|
Name |
Accession |
Description |
Interval |
E-value |
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
78-480 |
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: 715.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 158 LYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA 237
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 238 LALAE----------------------------------------------ILLHHAANSVKRVSMELGGLAPFIVFDSA 271
Cdd:TIGR01780 161 LALARlaeqagipkgvlnvitgsrakevgnvlttsplvrkisftgstnvgkILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 272 NVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDA 351
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKK-LKVGNGLDEGVTQGPLINEKAVEKVEKHIADA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 352 VSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIW 431
Cdd:TIGR01780 320 VEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIW 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1589401592 432 RVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 480
Cdd:TIGR01780 400 RVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
78-483 |
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: 682.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 158 LYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA 237
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 238 LALAE---------------------------------------------ILLHHAANSVKRVSMELGGLAPFIVFDSAN 272
Cdd:cd07103 161 LALAElaeeaglpagvlnvvtgspaeigealcasprvrkisftgstavgkLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 273 VDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAV 352
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKK-LKVGNGLDEGTDMGPLINERAVEKVEALVEDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 353 SKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWR 432
Cdd:cd07103 320 AKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1589401592 433 VAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 483
Cdd:cd07103 400 VAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVS 450
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
55-487 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 636.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 55 SAALLRTDSFVGGRWLPA--AATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMI 132
Cdd:PLN02278 19 NAGLLRTQGLIGGKWTDAydGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLII 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 133 QNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMIT 212
Cdd:PLN02278 99 ANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMIT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 213 RKVGAALAAGCTVVVKPAEDTPFSALALAEI---------------------------------------------LLHH 247
Cdd:PLN02278 179 RKVGPALAAGCTVVVKPSELTPLTALAAAELalqagippgvlnvvmgdapeigdallaspkvrkitftgstavgkkLMAG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 248 AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFE 327
Cdd:PLN02278 259 AAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQK-LVVGDGFE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 328 EGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEA 407
Cdd:PLN02278 338 EGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 408 IAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL 487
Cdd:PLN02278 418 IAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCLGNM 497
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
56-485 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 532.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 56 AALLRTDSFVGGRWLPA--AATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQ 133
Cdd:PRK11241 6 STLFRQQALINGEWLDAnnGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMME 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 134 NKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITR 213
Cdd:PRK11241 86 HQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 214 KVGAALAAGCTVVVKPAEDTPFSALALAEI---------------------------------------------LLHHA 248
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELairagipagvfnvvtgsagavggeltsnplvrklsftgsteigrqLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 249 ANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEE 328
Cdd:PRK11241 246 AKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSK-LHIGDGLEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 329 GTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAI 408
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589401592 409 AIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYG 485
Cdd:PRK11241 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIG 481
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
60-483 |
2.54e-178 |
|
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: 508.51 E-value: 2.54e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 60 RTDSFVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDD 137
Cdd:COG1012 5 EYPLFIGGEWVAAASgeTFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 138 LARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGA 217
Cdd:COG1012 85 LAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 218 ALAAGCTVVVKPAEDTPFSALALAEI------------------------LLHH---------------------AANSV 252
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELleeaglpagvlnvvtgdgsevgaaLVAHpdvdkisftgstavgrriaaaAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 253 KRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQ 332
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKA-LKVGDPLDPGTDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 333 GPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGK-NFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIA 411
Cdd:COG1012 324 GPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGgYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589401592 412 NAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSV-ECPFGGVKQSGLGREGSKYGIDEYLELKYVC 483
Cdd:COG1012 404 NDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVpQAPFGGVKQSGIGREGGREGLEEYTETKTVT 476
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
69-482 |
4.07e-158 |
|
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: 456.61 E-value: 4.07e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 69 WLPAAA-TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESG 147
Cdd:pfam00171 1 WVDSESeTIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 148 KPLKEAHGEILYSAFFLEWFSEEARRVYGDIIhTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVV 227
Cdd:pfam00171 81 KPLAEARGEVDRAIDVLRYYAGLARRLDGETL-PSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 228 KPAEDTPFSALALAEIL---------------------------------------------LHHAANSVKRVSMELGGL 262
Cdd:pfam00171 160 KPSELTPLTALLLAELFeeaglpagvlnvvtgsgaevgealvehpdvrkvsftgstavgrhiAEAAAQNLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 263 APFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVE 342
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKK-LKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 343 KVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYF 422
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1589401592 423 YSQDPAQIWRVAEQLEVGMVGVNEGLISSVE-CPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:pfam00171 399 FTSDLERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
109-483 |
8.97e-146 |
|
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: 423.93 E-value: 8.97e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 109 FCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRA 188
Cdd:cd07078 11 FKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGELA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 189 LVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEI------------------------L 244
Cdd:cd07078 91 IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELlaeaglppgvlnvvtgdgdevgaaL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 245 LHH---------------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRG 303
Cdd:cd07078 171 ASHprvdkisftgstavgkaimraAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHES 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 304 IHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGK-NFFEPTLLCNVTQ 382
Cdd:cd07078 251 IYDEFVERLVERVKA-LKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKgYFVPPTVLTDVDP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 383 DMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLIS-SVECPFGGVKQ 461
Cdd:cd07078 330 DMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGaEPSAPFGGVKQ 409
|
410 420
....*....|....*....|..
gi 1589401592 462 SGLGREGSKYGIDEYLELKYVC 483
Cdd:cd07078 410 SGIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
64-482 |
4.05e-129 |
|
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: 382.77 E-value: 4.05e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARI 141
Cdd:cd07088 1 YINGEFVPSSsgETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 142 ITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAA 221
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 222 GCTVVVKPAEDTPFSALALAEIL---------------------------------------------LHHAANSVKRVS 256
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVdeaglpagvlnivtgrgsvvgdalvahpkvgmisltgsteagqkiMEAAAENITKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 257 MELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLI 336
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKA-VKVGDPFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 337 NEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGK-NFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAAD 415
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGATLLTGGKRPEGEKgYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSE 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589401592 416 VGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07088 400 YGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
109-482 |
7.18e-113 |
|
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: 339.82 E-value: 7.18e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 109 FCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGD-IIHTPAKdrR 187
Cdd:cd07100 12 FLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADePIETDAG--K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 188 ALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEILL---------------HHAANSV 252
Cdd:cd07100 90 AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFReagfpegvfqnllidSDQVEAI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 253 -----------------------------KRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRG 303
Cdd:cd07100 170 iadprvrgvtltgseragravaaeagknlKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHED 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 304 IHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQD 383
Cdd:cd07100 250 VYDEFLEKFVEAMAA-LKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPTVLTDVTPG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 384 MLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSG 463
Cdd:cd07100 329 MPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVKRSG 408
|
410
....*....|....*....
gi 1589401592 464 LGREGSKYGIDEYLELKYV 482
Cdd:cd07100 409 YGRELGRFGIREFVNIKTV 427
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
78-483 |
2.82e-112 |
|
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: 339.16 E-value: 2.82e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEA-HGE 156
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLArTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 157 ILYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS 236
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDG-GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 237 ALALAEILL-------------------------HH--------------------AANSVKRVSMELGGLAPFIVFDSA 271
Cdd:cd07093 160 AWLLAELANeaglppgvvnvvhgfgpeagaalvaHPdvdlisftgetatgrtimraAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 272 NVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDA 351
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKA-LKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 352 VSKGATVVTGGKRHQL----GKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDP 427
Cdd:cd07093 319 RAEGATILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1589401592 428 AQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 483
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
112-482 |
4.02e-112 |
|
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: 339.14 E-value: 4.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVL 191
Cdd:cd07114 37 WRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEI------------------------LLHH 247
Cdd:cd07114 117 REPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagfppgvvnvvtgfgpetgeaLVEH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 248 ---------------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHD 306
Cdd:cd07114 197 plvakiaftggtetgrhiaraAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 307 AFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKN----FFEPTLLCNVTQ 382
Cdd:cd07114 277 EFVERLVARARA-IRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSGADLgagyFFEPTILADVTN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 383 DMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQS 462
Cdd:cd07114 356 DMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDS 435
|
410 420
....*....|....*....|
gi 1589401592 463 GLGREGSKYGIDEYLELKYV 482
Cdd:cd07114 436 GIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
64-482 |
2.97e-108 |
|
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: 329.55 E-value: 2.97e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAF--CRWREVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07091 7 FINNEFVDSVSgkTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFetGWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 140 RIITAESGKPLKE-AHGEILYSAFFLEWFSEEARRVYGDIIHTPaKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAA 218
Cdd:cd07091 87 ALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIPID-GNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 219 LAAGCTVVVKPAEDTPFSALALAEILL-------------------------HH--------------------AANS-V 252
Cdd:cd07091 166 LAAGNTVVLKPAEQTPLSALYLAELIKeagfppgvvnivpgfgptagaaissHMdvdkiaftgstavgrtimeaAAKSnL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 253 KRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQ 332
Cdd:cd07091 246 KKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEK-RVVGDPFDPDTFQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 333 GPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIAN 412
Cdd:cd07091 325 GPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERAN 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 413 AADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07091 405 DTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
76-483 |
5.86e-108 |
|
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: 328.02 E-value: 5.86e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 76 FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHG 155
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 156 EILYSAFFLEWFSEEARRVYGDII----HTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAE 231
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIpfdaSPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 232 DTPFSALALAEILL------------HHAANSV-------------------------------KRVSMELGGLAPFIVF 268
Cdd:cd07149 161 QTPLSALKLAELLLeaglpkgalnvvTGSGETVgdalvtdprvrmisftgspavgeaiarkaglKKVTLELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 269 DSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQV 348
Cdd:cd07149 241 ADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKK-LVVGDPLDEDTDVGPMISEAEAERIEEWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 349 NDAVSKGATVVTGGKRHQlgkNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPA 428
Cdd:cd07149 320 EEAVEGGARLLTGGKRDG---AILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQ 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1589401592 429 QIWRVAEQLEVGMVGVNEglISSVEC---PFGGVKQSGLGREGSKYGIDEYLELKYVC 483
Cdd:cd07149 397 KALKAARELEVGGVMIND--SSTFRVdhmPYGGVKESGTGREGPRYAIEEMTEIKLVC 452
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
76-482 |
2.97e-106 |
|
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: 323.90 E-value: 2.97e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 76 FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHG 155
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 156 EILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPF 235
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 236 SALALAEI---------------------------------------------LLHHAANSVKRVSMELGGLAPFIVFDS 270
Cdd:cd07150 161 IGLKIAEImeeaglpkgvfnvvtgggaevgdelvddprvrmvtftgstavgreIAEKAGRHLKKITLELGGKNPLIVLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 271 ANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVND 350
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASK-LKVGDPRDPDTVIGPLISPRQVERIKRQVED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 351 AVSKGATVVTGGKRHqlgKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQI 430
Cdd:cd07150 320 AVAKGAKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1589401592 431 WRVAEQLEVGMVGVNEGLISS-VECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07150 397 FKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
76-484 |
4.33e-106 |
|
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: 323.53 E-value: 4.33e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 76 FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHG 155
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 156 EILYSAFFLEWFSEEARRVYGDIIHTPAKD----RRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAE 231
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEynerRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 232 DTPFSALALAEILLH---------------------------------------------HAANSVKRVSMELGGLAPFI 266
Cdd:cd07145 161 NTPLTAIELAKILEEaglppgvinvvtgygsevgdeivtnpkvnmisftgstavglliasKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 267 VFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEK 346
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKK-LKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 347 QVNDAVSKGATVVTGGKRHQlgKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQD 426
Cdd:cd07145 320 LVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1589401592 427 PAQIWRVAEQLEVGMVGVNE-GLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCY 484
Cdd:cd07145 398 INRALKVARELEAGGVVINDsTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
112-482 |
1.15e-105 |
|
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: 321.40 E-value: 1.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVL 191
Cdd:cd07104 16 WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDVPGKESMVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS-ALALAEI---------LLH--------------- 246
Cdd:cd07104 96 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIfeeaglpkgVLNvvpgggseigdalve 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 247 H---------------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIH 305
Cdd:cd07104 176 HprvrmisftgstavgrhigelAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 306 DAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQlgkNFFEPTLLCNVTQDML 385
Cdd:cd07104 256 DEFVEKLVAKAKA-LPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEG---LFYQPTVLSDVTPDMP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 386 CTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSvEC--PFGGVKQSG 463
Cdd:cd07104 332 IFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVND-EPhvPFGGVKASG 410
|
410
....*....|....*....
gi 1589401592 464 LGREGSKYGIDEYLELKYV 482
Cdd:cd07104 411 GGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
111-482 |
1.22e-103 |
|
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: 316.97 E-value: 1.22e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 111 RWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALV 190
Cdd:cd07118 36 PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNLGDDMLGLV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 191 LKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEILL------------------------- 245
Cdd:cd07118 116 LREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIeaglpagvvnivtgygatvgqamte 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 246 HH--------------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIH 305
Cdd:cd07118 196 HPdvdmvsftgstrvgkaiaaaAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 306 DAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKN-FFEPTLLCNVTQDM 384
Cdd:cd07118 276 DAFVAAVVARSRK-VRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGlFYQPTIFTDVTPDM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 385 LCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGL 464
Cdd:cd07118 355 AIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGI 434
|
410
....*....|....*...
gi 1589401592 465 GREGSKYGIDEYLELKYV 482
Cdd:cd07118 435 GRELGRYGVEEYTELKTV 452
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
64-482 |
1.88e-103 |
|
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: 317.72 E-value: 1.88e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAF--CRWREVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07119 1 YIDGEWVEAASgkTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 140 RIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAAL 219
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPP-HVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 220 AAGCTVVVKPAEDTPFSALALAEIL-------------------------LHH--------------------AANSVKR 254
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIeeaglpagvvnlvtgsgatvgaelaESPdvdlvsftggtatgrsimraAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 255 VSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGP 334
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKK-IKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 335 LINEKAVEKVEKQVNDAVSKGATVVTGGKR---HQLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAI 410
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRptgDELAKGYFvEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1589401592 411 ANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
64-480 |
1.30e-102 |
|
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: 314.83 E-value: 1.30e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARI 141
Cdd:cd07138 2 YIDGAWVAPAgtETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 142 ITAESGKPLK---EAH-----GEILYSAFFLEWFSEEARRvygdiihtpakdRRALVLKQPIGVAAVITPWNFPSAMITR 213
Cdd:cd07138 82 ITLEMGAPITlarAAQvglgiGHLRAAADALKDFEFEERR------------GNSLVVREPIGVCGLITPWNWPLNQIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 214 KVGAALAAGCTVVVKPAEDTPFSALALAEIL---------------------------------------------LHHA 248
Cdd:cd07138 150 KVAPALAAGCTVVLKPSEVAPLSAIILAEILdeaglpagvfnlvngdgpvvgealsahpdvdmvsftgstragkrvAEAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 249 ANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAfVKAFAEAMKKNLRVGNGFEE 328
Cdd:cd07138 230 ADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAE-AEEIAAAAAEAYVVGDPRDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 329 GTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGG--KRHQLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEE 405
Cdd:cd07138 309 ATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgRPEGLERGYFvKPTVFADVTPDMTIAREEIFGPVLSIIPYDDED 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1589401592 406 EAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSvECPFGGVKQSGLGREGSKYGIDEYLELK 480
Cdd:cd07138 389 EAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP-GAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
78-480 |
4.98e-101 |
|
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: 310.23 E-value: 4.98e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 158 LYSAFFLEWFSEEARRVygDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA 237
Cdd:cd07106 81 GGAVAWLRYTASLDLPD--EVIEDDD-TRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 238 LALAEIL-----------------------LH--------------------HAANSVKRVSMELGGLAPFIVFDSANVD 274
Cdd:cd07106 158 LKLGELAqevlppgvlnvvsggdelgpaltSHpdirkisftgstatgkkvmaSAAKTLKRVTLELGGNDAAIVLPDVDID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 275 QAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSK 354
Cdd:cd07106 238 AVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAK-AAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 355 GATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVA 434
Cdd:cd07106 317 GAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVA 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1589401592 435 EQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 480
Cdd:cd07106 397 RRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
63-485 |
1.88e-100 |
|
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: 309.66 E-value: 1.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 63 SFVGGRWLPAA--ATFPVQDPASGA-ALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07131 1 NYIGGEWVDSAsgETFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 140 RIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAAL 219
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 220 AAGCTVVVKPAEDTPFSALALAEILLH------------------------H---------------------AANSVKR 254
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEaglppgvvnvvhgrgeevgealveHpdvdvvsftgstevgerigetCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 255 VSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGP 334
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKR-LRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 335 LINEKAVEKVEKQVNDAVSKGATVVTGGKR---HQLGK-NFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAI 410
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERltgGGYEKgYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1589401592 411 ANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI-SSVECPFGGVKQSGLG-REGSKYGIDEYLELK--YVCYG 485
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKavYVDYS 478
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
78-483 |
2.88e-100 |
|
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: 308.59 E-value: 2.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 158 LYSAFFLEWFSEEARRVYGDIIHTPA----KDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDT 233
Cdd:cd07094 83 DRAIDTLRLAAEEAERIRGEEIPLDAtqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 234 PFSALALAEILL------------------------------------------HHAANS-VKRVSMELGGLAPFIVFDS 270
Cdd:cd07094 163 PLSALELAKILVeagvpegvlqvvtgerevlgdafaadervamlsftgsaavgeALRANAgGKRIALELGGNAPVIVDRD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 271 ANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVND 350
Cdd:cd07094 243 ADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKK-LKVGDPLDEDTDVGPLISEEAAERVERWVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 351 AVSKGATVVTGGKRHqlgKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQI 430
Cdd:cd07094 322 AVEAGARLLCGGERD---GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1589401592 431 WRVAEQLEVGMVGVNEGLISSVE-CPFGGVKQSGLGREGSKYGIDEYLELKYVC 483
Cdd:cd07094 399 FKAAEKLEVGGVMVNDSSAFRTDwMPFGGVKESGVGREGVPYAMEEMTEEKTVV 452
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
112-483 |
6.09e-99 |
|
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: 302.23 E-value: 6.09e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVL 191
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEAYVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEI------------------------LLHH 247
Cdd:cd06534 90 REPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELlqeaglppgvvnvvpgggdevgaaLLSH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 248 ---------------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHD 306
Cdd:cd06534 170 prvdkisftgstavgkaimkaAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 307 AFVKAFAeamkknlrvgngfeegttqgplinekavekvekqvndavskgatvvtggkrhqlgknffepTLLCNVTQDMLC 386
Cdd:cd06534 250 EFVEKLV-------------------------------------------------------------TVLVDVDPDMPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 387 THEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI-SSVECPFGGVKQSGLG 465
Cdd:cd06534 269 AQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGVKNSGIG 348
|
410
....*....|....*...
gi 1589401592 466 REGSKYGIDEYLELKYVC 483
Cdd:cd06534 349 REGGPYGLEEYTRTKTVV 366
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
74-480 |
7.58e-99 |
|
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: 304.91 E-value: 7.58e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 74 ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAF--CRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLK 151
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFesGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 152 EA-HGEILYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPA 230
Cdd:cd07112 82 DAlAVDVPSAANTFRWYAEAIDKVYGEVAPTGP-DALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 231 EDTPFSALALAEI---------------------------------------------LLHHAANS-VKRVSMELGGLAP 264
Cdd:cd07112 161 EQSPLTALRLAELaleaglpagvlnvvpgfghtagealglhmdvdalaftgstevgrrFLEYSGQSnLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 265 FIVF-DSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEK 343
Cdd:cd07112 241 NIVFaDAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAARE-WKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 344 VEKQVNDAVSKGATVVTGGKRHQL--GKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGY 421
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRVLTetGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1589401592 422 FYSQDPAQIWRVAEQLEVGMVGVN---EGLISSvecPFGGVKQSGLGREGSKYGIDEYLELK 480
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNcfdEGDITT---PFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
78-484 |
7.65e-97 |
|
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: 299.93 E-value: 7.65e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRW-REVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHG- 155
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 156 EILYSAFFLEWFSEEARRVYGDIIHTPAKDR----RALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAE 231
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRggpgRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 232 DTPFSALALAEILL-------------------------HH--------------------AANSVKRVSMELGGLAPFI 266
Cdd:cd07089 161 DTPLSALLLGEIIAetdlpagvvnvvtgsdnavgealttDPrvdmvsftgstavgrrimaqAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 267 VFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFEEGTTQGPLINEKAVEKVEK 346
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFE-ALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 347 QVNDAVSKGATVVTGGKR-HQLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYS 424
Cdd:cd07089 320 YIARGRDEGARLVTGGGRpAGLDKGFYvEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 425 QDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCY 484
Cdd:cd07089 400 ADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
62-482 |
7.36e-96 |
|
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: 297.62 E-value: 7.36e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 62 DSFVGGRWLPAAATFPVQDPAS-GAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLAR 140
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 141 IITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALA 220
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 221 AGCTVVVKPAEDTPFSALALAEI------------------------LLHH---------------------AANSVKRV 255
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEIleeaglpagvfnlvmgsgsevgqaLVEHpdvdavsftgstavgrriaaaAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 256 SMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPL 335
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKA-LKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 336 INEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKN--FFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANA 413
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEgyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAND 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589401592 414 ADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNE---GLISSVecPFGGVKQSGLG-REGSKYGIDEYLELKYV 482
Cdd:cd07097 401 TEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLptaGVDYHV--PFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
64-482 |
1.37e-93 |
|
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: 292.39 E-value: 1.37e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFC-RWREVSAKERSSLLRKWYNLMIQNKDDLAR 140
Cdd:cd07144 11 FINNEFVKSSDgeTIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFEsWWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 141 IITAESGKPLKE-AHGEILYSAFFLEWFSEEARRVYGD-IIHTPAKdrRALVLKQPIGVAAVITPWNFPSAMITRKVGAA 218
Cdd:cd07144 91 IEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKtIPTSPNK--LAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 219 LAAGCTVVVKPAEDTPFSAL----------------------------ALAE-----------------ILLHHAANSVK 253
Cdd:cd07144 169 LAAGNTVVIKPAENTPLSLLyfanlvkeagfppgvvniipgygavagsALAEhpdvdkiaftgstatgrLVMKAAAQNLK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 254 RVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEEGTTQG 333
Cdd:cd07144 249 AVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYKVGSPFDDDTVVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 334 PLINEKAVEKVEKQVNDAVSKGATVVTGGKRH--QLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAI 410
Cdd:cd07144 329 PQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKApeGLGKGYFiPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKK 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1589401592 411 ANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07144 409 ANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
76-480 |
1.54e-93 |
|
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: 291.07 E-value: 1.54e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 76 FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHG 155
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 156 EILYSAFFLEWFSEEARRVYGDI----IHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAE 231
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVlpldISARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 232 DTPFSALALAEIL----LHHAANSV--------------------------------------KRVSMELGGLAPFIVFD 269
Cdd:cd07147 161 RTPLSALILGEVLaetgLPKGAFSVlpcsrddadllvtderikllsftgspavgwdlkaragkKKVVLELGGNAAVIVDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 270 SANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVN 349
Cdd:cd07147 241 DADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKA-LKTGDPKDDATDVGPMISESEAERVEGWVN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 350 DAVSKGATVVTGGKRHQlgkNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGL-AGYFySQDPA 428
Cdd:cd07147 320 EAVDAGAKLLTGGKRDG---ALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLqAGVF-TRDLE 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1589401592 429 QIWRVAEQLEVGMVGVNEglISSVEC---PFGGVKQSGLGREGSKYGIDEYLELK 480
Cdd:cd07147 396 KALRAWDELEVGGVVIND--VPTFRVdhmPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
64-482 |
1.82e-93 |
|
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: 291.40 E-value: 1.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR--WREVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07139 2 FIGGRWVAPSgsETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 140 RIITAESGKPLK-EAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAA 218
Cdd:cd07139 82 RLWTAENGMPISwSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 219 LAAGCTVVVKPAEDTPFSALALAEI-----------------------LLHH---------------------AANSVKR 254
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAaeeaglppgvvnvvpadrevgeyLVRHpgvdkvsftgstaagrriaavCGERLAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 255 VSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGP 334
Cdd:cd07139 242 VTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAA-LKVGDPLDPATQIGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 335 LINEKAVEKVEKQVNDAVSKGATVVTGGKR--HQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIAN 412
Cdd:cd07139 321 LASARQRERVEGYIAKGRAEGARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIAN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 413 AADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNeGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07139 401 DSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
80-483 |
1.03e-92 |
|
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: 288.95 E-value: 1.03e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 80 DPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEA-HGEIL 158
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 159 YSAFFLEWFSEEARRVYGDIIhtPAKDRrAL--VLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS 236
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVI--PVRGP-FLnyTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 237 ALALAEI---------------------------------------------LLHHAANSVKRVSMELGGLAPFIVFDSA 271
Cdd:cd07115 160 ALRIAELmaeagfpagvlnvvtgfgevagaalvehpdvdkitftgstavgrkIMQGAAGNLKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 272 NVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAeAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDA 351
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFT-SLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 352 VSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIW 431
Cdd:cd07115 319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1589401592 432 RVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 483
Cdd:cd07115 399 RVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVW 450
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
78-482 |
2.98e-92 |
|
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: 287.71 E-value: 2.98e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 158 LYSAFFLEWFSEEARRV---YGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTP 234
Cdd:cd07110 81 DDVAGCFEYYADLAEQLdakAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 235 FSALALAEI------------------------LLHH---------------------AANSVKRVSMELGGLAPFIVFD 269
Cdd:cd07110 161 LTELELAEIaaeaglppgvlnvvtgtgdeagapLAAHpgidkisftgstatgsqvmqaAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 270 SANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFEEGTTQGPLINEKAVEKVEKQVN 349
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAE-AIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 350 DAVSKGATVVTGGKRHQ-LGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDP 427
Cdd:cd07110 320 RGKEEGARLLCGGRRPAhLEKGYFiAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1589401592 428 AQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07110 400 ERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
80-482 |
3.74e-92 |
|
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: 287.58 E-value: 3.74e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 80 DPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILY 159
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 160 SAFFLEWFSEEARRVYGD---IIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS 236
Cdd:cd07099 82 ALEAIDWAARNAPRVLAPrkvPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 237 ALALAEILlhHAAN-------------------------------SV---KRV-----------SMELGGLAPFIVFDSA 271
Cdd:cd07099 162 GELLAEAW--AAAGppqgvlqvvtgdgatgaalidagvdkvaftgSVatgRKVmaaaaerlipvVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 272 NVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDA 351
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARA-LRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 352 VSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIW 431
Cdd:cd07099 319 VAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAE 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1589401592 432 RVAEQLEVGMVGVNEGLISSV--ECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07099 399 AIARRLEAGAVSINDVLLTAGipALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
124-482 |
2.39e-91 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 283.94 E-value: 2.39e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 124 LRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITP 203
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 204 WNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEIL--------------------------------------- 244
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVdeiglpkgvfnlvlgrgetvgqelagnpkvamvsmtgsv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 245 ------LHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKk 318
Cdd:PRK10090 161 sagekiMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 319 NLRVGNGFEEGTTQ-GPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAP 397
Cdd:PRK10090 240 AVQFGNPAERNDIAmGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 398 VIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYL 477
Cdd:PRK10090 320 VVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYL 399
|
....*
gi 1589401592 478 ELKYV 482
Cdd:PRK10090 400 QTQVV 404
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
78-482 |
3.48e-91 |
|
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: 284.90 E-value: 3.48e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 78 VQDPASGAALGMVADCGVREARAAVRAAYEAF-CRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGE 156
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFeSGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 157 ILYSAFFLEWFSEEARRVYGDIIhTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS 236
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETI-PLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 237 ALALAEIL---------------------------------------------LHHAANSVKRVSMELGGLAPFIVFDSA 271
Cdd:cd07109 160 ALRLAELAeeaglpagalnvvtglgaeagaalvahpgvdhisftgsvetgiavMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 272 NVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGfEEGTTQGPLINEKAVEKVEKQVNDA 351
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRA-LRVGPG-LEDPDLGPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 352 VSKGATVVTGGKRHQL---GKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPA 428
Cdd:cd07109 318 RARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1589401592 429 QIWRVAEQLEVGMVGVNE-GLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07109 398 RALRVARRLRAGQVFVNNyGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
64-482 |
1.70e-90 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 284.11 E-value: 1.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLP-AAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARII 142
Cdd:PRK13473 6 LINGELVAgEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 143 TAESGKPLKEA-HGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAA 221
Cdd:PRK13473 86 SLNCGKPLHLAlNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 222 GCTVVVKPAEDTPFSALALAEIL--------------------------------------------LHHAANSVKRVSM 257
Cdd:PRK13473 166 GNTVVLKPSEITPLTALKLAELAadilppgvlnvvtgrgatvgdalvghpkvrmvsltgsiatgkhvLSAAADSVKRTHL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 258 ELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLIN 337
Cdd:PRK13473 246 ELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVAT-LKVGDPDDEDTELGPLIS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 338 EKAVEKVEKQVNDAVSKG-ATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADV 416
Cdd:PRK13473 325 AAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDY 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1589401592 417 GLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:PRK13473 405 GLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
78-483 |
3.03e-90 |
|
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: 282.66 E-value: 3.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 158 LYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA 237
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPG-GSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 238 LALAEI-----------------------LLHH---------------------AANSVKRVSMELGGLAPFIVFDSANV 273
Cdd:cd07090 160 LLLAEIlteaglpdgvfnvvqgggetgqlLCEHpdvakvsftgsvptgkkvmsaAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 274 DQAVAGAMASKFRNTGQtcVCSN--QFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDA 351
Cdd:cd07090 240 ENAVNGAMMANFLSQGQ--VCSNgtRVFVQRSIKDEFTERLVERTKK-IRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 352 VSKGATVVTGGKRHQL-----GKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQD 426
Cdd:cd07090 317 KQEGAKVLCGGERVVPedgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1589401592 427 PAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 483
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
78-482 |
3.22e-90 |
|
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: 282.29 E-value: 3.22e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKE-AHGE 156
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 157 ILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS 236
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 237 ALALAEIL--------------------------------------------LHHAANSVKRVSMELGGLAPFIVFDSAN 272
Cdd:cd07092 161 TLLLAELAaevlppgvvnvvcgggasagdalvahprvrmvsltgsvrtgkkvARAAADTLKRVHLELGGKAPVIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 273 VDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVnDAV 352
Cdd:cd07092 241 LDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSA-IRVGDPDDEDTEMGPLNSAAQRERVAGFV-ERA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 353 SKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWR 432
Cdd:cd07092 319 PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1589401592 433 VAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07092 399 LSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
61-482 |
2.15e-88 |
|
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: 278.61 E-value: 2.15e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 61 TDSFVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR--WREVSAKERSSLLRKWYNLMIQNKD 136
Cdd:cd07142 4 TKLFINGQFVDAASgkTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 137 DLARIITAESGKPLKEA-HGEILYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKV 215
Cdd:cd07142 84 ELAALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADG-PHHVYTLHEPIGVVGQIIPWNFPLLMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 216 GAALAAGCTVVVKPAEDTPFSAL----------------------------ALAE-----------------ILLHHAAN 250
Cdd:cd07142 163 GPALACGNTIVLKPAEQTPLSALlaaklaaeaglpdgvlnivtgfgptagaAIAShmdvdkvaftgstevgkIIMQLAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 251 S-VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFV-KAFAEAMKKNlrVGNGFEE 328
Cdd:cd07142 243 SnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVeKAKARALKRV--VGDPFRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 329 GTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAI 408
Cdd:cd07142 321 GVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1589401592 409 AIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
64-484 |
1.13e-86 |
|
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: 274.41 E-value: 1.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAF-CRW-REVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07143 10 FINGEFVDSVhgGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFeTDWgLKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 140 RIITAESGKP-LKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKdRRALVLKQPIGVAAVITPWNFPSAMITRKVGAA 218
Cdd:cd07143 90 SIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIK-KLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 219 LAAGCTVVVKPAEDTPFSALALAEIL---------------------------------------------LHHAANS-V 252
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIpeagfppgvinvvsgygrtcgnaisshmdidkvaftgstlvgrkvMEAAAKSnL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 253 KRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQ 332
Cdd:cd07143 249 KKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKK-LKVGDPFAEDTFQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 333 GPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIAN 412
Cdd:cd07143 328 GPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRAN 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1589401592 413 AADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCY 484
Cdd:cd07143 408 DSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
80-483 |
1.26e-84 |
|
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: 268.06 E-value: 1.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 80 DPASGAALGMVADCGVREARAAVRAAYEAFCR--WReVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 158 LYSAFFLEWFSEEARRVYGDIIhTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA 237
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMI-EPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 238 LALAEIL----------------------------------------------LHHAANSVKRVSMELGGLAPFIVFDSA 271
Cdd:cd07120 161 AAIIRILaeipslpagvvnlftesgsegaahlvaspdvdvisftgstatgraiMAAAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 272 NVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDA 351
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLA-AVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 352 VSKGATVVTGGKRHQLGKN---FFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPA 428
Cdd:cd07120 320 IAAGAEVVLRGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1589401592 429 QIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 483
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
112-482 |
1.92e-84 |
|
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: 268.02 E-value: 1.92e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEIlysAFFLEWFSEEAR---RVYGDII--HTPAKDR 186
Cdd:cd07151 48 WAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEW---GAAMAITREAATfplRMEGRILpsDVPGKEN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 187 RalVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA-LALAEILLH------------------- 246
Cdd:cd07151 125 R--VYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGgLLLAKIFEEaglpkgvlnvvvgagseig 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 247 -----H---------------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLV 300
Cdd:cd07151 203 dafveHpvprlisftgstpvgrhigelAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 301 QRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHqlgKNFFEPTLLCNV 380
Cdd:cd07151 283 HEDVYDEFVEKFVERVKA-LPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 381 TQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLIS-SVECPFGGV 459
Cdd:cd07151 359 TNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGE 438
|
410 420
....*....|....*....|...
gi 1589401592 460 KQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07151 439 KNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
63-485 |
2.72e-84 |
|
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: 267.89 E-value: 2.72e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 63 SFVGGRWLPAAA-TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARI 141
Cdd:cd07086 1 GVIGGEWVGSGGeTFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 142 ITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAA 221
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 222 GCTVVVKPAEDTPFSALALAEILLH---------HAANSV---------------------------------------K 253
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEvleknglppGVVNLVtgggdggellvhdprvplvsftgstevgrrvgetvarrfG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 254 RVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQG 333
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQ-VRIGDPLDEGTLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 334 PLINEKAVEKVEKQVNDAVSKGATVVTGGKR--HQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIA 411
Cdd:cd07086 320 PLINQAAVEKYLNAIEIAKSQGGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAIN 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1589401592 412 NAADVGLAGYFYSQDPAQI--WRVAEQLEVGMVGVNEGLI-SSVECPFGGVKQSGLGREGSKYGIDEYLELK--YVCYG 485
Cdd:cd07086 400 NDVPQGLSSSIFTEDLREAfrWLGPKGSDCGIVNVNIPTSgAEIGGAFGGEKETGGGRESGSDAWKQYMRRStcTINYS 478
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
116-480 |
6.02e-84 |
|
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: 266.15 E-value: 6.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 116 SAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDII----HTPAKDRRALVL 191
Cdd:cd07146 38 TRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRDDGESFscdlTANGKARKIFTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEI------------------------LLHH 247
Cdd:cd07146 118 REPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLlyeaglppdmlsvvtgepgeigdeLITH 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 248 -------------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAF 308
Cdd:cd07146 198 pdvdlvtftggvavgkaiaATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEF 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 309 VKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHqlgKNFFEPTLLCNVTQDMLCTH 388
Cdd:cd07146 278 VDLLVEKSAA-LVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQRQ---GALYAPTVLDHVPPDAELVT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 389 EETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVE-CPFGGVKQSGLG-R 466
Cdd:cd07146 354 EETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGgK 433
|
410
....*....|....
gi 1589401592 467 EGSKYGIDEYLELK 480
Cdd:cd07146 434 EGVREAMKEMTNVK 447
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
80-478 |
3.83e-83 |
|
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: 264.17 E-value: 3.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 80 DPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILY 159
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 160 SAFFLEWFSEEARRVYgdiihTPAKDRRAL-------VLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAED 232
Cdd:cd07101 82 VAIVARYYARRAERLL-----KPRRRRGAIpvltrttVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 233 TPFSALALAEILL-------------------------------------------HHAANSVKRVSMELGGLAPFIVFD 269
Cdd:cd07101 157 TALTALWAVELLIeaglprdlwqvvtgpgsevggaivdnadyvmftgstatgrvvaERAGRRLIGCSLELGGKNPMIVLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 270 SANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFEEGTTQGPLINEKAVEKVEKQVN 349
Cdd:cd07101 237 DADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTR-ALRLGAALDYGPDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 350 DAVSKGATVVTGGK-RHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPA 428
Cdd:cd07101 316 DAVAKGATVLAGGRaRPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1589401592 429 QIWRVAEQLEVGMVGVNEGLIS---SVECPFGGVKQSGLGREGSKYGIDEYLE 478
Cdd:cd07101 396 RGRRIAARLRAGTVNVNEGYAAawaSIDAPMGGMKDSGLGRRHGAEGLLKYTE 448
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
64-482 |
4.26e-83 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 265.83 E-value: 4.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPA--AATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR-----WREVSAKERSSLLRKWYNLMIQNKD 136
Cdd:PLN02467 11 FIGGEWREPvlGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 137 DLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYG---DIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITR 213
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkqkAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 214 KVGAALAAGCTVVVKPAEDTPFSALALAEI------------------------LLHH---------------------A 248
Cdd:PLN02467 171 KVAPALAAGCTAVLKPSELASVTCLELADIcrevglppgvlnvvtglgteagapLASHpgvdkiaftgstatgrkimtaA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 249 ANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFEE 328
Cdd:PLN02467 251 AQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAK-NIKISDPLEE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 329 GTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKR-HQLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEE 406
Cdd:PLN02467 330 GCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRpEHLKKGFFiEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDE 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1589401592 407 AIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:PLN02467 410 AIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
64-480 |
5.31e-83 |
|
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: 264.70 E-value: 5.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARI 141
Cdd:cd07117 4 FINGEWVKGSsgETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 142 ITAESGKPLKEAHG-EILYSAFFLEWF-----SEEARRVYGDiihtpaKDRRALVLKQPIGVAAVITPWNFPSAMITRKV 215
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFagvirAEEGSANMID------EDTLSIVLREPIGVVGQIIPWNFPFLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 216 GAALAAGCTVVVKPAEDTPFSALALAEI-----------------------LLHH---------------------AANS 251
Cdd:cd07117 158 APALAAGNTVVIKPSSTTSLSLLELAKIiqdvlpkgvvnivtgkgsksgeyLLNHpgldklaftgstevgrdvaiaAAKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 252 VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFEEGTT 331
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFE-NVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 332 QGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGK----NFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEA 407
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGldkgFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589401592 408 IAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 480
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMK 469
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
61-482 |
1.70e-82 |
|
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: 263.44 E-value: 1.70e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 61 TDSFVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR---WREVSAKERSSLLRKWYNLMIQNK 135
Cdd:cd07141 7 TKIFINNEWHDSVSgkTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 136 DDLARIITAESGKPLKEAH-GEILYSAFFLEWFSEEARRVYGDIIhtPAK-DRRALVLKQPIGVAAVITPWNFPSAMITR 213
Cdd:cd07141 87 AYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTI--PMDgDFFTYTRHEPVGVCGQIIPWNFPLLMAAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 214 KVGAALAAGCTVVVKPAEDTPFSALALAEI------------------------LLHH---------------------- 247
Cdd:cd07141 165 KLAPALACGNTVVLKPAEQTPLTALYLASLikeagfppgvvnvvpgygptagaaISSHpdidkvaftgstevgkliqqaa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 248 AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNlRVGNGFE 327
Cdd:cd07141 245 GKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKR-VVGNPFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 328 EGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEA 407
Cdd:cd07141 324 PKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEV 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1589401592 408 IAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07141 404 IERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
72-478 |
2.55e-82 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 264.05 E-value: 2.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 72 AAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLK 151
Cdd:PRK09407 30 AGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 152 EAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKD--RRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKP 229
Cdd:PRK09407 110 HAFEEVLDVALTARYYARRAPKLLAPRRRAGALPvlTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 230 AEDTPFSALALAEILL-------------------------------------------HHAANSVKRVSMELGGLAPFI 266
Cdd:PRK09407 190 DSQTPLTALAAVELLYeaglprdlwqvvtgpgpvvgtalvdnadylmftgstatgrvlaEQAGRRLIGFSLELGGKNPMI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 267 VFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFEEGTTQGPLINEKAVEKVEK 346
Cdd:PRK09407 270 VLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVR-AMRLGAGYDYSADMGSLISEAQLETVSA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 347 QVNDAVSKGATVVTGGK-RHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQ 425
Cdd:PRK09407 349 HVDDAVAKGATVLAGGKaRPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTG 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1589401592 426 DPAQIWRVAEQLEVGMVGVNEGLIS---SVECPFGGVKQSGLGREGSKYGIDEYLE 478
Cdd:PRK09407 429 DTARGRAIAARIRAGTVNVNEGYAAawgSVDAPMGGMKDSGLGRRHGAEGLLKYTE 484
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
61-482 |
1.30e-81 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 261.68 E-value: 1.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 61 TDSFVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAF--CRWREVSAKERSSLLRKWYNLMIQNKD 136
Cdd:PLN02766 21 TKLFINGEFVDAASgkTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFdhGPWPRMSGFERGRIMMKFADLIEEHIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 137 DLARIITAESGK-PLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTpAKDRRALVLKQPIGVAAVITPWNFPSAMITRKV 215
Cdd:PLN02766 101 ELAALDTIDAGKlFALGKAVDIPAAAGLLRYYAGAADKIHGETLKM-SRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 216 GAALAAGCTVVVKPAEDTPFSAL----------------------------ALAE------------------ILLHHAA 249
Cdd:PLN02766 180 APALAAGCTMVVKPAEQTPLSALfyahlaklagvpdgvinvvtgfgptagaAIAShmdvdkvsftgstevgrkIMQAAAT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 250 NSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFEEG 329
Cdd:PLN02766 260 SNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAK-DWVVGDPFDPR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 330 TTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKrhQLGKN--FFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEA 407
Cdd:PLN02766 339 ARQGPQVDKQQFEKILSYIEHGKREGATLLTGGK--PCGDKgyYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1589401592 408 IAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:PLN02766 417 IKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
109-482 |
1.37e-80 |
|
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: 256.74 E-value: 1.37e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 109 FCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRA 188
Cdd:cd07105 13 FPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIPSDKPGTLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 189 LVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEIL------------LHH--------- 247
Cdd:cd07105 93 MVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFheaglpkgvlnvVTHspedapevv 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 248 ---------------------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLV 300
Cdd:cd07105 173 ealiahpavrkvnftgstrvgriiaetAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 301 QRGIHDAFVKAFAEAMKKnLRVGngfeeGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGK-RHQLGKNFFEPTLLCN 379
Cdd:cd07105 253 HESIADEFVEKLKAAAEK-LFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLaDESPSGTSMPPTILDN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 380 VTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEgliSSVE----CP 455
Cdd:cd07105 327 VTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHING---MTVHdeptLP 403
|
410 420
....*....|....*....|....*..
gi 1589401592 456 FGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07105 404 HGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
62-484 |
1.83e-80 |
|
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: 258.04 E-value: 1.83e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 62 DSFVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07559 2 DNFINGEWVAPSkgEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 140 RIITAESGKPLKEAHG-EILYSAFFLEWFSEEARRVYGDIiHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAA 218
Cdd:cd07559 82 VAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSL-SEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 219 LAAGCTVVVKPAEDTPFSALALAEI-----------------------LLHH---------------------AANSVKR 254
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELigdllpkgvvnvvtgfgseagkpLASHpriaklaftgsttvgrlimqyAAENLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 255 VSMELGGLAPFIVFDSA-----NVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKkNLRVGNGFEEG 329
Cdd:cd07559 241 VTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFE-AIKVGNPLDPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 330 TTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKN----FFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEE 405
Cdd:cd07559 320 TMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLdkgyFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 406 EAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK--YVC 483
Cdd:cd07559 400 EAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKniLVS 479
|
.
gi 1589401592 484 Y 484
Cdd:cd07559 480 Y 480
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
80-485 |
1.49e-77 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 249.65 E-value: 1.49e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 80 DPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILY 159
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 160 SAFFLEWFSEEARRVYGDIIHTPAK--DRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA 237
Cdd:PRK09406 87 CAKGFRYYAEHAEALLADEPADAAAvgASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 238 LALAEILLHH--------------------------------------------AANSVKRVSMELGGLAPFIVFDSANV 273
Cdd:PRK09406 167 LYLADLFRRAgfpdgcfqtllvgsgaveailrdprvaaatltgsepagravaaiAGDEIKKTVLELGGSDPFIVMPSADL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 274 DQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVS 353
Cdd:PRK09406 247 DRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAA-LRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 354 KGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRV 433
Cdd:PRK09406 326 AGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERF 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1589401592 434 AEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYG 485
Cdd:PRK09406 406 IDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
112-473 |
2.70e-77 |
|
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: 249.41 E-value: 2.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGD----IIHTPAKDRR 187
Cdd:cd07082 55 WPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDslpgDWFPGTKGKI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 188 ALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEiLLHHAA------------------ 249
Cdd:cd07082 135 AQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAE-AFHDAGfpkgvvnvvtgrgreigd 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 250 --------------------------NSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRG 303
Cdd:cd07082 214 plvthgridvisftgstevgnrlkkqHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHES 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 304 IHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRhqLGKNFFEPTLLCNVTQD 383
Cdd:cd07082 294 VADELVELLKEEVAK-LKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 384 MLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGlissveC-------PF 456
Cdd:cd07082 371 MRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSK------CqrgpdhfPF 444
|
410
....*....|....*..
gi 1589401592 457 GGVKQSGLGREGSKYGI 473
Cdd:cd07082 445 LGRKDSGIGTQGIGDAL 461
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
64-483 |
1.01e-76 |
|
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: 248.13 E-value: 1.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAAAT--FPVQDPASGAALGMVADCGVREARAAVRAAYEAF-CRWREVSAKERSSLLRKWYNLMIQNKDDLAR 140
Cdd:cd07113 3 FIDGRPVAGQSEkrLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 141 IITAESGKPLKEAHG-EILYSAFFLEWFSEEARRVYGDIIH----TPAKDR-RALVLKQPIGVAAVITPWNFPSAMITRK 214
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLApsipSMQGERyTAFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 215 VGAALAAGCTVVVKPAEDTPFSALALAEI-----------------------LLHH---------------------AAN 250
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELakeagipdgvlnvvngkgavgaqLISHpdvakvsftgsvatgkkigrqAAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 251 SVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGT 330
Cdd:cd07113 243 DLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSS-FQVGSPMDESV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 331 TQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQlGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIA 409
Cdd:cd07113 322 MFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA-GEGYFvQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQ 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1589401592 410 IANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 483
Cdd:cd07113 401 LINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
61-482 |
1.04e-76 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 250.11 E-value: 1.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 61 TDSFVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR--WREVSAKERSSLLRKWYNLMIQNKD 136
Cdd:PLN02466 58 TQLLINGQFVDAASgkTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 137 DLARIITAESGKPLKE-AHGEILYSAFFLEWFSEEARRVYGDIIhtPAKDRRAL-VLKQPIGVAAVITPWNFPSAMITRK 214
Cdd:PLN02466 138 ELAALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHGLTV--PADGPHHVqTLHEPIGVAGQIIPWNFPLLMFAWK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 215 VGAALAAGCTVVVKPAEDTPFSAL----------------------------ALAE-----------------ILLHHAA 249
Cdd:PLN02466 216 VGPALACGNTIVLKTAEQTPLSALyaakllheaglppgvlnvvsgfgptagaALAShmdvdklaftgstdtgkIVLELAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 250 NS-VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFV-KAFAEAMKKNlrVGNGFE 327
Cdd:PLN02466 296 KSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVeKAKARALKRV--VGDPFK 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 328 EGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEA 407
Cdd:PLN02466 374 KGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEV 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1589401592 408 IAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:PLN02466 454 IRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
78-482 |
1.15e-76 |
|
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: 247.66 E-value: 1.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLK-EAHGE 156
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 157 ILYSAFFLEWFSEEARRVYGDIIhTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFS 236
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETL-PFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 237 ALALAEI-----------------------LLHH---------------------AANSVKRVSMELGGLAPFIVFDSAN 272
Cdd:cd07108 160 VLLLAEIlaqvlpagvlnvitgygeecgaaLVDHpdvdkvtftgstevgkiiyraAADRLIPVSLELGGKSPMIVFPDAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 273 VDQAVAGAMAS-KFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDA 351
Cdd:cd07108 240 LDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSK-LKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 352 VS-KGATVVTGG---KRHQLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQD 426
Cdd:cd07108 319 LStSGATVLRGGplpGEGPLADGFFvQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1589401592 427 PAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYG-IDEYLELKYV 482
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
64-482 |
2.46e-76 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 247.49 E-value: 2.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARI 141
Cdd:PRK13252 10 YIDGAYVEATsgETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 142 ITAESGKPLKEAH-GEILYSAFFLEWFSEEARRVYGDIIHTPAKD----RRalvlkQPIGVAAVITPWNFPSAMITRKVG 216
Cdd:PRK13252 90 ETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSfvytRR-----EPLGVCAGIGAWNYPIQIACWKSA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 217 AALAAGCTVVVKPAEDTPFSALALAEI-----------------------LLHH---------------------AANSV 252
Cdd:PRK13252 165 PALAAGNAMIFKPSEVTPLTALKLAEIyteaglpdgvfnvvqgdgrvgawLTEHpdiakvsftggvptgkkvmaaAAASL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 253 KRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQtcVCSN--QFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGT 330
Cdd:PRK13252 245 KEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQ--VCTNgtRVFVQKSIKAAFEARLLERVER-IRIGDPMDPAT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 331 TQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQ---LGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEE 406
Cdd:PRK13252 322 NFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTeggFANGAFvAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1589401592 407 AIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:PRK13252 402 VIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
61-482 |
4.20e-73 |
|
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: 238.93 E-value: 4.20e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 61 TDSFVGGRWLPAAA--TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR--WREVSAKERSSLLRKWYNLMIQNKD 136
Cdd:cd07140 6 HQLFINGEFVDAEGgkTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 137 DLARIITAESGK----PLKEAHG-EILYSAFFLEWfseeARRVYGDIIH-TPAKDRRALVL--KQPIGVAAVITPWNFPS 208
Cdd:cd07140 86 ELATIESLDSGAvytlALKTHVGmSIQTFRYFAGW----CDKIQGKTIPiNQARPNRNLTLtkREPIGVCGIVIPWNYPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 209 AMITRKVGAALAAGCTVVVKPAEDTPFSALALAEI------------------------LLHH----------------- 247
Cdd:cd07140 162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtvkagfpkgvinilpgsgslvgqrLSDHpdvrklgftgstpigkh 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 248 -----AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRV 322
Cdd:cd07140 242 imkscAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKK-MKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 323 GNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFD 402
Cdd:cd07140 321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 403 TEEEAIAIANAADV--GLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 480
Cdd:cd07140 401 DGDVDGVLQRANDTeyGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480
|
..
gi 1589401592 481 YV 482
Cdd:cd07140 481 TV 482
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
80-473 |
1.98e-72 |
|
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: 236.81 E-value: 1.98e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 80 DPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAH-GEIL 158
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 159 YSAFFLEW--------FSEEARRVYGDIIHtpakdRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPA 230
Cdd:cd07098 82 VTCEKIRWtlkhgekaLRPESRPGGLLMFY-----KRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 231 EDTPFSALALAEIL------------------------------------------------LHHAANSVKRVSMELGGL 262
Cdd:cd07098 157 EQVAWSSGFFLSIIreclaacghdpdlvqlvtclpetaealtshpvidhitfigsppvgkkvMAAAAESLTPVVLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 263 APFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVE 342
Cdd:cd07098 237 DPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQA-LRQGPPLDGDVDVGAMISPARFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 343 KVEKQVNDAVSKGATVVTGGKRHQLGK----NFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGL 418
Cdd:cd07098 316 RLEELVADAVEKGARLLAGGKRYPHPEypqgHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1589401592 419 AGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVEC--PFGGVKQSGLGREGSKYGI 473
Cdd:cd07098 396 GASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGRFAGEEGL 452
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
78-482 |
6.10e-72 |
|
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: 234.96 E-value: 6.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 78 VQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEI 157
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 158 LYSAFFLEWFSEEARRVYGDIIHTPAkdrRAL--VLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPF 235
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGG---RNLhyTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 236 SALALAEILLHH--------------------------------------------AANSVKRVSMELGGLAPFIVFDSA 271
Cdd:cd07107 158 SALRLAELAREVlppgvfnilpgdgatagaalvrhpdvkrialigsvptgraimraAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 272 NVDQAVAGAMAS-KFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVND 350
Cdd:cd07107 238 DPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAA-IKVGDPTDPATTMGPLVSRQQYDRVMHYIDS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 351 AVSKGATVVTGGKR---HQLGKNFF-EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQD 426
Cdd:cd07107 317 AKREGARLVTGGGRpegPALEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1589401592 427 PAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:cd07107 397 ISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
112-482 |
6.12e-72 |
|
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: 234.88 E-value: 6.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVL 191
Cdd:cd07152 29 WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQGEILPSAP-GRLSLAR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSA-LALAEI---------LLH--------------- 246
Cdd:cd07152 108 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLfeeaglpagVLHvlpggadagealved 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 247 --------------------HAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHD 306
Cdd:cd07152 188 pnvamisftgstavgrkvgeAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVAD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 307 AFVKAFAeAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLgknFFEPTLLCNVTQDMLC 386
Cdd:cd07152 268 AYTAKLA-AKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTYDGL---FYRPTVLSGVKPGMPA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 387 THEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSvEC--PFGGVKQSGL 464
Cdd:cd07152 344 FDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVND-EPhnPFGGMGASGN 422
|
410
....*....|....*....
gi 1589401592 465 G-REGSKYGIDEYLELKYV 482
Cdd:cd07152 423 GsRFGGPANWEEFTQWQWV 441
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
112-480 |
2.22e-69 |
|
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: 228.28 E-value: 2.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVL 191
Cdd:cd07102 34 WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEALADIRVPEKDGFERYIR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEIL--------------------------- 244
Cdd:cd07102 114 REPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFaeaglpegvfqvlhlshetsaaliadp 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 245 -LHH----------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCvCS-NQFLVQRGIHD 306
Cdd:cd07102 194 rIDHvsftgsvaggraiqraAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSC-CSiERIYVHESIYD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 307 AFVKAFAEAMKkNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKR---HQLGKNFFEPTLLCNVTQD 383
Cdd:cd07102 273 AFVEAFVAVVK-GYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALfpeDKAGGAYLAPTVLTNVDHS 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 384 MLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSG 463
Cdd:cd07102 352 MRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSG 431
|
410
....*....|....*..
gi 1589401592 464 LGREGSKYGIDEYLELK 480
Cdd:cd07102 432 RGVTLSRLGYDQLTRPK 448
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
64-479 |
1.81e-68 |
|
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: 227.49 E-value: 1.81e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAAATFPVQDPA-SGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARII 142
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 143 TAESGKPLKEAHGEILYSAFFLEWFSEEARRvYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAG 222
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLR-LRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 223 CTVVVKPAEDTPFSALALAEIL--------------------------------------------LHHAANS------- 251
Cdd:cd07124 195 NTVVLKPAEDTPVIAAKLVEILeeaglppgvvnflpgpgeevgdylvehpdvrfiaftgsrevglrIYERAAKvqpgqkw 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 252 VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTT 331
Cdd:cd07124 275 LKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKA-LKVGDPEDPEVY 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 332 QGPLINEKAVEKVEKQVNDAVSKGaTVVTGGKR--HQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIA 409
Cdd:cd07124 354 MGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVleLAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALE 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589401592 410 IANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNE---GLISSVEcPFGGVKQSGLgreGSKYGIDEYLEL 479
Cdd:cd07124 433 IANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRkitGALVGRQ-PFGGFKMSGT---GSKAGGPDYLLQ 501
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
64-482 |
3.92e-67 |
|
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: 223.10 E-value: 3.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAAA-TFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR--W-REVSAKERSslLRKWYNLMIQNKDDLA 139
Cdd:TIGR04284 4 LIDGKLVAGSAgTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDEtdWsRDTALRVRC--LRQLRDALRAHVEELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 140 RIITAESGKPLKEAHGEILYSAFF-LEWFSEEA-----RRVYGDIIHTPAKDRRaLVLKQPIGVAAVITPWNFPSAMITR 213
Cdd:TIGR04284 82 ELTIAEVGAPRMLTAGAQLEGPVDdLGFAADLAesyawTTDLGVASPMGIPTRR-TLRREAVGVVGAITPWNFPHQINLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 214 KVGAALAAGCTVVVKPAEDTPFSALALAEILLHH---------------------------------------------- 247
Cdd:TIGR04284 161 KLGPALAAGNTVVLKPAPDTPWCAAVLGELIAEHtdfppgvvnivtssdhrlgallakdprvdmvsftgstatgravmad 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 248 AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMkKNLRVGNGFE 327
Cdd:TIGR04284 241 AAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATM-GSIKPGDPAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 328 EGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKR--HQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEE 405
Cdd:TIGR04284 320 PGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGRpaDRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDD 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589401592 406 EAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:TIGR04284 400 DAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLI 476
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
36-478 |
1.45e-64 |
|
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: 216.49 E-value: 1.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 36 GPAPGPAqlrcyAGRLAGLSAALLRTDSFVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWR 113
Cdd:cd07111 2 GPAPESA-----ACALAWLDAHDRSFGHFINGKWVKPEnrKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 114 EVSAKERSSLLrkwYNL--MIQNKDDL-ARIITAESGKPLKEAH-GEILYSAFFLEWFSEEARrvygdiihtpaKDRRAL 189
Cdd:cd07111 77 ALPGHVRARHL---YRIarHIQKHQRLfAVLESLDNGKPIRESRdCDIPLVARHFYHHAGWAQ-----------LLDTEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 190 VLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEI-----------------------LLH 246
Cdd:cd07111 143 AGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEIcaeaglppgvlnivtgngsfgsaLAN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 247 HA---------------------ANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIH 305
Cdd:cd07111 223 HPgvdkvaftgstevgralrratAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 306 DAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDML 385
Cdd:cd07111 303 EELIRKLKERMSH-LRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 386 CTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLG 465
Cdd:cd07111 382 IAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFG 461
|
490
....*....|...
gi 1589401592 466 REGSKYGIDEYLE 478
Cdd:cd07111 462 REGGKEGLYEYLR 474
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
59-480 |
5.50e-63 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 212.83 E-value: 5.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 59 LRTDSFVGGRWLPAA--ATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCR--WREVSAKERSSLLRKWYNLMIQN 134
Cdd:PRK09847 18 IENRLFINGEYTAAAenETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 135 KDDLARIITAESGKPLKEA-HGEILYSAFFLEWFSEEARRVYGDIIHTpAKDRRALVLKQPIGVAAVITPWNFPSAMITR 213
Cdd:PRK09847 98 AEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATT-SSHELAMIVREPVGVIAAIVPWNFPLLLTCW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 214 KVGAALAAGCTVVVKPAEDTPFSALALAEI---------------------------------------------LLHHA 248
Cdd:PRK09847 177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLakeaglpdgvlnvvtgfgheagqalsrhndidaiaftgstrtgkqLLKDA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 249 ANS-VKRVSMELGGLAPFIVF-DSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFaEAMKKNLRVGNGF 326
Cdd:PRK09847 257 GDSnMKRVWLEAGGKSANIVFaDCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALL-KQQAQNWQPGHPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 327 EEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGgkRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEE 406
Cdd:PRK09847 336 DPATTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQ 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1589401592 407 AIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 480
Cdd:PRK09847 414 ALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
61-474 |
6.07e-62 |
|
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: 209.30 E-value: 6.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 61 TDSFVGGRWLPAAAT--FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDL 138
Cdd:cd07085 1 LKLFINGEWVESKTTewLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 139 ARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPsAMITR-KVGA 217
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFP-AMIPLwMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 218 ALAAGCTVVVKPAEDTPFSALALAEI-----------------------LLHH---------------------AANSVK 253
Cdd:cd07085 160 AIACGNTFVLKPSERVPGAAMRLAELlqeaglpdgvlnvvhggkeavnaLLDHpdikavsfvgstpvgeyiyerAAANGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 254 RVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCV-CSNQFLVQrGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQ 332
Cdd:cd07085 240 RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMaLSVAVAVG-DEADEWIPKLVERAKK-LKVGAGDDPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 333 GPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGK----NFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAI 408
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGyengNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589401592 409 AIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVEC-PFGGVKQSGLGrEGSKYGID 474
Cdd:cd07085 398 AIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFfSFGGWKGSFFG-DLHFYGKD 463
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
80-482 |
6.80e-61 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 206.25 E-value: 6.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 80 DPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILY 159
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 160 SAFFLEWFSEearrvygdiiHTPA---------KDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPA 230
Cdd:PRK13968 93 SANLCDWYAE----------HGPAmlkaeptlvENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 231 EDTPFSALALAEILLH--------------------------------------------HAANSVKRVSMELGGLAPFI 266
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDagipqgvygwlnadndgvsqmindsriaavtvtgsvragaaigaQAGAALKKCVLELGGSDPFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 267 VFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEK 346
Cdd:PRK13968 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAA-LKMGDPRDEENALGPMARFDLRDELHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 347 QVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQD 426
Cdd:PRK13968 322 QVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTD 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1589401592 427 PAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 482
Cdd:PRK13968 402 ETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
111-476 |
1.55e-59 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 201.69 E-value: 1.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 111 RWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAH-GEILysafflewfseearRVYGDIIHT-------- 181
Cdd:cd07134 13 ALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlTEIL--------------PVLSEINHAikhlkkwm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 182 -PAKDR--------RALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEI--------- 243
Cdd:cd07134 79 kPKRVRtplllfgtKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIireafdede 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 244 -------------LLH----H----------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQ 290
Cdd:cd07134 159 vavfegdaevaqaLLElpfdHifftgspavgkivmaaAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 291 TCVCSNQFLVQRGIHDAFVKAFAEAMKKNLrvgnGFEEGTTQGP----LINEKAVEKVEKQVNDAVSKGATVVTGGKrHQ 366
Cdd:cd07134 239 TCIAPDYVFVHESVKDAFVEHLKAEIEKFY----GKDAARKASPdlarIVNDRHFDRLKGLLDDAVAKGAKVEFGGQ-FD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 367 LGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNE 446
Cdd:cd07134 314 AAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVND 393
|
410 420 430
....*....|....*....|....*....|..
gi 1589401592 447 GLISSVE--CPFGGVKQSGLGREGSKYGIDEY 476
Cdd:cd07134 394 VVLHFLNpnLPFGGVNNSGIGSYHGVYGFKAF 425
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
111-475 |
5.31e-58 |
|
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: 198.41 E-value: 5.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 111 RWreVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDII---HTPAKD-R 186
Cdd:cd07148 39 NW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIpmgLTPASAgR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 187 RALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEILlHHA------------ANSVK- 253
Cdd:cd07148 117 IAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLL-HEAglpegwcqavpcENAVAe 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 254 -------------------------------RVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQR 302
Cdd:cd07148 196 klvtdprvaffsfigsarvgwmlrsklapgtRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 303 GIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRhqLGKNFFEPTLLCNVTQ 382
Cdd:cd07148 276 EIADDFAQRLAAAAEK-LVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKR--LSDTTYAPTVLLDPPR 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 383 DMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVE-CPFGGVKQ 461
Cdd:cd07148 353 DAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQ 432
|
410
....*....|....
gi 1589401592 462 SGLGREGSKYGIDE 475
Cdd:cd07148 433 SGYGTGGIPYTMHD 446
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
124-476 |
2.08e-56 |
|
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: 193.59 E-value: 2.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 124 LRKWYNLMIQNKDDLARIITAESGKPLKEA--------HGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRralVLKQPI 195
Cdd:cd07135 33 LKQLYWAVKDNEEAIVEALKKDLGRPPFETlltevsgvKNDILHMLKNLKKWAKDEKVKDGPLAFMFGKPR---IRKEPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 196 GVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEI----------------------LLHH------ 247
Cdd:cd07135 110 GVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELvpkyldpdafqvvqggvpettaLLEQkfdkif 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 248 --------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFA 313
Cdd:cd07135 190 ytgsgrvgriiaeaAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELK 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 314 EAMKKnlRVGNGFEEGTTQGPLINEKAVEKVEKQVNDavSKGaTVVTGGKRHQlGKNFFEPTLLCNVTQDMLCTHEETFG 393
Cdd:cd07135 270 KVLDE--FYPGGANASPDYTRIVNPRHFNRLKSLLDT--TKG-KVVIGGEMDE-ATRFIPPTIVSDVSWDDSLMSEELFG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 394 PLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI--SSVECPFGGVKQSGLGREGSKY 471
Cdd:cd07135 344 PVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPFGGVGDSGYGAYHGKY 423
|
....*
gi 1589401592 472 GIDEY 476
Cdd:cd07135 424 GFDTF 428
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
116-484 |
6.32e-55 |
|
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: 189.27 E-value: 6.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 116 SAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAH--------GEILYSAFFLEWFSEEaRRVYGDIIHTPAKdrr 187
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlteiavvlGEIDHALKHLKKWMKP-RRVSVPLLLQPAK--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 188 ALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEILLHH-------------------- 247
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYfdpeavavveggvevatall 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 248 ----------------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIH 305
Cdd:cd07087 174 aepfdhifftgspavgkivmeaAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 306 DAFVkafaEAMKKNLR--VGNGFEEGTTQGPLINEKAVEKVEKQVNDAvskgaTVVTGGKRHQlGKNFFEPTLLCNVTQD 383
Cdd:cd07087 254 DELI----EELKKAIKefYGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGGQVDK-EERYIAPTILDDVSPD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 384 MLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI--SSVECPFGGVKQ 461
Cdd:cd07087 324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLhaAIPNLPFGGVGN 403
|
410 420
....*....|....*....|...
gi 1589401592 462 SGLGREGSKYGIDEYLELKYVCY 484
Cdd:cd07087 404 SGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
109-479 |
4.37e-53 |
|
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: 186.61 E-value: 4.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 109 FCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRA 188
Cdd:TIGR01237 82 FEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 189 LVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEIL------------------------ 244
Cdd:TIGR01237 162 QYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILeeaglpkgvvqfvpgsgsevgdyl 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 245 LHHAANS---------------------------VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQ 297
Cdd:TIGR01237 242 VDHPKTSlitftgsrevgtriferaakvqpgqkhLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSR 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 298 FLVQRGIHDAFVKAFAEAmKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGaTVVTGGKRHQLGKNFFEPTLL 377
Cdd:TIGR01237 322 AVVHEKVYDEVVERFVEI-TESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 378 CNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNE---GLISSVEc 454
Cdd:TIGR01237 400 ADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRnitGAIVGYQ- 478
|
410 420
....*....|....*....|....*
gi 1589401592 455 PFGGVKQSGLgreGSKYGIDEYLEL 479
Cdd:TIGR01237 479 PFGGFKMSGT---DSKAGGPDYLAL 500
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
118-483 |
3.04e-50 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 178.68 E-value: 3.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 118 KERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAH--------GEIlysAFFLEWFSE--EARRVYGDIIHTPAKdrr 187
Cdd:PTZ00381 29 EFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmtevlltvAEI---EHLLKHLDEylKPEKVDTVGVFGPGK--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 188 ALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALA-----------------------EIL 244
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAklltkyldpsyvrvieggvevttELL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 245 LHH-------------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIH 305
Cdd:PTZ00381 183 KEPfdhifftgsprvgklvmqaAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 306 DAFVKAFAEAMKKNLrvGNGFEEGTTQGPLINEKAVEKVEKQVNDavsKGATVVTGGKrHQLGKNFFEPTLLCNVTQDML 385
Cdd:PTZ00381 263 DKFIEALKEAIKEFF--GEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE-VDIENKYVAPTIIVNPDLDSP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 386 CTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGL--ISSVECPFGGVKQSG 463
Cdd:PTZ00381 337 LMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVfhLLNPNLPFGGVGNSG 416
|
410 420
....*....|....*....|
gi 1589401592 464 LGREGSKYGIDEYLELKYVC 483
Cdd:PTZ00381 417 MGAYHGKYGFDTFSHPKPVL 436
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
65-479 |
1.00e-49 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 177.82 E-value: 1.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 65 VGGRWLPAAATFPVQDPASGAAL-GMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIIT 143
Cdd:PRK03137 41 IGGERITTEDKIVSINPANKSEVvGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 144 AESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGC 223
Cdd:PRK03137 121 KEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 224 TVVVKPAEDTPFSALALAEIL--------------------------------------------LHHAANSV------- 252
Cdd:PRK03137 201 TVLLKPASDTPVIAAKFVEVLeeaglpagvvnfvpgsgsevgdylvdhpktrfitftgsrevglrIYERAAKVqpgqiwl 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 253 KRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGfEEGTTQ 332
Cdd:PRK03137 281 KRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKE-LTVGNP-EDNAYM 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 333 GPLINEKAVEKVEKQVNDAVSKGaTVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIAN 412
Cdd:PRK03137 359 GPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIAN 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 413 AADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNE---GLISSVEcPFGGVKQSGlgrEGSKYGIDEYLEL 479
Cdd:PRK03137 438 NTEYGLTGAVISNNREHLEKARREFHVGNLYFNRgctGAIVGYH-PFGGFNMSG---TDSKAGGPDYLLL 503
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
62-480 |
1.91e-49 |
|
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: 176.10 E-value: 1.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 62 DSFVGGRWLPAAAT--FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLA 139
Cdd:cd07116 2 DNFIGGEWVAPVKGeyFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 140 RIITAESGKPLKEAHG-EILYSAFFLEWFSEEARRVYGDIIHTPAkDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAA 218
Cdd:cd07116 82 VAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSISEIDE-NTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 219 LAAGCTVVVKPAEDTPFSALALAEI--------------------------------------------LLHHAANSVKR 254
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELigdllppgvvnvvngfgleagkplasskriakvaftgetttgrlIMQYASENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 255 VSMELGGLAPFIVFDS------ANVDQAVAGAMASKFrNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEE 328
Cdd:cd07116 241 VTLELGGKSPNIFFADvmdaddAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKA-IKQGNPLDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 329 GTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKN----FFEPTLLCNvTQDMLCTHEETFGPLAPVIKFDTE 404
Cdd:cd07116 319 ETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1589401592 405 EEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 480
Cdd:cd07116 398 EEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
109-474 |
1.12e-48 |
|
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: 172.84 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 109 FCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEwFSEEARRVYGDIIHTPAKDRRA 188
Cdd:cd07095 13 FPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKID-ISIKAYHERTGERATPMAQGRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 189 LVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEI------------------------- 243
Cdd:cd07095 92 VLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELweeaglppgvlnlvqggretgeala 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 244 ------------------LLHH--AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRG 303
Cdd:cd07095 172 ahegidgllftgsaatglLLHRqfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 304 -IHDAFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLL----C 378
Cdd:cd07095 252 aVGDAFLERLVEAAKR-LRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLSPGIIdvtdA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 379 NVTQDmlcthEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI-SSVECPFG 457
Cdd:cd07095 331 ADVPD-----EEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTgASSTAPFG 405
|
410
....*....|....*..
gi 1589401592 458 GVKQSGLGREGSKYGID 474
Cdd:cd07095 406 GVGLSGNHRPSAYYAAD 422
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
44-477 |
7.43e-48 |
|
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: 172.77 E-value: 7.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 44 LRCYAGRLAGLSAALLRTDSFVGGRWLPAAATFPVQDPASGAA-LGMVADCGVREARAAVRAAYEAFCRWREVSAKERSS 122
Cdd:cd07125 16 LEALADALKAFDEKEWEAIPIINGEETETGEGAPVIDPADHERtIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 123 LLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVIT 202
Cdd:cd07125 96 ILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCIS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 203 PWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEiLLHHA-----------------------ANSVKRVSM-- 257
Cdd:cd07125 176 PWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVE-LLHEAgvprdvlqlvpgdgeeigealvaHPRIDGVIFtg 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 258 ------------------------ELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFA 313
Cdd:cd07125 255 stetaklinralaerdgpilpliaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 314 EAMkKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNdAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLctHEETFG 393
Cdd:cd07125 335 GAM-ASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTE-LMRGEAWLIAPAPLDDGNGYFVAPGIIEIVGIFDL--TTEVFG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 394 PLAPVIKFDTEEEAIAIANAADV--GLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSV--ECPFGGVKQSGLgreGS 469
Cdd:cd07125 411 PILHVIRFKAEDLDEAIEDINATgyGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIvgRQPFGGWGLSGT---GP 487
|
....*...
gi 1589401592 470 KYGIDEYL 477
Cdd:cd07125 488 KAGGPNYL 495
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
64-469 |
1.74e-47 |
|
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: 170.85 E-value: 1.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIIT 143
Cdd:cd07130 2 VYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 144 AESGKPLKEAHGEIlysafflewfsEE-----------ARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMIT 212
Cdd:cd07130 82 LEMGKILPEGLGEV-----------QEmidicdfavglSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 213 RKVGAALAAGCTVVVKPAEDTPFSALALAEILL-----HHAANSV--------------------------------KRV 255
Cdd:cd07130 151 WNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVArvlekNGLPGAIaslvcggadvgealvkdprvplvsftgstavgRQV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 256 S-----------MELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGN 324
Cdd:cd07130 231 GqavaarfgrslLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQ-VRIGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 325 GFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLcNVTQDMLCTHEETFGPLAPVIKFDTE 404
Cdd:cd07130 310 PLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 405 EEAIAIANAADVGLAGYFYSQDPAQI--WRVAEQLEVGMVGVNEGlISSVEC--PFGGVKQSGLGRE-GS 469
Cdd:cd07130 389 EEAIAWNNEVPQGLSSSIFTTDLRNAfrWLGPKGSDCGIVNVNIG-TSGAEIggAFGGEKETGGGREsGS 457
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
116-466 |
2.25e-47 |
|
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: 169.59 E-value: 2.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 116 SAKERSSLLRKWYNLMIQNKDDLARIITAESGKplkEAHGEILYSAFFL-------------EWFSEEARRVygDIIHTP 182
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFGH---RSRHETLLAEILPsiagikharkhlkKWMKPSRRHV--GLLFLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 183 AKdrrALVLKQPIGVAAVITPWNFP-----SAMItrkvgAALAAGCTVVVKPAEDTPFSALALAEILLHH---------- 247
Cdd:cd07133 93 AK---AEVEYQPLGVVGIIVPWNYPlylalGPLI-----AALAAGNRVMIKPSEFTPRTSALLAELLAEYfdedevavvt 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 248 --------------------------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCS 295
Cdd:cd07133 165 ggadvaaafsslpfdhllftgstavgrhvmraAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 296 NQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEEGTtqgPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQL--GKNFFE 373
Cdd:cd07133 245 DYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPDYT---SIINERHYARLQGLLEDARAKGARVIELNPAGEDfaATRKLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 374 PTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGL--ISS 451
Cdd:cd07133 322 PTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLlhVAQ 401
|
410
....*....|....*
gi 1589401592 452 VECPFGGVKQSGLGR 466
Cdd:cd07133 402 DDLPFGGVGASGMGA 416
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
120-474 |
5.13e-45 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 163.44 E-value: 5.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 120 RSSLLRKWYNLMIQNKDDLARIITAESGKPLKEA--------HGEILYSAFFLEWFSEEaRRVYGDIIHTPAKDRralVL 191
Cdd:cd07136 22 RIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAymteigfvLSEINYAIKHLKKWMKP-KRVKTPLLNFPSKSY---IY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEI----------------------LLH--- 246
Cdd:cd07136 98 YEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIieetfdeeyvavveggveenqeLLDqkf 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 247 -----------------HAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFV 309
Cdd:cd07136 178 dyifftgsvrvgkivmeAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 310 KAFAEAMKKnlRVGNGFEEGTTQGPLINEKAVEKVEKQVndavsKGATVVTGGKrHQLGKNFFEPTLLCNVTQDMLCTHE 389
Cdd:cd07136 258 KELKEEIKK--FYGEDPLESPDYGRIINEKHFDRLAGLL-----DNGKIVFGGN-TDRETLYIEPTILDNVTWDDPVMQE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 390 ETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI--SSVECPFGGVKQSGLGRE 467
Cdd:cd07136 330 EIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMhlANPYLPFGGVGNSGMGSY 409
|
....*..
gi 1589401592 468 GSKYGID 474
Cdd:cd07136 410 HGKYSFD 416
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
111-468 |
1.47e-39 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 149.52 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 111 RWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVY--GDIIHT---PAKD 185
Cdd:PLN00412 68 AWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILgeGKFLVSdsfPGNE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 186 RRALVL--KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALAL---------------------AE 242
Cdd:PLN00412 148 RNKYCLtsKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMvhcfhlagfpkgliscvtgkgSE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 243 I----LLHHAAN-----------SVKR------VSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQ 301
Cdd:PLN00412 228 IgdflTMHPGVNcisftggdtgiAISKkagmvpLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVM 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 302 RGIHDAFVKAFAEAMKKnLRVGNGfEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQlgkNFFEPTLLCNVT 381
Cdd:PLN00412 308 ESVADALVEKVNAKVAK-LTVGPP-EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREG---NLIWPLLLDNVR 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 382 QDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVE-CPFGGVK 460
Cdd:PLN00412 383 PDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLK 462
|
....*...
gi 1589401592 461 QSGLGREG 468
Cdd:PLN00412 463 DSGIGSQG 470
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
64-479 |
7.29e-37 |
|
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: 141.95 E-value: 7.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLPAAATFPVQDP-ASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARII 142
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 143 TAESGKPLKEAHGEILYSAFFLEWFSEEARRVYG--DIIHTPAKDRRALVLkQPIGVAAVITPWNFPSAMITRKVGAALA 220
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFY-VGLGAGVVISPWNFPVAIFTGMIVAPVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 221 AGCTVVVKPAEDTPFSALALAEILlHHAA--------------------------------------------------- 249
Cdd:cd07083 181 VGNTVIAKPAEDAVVVGYKVFEIF-HEAGfppgvvqflpgvgeevgaylteherirginftgsletgkkiyeaaarlapg 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 250 -NSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEE 328
Cdd:cd07083 260 qTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAER-LSVGPPEEN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 329 GTTQGPLINEKAVEKVEKQVNDAVSKGaTVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAI 408
Cdd:cd07083 339 GTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDFAE 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1589401592 409 AIANAADV--GLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSV--ECPFGGVKQSGlgrEGSKYGIDEYLEL 479
Cdd:cd07083 418 ALEVANSTpyGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALvgVQPFGGFKLSG---TNAKTGGPHYLRR 489
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
113-484 |
2.68e-35 |
|
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: 136.39 E-value: 2.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 113 REVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAH-GEI--LYSAFFL------EWFSEEarRVYGDIIHTPA 183
Cdd:cd07137 16 RTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFrDEVsvLVSSCKLaikelkKWMAPE--KVKTPLTTFPA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 184 KdrrALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALA---------------------- 241
Cdd:cd07137 94 K---AEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAklipeyldtkaikvieggvpet 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 242 EILLHH--------------------AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKF-RNTGQTCVCSNQFLV 300
Cdd:cd07137 171 TALLEQkwdkifftgsprvgriimaaAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 301 QRGihdaFVKAFAEAMKKNLR--VGNGFEEGTTQGPLINEKAVEKVEKQVNDAvSKGATVVTGGKRHQlGKNFFEPTLLC 378
Cdd:cd07137 251 EES----FAPTLIDALKNTLEkfFGENPKESKDLSRIVNSHHFQRLSRLLDDP-SVADKIVHGGERDE-KNLYIEPTILL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 379 NVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSV--ECPF 456
Cdd:cd07137 325 DPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAidTLPF 404
|
410 420
....*....|....*....|....*...
gi 1589401592 457 GGVKQSGLGREGSKYGIDEYLELKYVCY 484
Cdd:cd07137 405 GGVGESGFGAYHGKFSFDAFSHKKAVLY 432
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
64-474 |
6.87e-35 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 136.24 E-value: 6.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 64 FVGGRWLP-AAATFPVQDPASGAAL--GMVADCGVREARAAVRAAYeaFCRWREVSAKERSSLLRKWYNLMIQNKDDLAR 140
Cdd:PRK09457 4 WINGDWIAgQGEAFESRNPVSGEVLwqGNDATAAQVDAAVRAARAA--FPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 141 IITAESGKPLKEAHGEI--------LYSAFFLEWFSEEArrvygdiihTPAKDRRALVLKQPIGVAAVITPWNFPSAMIT 212
Cdd:PRK09457 82 VIARETGKPLWEAATEVtaminkiaISIQAYHERTGEKR---------SEMADGAAVLRHRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 213 RKVGAALAAGCTVVVKPAEDTPFSA---------------------------LALAE----------------ILLHH-- 247
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAeltvklwqqaglpagvlnlvqggretgKALAAhpdidgllftgsantgYLLHRqf 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 248 AANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIH-DAFVKAFAEAMKKnLRVGNGF 326
Cdd:PRK09457 233 AGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKR-LTVGRWD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 327 EEGTT-QGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLcNVTQDMLCTHEETFGPLAPVIKFDTEE 405
Cdd:PRK09457 312 AEPQPfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 406 EAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLI-SSVECPFGGVKQSGLGREGSKYGID 474
Cdd:PRK09457 391 EAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTgASSAAPFGGVGASGNHRPSAYYAAD 460
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
60-482 |
3.53e-32 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 129.87 E-value: 3.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 60 RTDSFVGGRWLPAAAT--FPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDD 137
Cdd:PLN02419 113 RVPNLIGGSFVESQSSsfIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 138 LARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGA 217
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 218 ALAAGCTVVVKPAEDTPFSALALAEILLH-----------HAANSV---------------------------------K 253
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEaglpdgvlnivHGTNDTvnaicddediravsfvgsntagmhiyaraaakgK 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 254 RVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVqrgIHDAfvKAFAEAM---KKNLRVGNGFEEGT 330
Cdd:PLN02419 353 RIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVF---VGDA--KSWEDKLverAKALKVTCGSEPDA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 331 TQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKR-----HQLGkNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEE 405
Cdd:PLN02419 428 DLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpgYEKG-NFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFD 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 406 EAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLisSVECP---FGGVKQSGLGREG--SKYGIDEYLELK 480
Cdd:PLN02419 507 EAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI--PVPLPffsFTGNKASFAGDLNfyGKAGVDFFTQIK 584
|
..
gi 1589401592 481 YV 482
Cdd:PLN02419 585 LV 586
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
192-474 |
4.20e-32 |
|
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: 127.72 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 192 KQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEIL--------------------------- 244
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyldkecypvvlggveettellkqrf 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 245 --------------LHHAANS-VKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFV 309
Cdd:cd07132 178 dyifytgstsvgkiVMQAAAKhLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 310 KAFAEAMKKnlRVGNGFEEGTTQGPLINEKAVEKVEKQVndavsKGATVVTGGkRHQLGKNFFEPTLLCNVTQDMLCTHE 389
Cdd:cd07132 258 EALKKTLKE--FYGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVAIGG-QTDEKERYIAPTVLTDVKPSDPVMQE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 390 ETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSV--ECPFGGVKQSGLGRE 467
Cdd:cd07132 330 EIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTldSLPFGGVGNSGMGAY 409
|
....*..
gi 1589401592 468 GSKYGID 474
Cdd:cd07132 410 HGKYSFD 416
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
50-477 |
4.45e-32 |
|
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: 128.49 E-value: 4.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 50 RLAGLSAALL-------RTDSFVGGRWLPAAATFPVQDPAS-GAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERS 121
Cdd:TIGR01238 20 ELKPLEAQIHawadktwQAAPIIGHSYKADGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 122 SLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHtpakdrralvlkQPIGVAAVI 201
Cdd:TIGR01238 100 AKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSV------------ESRGVFVCI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 202 TPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEILLH-------------------HAANSVKRVS------ 256
Cdd:TIGR01238 168 SPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEagfpagtiqllpgrgadvgAALTSDPRIAgvaftg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 257 -----------------------MELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFA 313
Cdd:TIGR01238 248 stevaqlinqtlaqredapvpliAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 314 EAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATV---VTGGKRHQLGKNFFEPTLLcnVTQDMLCTHEE 390
Cdd:TIGR01238 328 GAMQE-LKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLF--ELDDIAELSEE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 391 TFGPLAPVIKF--DTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVEC--PFGGvkqSGLGR 466
Cdd:TIGR01238 405 VFGPVLHVVRYkaRELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGG---QGLSG 481
|
490
....*....|.
gi 1589401592 467 EGSKYGIDEYL 477
Cdd:TIGR01238 482 TGPKAGGPHYL 492
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
113-487 |
6.73e-29 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 119.06 E-value: 6.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 113 REVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAH----GEILYSAFFL-----EWFSEEarRVYGDIIHTPA 183
Cdd:PLN02203 23 RTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYrdevGVLTKSANLAlsnlkKWMAPK--KAKLPLVAFPA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 184 KdrrALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALA---------------------- 241
Cdd:PLN02203 101 T---AEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAanipkyldskavkvieggpavg 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 242 EILLHH--------------------AANSVKRVSMELGGLAPFIV--FDSA-NVDQAVAGAMASKFRN-TGQTCVCSNQ 297
Cdd:PLN02203 178 EQLLQHkwdkifftgsprvgriimtaAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAIDY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 298 FLVQRGihdaFVKAFAEAMKKNLR--VGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKgATVVTGGKRHQlgKNFF-EP 374
Cdd:PLN02203 258 VLVEER----FAPILIELLKSTIKkfFGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSIDE--KKLFiEP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 375 TLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSV-- 452
Cdd:PLN02203 331 TILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcd 410
|
410 420 430
....*....|....*....|....*....|....*
gi 1589401592 453 ECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL 487
Cdd:PLN02203 411 SLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSL 445
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
63-477 |
2.82e-28 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 117.63 E-value: 2.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 63 SFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARII 142
Cdd:PLN02315 23 CYVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 143 TAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAG 222
Cdd:PLN02315 103 SLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 223 CTVVVKPAEDTPFSALAL------------------------AEI-----------------------LLHHAANS-VKR 254
Cdd:PLN02315 183 NCVVWKGAPTTPLITIAMtklvaevleknnlpgaiftsfcggAEIgeaiakdtriplvsftgsskvglMVQQTVNArFGK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 255 VSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnLRVGNGFEEGTTQGP 334
Cdd:PLN02315 263 CLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQ-VKIGDPLEKGTLLGP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 335 LINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLcNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAA 414
Cdd:PLN02315 342 LHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSV 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1589401592 415 DVGLAGYFYSQDPAQI--WRVAEQLEVGMVGVN---EGliSSVECPFGGVKQSGLGREGSKYGIDEYL 477
Cdd:PLN02315 421 PQGLSSSIFTRNPETIfkWIGPLGSDCGIVNVNiptNG--AEIGGAFGGEKATGGGREAGSDSWKQYM 486
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
51-465 |
3.35e-27 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 115.73 E-value: 3.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 51 LAGLSAALlrtDSFVGGRWL---------PAAATFPVQDPA-SGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKER 120
Cdd:PRK11905 538 LAALDEAL---NAFAAKTWHaapllaggdVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAER 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 121 SSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHtpakdrralvlkQPIGVAAV 200
Cdd:PRK11905 615 AAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGH------------KPLGPVVC 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 201 ITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSAlALAEILLHHA-----------------------ANSVKRV-- 255
Cdd:PRK11905 683 ISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIA-ARAVRLLHEAgvpkdalqllpgdgrtvgaalvaDPRIAGVmf 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 256 --SME------------LGGLAPFI----------VFDSANVDQAVAGAMASKFRNTGQTC-----VCsnqflVQRGIHD 306
Cdd:PRK11905 762 tgSTEvarliqrtlakrSGPPVPLIaetggqnamiVDSSALPEQVVADVIASAFDSAGQRCsalrvLC-----LQEDVAD 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 307 AFVKAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVvtggKRHQLGKN-----FFEPTLL-CNV 380
Cdd:PRK11905 837 RVLTMLKGAMDE-LRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLPAEtekgtFVAPTLIeIDS 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 381 TQDMlctHEETFGPLAPVIKFDteeEAIAIANAADVGLAGY-----FYSQDPAQIWRVAEQLEVGMVGVNEGLISSV--E 453
Cdd:PRK11905 912 ISDL---EREVFGPVLHVVRFK---ADELDRVIDDINATGYgltfgLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVvgV 985
|
490
....*....|..
gi 1589401592 454 CPFGGVKQSGLG 465
Cdd:PRK11905 986 QPFGGEGLSGTG 997
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
41-477 |
7.12e-27 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 114.91 E-value: 7.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 41 PAQLRCYAGRLAGLSAALLRTDSFVGGrwlpAAATFPVQDPASGA-ALGMVADCGVREARAAVRAAYEAFCRWREVSAKE 119
Cdd:PRK11904 533 RSELEPLAAAIAAFLEKQWQAGPIING----EGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEE 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 120 RSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHT--PAKDRRALVLkQPIGV 197
Cdd:PRK11904 609 RAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLpgPTGESNELRL-HGRGV 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 198 AAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSAlALAEILLHHA----------------------------- 248
Cdd:PRK11904 688 FVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIA-AEAVKLLHEAgipkdvlqllpgdgatvgaaltadpriag 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 249 ---------ANSVKRV-SMELGGLAPFI---------VFDS-ANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAF 308
Cdd:PRK11904 767 vaftgstetARIINRTlAARDGPIVPLIaetggqnamIVDStALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRV 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 309 VKAFAEAMkKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVnDAVSKGATVVTGGKRHQLGKN--FFEPTL--LCNVTQdm 384
Cdd:PRK11904 847 IEMLKGAM-AELKVGDPRLLSTDVGPVIDAEAKANLDAHI-ERMKREARLLAQLPLPAGTENghFVAPTAfeIDSISQ-- 922
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 385 lcTHEETFGPLAPVIKFDteeEAIAIANAADVGLAGY-----FYSQDPAQIWRVAEQLEVGMVGVNEGLISSV--ECPFG 457
Cdd:PRK11904 923 --LEREVFGPILHVIRYK---ASDLDKVIDAINATGYgltlgIHSRIEETADRIADRVRVGNVYVNRNQIGAVvgVQPFG 997
|
490 500
....*....|....*....|
gi 1589401592 458 GvkqSGLGREGSKYGIDEYL 477
Cdd:PRK11904 998 G---QGLSGTGPKAGGPHYL 1014
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
50-465 |
6.50e-25 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 108.91 E-value: 6.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 50 RLAGLSAALLRTDS-------FVGGRWLPAAATfPVQDPASGAAL-GMVADCGVREARAAVRAAYEAFCRWREVSAKERS 121
Cdd:PRK11809 629 RLASLSSALLASAHqkwqaapMLEDPVAAGEMS-PVINPADPRDIvGYVREATPAEVEQALESAVNAAPIWFATPPAERA 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 122 SLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHtpakdrralvlkQPIGVAAVI 201
Cdd:PRK11809 708 AILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTH------------RPLGPVVCI 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 202 TPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSAlALAEILLHHA---ANSVK-----------------RVS--M-- 257
Cdd:PRK11809 776 SPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIA-AQAVRILLEAgvpAGVVQllpgrgetvgaalvadaRVRgvMft 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 258 ----------------------------ELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFV 309
Cdd:PRK11809 855 gstevarllqrnlagrldpqgrpipliaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTL 934
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 310 KAFAEAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATV----VTGGKRHQLGkNFFEPTL--LCNVTQd 383
Cdd:PRK11809 935 KMLRGAMAE-CRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVfqaaRENSEDWQSG-TFVPPTLieLDSFDE- 1011
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 384 mlcTHEETFGPLAPVIKFdteEEAIAIANAADVGLAGY-----FYSQDPAQIWRVAEQLEVGMVGVNEGLISSVEC--PF 456
Cdd:PRK11809 1012 ---LKREVFGPVLHVVRY---NRNQLDELIEQINASGYgltlgVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvqPF 1085
|
....*....
gi 1589401592 457 GGVKQSGLG 465
Cdd:PRK11809 1086 GGEGLSGTG 1094
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
50-402 |
9.45e-24 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 105.41 E-value: 9.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 50 RLAGLSAALLRTD-------SFVGGRwLPAAATFPVQDPASGA-ALGMVADCGVREARAAVRAAYEAFCRWREVSAKERS 121
Cdd:COG4230 540 VLAALSAALAAAAekqwqaaPLIAGE-AASGEARPVRNPADHSdVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERA 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 122 SLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGdiihtpakdrrALVLKQPIGVAAVI 201
Cdd:COG4230 619 AILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFA-----------APTVLRGRGVFVCI 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 202 TPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEILlhHAA--------------NSV-------KRV----- 255
Cdd:COG4230 688 SPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLL--HEAgvpadvlqllpgdgETVgaalvadPRIagvaf 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 256 --SME------------LGGLAPFI----------VFDSANVDQAVAGAMASKFRNTGQTC-----VCsnqflVQRGIHD 306
Cdd:COG4230 766 tgSTEtarlinrtlaarDGPIVPLIaetggqnamiVDSSALPEQVVDDVLASAFDSAGQRCsalrvLC-----VQEDIAD 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 307 AFVKAFAEAMkKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVvtggKRHQLGKN-----FFEPTL--LCN 379
Cdd:COG4230 841 RVLEMLKGAM-AELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLV----HQLPLPEEcangtFVAPTLieIDS 915
|
410 420
....*....|....*....|...
gi 1589401592 380 VTQdmLctHEETFGPLAPVIKFD 402
Cdd:COG4230 916 ISD--L--EREVFGPVLHVVRYK 934
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
188-487 |
1.80e-21 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 97.04 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 188 ALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEILLHHAANSVKRVS----------- 256
Cdd:PLN02174 106 AEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVegavtettall 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 257 -------------------------------MELGGLAPFIVFDSANVDQAVAGAMASKFR-NTGQTCVCSNQFLVQRgi 304
Cdd:PLN02174 186 eqkwdkifytgsskigrvimaaaakhltpvvLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTK-- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 305 hdAFVKAFAEAMKKNLRV--GNGFEEGTTQGPLINEKAVEKV-----EKQVNDavskgaTVVTGGKRHQlgKNF-FEPTL 376
Cdd:PLN02174 264 --EYAPKVIDAMKKELETfyGKNPMESKDMSRIVNSTHFDRLsklldEKEVSD------KIVYGGEKDR--ENLkIAPTI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 377 LCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSV--EC 454
Cdd:PLN02174 334 LLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTL 413
|
330 340 350
....*....|....*....|....*....|...
gi 1589401592 455 PFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL 487
Cdd:PLN02174 414 PFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSL 446
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
112-439 |
2.37e-15 |
|
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: 78.05 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAhGEILYSAFFLEWFSE--EARRVYGDIIHTPAKDRRAL 189
Cdd:cd07084 15 ARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFviYSYRIPHEPGNHLGQGLKQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 190 VLKQ--PIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTP-------------------------FSALALAE 242
Cdd:cd07084 94 SHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSivmqimvrllhyagllppedvtlinGDGKTMQA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 243 ILLHHAANSVK------------------RVSMELGGLAPFIVFDSAnvdQAVAgAMASKFRNTgqTCVCSNQFLVQRGI 304
Cdd:cd07084 174 LLLHPNPKMVLftgssrvaeklaldakqaRIYLELAGFNWKVLGPDA---QAVD-YVAWQCVQD--MTACSGQKCTAQSM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 305 hdAFV------KAFAEAMKKNLRvgNGFEEGTTQGPLINekavEKVEKQVNDAVSKGATVVTGG----KRHQLGKNF--F 372
Cdd:cd07084 248 --LFVpenwskTPLVEKLKALLA--RRKLEDLLLGPVQT----FTTLAMIAHMENLLGSVLLFSgkelKNHSIPSIYgaC 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589401592 373 EPTLLCNVTQDMLCTH----EETFGPLAPVIKF-DTEEEAIAIANAADVG-LAGYFYSQDPAQIWRVAEQLEV 439
Cdd:cd07084 320 VASALFVPIDEILKTYelvtEEIFGPFAIVVEYkKDQLALVLELLERMHGsLTAAIYSNDPIFLQELIGNLWV 392
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
62-441 |
4.64e-15 |
|
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: 77.31 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 62 DSFVGGRWL-PAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLAR 140
Cdd:cd07128 2 QSYVAGQWHaGTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 141 IiTAESGKPLKEAHGEILYSAFFLEWFSEEARR--------VYGDIIHTpAKD-----RRALVLKQpiGVAAVITPWNFP 207
Cdd:cd07128 82 L-SAATGATRRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPL-SKDgtfvgQHILTPRR--GVAVHINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 208 SAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEI---------------------LLHH------------------- 247
Cdd:cd07128 158 VWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDivesgllpegalqlicgsvgdLLDHlgeqdvvaftgsaataakl 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 248 ------AANSVkRVSME---LGG--LAPFIVFDSANVD---QAVAGAMASKfrnTGQTCVCSNQFLVQRGIHDAFVKAFA 313
Cdd:cd07128 238 rahpniVARSI-RFNAEadsLNAaiLGPDATPGTPEFDlfvKEVAREMTVK---AGQKCTAIRRAFVPEARVDAVIEALK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 314 EAMKKnLRVGNGFEEGTTQGPLINEKAVEKVEKQVnDAVSKGATVVTGGKRHQLGKN-------FFEPTLL-CNVTQDML 385
Cdd:cd07128 314 ARLAK-VVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRFEVVGadaekgaFFPPTLLlCDDPDAAT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1589401592 386 CTHE-ETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAqiwrVAEQLEVGM 441
Cdd:cd07128 392 AVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPA----FARELVLGA 444
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
63-437 |
5.76e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 77.05 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 63 SFVGGRWLP-AAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARI 141
Cdd:PRK11903 7 NYVAGRWQAgSGAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 142 ITAESGKPLKEAHGEILYSAFFLEWFSEEARRVyGDIIHTPAKDRRAL----------VLKQPIGVAAVITPWNFPSAMI 211
Cdd:PRK11903 87 ATANSGTTRNDSAVDIDGGIFTLGYYAKLGAAL-GDARLLRDGEAVQLgkdpafqgqhVLVPTRGVALFINAFNFPAWGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 212 TRKVGAALAAGCTVVVKPAEDT-----------------PFSALAL--------------------------AEILLHHA 248
Cdd:PRK11903 166 WEKAAPALLAGVPVIVKPATATawltqrmvkdvvaagilPAGALSVvcgssaglldhlqpfdvvsftgsaetAAVLRSHP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 249 A---NSVkRVSME-----LGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKnL 320
Cdd:PRK11903 246 AvvqRSV-RVNVEadslnSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAK-T 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 321 RVGNGFEEGTTQGPLINEKAVEKVEKQVnDAVSKGATVVTGGKRHQL------GKNFFEPTLL-CNVTQDMLCTHE-ETF 392
Cdd:PRK11903 324 TVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFALvdadpaVAACVGPTLLgASDPDAATAVHDvEVF 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1589401592 393 GPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQL 437
Cdd:PRK11903 403 GPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALEL 447
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
112-438 |
6.14e-09 |
|
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: 57.94 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 112 WREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARR-VYGDIIHTPAKDRRALV 190
Cdd:cd07129 15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgSWLDARIDPADPDRQPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 191 -------LKQPIGVAAVITPWNFPSAMITrkVG----AALAAGCTVVVKPAEDTPFSALALAEI---------------- 243
Cdd:cd07129 95 prpdlrrMLVPLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKAHPAHPGTSELVARAiraalratglpagvfs 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 244 LLHHAANSV------------------------------KR-----VSMELGGLAPFIVFDSA---NVDQAVAGAMASKF 285
Cdd:cd07129 173 LLQGGGREVgvalvkhpaikavgftgsrrggralfdaaaARpepipFYAELGSVNPVFILPGAlaeRGEAIAQGFVGSLT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 286 RNTGQTCVCSNQFLVQRGIH-DAFVKAFAEAMKKnlrvgngfeegTTQGPLINEKAVEKVEKQVNDAVS-KGATVVTGGK 363
Cdd:cd07129 253 LGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAA-----------APAQTMLTPGIAEAYRQGVEALAAaPGVRVLAGGA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1589401592 364 RHQlGKNFFEPTLLCNVTQDMLCT---HEETFGPLAPVIKFDteeeaiaianaadvglagyfysqDPAQIWRVAEQLE 438
Cdd:cd07129 322 AAE-GGNQAAPTLFKVDAAAFLADpalQEEVFGPASLVVRYD-----------------------DAAELLAVAEALE 375
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
111-241 |
1.51e-03 |
|
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: 40.67 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589401592 111 RWREVSAKER----SSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHgeilysafflewfseEARRVYGDIIHTpakdr 186
Cdd:cd07077 35 RLASEAVSERgayiRSLIANWIAMMGCSESKLYKNIDTERGITASVGH---------------IQDVLLPDNGET----- 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1589401592 187 raLVLKQPIGVAAVITPWNFPSAMITrKVGAALAAGCTVVVKPAEDTPFSALALA 241
Cdd:cd07077 95 --YVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALA 146
|
|
| |
