA----LAELASQAGIPSGVYNVIPCSRknakEVGEAICTDPLVSKISFTGSTTT 288
Cdd:cd07130 151 WNAAIALVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGA----DVGEALVKDPRVPLVSFTGSTAV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 289 GKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnL 368
Cdd:cd07130 227 GRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQ-V 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 369 RVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLcNVTQDMLCTHEETFGPLAPVIK 448
Cdd:cd07130 306 RIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLK 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507229 449 FDTEEEAIAIANAADVGLAGYFYSQDPAQI--WRVAEQLEVGMVGVNEGlISSVEC--PFGGVKQSGLGRE-GS 517
Cdd:cd07130 385 FDTLEEAIAWNNEVPQGLSSSIFTTDLRNAfrWLGPKGSDCGIVNVNIG-TSGAEIggAFGGEKETGGGREsGS 457
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
118-531 |
4.21e-62 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 211.43 E-value: 4.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 118 KERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAH--------GEIlysAFFLEWFSE--EARRVYGDIIHTPAKdrr 187
Cdd:PTZ00381 29 EFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmtevlltvAEI---EHLLKHLDEylKPEKVDTVGVFGPGK--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 188 ALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAgIPSGVYNVIpcsrKNAKEV 267
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVI----EGGVEV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 268 GEAICTDPLvSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFL 347
Cdd:PTZ00381 178 TTELLKEPF-DHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 348 VQRGIHDAFVKAFAEAMKKNLrvGNGFEEGTTQGPLINEKAVEKVEKQVNDavsKGATVVTGGKrHQLGKNFFEPTLLCN 427
Cdd:PTZ00381 257 VHRSIKDKFIEALKEAIKEFF--GEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE-VDIENKYVAPTIIVN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 428 VTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGL--ISSVECPFG 505
Cdd:PTZ00381 331 PDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVfhLLNPNLPFG 410
|
410 420
....*....|....*....|....*.
gi 4507229 506 GVKQSGLGREGSKYGIDEYLELKYVC 531
Cdd:PTZ00381 411 GVGNSGMGAYHGKYGFDTFSHPKPVL 436
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
116-514 |
1.33e-56 |
|
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: 195.40 E-value: 1.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 116 SAKERSSLLRKWYNLMIQNKDDLARIITAESGKplkEAHGEILYSAFFL-------------EWFSEEARRVygDIIHTP 182
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFGH---RSRHETLLAEILPsiagikharkhlkKWMKPSRRHV--GLLFLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 183 AKdrrALVLKQPIGVAAVITPWNFP-----SAMItrkvgAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVI 257
Cdd:cd07133 93 AK---AEVEYQPLGVVGIIVPWNYPlylalGPLI-----AALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAVVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 258 pcsrkNAKEVGEAICT---DPLVskisFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFR 334
Cdd:cd07133 165 -----GGADVAAAFSSlpfDHLL----FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 335 NTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEEGTtqgPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQ 414
Cdd:cd07133 236 NAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPDYT---SIINERHYARLQGLLEDARAKGARVIELNPAGE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 415 L--GKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGV 492
Cdd:cd07133 313 DfaATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTI 392
|
410 420
....*....|....*....|....
gi 4507229 493 NEGL--ISSVECPFGGVKQSGLGR 514
Cdd:cd07133 393 NDTLlhVAQDDLPFGGVGASGMGA 416
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
64-527 |
1.86e-56 |
|
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: 196.65 E-value: 1.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLPAAATFPVQDP-ASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARII 142
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 143 TAESGKPLKEAHGEILYSAFFLEWFSEEARRVYG--DIIHTPAKDRRALVLkQPIGVAAVITPWNFPSAMITRKVGAALA 220
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFY-VGLGAGVVISPWNFPVAIFTGMIVAPVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 221 AGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPcsrKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAAN-- 298
Cdd:cd07083 181 VGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLP---GVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARla 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 299 ----SVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGF 374
Cdd:cd07083 258 pgqtWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAER-LSVGPPE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 375 EEGTTQGPLINEKAVEKVEKQVNDAVSKGaTVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEE 454
Cdd:cd07083 337 ENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDF 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507229 455 AIAIANAADV--GLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSV--ECPFGGVKQSGlgrEGSKYGIDEYLEL 527
Cdd:cd07083 416 AEALEVANSTpyGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALvgVQPFGGFKLSG---TNAKTGGPHYLRR 489
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
120-522 |
7.04e-55 |
|
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: 191.18 E-value: 7.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 120 RSSLLRKWYNLMIQNKDDLARIITAESGKPLKEA--------HGEILYSAFFLEWFSEEaRRVYGDIIHTPAKDRralVL 191
Cdd:cd07136 22 RIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAymteigfvLSEINYAIKHLKKWMKP-KRVKTPLLNFPSKSY---IY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVipcsrKNAKEVGEAI 271
Cdd:cd07136 98 YEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAVV-----EGGVEENQEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 272 CTDPlVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRG 351
Cdd:cd07136 173 LDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHES 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 352 IHDAFVKAFAEAMKKnlRVGNGFEEGTTQGPLINEKAVEKVEKQVndavsKGATVVTGGKrHQLGKNFFEPTLLCNVTQD 431
Cdd:cd07136 252 VKEKFIKELKEEIKK--FYGEDPLESPDYGRIINEKHFDRLAGLL-----DNGKIVFGGN-TDRETLYIEPTILDNVTWD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 432 MLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI--SSVECPFGGVKQ 509
Cdd:cd07136 324 DPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMhlANPYLPFGGVGN 403
|
410
....*....|...
gi 4507229 510 SGLGREGSKYGID 522
Cdd:cd07136 404 SGMGSYHGKYSFD 416
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
64-522 |
6.75e-51 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 181.31 E-value: 6.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 64 FVGGRWLP-AAATFPVQDPASGAAL--GMVADCGVREARAAVRAAYeaFCRWREVSAKERSSLLRKWYNLMIQNKDDLAR 140
Cdd:PRK09457 4 WINGDWIAgQGEAFESRNPVSGEVLwqGNDATAAQVDAAVRAARAA--FPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 141 IITAESGKPLKEAHGEI--------LYSAFFLEWFSEEArrvygdiihTPAKDRRALVLKQPIGVAAVITPWNFPSAMIT 212
Cdd:PRK09457 82 VIARETGKPLWEAATEVtaminkiaISIQAYHERTGEKR---------SEMADGAAVLRHRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 213 RKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPcsrkNAKEVGEAICTDPLVSKISFTGSTTTGkIL 292
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQ----GGRETGKALAAHPDIDGLLFTGSANTG-YL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 293 LHH--AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIH-DAFVKAFAEAMKKnLR 369
Cdd:PRK09457 228 LHRqfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKR-LT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 370 VGNGFEEGTT-QGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLcNVTQDMLCTHEETFGPLAPVIK 448
Cdd:PRK09457 307 VGRWDAEPQPfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVR 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507229 449 FDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI-SSVECPFGGVKQSGLGREGSKYGID 522
Cdd:PRK09457 386 YDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTgASSAAPFGGVGASGNHRPSAYYAAD 460
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
111-516 |
1.24e-50 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 180.72 E-value: 1.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 111 RWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVY--GDIIHT---PAKD 185
Cdd:PLN00412 68 AWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILgeGKFLVSdsfPGNE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 186 RRALVL--KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVynvIPCSRKN 263
Cdd:PLN00412 148 RNKYCLtsKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGL---ISCVTGK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 264 AKEVGEAICTDPLVSKISFTGSTTtgKILLHHAANSVKrVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCS 343
Cdd:PLN00412 225 GSEIGDFLTMHPGVNCISFTGGDT--GIAISKKAGMVP-LQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 344 NQFLVQRGIHDAFVKAFAEAMKKnLRVGNGfEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQlgkNFFEPT 423
Cdd:PLN00412 302 KVVLVMESVADALVEKVNAKVAK-LTVGPP-EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREG---NLIWPL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 424 LLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVE-C 502
Cdd:PLN00412 377 LLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhF 456
|
410
....*....|....
gi 4507229 503 PFGGVKQSGLGREG 516
Cdd:PLN00412 457 PFQGLKDSGIGSQG 470
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
60-530 |
1.32e-49 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 180.33 E-value: 1.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 60 RTDSFVGGRWLPAAAT--FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDD 137
Cdd:PLN02419 113 RVPNLIGGSFVESQSSsfIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 138 LARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGA 217
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 218 ALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIpcsrKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAA 297
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIV----HGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 298 NSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVqrgIHDAfvKAFAEAM---KKNLRVGNGF 374
Cdd:PLN02419 349 AKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVF---VGDA--KSWEDKLverAKALKVTCGS 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 375 EEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKR-----HQLGkNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKF 449
Cdd:PLN02419 424 EPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpgYEKG-NFIGPTILSGVTPDMECYKEEIFGPVLVCMQA 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 450 DTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLisSVECP---FGGVKQSGLGREG--SKYGIDEY 524
Cdd:PLN02419 503 NSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI--PVPLPffsFTGNKASFAGDLNfyGKAGVDFF 580
|
....*.
gi 4507229 525 LELKYV 530
Cdd:PLN02419 581 TQIKLV 586
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
50-525 |
6.20e-48 |
|
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: 173.56 E-value: 6.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 50 RLAGLSAALL-------RTDSFVGGRWLPAAATFPVQDPAS-GAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERS 121
Cdd:TIGR01238 20 ELKPLEAQIHawadktwQAAPIIGHSYKADGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 122 SLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHtpakdrralvlkQPIGVAAVI 201
Cdd:TIGR01238 100 AKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSV------------ESRGVFVCI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 202 TPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPcsrKNAKEVGEAICTDPLVSKIS 281
Cdd:TIGR01238 168 SPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLP---GRGADVGAALTSDPRIAGVA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 282 FTGSTTTG----KILLHHAANSVKRVSmELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFV 357
Cdd:TIGR01238 245 FTGSTEVAqlinQTLAQREDAPVPLIA-ETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 358 KAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATV---VTGGKRHQLGKNFFEPTLLcnVTQDMLC 434
Cdd:TIGR01238 324 TMIQGAMQE-LKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLF--ELDDIAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 435 THEETFGPLAPVIKF--DTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVEC--PFGGvkqS 510
Cdd:TIGR01238 401 LSEEVFGPVLHVVRYkaRELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGG---Q 477
|
490
....*....|....*
gi 4507229 511 GLGREGSKYGIDEYL 525
Cdd:TIGR01238 478 GLSGTGPKAGGPHYL 492
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
113-532 |
1.19e-42 |
|
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: 157.57 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 113 REVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAH-GEI--LYSAFFL------EWFSEEarRVYGDIIHTPA 183
Cdd:cd07137 16 RTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFrDEVsvLVSSCKLaikelkKWMAPE--KVKTPLTTFPA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 184 KdrrALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVyNVIpcsrKN 263
Cdd:cd07137 94 K---AEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAI-KVI----EG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 264 AKEVGEAIcTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKF-RNTGQTCVC 342
Cdd:cd07137 166 GVPETTAL-LEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 343 SNQFLVQRGihdaFVKAFAEAMKKNLR--VGNGFEEGTTQGPLINEKAVEKVEKQVNDAvSKGATVVTGGKRHQlGKNFF 420
Cdd:cd07137 245 PDYVLVEES----FAPTLIDALKNTLEkfFGENPKESKDLSRIVNSHHFQRLSRLLDDP-SVADKIVHGGERDE-KNLYI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 421 EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSV 500
Cdd:cd07137 319 EPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYA 398
|
410 420 430
....*....|....*....|....*....|....
gi 4507229 501 --ECPFGGVKQSGLGREGSKYGIDEYLELKYVCY 532
Cdd:cd07137 399 idTLPFGGVGESGFGAYHGKFSFDAFSHKKAVLY 432
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
41-525 |
3.31e-42 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 161.91 E-value: 3.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 41 PAQLRCYAGRLAGLSAALLRTDSFVGGrwlpAAATFPVQDPASGA-ALGMVADCGVREARAAVRAAYEAFCRWREVSAKE 119
Cdd:PRK11904 533 RSELEPLAAAIAAFLEKQWQAGPIING----EGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEE 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 120 RSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHT--PAKDRRALVLkQPIGV 197
Cdd:PRK11904 609 RAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLpgPTGESNELRL-HGRGV 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 198 AAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLV 277
Cdd:PRK11904 688 FVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGD---GATVGAALTADPRI 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 278 SKISFTGSTTTGKIL---LhhAANSVKRVSM--ELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGI 352
Cdd:PRK11904 765 AGVAFTGSTETARIInrtL--AARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDI 842
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 353 HDAFVKAFAEAMkKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVnDAVSKGATVVTGGKRHQLGKN--FFEPTL--LCNV 428
Cdd:PRK11904 843 ADRVIEMLKGAM-AELKVGDPRLLSTDVGPVIDAEAKANLDAHI-ERMKREARLLAQLPLPAGTENghFVAPTAfeIDSI 920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 429 TQdmlcTHEETFGPLAPVIKFDTEeeaiaianaadvGLA---------GY-----FYSQDPAQIWRVAEQLEVGMVGVNE 494
Cdd:PRK11904 921 SQ----LEREVFGPILHVIRYKAS------------DLDkvidainatGYgltlgIHSRIEETADRIADRVRVGNVYVNR 984
|
490 500 510
....*....|....*....|....*....|...
gi 4507229 495 GLISSV--ECPFGGvkqSGLGREGSKYGIDEYL 525
Cdd:PRK11904 985 NQIGAVvgVQPFGG---QGLSGTGPKAGGPHYL 1014
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
63-525 |
5.64e-42 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 157.30 E-value: 5.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 63 SFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARII 142
Cdd:PLN02315 23 CYVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 143 TAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAG 222
Cdd:PLN02315 103 SLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 223 CTVVVKPAEDTPFSALAL----AELASQAGIPSGVYNVIpCSrknAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAAN 298
Cdd:PLN02315 183 NCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSF-CG---GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 299 SVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGT 378
Cdd:PLN02315 259 RFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQ-VKIGDPLEKGT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 379 TQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLcNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAI 458
Cdd:PLN02315 338 LLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEI 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4507229 459 ANAADVGLAGYFYSQDPAQI--WRVAEQLEVGMVGVN---EGliSSVECPFGGVKQSGLGREGSKYGIDEYL 525
Cdd:PLN02315 417 NNSVPQGLSSSIFTRNPETIfkWIGPLGSDCGIVNVNiptNG--AEIGGAFGGEKATGGGREAGSDSWKQYM 486
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
51-513 |
6.59e-42 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 161.19 E-value: 6.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 51 LAGLSAALlrtDSFVGGRWL---------PAAATFPVQDPA-SGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKER 120
Cdd:PRK11905 538 LAALDEAL---NAFAAKTWHaapllaggdVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAER 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 121 SSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHtpakdrralvlkQPIGVAAV 200
Cdd:PRK11905 615 AAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGH------------KPLGPVVC 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 201 ITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKI 280
Cdd:PRK11905 683 ISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGD---GRTVGAALVADPRIAGV 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 281 SFTGSTTTGKI----LLHHAANSVKRVSmELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTC-----VCsnqflVQRG 351
Cdd:PRK11905 760 MFTGSTEVARLiqrtLAKRSGPPVPLIA-ETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCsalrvLC-----LQED 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 352 IHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVvtggKRHQLGKN-----FFEPTLL- 425
Cdd:PRK11905 834 VADRVLTMLKGAMDE-LRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLPAEtekgtFVAPTLIe 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 426 CNVTQDMlctHEETFGPLAPVIKFDteeEAIAIANAADVGLAGY-----FYSQDPAQIWRVAEQLEVGMVGVNEGLISSV 500
Cdd:PRK11905 909 IDSISDL---EREVFGPVLHVVRFK---ADELDRVIDDINATGYgltfgLHSRIDETIAHVTSRIRAGNIYVNRNIIGAV 982
|
490
....*....|....*
gi 4507229 501 --ECPFGGVKQSGLG 513
Cdd:PRK11905 983 vgVQPFGGEGLSGTG 997
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
192-522 |
4.94e-40 |
|
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: 150.45 E-value: 4.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELasqagIP----SGVYNVIpcsrknakeV 267
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPkyldKECYPVV---------L 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 268 GEAICTDPLVS----KISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCS 343
Cdd:cd07132 164 GGVEETTELLKqrfdYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 344 NQFLVQRGIHDAFVKAFAEAMKKnlRVGNGFEEGTTQGPLINEKAVEKVEKQVndavsKGATVVTGGkRHQLGKNFFEPT 423
Cdd:cd07132 244 DYVLCTPEVQEKFVEALKKTLKE--FYGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVAIGG-QTDEKERYIAPT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 424 LLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSV--E 501
Cdd:cd07132 316 VLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTldS 395
|
330 340
....*....|....*....|.
gi 4507229 502 CPFGGVKQSGLGREGSKYGID 522
Cdd:cd07132 396 LPFGGVGNSGMGAYHGKYSFD 416
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
50-450 |
1.79e-38 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 150.86 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 50 RLAGLSAALLRTD-------SFVGGRwLPAAATFPVQDPASGA-ALGMVADCGVREARAAVRAAYEAFCRWREVSAKERS 121
Cdd:COG4230 540 VLAALSAALAAAAekqwqaaPLIAGE-AASGEARPVRNPADHSdVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERA 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 122 SLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGdiihtpakdrrALVLKQPIGVAAVI 201
Cdd:COG4230 619 AILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFA-----------APTVLRGRGVFVCI 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 202 TPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAICTDPLVSKIS 281
Cdd:COG4230 688 SPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGD---GETVGAALVADPRIAGVA 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 282 FTGSTTTGKI----LLHHAANSVKRVSmELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTC-----VCsnqflVQRGI 352
Cdd:COG4230 765 FTGSTETARLinrtLAARDGPIVPLIA-ETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCsalrvLC-----VQEDI 838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 353 HDAFVKAFAEAMkKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVvtggKRHQLGKN-----FFEPTL--L 425
Cdd:COG4230 839 ADRVLEMLKGAM-AELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLV----HQLPLPEEcangtFVAPTLieI 913
|
410 420
....*....|....*....|....*
gi 4507229 426 CNVTQdmLctHEETFGPLAPVIKFD 450
Cdd:COG4230 914 DSISD--L--EREVFGPVLHVVRYK 934
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
50-513 |
9.38e-38 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 148.97 E-value: 9.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 50 RLAGLSAALLRTDS-------FVGGRWLPAAATfPVQDPASGAAL-GMVADCGVREARAAVRAAYEAFCRWREVSAKERS 121
Cdd:PRK11809 629 RLASLSSALLASAHqkwqaapMLEDPVAAGEMS-PVINPADPRDIvGYVREATPAEVEQALESAVNAAPIWFATPPAERA 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 122 SLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHtpakdrralvlkQPIGVAAVI 201
Cdd:PRK11809 708 AILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTH------------RPLGPVVCI 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 202 TPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPcsrKNAKEVGEAICTDPLVSKIS 281
Cdd:PRK11809 776 SPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLP---GRGETVGAALVADARVRGVM 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 282 FTGSTTTGKILlhhAANSVKRVS---------MELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGI 352
Cdd:PRK11809 853 FTGSTEVARLL---QRNLAGRLDpqgrpipliAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDV 929
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 353 HDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATV----VTGGKRHQLGkNFFEPTL--LC 426
Cdd:PRK11809 930 ADRTLKMLRGAMAE-CRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVfqaaRENSEDWQSG-TFVPPTLieLD 1007
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 427 NVTQdmlcTHEETFGPLAPVIKFdteEEAIAIANAADVGLAGY-----FYSQDPAQIWRVAEQLEVGMVGVNEGLISSVE 501
Cdd:PRK11809 1008 SFDE----LKREVFGPVLHVVRY---NRNQLDELIEQINASGYgltlgVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVV 1080
|
490
....*....|....
gi 4507229 502 C--PFGGVKQSGLG 513
Cdd:PRK11809 1081 GvqPFGGEGLSGTG 1094
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
113-535 |
8.29e-36 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 139.48 E-value: 8.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 113 REVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAH----GEILYSAFFL-----EWFSEEarRVYGDIIHTPA 183
Cdd:PLN02203 23 RTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYrdevGVLTKSANLAlsnlkKWMAPK--KAKLPLVAFPA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 184 KdrrALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAelasqAGIP----SGVYNVIpc 259
Cdd:PLN02203 101 T---AEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA-----ANIPkyldSKAVKVI-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 260 srKNAKEVGEAICTDPLvSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIV--FDSA-NVDQAVAGAMASKFRN- 335
Cdd:PLN02203 171 --EGGPAVGEQLLQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGSc 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 336 TGQTCVCSNQFLVQRGihdaFVKAFAEAMKKNLR--VGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKgATVVTGGKRH 413
Cdd:PLN02203 248 AGQACIAIDYVLVEER----FAPILIELLKSTIKkfFGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSID 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 414 QlgKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGV 492
Cdd:PLN02203 323 E--KKLFiEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTF 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 4507229 493 NEGLISSV--ECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL 535
Cdd:PLN02203 401 NDAIIQYAcdSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSL 445
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
188-535 |
2.52e-29 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 120.92 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 188 ALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVipcsrknakeV 267
Cdd:PLN02174 106 AEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVV----------E 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 268 GEAICTDPLVS----KISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFR-NTGQTCVC 342
Cdd:PLN02174 176 GAVTETTALLEqkwdKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACIS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 343 SNQFLVQRgihdAFVKAFAEAMKKNLRV--GNGFEEGTTQGPLINEKAVEKV-----EKQVNDavskgaTVVTGGKRHQl 415
Cdd:PLN02174 256 PDYILTTK----EYAPKVIDAMKKELETfyGKNPMESKDMSRIVNSTHFDRLsklldEKEVSD------KIVYGGEKDR- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 416 gKNF-FEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNE 494
Cdd:PLN02174 325 -ENLkIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVND 403
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 4507229 495 GLISSV--ECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL 535
Cdd:PLN02174 404 IAVHLAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSL 446
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
112-487 |
2.71e-27 |
|
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: 114.26 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAhGEILYSAFFLEWFSE--EARRVYGDIIHTPAKDRRAL 189
Cdd:cd07084 15 ARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFviYSYRIPHEPGNHLGQGLKQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 190 VLKQ--PIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGI-PSGVYNVIpCSRKNAke 266
Cdd:cd07084 94 SHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLI-NGDGKT-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 267 vGEAICTDPLVSKISFTGSTTTGKILLHHAANSvkRVSMELGGLAPFIVFDSAnvdQAVAgAMASKFRNTgqTCVCSNQF 346
Cdd:cd07084 171 -MQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDA---QAVD-YVAWQCVQD--MTACSGQK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 347 LVQRGIhdAFV------KAFAEAMKKNLRvgNGFEEGTTQGPLINekavEKVEKQVNDAVSKGATVVTGG----KRHQLG 416
Cdd:cd07084 242 CTAQSM--LFVpenwskTPLVEKLKALLA--RRKLEDLLLGPVQT----FTTLAMIAHMENLLGSVLLFSgkelKNHSIP 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4507229 417 KNF--FEPTLLCNVTQDMLCTH----EETFGPLAPVIKF-DTEEEAIAIANAADVG-LAGYFYSQDPAQIWRVAEQLEV 487
Cdd:cd07084 314 SIYgaCVASALFVPIDEILKTYelvtEEIFGPFAIVVEYkKDQLALVLELLERMHGsLTAAIYSNDPIFLQELIGNLWV 392
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
112-486 |
2.65e-24 |
|
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: 105.70 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARR-VYGDIIHTPAKDRRALV 190
Cdd:cd07129 15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgSWLDARIDPADPDRQPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 191 -------LKQPIGVAAVITPWNFPSAMITrkVG----AALAAGCTVVVKPAEDTPFSALALAELASQA----GIPSGVYN 255
Cdd:cd07129 95 prpdlrrMLVPLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLPAGVFS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 256 VIPCSRKnakEVGEAICTDPLVSKISFTGSTTTGKILLHHAAnsvKR-----VSMELGGLAPFIVFDSA---NVDQAVAG 327
Cdd:cd07129 173 LLQGGGR---EVGVALVKHPAIKAVGFTGSRRGGRALFDAAA---ARpepipFYAELGSVNPVFILPGAlaeRGEAIAQG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 328 AMASKFRNTGQTCVCSNQFLVQRGIH-DAFVKAFAEAMKKnlrvgngfeegTTQGPLINEKAVEKVEKQVNDAVS-KGAT 405
Cdd:cd07129 247 FVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAA-----------APAQTMLTPGIAEAYRQGVEALAAaPGVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 406 VVTGGKRHQlGKNFFEPTLLCNVTQDMLCT---HEETFGPLAPVIKFDteeeaiaianaadvglagyfysqDPAQIWRVA 482
Cdd:cd07129 316 VLAGGAAAE-GGNQAAPTLFKVDAAAFLADpalQEEVFGPASLVVRYD-----------------------DAAELLAVA 371
|
....
gi 4507229 483 EQLE 486
Cdd:cd07129 372 EALE 375
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
197-511 |
2.68e-23 |
|
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: 103.44 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 197 VAAViTPWNFPSamitrkVGAALAA-----GCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSrknAKEVGEAI 271
Cdd:cd07123 174 VYAV-SPFNFTA------IGGNLAGapalmGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGD---GPVVGDTV 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 272 CTDPLVSKISFTGSTTTGKILLHHAANSVK------RVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQ 345
Cdd:cd07123 244 LASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 346 FLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDA-VSKGATVVTGGKRHQLGKNFFEPTL 424
Cdd:cd07123 324 AYVPESLWPEVKERLLEELKE-IKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAkSDPEAEIIAGGKCDDSVGYFVEPTV 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 425 LcnVTQD----MLCthEETFGPLAPVIKFDTEEEAIAIANAADV---GLAGYFYSQDPAQIWRVAEQLE--VGMVGVNEG 495
Cdd:cd07123 403 I--ETTDpkhkLMT--EEIFGPVLTVYVYPDSDFEETLELVDTTspyALTGAIFAQDRKAIREATDALRnaAGNFYINDK 478
|
330
....*....|....*...
gi 4507229 496 LISSV--ECPFGGVKQSG 511
Cdd:cd07123 479 PTGAVvgQQPFGGARASG 496
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
63-485 |
5.32e-23 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 102.48 E-value: 5.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 63 SFVGGRWLP-AAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARI 141
Cdd:PRK11903 7 NYVAGRWQAgSGAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 142 ITAESGKPLKEAHGEILYSAFFLEWFSEEARRVyGDIIHTPAKDRRAL----------VLKQPIGVAAVITPWNFPSAMI 211
Cdd:PRK11903 87 ATANSGTTRNDSAVDIDGGIFTLGYYAKLGAAL-GDARLLRDGEAVQLgkdpafqgqhVLVPTRGVALFINAFNFPAWGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 212 TRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGI-PSGVYNVIpCSrknakevGEAICTDPLVSK--ISFTGSTTT 288
Cdd:PRK11903 166 WEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVV-CG-------SSAGLLDHLQPFdvVSFTGSAET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 289 GKILLHHAA---NSVkRVSME-----LGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAF 360
Cdd:PRK11903 238 AAVLRSHPAvvqRSV-RVNVEadslnSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 361 AEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVnDAVSKGATVVTGGKRHQL------GKNFFEPTLL-CNVTQDML 433
Cdd:PRK11903 317 AARLAK-TTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFALvdadpaVAACVGPTLLgASDPDAAT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 4507229 434 CTHE-ETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQL 485
Cdd:PRK11903 395 AVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALEL 447
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
62-489 |
1.34e-22 |
|
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: 101.19 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 62 DSFVGGRWL-PAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLAR 140
Cdd:cd07128 2 QSYVAGQWHaGTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 141 IiTAESGKPLKEAHGEILYSAFFLEWFSEEARR--------VYGDIIHTpAKD-----RRALVLKQpiGVAAVITPWNFP 207
Cdd:cd07128 82 L-SAATGATRRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPL-SKDgtfvgQHILTPRR--GVAVHINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 208 SAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGI-PSGVYNVIPCSrknakeVGEAIctDPLVSK--ISFTG 284
Cdd:cd07128 158 VWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS------VGDLL--DHLGEQdvVAFTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 285 STTTGKILLHH---AANSVkRVSME---LGG--LAPFIVFDSANVD---QAVAGAMASKfrnTGQTCVCSNQFLVQRGIH 353
Cdd:cd07128 230 SAATAAKLRAHpniVARSI-RFNAEadsLNAaiLGPDATPGTPEFDlfvKEVAREMTVK---AGQKCTAIRRAFVPEARV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 354 DAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVnDAVSKGATVVTGGKRHQLGKN-------FFEPTLL- 425
Cdd:cd07128 306 DAVIEALKARLAK-VVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRFEVVGadaekgaFFPPTLLl 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507229 426 CNVTQDMLCTHE-ETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAqiwrVAEQLEVGM 489
Cdd:cd07128 384 CDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPA----FARELVLGA 444
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
111-370 |
1.08e-07 |
|
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: 54.15 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 111 RWREVSAKER----SSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHgeilysafflewfseEARRVYGDIIHTpakdr 186
Cdd:cd07077 35 RLASEAVSERgayiRSLIANWIAMMGCSESKLYKNIDTERGITASVGH---------------IQDVLLPDNGET----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 187 raLVLKQPIGVAAVITPWNFPSAMITrKVGAALAAGCTVVVKPAEDTPFSALALAeLASQAGIPS-GVYNVIPCSRKNAK 265
Cdd:cd07077 95 --YVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALA-LLFQAADAAhGPKILVLYVPHPSD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 266 EVGEAICTDPLVSKISFTGSTTTGKILLHHAANsvKRVsMELGGLAPFIVFDS-ANVDQAVAGAMASKFRNtGQTCVcSN 344
Cdd:cd07077 171 ELAEELLSHPKIDLIVATGGRDAVDAAVKHSPH--IPV-IGFGAGNSPVVVDEtADEERASGSVHDSKFFD-QNACA-SE 245
|
250 260
....*....|....*....|....*.
gi 4507229 345 QFLVqrgIHDAFVKAFAEAMKKNLRV 370
Cdd:cd07077 246 QNLY---VVDDVLDPLYEEFKLKLVV 268
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
194-488 |
3.53e-07 |
|
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: 52.87 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 194 PIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAedtPFSALALA-------ELASQAGIPSGVynVIPCSRKNAKE 266
Cdd:cd07127 193 PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPH---PAAILPLAitvqvarEVLAEAGFDPNL--VTLAADTPEEP 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 267 VGEAICTDPLVSKISFTGSTTTGKILLHHAANsvKRVSMELGGLAPFIVfDSANVDQAVAGAMASKFR-NTGQTCVCSNQ 345
Cdd:cd07127 268 IAQTLATRPEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVV-DSTDDLKAMLRNLAFSLSlYSGQMCTTPQN 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 346 FLVQR-GI--------HDAFVKAFAEAMKKNLrvGNGFEEGTTQGPLINEKAVEKVEKqvndaVSKGATVVTGGKrhQLG 416
Cdd:cd07127 345 IYVPRdGIqtddgrksFDEVAADLAAAIDGLL--ADPARAAALLGAIQSPDTLARIAE-----ARQLGEVLLASE--AVA 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 417 KNFFE------PTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADV---GLAGYFYSQDPAQIWRVAE-QLE 486
Cdd:cd07127 416 HPEFPdarvrtPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVRehgAMTVGVYSTDPEVVERVQEaALD 495
|
..
gi 4507229 487 VG 488
Cdd:cd07127 496 AG 497
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
189-362 |
3.32e-06 |
|
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: 49.57 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 189 LVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGV-YNVIPCSRKNAKEV 267
Cdd:cd07081 90 LIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGApENLIGWIDNPSIEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 268 GEAICTDPLVSKISFTGstttGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFL 347
Cdd:cd07081 170 AQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVI 245
|
170
....*....|....*
gi 4507229 348 VQRGIHDAFVKAFAE 362
Cdd:cd07081 246 VVDSVYDEVMRLFEG 260
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
112-450 |
5.47e-05 |
|
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: 45.95 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 112 WREVSAKErSSLLRKwynlmIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARR-------VYGDIIHTPAK 184
Cdd:cd07126 64 YGDVSHRV-AHELRK-----PEVEDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRflarsfnVPGDHQGQQSS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 185 DRRalvlkQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNA 264
Cdd:cd07126 138 GYR-----WPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTM 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 265 KEVGEAicTDPLVskISFTGSTTTGkillHHAANSVK-RVSMELGG-----LAPfivfDSANVDQAVAGAMASKFRNTGQ 338
Cdd:cd07126 213 NKILLE--ANPRM--TLFTGSSKVA----ERLALELHgKVKLEDAGfdwkiLGP----DVSDVDYVAWQCDQDAYACSGQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507229 339 TcvCSNQFL-------VQRGIHDAfVKAFAEamKKNLrvgngfeEGTTQGPLI---NEKAVEKVEKQvndAVSKGATVVT 408
Cdd:cd07126 281 K--CSAQSIlfahenwVQAGILDK-LKALAE--QRKL-------EDLTIGPVLtwtTERILDHVDKL---LAIPGAKVLF 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 4507229 409 GGK---RHQLGKNF--FEPT--------LLCNVTQDMLCTheETFGPLAPVIKFD 450
Cdd:cd07126 346 GGKpltNHSIPSIYgaYEPTavfvpleeIAIEENFELVTT--EVFGPFQVVTEYK 398
|
|
| |
