|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
28-522 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 988.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 28 RLMTTDTQSVAAKLSSSGLLRSQALIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTA 107
Cdd:PLN02278 4 RASSMDAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 108 AERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGV 187
Cdd:PLN02278 84 SERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 188 VGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKI 267
Cdd:PLN02278 164 VGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 268 TFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAF 347
Cdd:PLN02278 244 TFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 348 AKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFG 427
Cdd:PLN02278 324 SKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 428 PVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGM 507
Cdd:PLN02278 404 PVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGI 483
|
490
....*....|....*
gi 807201085 508 DEYLEMKYVCLGSMS 522
Cdd:PLN02278 484 DEYLEIKYVCLGNMN 498
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
68-518 |
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: 829.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 68 VHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEV 147
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 148 SYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTA 227
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 228 LAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDAD 307
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 308 LEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEATS 387
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 388 KGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRV 467
Cdd:cd07103 321 KGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 807201085 468 TEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYVCL 518
Cdd:cd07103 401 AEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
68-514 |
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: 699.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 68 VHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEV 147
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 148 SYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTA 227
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 228 LAAAELSIQAGIPPGVVNVVMGN-APDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDA 306
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGSrAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 307 DLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEAT 386
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 387 SKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWR 466
Cdd:TIGR01780 321 EKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 807201085 467 VTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMK 514
Cdd:TIGR01780 401 VAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
48-518 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 696.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 48 RSQALIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEE 127
Cdd:COG1012 5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 128 LGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGP 207
Cdd:COG1012 85 LAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 208 ALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATV 287
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 288 KKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQG 367
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 368 PLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSL-GMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMAN 446
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALAN 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807201085 447 DTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEV-APFGGVKQSGLGREGSKYGMDEYLEMKYVCL 518
Cdd:COG1012 405 DTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
40-519 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 666.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 40 KLSSSGLLRSQALIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYD 119
Cdd:PRK11241 2 QLNDSTLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 120 LIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLA 199
Cdd:PRK11241 82 LMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 200 MITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKL 279
Cdd:PRK11241 162 MITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 280 MEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDG 359
Cdd:PRK11241 242 MEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 360 FTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDE 439
Cdd:PRK11241 322 LEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 440 EAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYVCLG 519
Cdd:PRK11241 402 DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIG 481
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
57-516 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 635.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 57 WVDAyDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQ 136
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 137 GKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPlADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVV 216
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSD-PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 217 IKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGG 296
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 297 NAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQ 376
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 377 KVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYI 456
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807201085 457 FSTNIKRAWRVTEALEYGIVGVNEGLVST-EVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:pfam00171 399 FTSDLERALRVARRLEAGMVWINDYTTGDaDGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
89-518 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 583.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 89 NDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDI 168
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 169 IPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVM 248
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 249 GNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCV 328
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 329 CANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKR-HSLGMTFYE 407
Cdd:cd07078 241 AASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRlEGGKGYFVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 408 PTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEV 487
Cdd:cd07078 321 PTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEP 400
|
410 420 430
....*....|....*....|....*....|..
gi 807201085 488 -APFGGVKQSGLGREGSKYGMDEYLEMKYVCL 518
Cdd:cd07078 401 sAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
53-516 |
0e+00 |
|
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: 550.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLM 132
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 133 TLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACG 212
Cdd:cd07088 82 VEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 213 CTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSL 292
Cdd:cd07088 162 NTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 293 ELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINE 372
Cdd:cd07088 242 ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 373 AAVQKVEYFVDEATSKGAKVLVGGKRHSLGM-TFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAG 451
Cdd:cd07088 322 AALDKVEEMVERAVEAGATLLTGGKRPEGEKgYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807201085 452 LAAYIFSTNIKRAWRVTEALEYGIVGVNEGlvSTEVAP--FGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07088 402 LTSYIYTENLNTAMRATNELEFGETYINRE--NFEAMQgfHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
50-516 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 522.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 50 QALIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWS--KLTAAERSRYLRKWYDLIMAHKEE 127
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWwrKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 128 LGQLMTLEQGKPLKEA--------IGEVSYGAGFIEfsaeegkRIYGDIIPSPlaDRRL-FVLKQPVGVVGAITPWNFPL 198
Cdd:cd07091 85 LAALESLDNGKPLEESakgdvalsIKCLRYYAGWAD-------KIQGKTIPID--GNFLaYTRREPIGVCGQIIPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 199 AMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKK 278
Cdd:cd07091 156 LMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 279 LMEGAAAT-VKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVG 357
Cdd:cd07091 236 IMEAAAKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 358 DGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKT 437
Cdd:cd07091 316 DPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKT 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807201085 438 DEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
68-518 |
0e+00 |
|
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: 515.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 68 VHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAI-GE 146
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 147 VSYGAGFIEFSAEEGKRIYGDIIPSPlADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLT 226
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 227 ALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDA 306
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 307 DLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEAT 386
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 387 SKGAKVLVGGKRHSLGMT----FYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIK 462
Cdd:cd07093 320 AEGATILTGGGRPELPDLeggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 807201085 463 RAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYVCL 518
Cdd:cd07093 400 RAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
68-516 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 515.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 68 VHNPATGEVITDVPCMGGRETNDAISSAYDAFSS--WSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIG 145
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 146 EVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPL 225
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 226 TALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDD 305
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 306 ADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEA 385
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 386 TSKGAKVLVGGKRHSLGMT----FYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNI 461
Cdd:cd07114 321 REEGARVLTGGERPSGADLgagyFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 807201085 462 KRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07114 401 ARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
53-516 |
9.77e-171 |
|
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: 491.06 E-value: 9.77e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSS--WSKLTAAERSRYLRKWYDLIMAHKEELGQ 130
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 131 LMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPlADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALA 210
Cdd:cd07119 82 LETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVP-PHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 211 CGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKV 290
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 291 SLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLI 370
Cdd:cd07119 241 ALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 371 NEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGM----TFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMAN 446
Cdd:cd07119 321 SAEHREKVLSYIQLGKEEGARLVCGGKRPTGDElakgYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLAN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 447 DTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07119 401 DTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
68-514 |
2.26e-170 |
|
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: 488.58 E-value: 2.26e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 68 VHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEV 147
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 148 SYGAGFIEFSAE---EGKRIYGDiipsplADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTP 224
Cdd:cd07106 81 GGAVAWLRYTASldlPDEVIEDD------DTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 225 LTALAAAELsIQAGIPPGVVNVVMGNApDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFD 304
Cdd:cd07106 155 LCTLKLGEL-AQEVLPPGVLNVVSGGD-ELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 305 DADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDE 384
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 385 ATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRA 464
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 807201085 465 WRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMK 514
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
66-518 |
2.99e-170 |
|
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: 488.78 E-value: 2.99e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 66 IKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIG 145
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 146 EVSYGAGFIEFSAEEGKRIYGDIIPS---PLADRRL-FVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSE 221
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVdayEYNERRIaFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 222 LTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCI 301
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 302 IFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYF 381
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 382 VDEATSKGAKVLVGGKRhsLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNI 461
Cdd:cd07145 321 VNDAVEKGGKILYGGKR--DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDI 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 807201085 462 KRAWRVTEALEYGIVGVNE-GLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYVCL 518
Cdd:cd07145 399 NRALKVARELEAGGVVINDsTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
66-518 |
4.20e-170 |
|
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: 488.26 E-value: 4.20e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 66 IKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIG 145
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 146 EVSYGAGFIEFSAEEGKRIYGDIIP---SPLADRRL-FVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSE 221
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPfdaSPGGEGRIgFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 222 LTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAatVKKVSLELGGNAPCI 301
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 302 IFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYF 381
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 382 VDEATSKGAKVLVGGKRHSlgmTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNI 461
Cdd:cd07149 319 VEEAVEGGARLLTGGKRDG---AILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 462 KRAWRVTEALEYGIVGVNEglVST---EVAPFGGVKQSGLGREGSKYGMDEYLEMKYVCL 518
Cdd:cd07149 396 QKALKAARELEVGGVMIND--SSTfrvDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
68-516 |
3.50e-165 |
|
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: 475.67 E-value: 3.50e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 68 VHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEV 147
Cdd:cd07150 3 DLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 148 SYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTA 227
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 228 LAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDAD 307
Cdd:cd07150 163 LKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 308 LEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEATS 387
Cdd:cd07150 243 LDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 388 KGAKVLVGGKRHSLgmtFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRV 467
Cdd:cd07150 323 KGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 807201085 468 TEALEYGIVGVNEGLVSTE-VAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07150 400 AERLESGMVHINDPTILDEaHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
53-514 |
1.97e-164 |
|
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: 474.30 E-value: 1.97e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLM 132
Cdd:cd07138 3 IDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 133 TLEQGKPLKEAIG-EVSYGAGFIEFSAEEGKRIygdiipsPLADRR--LFVLKQPVGVVGAITPWNFPLAMITRKVGPAL 209
Cdd:cd07138 83 TLEMGAPITLARAaQVGLGIGHLRAAADALKDF-------EFEERRgnSLVVREPIGVCGLITPWNWPLNQIVLKVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 210 ACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKK 289
Cdd:cd07138 156 AAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 290 VSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPL 369
Cdd:cd07138 236 VALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 370 INEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMT---FYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMAN 446
Cdd:cd07138 316 ASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEGLErgyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIAN 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807201085 447 DTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEvAPFGGVKQSGLGREGSKYGMDEYLEMK 514
Cdd:cd07138 396 DTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPG-APFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
52-516 |
5.24e-164 |
|
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: 473.76 E-value: 5.24e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 52 LIGGKWVDAYDGKTIKVHNPATG-EVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQ 130
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 131 LMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALA 210
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 211 CGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKV 290
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 291 SLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLI 370
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 371 NEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMT----FYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMAN 446
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYekgyFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807201085 447 DTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEV-APFGGVKQSGLG-REGSKYGMDEYLEMKYV 516
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVhLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
89-516 |
8.92e-164 |
|
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: 471.24 E-value: 8.92e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 89 NDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDI 168
Cdd:cd07104 3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 169 IPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLT-ALAAAELSIQAGIPPGVVNVV 247
Cdd:cd07104 83 LPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 248 MGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTC 327
Cdd:cd07104 163 PGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQIC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 328 VCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLgmtFYE 407
Cdd:cd07104 243 MAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEGL---FYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 408 PTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTE- 486
Cdd:cd07104 320 PTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDEp 399
|
410 420 430
....*....|....*....|....*....|
gi 807201085 487 VAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07104 400 HVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
68-516 |
3.00e-158 |
|
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: 458.35 E-value: 3.00e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 68 VHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEV 147
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 148 SYGAGFIEFSAE--EGKRIYGDI-IPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTP 224
Cdd:cd07110 81 DDVAGCFEYYADlaEQLDAKAERaVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 225 LTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFD 304
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 305 DADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDE 384
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 385 ATSKGAKVLVGGKRHSLGMT--FYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIK 462
Cdd:cd07110 321 GKEEGARLLCGGRRPAHLEKgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 807201085 463 RAWRVTEALEYGIVGVN-EGLVSTEvAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07110 401 RCDRVAEALEAGIVWINcSQPCFPQ-APWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
52-516 |
1.75e-157 |
|
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: 456.71 E-value: 1.75e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 52 LIGGKWVDAYDGKtiKVHNPA-TGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQ 130
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 131 LMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALA 210
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 211 CGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKV 290
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 291 SLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLI 370
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 371 NEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMT--FYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDT 448
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEgyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDT 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 449 NAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEV-APFGGVKQSGLG-REGSKYGMDEYLEMKYV 516
Cdd:cd07097 402 EFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYhVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
70-518 |
3.70e-157 |
|
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: 455.36 E-value: 3.70e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 70 NPATGEVITDVPcMGGRETND-AISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEA-IGEV 147
Cdd:cd07115 3 NPATGELIARVA-QASAEDVDaAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 148 SYGAGFIEFSAEEGKRIYGDIIPspLADRRL-FVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLT 226
Cdd:cd07115 82 PRAADTFRYYAGWADKIEGEVIP--VRGPFLnYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 227 ALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDA 306
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 307 DLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEAT 386
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 387 SKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWR 466
Cdd:cd07115 320 EEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 807201085 467 VTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYVCL 518
Cdd:cd07115 400 VAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
50-516 |
7.09e-157 |
|
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: 455.65 E-value: 7.09e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 50 QALIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAF---SSWSKLTAAERSRYLRKWYDLIMAHKE 126
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 127 ELGQLMTLEQGKP--------LKEAIGEVSYGAGFIEfsaeegkRIYGDIIPsplADRRLFVL--KQPVGVVGAITPWNF 196
Cdd:cd07141 88 YLASLETLDNGKPfsksylvdLPGAIKVLRYYAGWAD-------KIHGKTIP---MDGDFFTYtrHEPVGVCGQIIPWNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 197 PLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVG 276
Cdd:cd07141 158 PLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 277 KKLMEGAAAT-VKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMK 355
Cdd:cd07141 238 KLIQQAAGKSnLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 356 VGDGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKF 435
Cdd:cd07141 318 VGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 436 KTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKY 515
Cdd:cd07141 398 KTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKT 477
|
.
gi 807201085 516 V 516
Cdd:cd07141 478 V 478
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
63-514 |
7.52e-157 |
|
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: 454.75 E-value: 7.52e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 63 GKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSS--WSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPL 140
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 141 KEAI-GEVSYGAGFIEFSAEEGKRIYGDIIPSPlADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKP 219
Cdd:cd07112 81 SDALaVDVPSAANTFRWYAEAIDKVYGEVAPTG-PDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 220 SELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAAT-VKKVSLELGGNA 298
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 299 PCIIFDDA-DLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQK 377
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 378 VEYFVDEATSKGAKVLVGGKRHSL--GMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAY 455
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRVLTetGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807201085 456 IFSTNIKRAWRVTEALEYGIVGVN---EGLVSTevaPFGGVKQSGLGREGSKYGMDEYLEMK 514
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNcfdEGDITT---PFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
47-516 |
1.40e-156 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 454.75 E-value: 1.40e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 47 LRSQALIGGKWVDAyDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKE 126
Cdd:PRK13473 1 MQTKLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 127 ELGQLMTLEQGKPLKEAIG-EVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKV 205
Cdd:PRK13473 80 EFARLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 206 GPALACGCTVVIKPSELTPLTALAAAELSIQAgIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAA 285
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 286 TVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVE 365
Cdd:PRK13473 239 SVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 366 QGPLINEAAVQKVEYFVDEATSKG-AKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQM 444
Cdd:PRK13473 319 LGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRW 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807201085 445 ANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:PRK13473 399 ANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
52-501 |
3.53e-156 |
|
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: 453.56 E-value: 3.53e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 52 LIGGKWVDAyDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQL 131
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 132 MTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALAC 211
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 212 GCTVVIKPSELTPLTALAAAELSIQA----GIPPGVVNVVMGNApDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATV 287
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 288 KKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQG 367
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 368 PLINEAAVQKVEYFVDEATSKGAKVLVGGKR--HSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMA 445
Cdd:cd07086 320 PLINQAAVEKYLNAIEIAKSQGGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAIN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 807201085 446 NDTNAGLAAYIFSTNIKRA--WRVTEALEYGIVGVNEGLVSTEV-APFGGVKQSGLGRE 501
Cdd:cd07086 400 NDVPQGLSSSIFTEDLREAfrWLGPKGSDCGIVNVNIPTSGAEIgGAFGGEKETGGGRE 458
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
98-518 |
9.03e-156 |
|
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: 448.60 E-value: 9.03e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 98 AFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRR 177
Cdd:cd06534 6 AFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 178 LFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDA 257
Cdd:cd06534 86 AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 258 LLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQE 337
Cdd:cd06534 166 LLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 338 GIYDKFANAFAkavqnmkvgdgftegveqgplineaavqkveyfvdeatskgakvlvggkrhslgmtfyepTVVTGVNSE 417
Cdd:cd06534 246 SIYDEFVEKLV------------------------------------------------------------TVLVDVDPD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 418 MLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEV-APFGGVKQS 496
Cdd:cd06534 266 MPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPeAPFGGVKNS 345
|
410 420
....*....|....*....|..
gi 807201085 497 GLGREGSKYGMDEYLEMKYVCL 518
Cdd:cd06534 346 GIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
53-516 |
4.02e-155 |
|
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: 451.09 E-value: 4.02e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAF-SSWSKLTAAERSRYLRKWYDLIMAHKEELGQL 131
Cdd:cd07144 12 INNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFeSWWSKVTGEERGELLDKLADLVEKNRDLLAAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 132 MTLEQGKPLKE-AIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRlFVLKQPVGVVGAITPWNFPLAMITRKVGPALA 210
Cdd:cd07144 92 EALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLA-YTLHEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 211 CGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKV 290
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 291 SLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAV-QNMKVGDGFTEGVEQGPL 369
Cdd:cd07144 251 TLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 370 INEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMT---FYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMAN 446
Cdd:cd07144 331 VSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGkgyFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKAN 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 447 DTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07144 411 DTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
69-516 |
7.98e-154 |
|
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: 446.78 E-value: 7.98e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 69 HNPATGEVITDVPCMGGRETNDAISSAYDAFSS--WSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGE 146
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 147 VSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLT 226
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 227 ALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDA 306
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 307 DLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEAT 386
Cdd:cd07118 242 DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 387 SKGAKVLVGGKRHSLGM-TFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAW 465
Cdd:cd07118 322 AEGATLLLGGERLASAAgLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 807201085 466 RVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07118 402 TVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
48-516 |
2.53e-152 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 444.95 E-value: 2.53e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 48 RSQALIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFS-----SWSKLTAAERSRYLRKWYDLIM 122
Cdd:PLN02467 7 RRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnkgkDWARTTGAVRAKYLRAIAAKIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 123 AHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAE--EGKRIYGDI-IPSPLADRRLFVLKQPVGVVGAITPWNFPLA 199
Cdd:PLN02467 87 ERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADlaEALDAKQKApVSLPMETFKGYVLKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 200 MITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKL 279
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 280 MEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDG 359
Cdd:PLN02467 247 MTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 360 FTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKR-HSLGMTFY-EPTVVTGVNSEMLLAKEEVFGPVAPLLKFKT 437
Cdd:PLN02467 327 LEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRpEHLKKGFFiEPTIITDVTTSMQIWREEVFGPVLCVKTFST 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807201085 438 DEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:PLN02467 407 EDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
66-518 |
8.21e-151 |
|
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: 439.18 E-value: 8.21e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 66 IKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIG 145
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 146 EVSYGAGFIEFSAEEGKRIYGDIIPSPLA----DRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSE 221
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDATqgsdNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 222 LTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLmeGAAATVKKVSLELGGNAPCI 301
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 302 IFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYF 381
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 382 VDEATSKGAKVLVGGKRHSlgmTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNI 461
Cdd:cd07094 319 VEEAVEAGARLLCGGERDG---ALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 807201085 462 KRAWRVTEALEYGIVGVNEG-LVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYVCL 518
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSsAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
68-516 |
2.42e-150 |
|
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: 437.91 E-value: 2.42e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 68 VHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAI-GE 146
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 147 VSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLT 226
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 227 ALAAAELsIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDA 306
Cdd:cd07092 161 TLLLAEL-AAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 307 DLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEAt 386
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERA- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 387 SKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWR 466
Cdd:cd07092 319 PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 807201085 467 VTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07092 399 LSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
68-514 |
6.11e-150 |
|
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: 437.06 E-value: 6.11e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 68 VHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWS-KLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKP------- 139
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPvmtaram 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 140 -LKEAIGEVSYGAGFIEFsaEEGKRIYGDIIPSPLADRRLfVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIK 218
Cdd:cd07089 81 qVDGPIGHLRYFADLADS--FPWEFDLPVPALRGGPGRRV-VRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 219 PSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNA 298
Cdd:cd07089 158 PAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 299 PCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKV 378
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 379 EYFVDEATSKGAKVLVGGKR-HSLGMTFY-EPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYI 456
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRpAGLDKGFYvEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 807201085 457 FSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMK 514
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
68-517 |
6.25e-149 |
|
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: 434.42 E-value: 6.25e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 68 VHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEV 147
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 148 SYGAGFIEFSAEEGKRIYGDIIPSPlADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTA 227
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLP-GGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 228 LAAAELSIQAGIPPGVVNVVMGNApDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDAD 307
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 308 LEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEATS 387
Cdd:cd07090 239 LENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 388 KGAKVLVGGKRHSLGM----TFY-EPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIK 462
Cdd:cd07090 319 EGAKVLCGGERVVPEDglenGFYvSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQ 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 807201085 463 RAWRVTEALEYGIVGVNE-GLVSTEVaPFGGVKQSGLGREGSKYGMDEYLEMKYVC 517
Cdd:cd07090 399 RAHRVIAQLQAGTCWINTyNISPVEV-PFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
53-516 |
4.02e-148 |
|
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: 433.49 E-value: 4.02e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAF-SSWS-KLTAAERSRYLRKWYDLIMAHKEELGQ 130
Cdd:cd07143 11 INGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFeTDWGlKVSGSKRGRCLSKLADLMERNLDYLAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 131 LMTLEQGKPLKEAIG-EVSYGAGFIEFSAEEGKRIYGDIIPSPlADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPAL 209
Cdd:cd07143 91 IEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVIETD-IKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 210 ACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAAT-VK 288
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSnLK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 289 KVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGP 368
Cdd:cd07143 250 KVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 369 LINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDT 448
Cdd:cd07143 330 QVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDS 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807201085 449 NAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07143 410 TYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
53-514 |
7.72e-148 |
|
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: 432.00 E-value: 7.72e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSS--WSKLTAAERSRYLRKWYDLIMAHKEELGQ 130
Cdd:cd07139 3 IGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 131 LMTLEQGKPLK-EAIGEVSYGAGFIEFsaeegkriYGDIIPS-PLADRR-------LFVLKQPVGVVGAITPWNFPLAMI 201
Cdd:cd07139 83 LWTAENGMPISwSRRAQGPGPAALLRY--------YAALARDfPFEERRpgsggghVLVRREPVGVVAAIVPWNAPLFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 202 TRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNApDIGDALLASPQVRKITFTGSTKVGKKLME 281
Cdd:cd07139 155 ALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR-EVGEYLVRHPGVDKVSFTGSTAAGRRIAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 282 GAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFT 361
Cdd:cd07139 234 VCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 362 EGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKR--HSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDE 439
Cdd:cd07139 314 PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 807201085 440 EAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNeGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMK 514
Cdd:cd07139 394 DAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETK 467
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
49-516 |
9.48e-147 |
|
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: 429.61 E-value: 9.48e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 49 SQALIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFS--SWSKLTAAERSRYLRKWYDLIMAHKE 126
Cdd:cd07142 4 TKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 127 ELGQLMTLEQGKPLKEA-IGEVSYGAGFIEFSAEEGKRIYGDIIPsplADRRLFV--LKQPVGVVGAITPWNFPLAMITR 203
Cdd:cd07142 84 ELAALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLP---ADGPHHVytLHEPIGVVGQIIPWNFPLLMFAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 204 KVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGA 283
Cdd:cd07142 161 KVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 284 AAT-VKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTE 362
Cdd:cd07142 241 AKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 363 GVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAI 442
Cdd:cd07142 321 GVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807201085 443 QMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
52-514 |
3.26e-146 |
|
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: 428.30 E-value: 3.26e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 52 LIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQL 131
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 132 MTLEQGKPLKE--------AIGEVSYGAGFIEfsAEEG--KRIYGDIIPspladrrlFVLKQPVGVVGAITPWNFPLAMI 201
Cdd:cd07559 84 ETLDNGKPIREtlaadiplAIDHFRYFAGVIR--AQEGslSEIDEDTLS--------YHFHEPLGVVGQIIPWNFPLLMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 202 TRKVGPALACGCTVVIKPSELTPLTALAAAELsIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLME 281
Cdd:cd07559 154 AWKLAPALAAGNTVVLKPASQTPLSILVLMEL-IGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 282 GAAATVKKVSLELGGNAPCIIFDDA-----DLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKV 356
Cdd:cd07559 233 YAAENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 357 GDGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMT----FYEPTVVTGVNSEMLLAKEEVFGPVAPL 432
Cdd:cd07559 313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLdkgyFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 433 LKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLE 512
Cdd:cd07559 393 ITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQ 472
|
..
gi 807201085 513 MK 514
Cdd:cd07559 473 TK 474
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
66-518 |
3.10e-144 |
|
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: 422.15 E-value: 3.10e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 66 IKVHNPATGEVITDVPcmggRETNDAISSAYD-AFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAI 144
Cdd:cd07146 1 LEVRNPYTGEVVGTVP----AGTEEALREALAlAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 145 GEVSYGAGFIEFSAEEGKRIYGDIIPSPLAD----RRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPS 220
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFSCDLTAngkaRKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 221 ELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLmeGAAATVKKVSLELGGNAPC 300
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 301 IIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEY 380
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 381 FVDEATSKGAKVLVGGKRHSlgmTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTN 460
Cdd:cd07146 315 RVEEAIAQGARVLLGNQRQG---ALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 461 IKRAWRVTEALEYGIVGVNEGL-VSTEVAPFGGVKQSGLG-REGSKYGMDEYLEMKYVCL 518
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNEVPgFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
89-509 |
7.19e-143 |
|
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: 418.02 E-value: 7.19e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 89 NDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGkriygdi 168
Cdd:cd07100 2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENA------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 169 iPSPLADRRL-------FVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPP 241
Cdd:cd07100 75 -EAFLADEPIetdagkaYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 242 GVVNVVMGNAPDIgDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFR 321
Cdd:cd07100 154 GVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 322 NTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSL 401
Cdd:cd07100 233 NAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 402 GMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEG 481
Cdd:cd07100 313 PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGM 392
|
410 420
....*....|....*....|....*...
gi 807201085 482 LVSTEVAPFGGVKQSGLGREGSKYGMDE 509
Cdd:cd07100 393 VKSDPRLPFGGVKRSGYGRELGRFGIRE 420
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
55-516 |
1.83e-142 |
|
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: 418.25 E-value: 1.83e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 55 GKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTL 134
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 135 EQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCT 214
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 215 VVIKPSELTPLTA-LAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLE 293
Cdd:cd07151 161 VVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 294 LGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEA 373
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 374 AVQKVEYFVDEATSKGAKVLVGGKRHSLGMtfyEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLA 453
Cdd:cd07151 321 QVDGLLDKIEQAVEEGATLLVGGEAEGNVL---EPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLS 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807201085 454 AYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTE-VAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07151 398 GAVFTSDLERGVQFARRIDAGMTHINDQPVNDEpHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
53-514 |
2.66e-142 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 418.06 E-value: 2.66e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLM 132
Cdd:TIGR01804 2 IDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 133 TLEQGKPLKEAI-GEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRrLFVLKQPVGVVGAITPWNFPLAMITRKVGPALAC 211
Cdd:TIGR01804 82 TLDTGKTLQETIvADMDSGADVFEFFAGLAPALNGEIIPLGGPSF-AYTIREPLGVCVGIGAWNYPLQIASWKIAPALAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 212 GCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVS 291
Cdd:TIGR01804 161 GNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 292 LELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLIN 371
Cdd:TIGR01804 241 MELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLIS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 372 EAAVQKVEYFVDEATSKGAKVLVGGKR---HSLGM-TFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMAND 447
Cdd:TIGR01804 321 AAHRDKVLSYIEKGKAEGATLATGGGRpenVGLQNgFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARAND 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807201085 448 TNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMK 514
Cdd:TIGR01804 401 TEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
87-516 |
2.06e-141 |
|
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: 414.28 E-value: 2.06e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 87 ETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYG 166
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 167 DIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNV 246
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 247 VM---GNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNT 323
Cdd:cd07105 161 VThspEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 324 GQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDgftegVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGK-RHSLG 402
Cdd:cd07105 241 GQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLaDESPS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 403 MTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGL 482
Cdd:cd07105 316 GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMT 395
|
410 420 430
....*....|....*....|....*....|....*
gi 807201085 483 VSTE-VAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07105 396 VHDEpTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
68-516 |
7.89e-140 |
|
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: 411.24 E-value: 7.89e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 68 VHNPATGEVITDVPCMGGRETNDAISSAYDAFSS-WSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGE 146
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 147 VSYGAGFIEFSAEEGKRIYGDIIPsPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLT 226
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 227 ALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDA 306
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 307 DLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGfTEGVEQGPLINEAAVQKVEYFVDEAT 386
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPG-LEDPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 387 SKGAKVLVGGKR---HSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKR 463
Cdd:cd07109 319 ARGARIVAGGRIaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 807201085 464 AWRVTEALEYGIVGVNE----GLVSTevaPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07109 399 ALRVARRLRAGQVFVNNygagGGIEL---PFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
52-514 |
7.24e-138 |
|
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: 406.84 E-value: 7.24e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 52 LIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQL 131
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 132 MTLEQGKPLKE--------AIGEVSYGAGFIEfsAEEGKRIYGDiipsplADRRLFVLKQPVGVVGAITPWNFPLAMITR 203
Cdd:cd07117 84 ETLDNGKPIREtravdiplAADHFRYFAGVIR--AEEGSANMID------EDTLSIVLREPIGVVGQIIPWNFPFLMAAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 204 KVGPALACGCTVVIKPSELTPLTALAAAELsIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGA 283
Cdd:cd07117 156 KLAPALAAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 284 AATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEG 363
Cdd:cd07117 235 AKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 364 VEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMT----FYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDE 439
Cdd:cd07117 315 TQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLdkgfFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTED 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 807201085 440 EAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMK 514
Cdd:cd07117 395 EVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMK 469
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
48-519 |
4.33e-137 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 405.42 E-value: 4.33e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 48 RSQALIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEE 127
Cdd:PRK13252 6 LQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 128 LGQLMTLEQGKPLKEAI-GEVSYGAGFIEFSAEEGKRIYGDIIPSPLAD----RRlfvlkQPVGVVGAITPWNFPLAMIT 202
Cdd:PRK13252 86 LAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSfvytRR-----EPLGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 203 RKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNApDIGDALLASPQVRKITFTGSTKVGKKLMEG 282
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 283 AAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTE 362
Cdd:PRK13252 240 AAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 363 GVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGM----TFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTD 438
Cdd:PRK13252 320 ATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGfangAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 439 EEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNE-GLVSTEvAPFGGVKQSGLGREGSKYGMDEYLEMK--Y 515
Cdd:PRK13252 400 DEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwGESPAE-MPVGGYKQSGIGRENGIATLEHYTQIKsvQ 478
|
....
gi 807201085 516 VCLG 519
Cdd:PRK13252 479 VEMG 482
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
53-516 |
1.05e-136 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 404.97 E-value: 1.05e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFS--SWSKLTAAERSRYLRKWYDLIMAHKEELGQ 130
Cdd:PLN02766 25 INGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 131 LMTLEQGK-PLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPsplADRRL--FVLKQPVGVVGAITPWNFPLAMITRKVGP 207
Cdd:PLN02766 105 LDTIDAGKlFALGKAVDIPAAAGLLRYYAGAADKIHGETLK---MSRQLqgYTLKEPIGVVGHIIPWNFPSTMFFMKVAP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 208 ALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAAT- 286
Cdd:PLN02766 182 ALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSn 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 287 VKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQ 366
Cdd:PLN02766 262 LKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 367 GPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMAN 446
Cdd:PLN02766 342 GPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKAN 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 447 DTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:PLN02766 422 NTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
66-514 |
1.35e-136 |
|
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: 402.78 E-value: 1.35e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 66 IKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIG 145
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 146 EVSYGAGFIEFSAEEGKRIYGDIIP---SPLAD-RRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSE 221
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldiSARGEgRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 222 LTPLTALAAAELSIQAGIPPGVVNVVMGNAPDiGDALLASPQVRKITFTGSTKVGKKLMEGAAAtvKKVSLELGGNAPCI 301
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 302 IFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYF 381
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 382 VDEATSKGAKVLVGGKRHSlgmTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNI 461
Cdd:cd07147 318 VNEAVDAGAKLLTGGKRDG---ALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 807201085 462 KRAWRVTEALEYGIVGVNEglVST---EVAPFGGVKQSGLGREGSKYGMDEYLEMK 514
Cdd:cd07147 395 EKALRAWDELEVGGVVIND--VPTfrvDHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
69-516 |
1.67e-136 |
|
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: 402.37 E-value: 1.67e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 69 HNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVS 148
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 149 YGAGFIEFSAEEGKRIYGD---IIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPL 225
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPrkvPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 226 TALAAAELSIQAGIPPGVVNVVMGNAPdIGDALLASPqVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDD 305
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGA-TGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 306 ADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEA 385
Cdd:cd07099 239 ADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 386 TSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAW 465
Cdd:cd07099 319 VAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAE 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 807201085 466 RVTEALEYGIVGVNEGLVSTEV--APFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07099 399 AIARRLEAGAVSINDVLLTAGIpaLPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
49-516 |
1.08e-135 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 403.42 E-value: 1.08e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 49 SQALIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSS--WSKLTAAERSRYLRKWYDLIMAHKE 126
Cdd:PLN02466 58 TQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 127 ELGQLMTLEQGKPLKEAIG-EVSYGAGFIEFSAEEGKRIYGDIIPSPlADRRLFVLKQPVGVVGAITPWNFPLAMITRKV 205
Cdd:PLN02466 138 ELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPAD-GPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 206 GPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAA- 284
Cdd:PLN02466 217 GPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAk 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 285 ATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFA-NAFAKAVQNMkVGDGFTEG 363
Cdd:PLN02466 297 SNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVeKAKARALKRV-VGDPFKKG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 364 VEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQ 443
Cdd:PLN02466 376 VEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIR 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807201085 444 MANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:PLN02466 456 RANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
32-512 |
3.73e-135 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 401.56 E-value: 3.73e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 32 TDTQSVAAKLSSSGLLRSQALIGGkwVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERS 111
Cdd:PRK09407 2 TTTALPMPAPSALTFERLRRLTAR--VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 112 RYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGfiefsaeeGKRIYGDIIPSPLADRR----------LFVL 181
Cdd:PRK09407 80 AVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVAL--------TARYYARRAPKLLAPRRragalpvltkTTEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 182 KQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLAs 261
Cdd:PRK09407 152 RQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVD- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 262 pQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYD 341
Cdd:PRK09407 231 -NADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 342 KFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGK-RHSLGMTFYEPTVVTGVNSEMLL 420
Cdd:PRK09407 310 EFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKaRPDLGPLFYEPTVLTGVTPDMEL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 421 AKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLV----STEvAPFGGVKQS 496
Cdd:PRK09407 390 AREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAaawgSVD-APMGGMKDS 468
|
490
....*....|....*.
gi 807201085 497 GLGREGSKYGMDEYLE 512
Cdd:PRK09407 469 GLGRRHGAEGLLKYTE 484
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
68-516 |
2.09e-134 |
|
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: 397.50 E-value: 2.09e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 68 VHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLK-EAIGE 146
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 147 VSYGAGFIEFSAEEGKRIYGDIIPspLADRRL-FVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPL 225
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP--FGPDVLtYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 226 TALAAAELsIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDD 305
Cdd:cd07108 159 AVLLLAEI-LAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 306 ADLEVALKGALA-TKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDE 384
Cdd:cd07108 238 ADLDDAVDGAIAgMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 385 ATS-KGAKVLVGGKRHSLGMT----FYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFST 459
Cdd:cd07108 318 GLStSGATVLRGGPLPGEGPLadgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 807201085 460 NIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGM-DEYLEMKYV 516
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMlEHFTQKKTV 455
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
50-505 |
7.96e-134 |
|
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: 396.56 E-value: 7.96e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 50 QALIGGKWVDAyDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSK-LTAAERSRYLRKWYDLIMAHKEEL 128
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 129 GQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVL----KQPVGVVGAITPWNFPLAMITRK 204
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIaqvrREPLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 205 VGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEgaA 284
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK--Q 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 285 ATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGV 364
Cdd:cd07082 240 HPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 365 EQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRhsLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQM 444
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 807201085 445 ANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEglvSTE----VAPFGGVKQSGLGREGSKY 505
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINS---KCQrgpdHFPFLGRKDSGIGTQGIGD 459
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
53-518 |
1.43e-132 |
|
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: 393.35 E-value: 1.43e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAF-SSWSKLTAAERSRYLRKWYDLIMAHKEELGQL 131
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 132 MTLEQGKP--LKEAIgEVSYGAGFIEFSAEEGKRIYGDI----IPSPLADR-RLFVLKQPVGVVGAITPWNFPLAMITRK 204
Cdd:cd07113 84 ETLCSGKSihLSRAF-EVGQSANFLRYFAGWATKINGETlapsIPSMQGERyTAFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 205 VGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNApDIGDALLASPQVRKITFTGSTKVGKKLMEGAA 284
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 285 ATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGV 364
Cdd:cd07113 242 SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 365 EQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQM 444
Cdd:cd07113 322 MFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQL 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807201085 445 ANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYVCL 518
Cdd:cd07113 402 INDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
70-518 |
2.08e-132 |
|
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: 392.09 E-value: 2.08e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 70 NPATGEVITDVPCMGGRETNDAISSAYDAF--SSWSKlTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEV 147
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 148 SYGAGFIEFSAEEGKRIYGDII-PSPlaDRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLT 226
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIePEP--GSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 227 ALAAAELSIQA-GIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDD 305
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 306 ADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEA 385
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 386 TSKGAKVLVGGKRHSLGMT---FYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIK 462
Cdd:cd07120 320 IAAGAEVVLRGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 807201085 463 RAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYVCL 518
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
50-516 |
1.11e-131 |
|
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: 391.47 E-value: 1.11e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 50 QALIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAF--SSWSKLTAAERSRYLRKWYDLIMAHKEE 127
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFenGEWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 128 LGQLMTLEQGK----PLKEAIG----EVSYGAGFIEfsaeegkRIYGDIIPSPLA--DRRL-FVLKQPVGVVGAITPWNF 196
Cdd:cd07140 87 LATIESLDSGAvytlALKTHVGmsiqTFRYFAGWCD-------KIQGKTIPINQArpNRNLtLTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 197 PLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVG 276
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 277 KKLMEGAA-ATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMK 355
Cdd:cd07140 240 KHIMKSCAvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 356 VGDGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKF 435
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 436 KTD--EEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEM 513
Cdd:cd07140 400 DDGdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKT 479
|
...
gi 807201085 514 KYV 516
Cdd:cd07140 480 KTV 482
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
69-512 |
2.94e-129 |
|
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: 383.97 E-value: 2.94e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 69 HNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVs 148
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 149 ygagfieFSAEEGKRIYGDIIPSPLADRR----------LFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIK 218
Cdd:cd07101 80 -------LDVAIVARYYARRAERLLKPRRrrgaipvltrTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 219 PSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLAspQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNA 298
Cdd:cd07101 153 PDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 299 PCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKV 378
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 379 EYFVDEATSKGAKVLVGGK-RHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIF 457
Cdd:cd07101 311 TAHVDDAVAKGATVLAGGRaRPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVW 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 807201085 458 STNIKRAWRVTEALEYGIVGVNEGLVSTEV---APFGGVKQSGLGREGSKYGMDEYLE 512
Cdd:cd07101 391 TRDGARGRRIAARLRAGTVNVNEGYAAAWAsidAPMGGMKDSGLGRRHGAEGLLKYTE 448
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
114-518 |
1.39e-128 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 380.62 E-value: 1.39e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 114 LRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITP 193
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 194 WNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGST 273
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 274 KVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQN 353
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 354 MKVGDGFTEG-VEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPL 432
Cdd:PRK10090 241 VQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 433 LKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLE 512
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQ 400
|
....*.
gi 807201085 513 MKYVCL 518
Cdd:PRK10090 401 TQVVYL 406
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
53-512 |
4.91e-126 |
|
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: 376.74 E-value: 4.91e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLM 132
Cdd:cd07111 26 INGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 133 TLEQGKPLKE--------AIGEVSYGAGFIEFSAEEgkriygdiipspLADRrlfvlkQPVGVVGAITPWNFPLAMITRK 204
Cdd:cd07111 106 SLDNGKPIREsrdcdiplVARHFYHHAGWAQLLDTE------------LAGW------KPVGVVGQIVPWNFPLLMLAWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 205 VGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNApDIGDALLASPQVRKITFTGSTKVGKKLMEGAA 284
Cdd:cd07111 168 ICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 285 ATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGV 364
Cdd:cd07111 247 GTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 365 EQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQM 444
Cdd:cd07111 327 DMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVAL 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807201085 445 ANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLE 512
Cdd:cd07111 407 ANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
50-508 |
2.15e-122 |
|
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: 367.23 E-value: 2.15e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 50 QALIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELG 129
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 130 QLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPlAMITR-KVGPA 208
Cdd:cd07085 82 RLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFP-AMIPLwMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 209 LACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGnAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVK 288
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 289 KVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGP 368
Cdd:cd07085 240 RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 369 LINEAAVQKVEYFVDEATSKGAKVLVGGKRHSlgMTFYE------PTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAI 442
Cdd:cd07085 320 VISPAAKERIEGLIESGVEEGAKLVLDGRGVK--VPGYEngnfvgPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807201085 443 QMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGL-VSTEVAPFGGVKQSGLGrEGSKYGMD 508
Cdd:cd07085 398 AIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIpVPLAFFSFGGWKGSFFG-DLHFYGKD 463
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
74-516 |
2.21e-122 |
|
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: 366.23 E-value: 2.21e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 74 GEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGF 153
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 154 IEFSAEEGKRIYGDIIPSPlADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTA-LAAAE 232
Cdd:cd07152 81 LHEAAGLPTQPQGEILPSA-PGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 233 LSIQAGIPPGVVNVVMGnAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVAL 312
Cdd:cd07152 160 LFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 313 KGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKV 392
Cdd:cd07152 239 SNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 393 LVGGKRHSLgmtFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALE 472
Cdd:cd07152 319 EAGGTYDGL---FYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 807201085 473 YGIVGVNEGLVSTE-VAPFGGVKQSGLG-REGSKYGMDEYLEMKYV 516
Cdd:cd07152 396 TGMLHINDQTVNDEpHNPFGGMGASGNGsRFGGPANWEEFTQWQWV 441
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
68-516 |
8.60e-120 |
|
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: 359.77 E-value: 8.60e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 68 VHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEV 147
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 148 SYGAGFIEFSAEEGKRIYGDIIPSPLADRrLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTA 227
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNL-HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 228 LAAAELsIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDAD 307
Cdd:cd07107 160 LRLAEL-AREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 308 LEVALKGALA-TKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEAT 386
Cdd:cd07107 239 PEAAADAAVAgMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 387 SKGAKVLVGGKR---HSLGMTFY-EPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIK 462
Cdd:cd07107 319 REGARLVTGGGRpegPALEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 807201085 463 RAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07107 399 QAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
52-511 |
7.19e-113 |
|
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: 344.21 E-value: 7.19e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 52 LIGGKWVDAydGKTIKVHNPA-TGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQ 130
Cdd:cd07124 36 VIGGKEVRT--EEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 131 LMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPS-PLADRRLFVlkQPVGVVGAITPWNFPLAMITRKVGPAL 209
Cdd:cd07124 114 WMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMvPGEDNRYVY--RPLGVGAVISPWNFPLAILAGMTTAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 210 ACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAAT--- 286
Cdd:cd07124 192 VTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 287 ---VKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEG 363
Cdd:cd07124 272 qkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 364 VEQGPLINEAAVQKVEYFVDEATSKGaKVLVGGKR--HSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEA 441
Cdd:cd07124 352 VYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVleLAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEA 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807201085 442 IQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEG----LVstEVAPFGGVKQSGLgreGSKYGMDEYL 511
Cdd:cd07124 431 LEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKitgaLV--GRQPFGGFKMSGT---GSKAGGPDYL 499
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
47-514 |
5.32e-109 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 333.40 E-value: 5.32e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 47 LRSQALIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSS--WSKLTAAERSRYLRKWYDLIMAH 124
Cdd:PRK09847 18 IENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 125 KEELGQLMTLEQGKPLKEAI-GEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVlKQPVGVVGAITPWNFPLAMITR 203
Cdd:PRK09847 98 AEELALLETLDTGKPIRHSLrDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIV-REPVGVIAAIVPWNFPLLLTCW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 204 KVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGA 283
Cdd:PRK09847 177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 284 A-ATVKKVSLELGGNAPCIIFDDA-DLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFT 361
Cdd:PRK09847 257 GdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 362 EGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGgkRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEA 441
Cdd:PRK09847 337 PATTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807201085 442 IQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMK 514
Cdd:PRK09847 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
69-517 |
4.66e-107 |
|
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: 327.72 E-value: 4.66e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 69 HNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEA-IGEV 147
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 148 SYGAGFIEFSAEEGKRIygdIIPSPLADRRLFVLK------QPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSE 221
Cdd:cd07098 81 LVTCEKIRWTLKHGEKA---LRPESRPGGLLMFYKrarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 222 LT-----PLTALAAAELSIqAGIPPGVVNVVMGnAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGG 296
Cdd:cd07098 158 QVawssgFFLSIIRECLAA-CGHDPDLVQLVTC-LPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 297 NAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQ 376
Cdd:cd07098 236 KDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 377 KVEYFVDEATSKGAKVLVGGKRHSLGM----TFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGL 452
Cdd:cd07098 316 RLEELVADAVEKGARLLAGGKRYPHPEypqgHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807201085 453 AAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVA--PFGGVKQSGLGREGSKYGMDEYLEMKYVC 517
Cdd:cd07098 396 GASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
69-508 |
6.70e-107 |
|
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: 326.51 E-value: 6.70e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 69 HNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVS 148
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 149 YGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTAL 228
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 229 AAAELSIQAGIPPGVVNVVMGNAPDiGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADL 308
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 309 EVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEATSK 388
Cdd:cd07102 240 DAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 389 GAKVLVGGKRHSL---GMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAW 465
Cdd:cd07102 320 GARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAE 399
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 807201085 466 RVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMD 508
Cdd:cd07102 400 ALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYD 442
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
54-503 |
2.59e-106 |
|
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: 326.09 E-value: 2.59e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 54 GGKWVDAydGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMT 133
Cdd:cd07130 4 DGEWGGG--GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 134 LEQGKPLKEAIGEVSYgagFI---EFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLA------MItrk 204
Cdd:cd07130 82 LEMGKILPEGLGEVQE---MIdicDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAvwgwnaAI--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 205 vgpALACGCTVVIKPSELTPLTALAAAELSIQA----GIPPGVVNVVMGNApDIGDALLASPQVRKITFTGSTKVGKKLM 280
Cdd:cd07130 156 ---ALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGA-DVGEALVKDPRVPLVSFTGSTAVGRQVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 281 EGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGF 360
Cdd:cd07130 232 QAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 361 TEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGvNSEMLLAKEEVFGPVAPLLKFKTDEE 440
Cdd:cd07130 312 DDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEG-LSDAPIVKEETFAPILYVLKFDTLEE 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807201085 441 AIQMANDTNAGLAAYIFSTNIKRAWRVTEAL--EYGIVGVNEGLVSTEV-APFGGVKQSGLGRE-GS 503
Cdd:cd07130 391 AIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSGAEIgGAFGGEKETGGGREsGS 457
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
53-514 |
3.78e-105 |
|
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: 323.25 E-value: 3.78e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLM 132
Cdd:cd07116 5 IGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 133 TLEQGKPLKE--------AIGEVSYGAGFIEfsAEEG--KRIYGDIIPspladrrlFVLKQPVGVVGAITPWNFPLAMIT 202
Cdd:cd07116 85 TWDNGKPVREtlaadiplAIDHFRYFAGCIR--AQEGsiSEIDENTVA--------YHFHEPLGVVGQIIPWNFPLLMAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 203 RKVGPALACGCTVVIKPSELTPLTALAAAELsIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEG 282
Cdd:cd07116 155 WKLAPALAAGNCVVLKPAEQTPASILVLMEL-IGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 283 AAATVKKVSLELGGNAPCIIF------DDADLEVALKGALATKFrNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKV 356
Cdd:cd07116 234 ASENIIPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 357 GDGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMT----FYEPTVVTGVNSeMLLAKEEVFGPVAPL 432
Cdd:cd07116 313 GNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKGGNK-MRIFQEEIFGPVLAV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 433 LKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLE 512
Cdd:cd07116 392 TTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQ 471
|
..
gi 807201085 513 MK 514
Cdd:cd07116 472 TK 473
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
70-519 |
5.22e-105 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 322.07 E-value: 5.22e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 70 NPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSY 149
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 150 GAGFIEFSAEEGKRIYGDIiPSPLAD---RRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLT 226
Cdd:PRK09406 87 CAKGFRYYAEHAEALLADE-PADAAAvgaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 227 ALAAAELSIQAGIPPGVVNVVMGNAPDIgDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDA 306
Cdd:PRK09406 166 ALYLADLFRRAGFPDGCFQTLLVGSGAV-EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 307 DLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEAT 386
Cdd:PRK09406 245 DLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 387 SKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWR 466
Cdd:PRK09406 325 AAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQER 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 807201085 467 VTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYVCLG 519
Cdd:PRK09406 405 FIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
49-516 |
9.79e-105 |
|
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: 322.10 E-value: 9.79e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 49 SQALIGGKWVDAYDGkTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAF--SSWSKLTAAeRSRYLRKWYDLIMAHKE 126
Cdd:TIGR04284 1 SRLLIDGKLVAGSAG-TFPTVNPATEEVLGVAADATAADMDAAIAAARRAFdeTDWSRDTAL-RVRCLRQLRDALRAHVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 127 ELGQLMTLEQGKP--------LKEAIGEVSYGAGFIEfsAEEGKRIYGDIIPSPLADRRLfVLKQPVGVVGAITPWNFPL 198
Cdd:TIGR04284 79 ELRELTIAEVGAPrmltagaqLEGPVDDLGFAADLAE--SYAWTTDLGVASPMGIPTRRT-LRREAVGVVGAITPWNFPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 199 AMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQ-AGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGK 277
Cdd:TIGR04284 156 QINLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIAEhTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 278 KLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVG 357
Cdd:TIGR04284 236 AVMADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 358 DGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKR---HSLGMtFYEPTVVTGVNSEMLLAKEEVFGPVAPLLK 434
Cdd:TIGR04284 316 DPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGRpadRDRGF-FVEPTVIAGLDNNARVAREEIFGPVLTVIA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 435 FKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMK 514
Cdd:TIGR04284 395 HDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETK 474
|
..
gi 807201085 515 YV 516
Cdd:TIGR04284 475 LI 476
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
70-516 |
9.53e-95 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 295.62 E-value: 9.53e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 70 NPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSY 149
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 150 GAGFIEFSAEEGkriygdiiPSPLADRRLFVLKQ-------PVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSEL 222
Cdd:PRK13968 93 SANLCDWYAEHG--------PAMLKAEPTLVENQqavieyrPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 223 TPLTALAAAELSIQAGIPPGVVNVVmgNAPDIG-DALLASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCI 301
Cdd:PRK13968 165 VMGCAQLIAQVFKDAGIPQGVYGWL--NADNDGvSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 302 IFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYF 381
Cdd:PRK13968 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 382 VDEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNI 461
Cdd:PRK13968 323 VEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDE 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 807201085 462 KRAWRVTEALEYGIVGVNEGLVSTEVAPFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:PRK13968 403 TQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
52-511 |
6.27e-93 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 292.61 E-value: 6.27e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 52 LIGGKWVDAYDgkTIKVHNPA-TGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQ 130
Cdd:PRK03137 40 IIGGERITTED--KIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 131 LMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRiYGDiiPSPLADR-----RLFVlkQPVGVVGAITPWNFPLAMITRKV 205
Cdd:PRK03137 118 WLVKEAGKPWAEADADTAEAIDFLEYYARQMLK-LAD--GKPVESRpgehnRYFY--IPLGVGVVISPWNFPFAIMAGMT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 206 GPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAA 285
Cdd:PRK03137 193 LAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 286 T------VKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDG 359
Cdd:PRK03137 273 VqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 360 fTEGVEQGPLINEAAVQKVEYFVdEATSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDE 439
Cdd:PRK03137 353 -EDNAYMGPVINQASFDKIMSYI-EIGKEEGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFD 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807201085 440 EAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVA--PFGGVKQSGlgrEGSKYGMDEYL 511
Cdd:PRK03137 431 HALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGyhPFGGFNMSG---TDSKAGGPDYL 501
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
66-509 |
9.54e-92 |
|
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: 287.78 E-value: 9.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 66 IKVHNPATGEVITDVPCMGGRETNDAISSAYDAF---SSWskLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKE 142
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFldrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 143 AIGEVSYGAGFIEFSAEEGKRIYGDIIPSPL----ADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIK 218
Cdd:cd07148 79 AKVEVTRAIDGVELAADELGQLGGREIPMGLtpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 219 PSELTPLTALAAAELSIQAGIPPGVVNVVMGNApDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKkVSLELGGNA 298
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCEN-AVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGTR-CALEHGGAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 299 PCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKV 378
Cdd:cd07148 237 PVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 379 EYFVDEATSKGAKVLVGGKRhsLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFS 458
Cdd:cd07148 317 EEWVNEAVAAGARLLCGGKR--LSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 807201085 459 TNIKRAWRVTEALEYGIVGVNEGLV-STEVAPFGGVKQSGLGREGSKYGMDE 509
Cdd:cd07148 395 KDLDVALKAVRRLDATAVMVNDHTAfRVDWMPFAGRRQSGYGTGGIPYTMHD 446
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
89-508 |
1.28e-88 |
|
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: 278.77 E-value: 1.28e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 89 NDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDi 168
Cdd:cd07095 3 DAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTGE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 169 IPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVM 248
Cdd:cd07095 82 RATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 249 GnAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKV-SLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTC 327
Cdd:cd07095 162 G-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKIlALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 328 VCANRILVQEGIY-DKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFY 406
Cdd:cd07095 241 TCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 407 EPTV--VTGVNSemlLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTN---IKRAWRVTEAleyGIVGVNE- 480
Cdd:cd07095 321 SPGIidVTDAAD---VPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDealFERFLARIRA---GIVNWNRp 394
|
410 420 430
....*....|....*....|....*....|
gi 807201085 481 --GLVSTevAPFGGVKQSGLGREGSKYGMD 508
Cdd:cd07095 395 ttGASST--APFGGVGLSGNHRPSAYYAAD 422
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
52-516 |
1.21e-86 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 275.22 E-value: 1.21e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 52 LIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQL 131
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 132 MTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPlAMITRKVGP-ALA 210
Cdd:TIGR01722 84 ITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFP-AMIPLWMFPiAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 211 CGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIgDALLASPQVRKITFTGSTKVGKKLMEGAAATVKKV 290
Cdd:TIGR01722 163 CGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAV-DRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 291 SLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVcANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLI 370
Cdd:TIGR01722 242 QALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCM-AISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 371 NEAAVQKVEYFVDEATSKGAKVLVGG-----KRHSLGmTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMA 445
Cdd:TIGR01722 321 TPQAKDRVASLIAGGAAEGAEVLLDGrgykvDGYEEG-NWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807201085 446 NDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGL-VSTEVAPFGGVKQSGLGREG--SKYGMDEYLEMKYV 516
Cdd:TIGR01722 400 NASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIpVPLPYFSFTGWKDSFFGDHHiyGKQGTHFYTRGKTV 473
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
53-516 |
2.15e-83 |
|
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: 267.52 E-value: 2.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVDAYDGKTIkVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLM 132
Cdd:cd07083 23 IGGEWVDTKERMVS-VSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 133 TLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGD---IIPSPLADRRLFVlkQPVGVVGAITPWNFPLAMITRKVGPAL 209
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPaveVVPYPGEDNESFY--VGLGAGVVISPWNFPVAIFTGMIVAPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 210 ACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAA----- 284
Cdd:cd07083 180 AVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAArlapg 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 285 -ATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEG 363
Cdd:cd07083 260 qTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 364 VEQGPLINEAAVQKVEYFVDEATSKGaKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDE--EA 441
Cdd:cd07083 340 TDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEA 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807201085 442 IQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVA--PFGGVKQSGLG-REGSKYGMDEYLEMKYV 516
Cdd:cd07083 419 LEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGvqPFGGFKLSGTNaKTGGPHYLRRFLEMKAV 496
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
52-511 |
5.24e-83 |
|
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: 266.73 E-value: 5.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 52 LIGGKWVDAyDGKTIKVhNPA-TGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQ 130
Cdd:TIGR01237 36 VINGERVET-ENKIVSI-NPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 131 LMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALA 210
Cdd:TIGR01237 114 LLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 211 CGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAAT---- 286
Cdd:TIGR01237 194 TGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVqpgq 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 287 --VKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGV 364
Cdd:TIGR01237 274 khLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 365 EQGPLINEAAVQKVEYFVDEATSKGaKVLVGGKRHSLGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQM 444
Cdd:TIGR01237 354 YVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEI 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807201085 445 ANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVA--PFGGVKQSGLgreGSKYGMDEYL 511
Cdd:TIGR01237 433 ANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGyqPFGGFKMSGT---DSKAGGPDYL 498
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
110-509 |
1.63e-80 |
|
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: 257.45 E-value: 1.63e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 110 RSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEA-IGEVSYGAGFIEFSAE------EGKRIYgdiIPSPLADRRLFVLK 182
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAyLTEIAVVLGEIDHALKhlkkwmKPRRVS---VPLLLQPAKAYVIP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 183 QPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELsIQAGIPPGVVNVVMGnAPDIGDALLASP 262
Cdd:cd07087 99 EPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKL-IPKYFDPEAVAVVEG-GVEVATALLAEP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 263 qVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDK 342
Cdd:cd07087 177 -FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 343 FANAFAKAVQNMkvgdgFTEGVEQ----GPLINEAAVQKVEYFVDeatskGAKVLVGGKRHSLGMTFyEPTVVTGVNSEM 418
Cdd:cd07087 256 LIEELKKAIKEF-----YGEDPKEspdyGRIINERHFDRLASLLD-----DGKVVIGGQVDKEERYI-APTILDDVSPDS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 419 LLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGL--VSTEVAPFGGVKQS 496
Cdd:cd07087 325 PLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLlhAAIPNLPFGGVGNS 404
|
410
....*....|...
gi 807201085 497 GLGREGSKYGMDE 509
Cdd:cd07087 405 GMGAYHGKAGFDT 417
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
53-508 |
8.48e-80 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 257.58 E-value: 8.48e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVdAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLM 132
Cdd:PRK09457 5 INGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 133 TLEQGKPLKEAIGEVSYGAGFIEFSAeegkRIYGDIIP---SPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPAL 209
Cdd:PRK09457 84 ARETGKPLWEAATEVTAMINKIAISI----QAYHERTGekrSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 210 ACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGnAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATVKK 289
Cdd:PRK09457 160 LAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 290 V-SLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIY-DKFANAFAKAVQNMKVGDGFTEgvEQ- 366
Cdd:PRK09457 239 IlALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDAE--PQp 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 367 --GPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTV--VTGVNSemlLAKEEVFGPVAPLLKFKTDEEAI 442
Cdd:PRK09457 317 fmGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIidVTGVAE---LPDEEYFGPLLQVVRYDDFDEAI 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807201085 443 QMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNE---GLVSTevAPFGGVKQSGLGREGSKYGMD 508
Cdd:PRK09457 394 RLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKpltGASSA--APFGGVGASGNHRPSAYYAAD 460
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
52-499 |
4.09e-79 |
|
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: 256.74 E-value: 4.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 52 LIGGKwvDAYDGKTIKVHNPATGEVITdvpcmgGR-------ETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAH 124
Cdd:cd07125 36 IINGE--ETETGEGAPVIDPADHERTI------GEvsladaeDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEAN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 125 KEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRK 204
Cdd:cd07125 108 RGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 205 VGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKK----LM 280
Cdd:cd07125 188 IAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLinraLA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 281 EGAAATVkKVSLELGG-NApcIIFDD-ADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGD 358
Cdd:cd07125 268 ERDGPIL-PLIAETGGkNA--MIVDStALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 359 GFTEGVEQGPLINEAAVQKVEYFVDEAtSKGAKVLVGGKRHSLGMTFYEPTVVTGVNSEMLlaKEEVFGPVAPLLKFKTD 438
Cdd:cd07125 345 PWDLSTDVGPLIDKPAGKLLRAHTELM-RGEAWLIAPAPLDDGNGYFVAPGIIEIVGIFDL--TTEVFGPILHVIRFKAE 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 807201085 439 --EEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVS--TEVAPFGGVKQSGLG 499
Cdd:cd07125 422 dlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGaiVGRQPFGGWGLSGTG 486
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
91-510 |
1.53e-75 |
|
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: 244.82 E-value: 1.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 91 AISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAI-GEVSYGAGFIEFSAE------EGKR 163
Cdd:cd07135 10 IHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKnlkkwaKDEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 164 IYGDIIPSPLAdrRLFVLKQPVGVVGAITPWNFPLaMITrkVGP---ALACGCTVVIKPSELTPLTALAAAELsIQAGIP 240
Cdd:cd07135 90 VKDGPLAFMFG--KPRIRKEPLGVVLIIGPWNYPV-LLA--LSPlvgAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 241 PGVVNVVMGNAPDIGdALLASPqVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKF 320
Cdd:cd07135 164 PDAFQVVQGGVPETT-ALLEQK-FDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 321 RNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMkVGDGFTEGVEQGPLINEAAVQKVEYFVDeaTSKGaKVLVGGKRhS 400
Cdd:cd07135 242 GNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEF-YPGGANASPDYTRIVNPRHFNRLKSLLD--TTKG-KVVIGGEM-D 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 401 LGMTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNE 480
Cdd:cd07135 317 EATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVIND 396
|
410 420 430
....*....|....*....|....*....|..
gi 807201085 481 GL--VSTEVAPFGGVKQSGLGREGSKYGMDEY 510
Cdd:cd07135 397 TLihVGVDNAPFGGVGDSGYGAYHGKYGFDTF 428
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
102-506 |
4.67e-74 |
|
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: 240.98 E-value: 4.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 102 WSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEA--------IGEVSYGAGFIEfSAEEGKRIygdiiPSPL 173
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVdlteilpvLSEINHAIKHLK-KWMKPKRV-----RTPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 174 --ADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELsIQAGIPPGVVNVVMGNA 251
Cdd:cd07134 88 llFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKI-IREAFDEDEVAVFEGDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 252 pDIGDALLASPqVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCAN 331
Cdd:cd07134 167 -EVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 332 RILVQEGIYDKFANAFAKAVQNMKvgdGFTEGVEQGP----LINEAAVQKVEYFVDEATSKGAKVLVGGKrHSLGMTFYE 407
Cdd:cd07134 245 YVFVHESVKDAFVEHLKAEIEKFY---GKDAARKASPdlarIVNDRHFDRLKGLLDDAVAKGAKVEFGGQ-FDAAQRYIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 408 PTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVstEV 487
Cdd:cd07134 321 PTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVL--HF 398
|
410 420
....*....|....*....|...
gi 807201085 488 A----PFGGVKQSGLGREGSKYG 506
Cdd:cd07134 399 LnpnlPFGGVNNSGIGSYHGVYG 421
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
52-502 |
6.00e-73 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 240.04 E-value: 6.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 52 LIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQL 131
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 132 MTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIY--GDIIPS---PLADRRLFVL--KQPVGVVGAITPWNFPLAMITRK 204
Cdd:PLN00412 99 LVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILgeGKFLVSdsfPGNERNKYCLtsKIPLGVVLAIPPFNYPVNLAVSK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 205 VGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTG---STKVGKKlme 281
Cdd:PLN00412 179 IAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGgdtGIAISKK--- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 282 gaaATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGfT 361
Cdd:PLN00412 256 ---AGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-E 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 362 EGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSlgmTFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEA 441
Cdd:PLN00412 332 DDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREG---NLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEG 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807201085 442 IQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLV-STEVAPFGGVKQSGLGREG 502
Cdd:PLN00412 409 IHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPArGPDHFPFQGLKDSGIGSQG 470
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
110-508 |
1.54e-71 |
|
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: 234.71 E-value: 1.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 110 RSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEA-IGEVSYgagfiefsaeegkrIYGDI---------------IPSPL 173
Cdd:cd07136 22 RIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAyMTEIGF--------------VLSEInyaikhlkkwmkpkrVKTPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 174 AD--RRLFVLKQPVGVVGAITPWNFPLAMItrkVGP---ALACGCTVVIKPSELTPLTALAAAELsIQAGIPPGVVNVVM 248
Cdd:cd07136 88 LNfpSKSYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 249 GNApDIGDALLASPqVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCV 328
Cdd:cd07136 164 GGV-EENQELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 329 CANRILVQEGIYDKFANAFAKAVQNMKvGDGFTEGVEQGPLINEAAVQKVEYFVDEatskgAKVLVGGK--RHSLgmtFY 406
Cdd:cd07136 242 APDYVLVHESVKEKFIKELKEEIKKFY-GEDPLESPDYGRIINEKHFDRLAGLLDN-----GKIVFGGNtdRETL---YI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 407 EPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGL--VS 484
Cdd:cd07136 313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTImhLA 392
|
410 420
....*....|....*....|....
gi 807201085 485 TEVAPFGGVKQSGLGREGSKYGMD 508
Cdd:cd07136 393 NPYLPFGGVGNSGMGSYHGKYSFD 416
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
51-511 |
4.51e-71 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 235.50 E-value: 4.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 51 ALIGGKWvdAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQ 130
Cdd:PLN02315 23 CYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 131 LMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAMITRKVGPALA 210
Cdd:PLN02315 101 LVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 211 CGCTVVIKPSELTPLTALAA----AELSIQAGIPPGVVNVVMGNApDIGDALLASPQVRKITFTGSTKVGKKLMEGAAAT 286
Cdd:PLN02315 181 CGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCGGA-EIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 287 VKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQ 366
Cdd:PLN02315 260 FGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 367 GPLINEAAVQKVEYFVDEATSKGAKVLVGGKRHSLGMTFYEPTVVTgVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMAN 446
Cdd:PLN02315 340 GPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINN 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807201085 447 DTNAGLAAYIFSTN--IKRAWRVTEALEYGIVGVNEGLVSTEV-APFGGVKQSGLGREGSKYGMDEYL 511
Cdd:PLN02315 419 SVPQGLSSSIFTRNpeTIFKWIGPLGSDCGIVNVNIPTNGAEIgGAFGGEKATGGGREAGSDSWKQYM 486
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
179-521 |
5.29e-69 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 229.53 E-value: 5.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 179 FVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELsIQAGIPPGVVNVVMGNAPDIgDAL 258
Cdd:PTZ00381 104 YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL-LTKYLDPSYVRVIEGGVEVT-TEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 259 LASPqVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEG 338
Cdd:PTZ00381 182 LKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 339 IYDKFANAFAKAVQNMkVGDGFTEGVEQGPLINEAAVQKVEYFVDEatsKGAKVLVGGKrHSLGMTFYEPTVVTGVNSEM 418
Cdd:PTZ00381 261 IKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE-VDIENKYVAPTIIVNPDLDS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 419 LLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGL--VSTEVAPFGGVKQS 496
Cdd:PTZ00381 336 PLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVfhLLNPNLPFGGVGNS 415
|
330 340
....*....|....*....|....*
gi 807201085 497 GLGREGSKYGMDEYLEMKYVCLGSM 521
Cdd:PTZ00381 416 GMGAYHGKYGFDTFSHPKPVLNKST 440
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
180-516 |
8.37e-69 |
|
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: 227.37 E-value: 8.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 180 VLKQPVGVVGAITPWNFPLaMITrkVGP---ALACGCTVVIKPSELTPLTALAAAELsIQAGIPPGVVNVVMGnAPDIGD 256
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPL-YLA--LGPliaALAAGNRVMIKPSEFTPRTSALLAEL-LAEYFDEDEVAVVTG-GADVAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 257 ALLASPqVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQ 336
Cdd:cd07133 172 AFSSLP-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVP 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 337 EGIYDKFANAFAKAVQNMkvgdgFTEGVEQ---GPLINEAAVQKVEYFVDEATSKGAKVL---VGGKRHSLGMTFyEPTV 410
Cdd:cd07133 251 EDKLEEFVAAAKAAVAKM-----YPTLADNpdyTSIINERHYARLQGLLEDARAKGARVIelnPAGEDFAATRKL-PPTL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 411 VTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGL--VSTEVA 488
Cdd:cd07133 325 VLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLlhVAQDDL 404
|
330 340
....*....|....*....|....*...
gi 807201085 489 PFGGVKQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07133 405 PFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
29-516 |
1.11e-65 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 223.47 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 29 LMTTDTQSVAAKLSSsgllRSQALIGGKWVDAYDGKTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAA 108
Cdd:PLN02419 98 LSTSPEQSTQPQMPP----RVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPIT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 109 ERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPVGVV 188
Cdd:PLN02419 174 TRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVC 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 189 GAITPWNFPlAMITRKVGP-ALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNApDIGDALLASPQVRKI 267
Cdd:PLN02419 254 AGICPFNFP-AMIPLWMFPvAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTN-DTVNAICDDEDIRAV 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 268 TFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRIlVQEGIYDKFANAF 347
Cdd:PLN02419 332 SFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV-VFVGDAKSWEDKL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 348 AKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEATSKGAKVLVGGKR-----HSLGmTFYEPTVVTGVNSEMLLAK 422
Cdd:PLN02419 411 VERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpgYEKG-NFIGPTILSGVTPDMECYK 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 423 EEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGL-VSTEVAPFGGVKQSGLGRE 501
Cdd:PLN02419 490 EEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIpVPLPFFSFTGNKASFAGDL 569
|
490
....*....|....*..
gi 807201085 502 G--SKYGMDEYLEMKYV 516
Cdd:PLN02419 570 NfyGKAGVDFFTQIKLV 586
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
35-511 |
1.79e-60 |
|
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: 207.07 E-value: 1.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 35 QSVAAKLSSSGLLRSQAL--IGGKWVDayDGKTIKVHNPATGEVIT-DVPCMGGRETNDAISSAYDAFSSWSKLTAAERS 111
Cdd:TIGR01238 22 KPLEAQIHAWADKTWQAApiIGHSYKA--DGEAQPVTNPADRRDIVgQVFHANLAHVQAAIDSAQQAFPTWNATPAKERA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 112 RYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKriygDIIPSPLAdrrlfvlkQPVGVVGAI 191
Cdd:TIGR01238 100 AKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVR----DVLGEFSV--------ESRGVFVCI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 192 TPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTG 271
Cdd:TIGR01238 168 SPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 272 STKVG----KKLMEGAAATVKKVSlELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCvCANRIL-VQEGIYDKFANA 346
Cdd:TIGR01238 248 STEVAqlinQTLAQREDAPVPLIA-ETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRC-SALRVLcVQEDVADRVLTM 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 347 FAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEATSKG---AKVLVGGKRHSLGMTFYEPTVVTGVNSEMLlaKE 423
Cdd:TIGR01238 326 IQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFELDDIAEL--SE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 424 EVFGPVAPLLKFKTDE--EAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVA--PFGGvkqSGLG 499
Cdd:TIGR01238 404 EVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGG---QGLS 480
|
490
....*....|..
gi 807201085 500 REGSKYGMDEYL 511
Cdd:TIGR01238 481 GTGPKAGGPHYL 492
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
90-508 |
6.73e-60 |
|
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: 203.99 E-value: 6.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 90 DAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEA-IGEVSYGAGFIEFSAEEGKRIYGDI 168
Cdd:cd07132 2 EAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAvLSEILLVKNEIKYAISNLPEWMKPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 169 -IPSPLADR--RLFVLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELsIQAGIPPGVVN 245
Cdd:cd07132 82 pVKKNLATLldDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-IPKYLDKECYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 246 VVMGNAPDIGDALlaspQVR--KITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNT 323
Cdd:cd07132 161 VVLGGVEETTELL----KQRfdYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 324 GQTCVCANRILVQEGIYDKFANAFAKAVQNMkVGDGFTEGVEQGPLINEAAVQKVEYFVdeatsKGAKVLVGGkRHSLGM 403
Cdd:cd07132 237 GQTCIAPDYVLCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVAIGG-QTDEKE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 404 TFYEPTVVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLV 483
Cdd:cd07132 310 RYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIM 389
|
410 420
....*....|....*....|....*..
gi 807201085 484 --STEVAPFGGVKQSGLGREGSKYGMD 508
Cdd:cd07132 390 hyTLDSLPFGGVGNSGMGAYHGKYSFD 416
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
52-511 |
3.49e-54 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 196.96 E-value: 3.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 52 LIGGkwvdayDGKTIKVHNPA-TGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQ 130
Cdd:PRK11904 556 IING------EGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 131 LMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGD--IIPSPLA-DRRLFVlkQPVGVVGAITPWNFPLAMITRKVGP 207
Cdd:PRK11904 630 LCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGApeKLPGPTGeSNELRL--HGRGVFVCISPWNFPLAIFLGQVAA 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 208 ALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKL------ME 281
Cdd:PRK11904 708 ALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInrtlaaRD 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 282 GAAatvkkVSL--ELGG-NApcIIFDD-ADLEVALKGALATKFRNTGQTCvCANRIL-VQEGIYDKFANAFAKAVQNMKV 356
Cdd:PRK11904 788 GPI-----VPLiaETGGqNA--MIVDStALPEQVVDDVVTSAFRSAGQRC-SALRVLfVQEDIADRVIEMLKGAMAELKV 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 357 GDGFTEGVEQGPLINEAAVQKVEYFVdEATSKGAKVLVGGKRHSLGM--TFYEPTVVTGVNSEMLlaKEEVFGPVAPLLK 434
Cdd:PRK11904 860 GDPRLLSTDVGPVIDAEAKANLDAHI-ERMKREARLLAQLPLPAGTEngHFVAPTAFEIDSISQL--EREVFGPILHVIR 936
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 435 FKTDE--EAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNE---GLVsTEVAPFGGvkqSGLGREGSKYGMDE 509
Cdd:PRK11904 937 YKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRnqiGAV-VGVQPFGG---QGLSGTGPKAGGPH 1012
|
..
gi 807201085 510 YL 511
Cdd:PRK11904 1013 YL 1014
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
59-499 |
6.09e-54 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 196.62 E-value: 6.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 59 DAYDGKTIKVHNPA-TGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQG 137
Cdd:PRK11905 562 GDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 138 KPLKEAIGEVSYGAGFIEFSAEEGKRIYGDIIPSPLadrrlfvlkqpvGVVGAITPWNFPLAMITRKVGPALACGCTVVI 217
Cdd:PRK11905 642 KTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPL------------GPVVCISPWNFPLAIFTGQIAAALVAGNTVLA 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 218 KPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGK---KLMegAAATVKKVSL-- 292
Cdd:PRK11905 710 KPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARliqRTL--AKRSGPPVPLia 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 293 ELGG-NApcIIFDDADL-EVALKGALATKFRNTGQTCvCANRIL-VQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPL 369
Cdd:PRK11905 788 ETGGqNA--MIVDSSALpEQVVADVIASAFDSAGQRC-SALRVLcLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPV 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 370 INEAAVQKVEYFVDEATSKGAKVlvggKRHSLGM-----TFYEPTV--VTGVnSEMllaKEEVFGPVAPLLKFKTDE--- 439
Cdd:PRK11905 865 IDAEAQANIEAHIEAMRAAGRLV----HQLPLPAetekgTFVAPTLieIDSI-SDL---EREVFGPVLHVVRFKADEldr 936
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807201085 440 --EAIqmaNDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVA--PFGGVKQSGLG 499
Cdd:PRK11905 937 viDDI---NATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGvqPFGGEGLSGTG 997
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
180-516 |
1.07e-53 |
|
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: 187.23 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 180 VLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELsIQAGIPPGVVNVVMGnAPDIGDALL 259
Cdd:cd07137 97 IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYLDTKAIKVIEG-GVPETTALL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 260 ASpQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKF-RNTGQTCVCANRILVQEG 338
Cdd:cd07137 175 EQ-KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEES 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 339 iydkFANAFAKAVQNMK---VGDGFTEGVEQGPLINEAAVQKVEYFVDEaTSKGAKVLVGGKRHSLGMtFYEPTVVTGVN 415
Cdd:cd07137 254 ----FAPTLIDALKNTLekfFGENPKESKDLSRIVNSHHFQRLSRLLDD-PSVADKIVHGGERDEKNL-YIEPTILLDPP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 416 SEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVA--PFGGV 493
Cdd:cd07137 328 LDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDtlPFGGV 407
|
330 340
....*....|....*....|...
gi 807201085 494 KQSGLGREGSKYGMDEYLEMKYV 516
Cdd:cd07137 408 GESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
51-499 |
1.24e-50 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 186.68 E-value: 1.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 51 ALIGGKwvdAYDGKTIKVHNPA-TGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELG 129
Cdd:COG4230 560 PLIAGE---AASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELM 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 130 QLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGKRIYGDiiPSPLadrrlfvlkQPVGVVGAITPWNFPLAMITRKVGPAL 209
Cdd:COG4230 637 ALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAA--PTVL---------RGRGVFVCISPWNFPLAIFTGQVAAAL 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 210 ACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGK----KLmegAAA 285
Cdd:COG4230 706 AAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARlinrTL---AAR 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 286 TVKKVSL--ELGG-NApcIIFDD-ADLEVALKGALATKFRNTGQTCvCANRIL-VQEGIYDKFANAFAKAVQNMKVGDGF 360
Cdd:COG4230 783 DGPIVPLiaETGGqNA--MIVDSsALPEQVVDDVLASAFDSAGQRC-SALRVLcVQEDIADRVLEMLKGAMAELRVGDPA 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 361 TEGVEQGPLINEAAVQKVEYFVDEATSKGAKVlvggkrHSLGM-------TFYEPTVVTgVNSemlLA--KEEVFGPVAP 431
Cdd:COG4230 860 DLSTDVGPVIDAEARANLEAHIERMRAEGRLV------HQLPLpeecangTFVAPTLIE-IDS---ISdlEREVFGPVLH 929
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 432 LLKFKTDE-----EAIqmaNDTNAGLAAYIFSTNIKRAWRVTEALEYG-----------IVGVNeglvstevaPFGGVKQ 495
Cdd:COG4230 930 VVRYKADEldkviDAI---NATGYGLTLGVHSRIDETIDRVAARARVGnvyvnrniigaVVGVQ---------PFGGEGL 997
|
....
gi 807201085 496 SGLG 499
Cdd:COG4230 998 SGTG 1001
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
39-499 |
2.50e-44 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 168.23 E-value: 2.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 39 AKLSSsGLLRS-------QALIGGKwvdAYDGKTIKVHNPA-TGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAER 110
Cdd:PRK11809 631 ASLSS-ALLASahqkwqaAPMLEDP---VAAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAER 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 111 SRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIefsaeegkRIYGDIIpspladRRLFVLK--QPVGVV 188
Cdd:PRK11809 707 AAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFL--------RYYAGQV------RDDFDNDthRPLGPV 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 189 GAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKIT 268
Cdd:PRK11809 773 VCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVM 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 269 FTGSTKVGKKLMEGAAATV----KKVSL--ELGG-NApcIIFDDADL-EVALKGALATKFRNTGQTCvCANRIL-VQEGI 339
Cdd:PRK11809 853 FTGSTEVARLLQRNLAGRLdpqgRPIPLiaETGGqNA--MIVDSSALtEQVVADVLASAFDSAGQRC-SALRVLcLQDDV 929
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 340 YDKFANAFAKAVQNMKVG--DGFTEGVeqGPLINEAAVQKVEYFVDEATSKGAKV----LVGGKRHSLGmTFYEPTVVTG 413
Cdd:PRK11809 930 ADRTLKMLRGAMAECRMGnpDRLSTDI--GPVIDAEAKANIERHIQAMRAKGRPVfqaaRENSEDWQSG-TFVPPTLIEL 1006
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 414 VNSEMLlaKEEVFGPVAPLLKFKTDE--EAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLVSTEVA--P 489
Cdd:PRK11809 1007 DSFDEL--KREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvqP 1084
|
490
....*....|
gi 807201085 490 FGGVKQSGLG 499
Cdd:PRK11809 1085 FGGEGLSGTG 1094
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
51-497 |
2.11e-43 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 161.22 E-value: 2.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 51 ALIGGKWVdaYDGKTIKVHNPAT-GEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSR-YLR-------KWYDLI 121
Cdd:cd07123 35 LVIGGKEV--RTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAiFLKaadllsgKYRYEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 122 MAhKEELGQLMTLEQGKplKEAIGEVsygAGFIEFSAEEGKRIYGDIIPSPLADRRLFVLKQPV-GVVGAITPWNF---- 196
Cdd:cd07123 113 NA-ATMLGQGKNVWQAE--IDAACEL---IDFLRFNVKYAEELYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFtaig 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 197 ---PLAmitrkvgPALAcGCTVVIKPSEltplTALAAAELSIQ----AGIPPGVVNVVMGNAPDIGDALLASPQVRKITF 269
Cdd:cd07123 187 gnlAGA-------PALM-GNVVLWKPSD----TAVLSNYLVYKileeAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 270 TGSTKVGKKLMEGAAA------TVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKF 343
Cdd:cd07123 255 TGSTPTFKSLWKQIGEnldryrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 344 ANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVDEA-TSKGAKVLVGGK-RHSLGMtFYEPTVVTGVNSEMLLA 421
Cdd:cd07123 335 KERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAkSDPEAEIIAGGKcDDSVGY-FVEPTVIETTDPKHKLM 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 422 KEEVFGPVAPLLKFKTD--EEAIQMANDTNA-GLAAYIFSTN---IKRAwrvTEALEY--GIVGVNE---GLVsteVA-- 488
Cdd:cd07123 414 TEEIFGPVLTVYVYPDSdfEETLELVDTTSPyALTGAIFAQDrkaIREA---TDALRNaaGNFYINDkptGAV---VGqq 487
|
....*....
gi 807201085 489 PFGGVKQSG 497
Cdd:cd07123 488 PFGGARASG 496
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
180-521 |
6.55e-42 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 156.43 E-value: 6.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 180 VLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTA--LAAAelsIQAGIPPGVVNVVMGnAPDIGDA 257
Cdd:PLN02203 104 VVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSafLAAN---IPKYLDSKAVKVIEG-GPAVGEQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 258 LLASPQvRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCII--FDDA-DLEVALKGALATKFRN-TGQTCVCANRI 333
Cdd:PLN02203 180 LLQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAIDYV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 334 LVQEgiydKFANAFAKAVQNMK---VGDGFTEGVEQGPLINEAAVQKVEYFVDEATSKgAKVLVGGKRHSLGMtFYEPTV 410
Cdd:PLN02203 259 LVEE----RFAPILIELLKSTIkkfFGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSIDEKKL-FIEPTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 411 VTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLV--STEVA 488
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIqyACDSL 412
|
330 340 350
....*....|....*....|....*....|...
gi 807201085 489 PFGGVKQSGLGREGSKYGMDEYLEMKYVCLGSM 521
Cdd:PLN02203 413 PFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSL 445
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
180-521 |
1.77e-39 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 149.81 E-value: 1.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 180 VLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELsIQAGIPPGVVNVVMGNAPDIgdALL 259
Cdd:PLN02174 108 IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTET--TAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 260 ASPQVRKITFTGSTKVGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFR-NTGQTCVCANRILVQEG 338
Cdd:PLN02174 185 LEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 339 IYDKFANAFAKAVQNMkVGDGFTEGVEQGPLINEAAVQKVEYFVDEATSKGaKVLVGGKRHSLGMTFyEPTVVTGVNSEM 418
Cdd:PLN02174 265 YAPKVIDAMKKELETF-YGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSD-KIVYGGEKDRENLKI-APTILLDVPLDS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 419 LLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFSTNIKRAWRVTEALEYGIVGVNEGLV--STEVAPFGGVKQS 496
Cdd:PLN02174 342 LIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVhlALHTLPFGGVGES 421
|
330 340
....*....|....*....|....*
gi 807201085 497 GLGREGSKYGMDEYLEMKYVCLGSM 521
Cdd:PLN02174 422 GMGAYHGKFSFDAFSHKKAVLYRSL 446
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
91-446 |
4.59e-32 |
|
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: 128.04 E-value: 4.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 91 AISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEE-------GKR 163
Cdd:cd07129 4 AAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLvregswlDAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 164 I---YGDIIPSPLAD-RRLFVlkqPVGVVGAITPWNFPLAMITrkVG----PALACGCTVVIKP-------SELTPLTAL 228
Cdd:cd07129 84 IdpaDPDRQPLPRPDlRRMLV---PLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKAhpahpgtSELVARAIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 229 AAAElsiQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEGAAA--TVKKVSLELGGNAPCIIFDDA 306
Cdd:cd07129 159 AALR---ATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 307 DLE--VALKGALATKFR-NTGQTCVCANRILVQEGI-YDKFANAFAKAVQNMKVGDGFTEGVEQGpliNEAAVQKVeyfv 382
Cdd:cd07129 236 LAErgEAIAQGFVGSLTlGAGQFCTNPGLVLVPAGPaGDAFIAALAEALAAAPAQTMLTPGIAEA---YRQGVEAL---- 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807201085 383 deATSKGAKVLVGGKRHSLGMTfYEPTVVTgVNSEMLLAK----EEVFGPVAPLLKFKTDEEAIQMAN 446
Cdd:cd07129 309 --AAAPGVRVLAGGAAAEGGNQ-AAPTLFK-VDAAAFLADpalqEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
89-489 |
1.85e-27 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 114.64 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 89 NDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKEAigeVSYGAGFIEFSAEEgKRIYGDI 168
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA---ENICGDQVQLRARA-FVIYSYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 169 IPSPLADRRLFVLKQ-------PVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGI-P 240
Cdd:cd07084 78 IPHEPGNHLGQGLKQqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 241 PGVVNVVMGNApDIGDALLASPQVRKITFTGSTKVGKKLMEGAAATvkKVSLELGGNAPCIIFDDAD-LEVALKGALATK 319
Cdd:cd07084 158 PEDVTLINGDG-KTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQaVDYVAWQCVQDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 320 FRNTGQTCVCANRILVQEgiyDKFANAFAKAVQNmKVGDGFTEGVEQGPLINEAAVQKVEYFVDEAtskGAKVLVGGKRH 399
Cdd:cd07084 235 TACSGQKCTAQSMLFVPE---NWSKTPLVEKLKA-LLARRKLEDLLLGPVQTFTTLAMIAHMENLL---GSVLLFSGKEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 400 SL--GMTFYEPTVVTGV-------NSEMLLAKEEVFGPVAPLLKFKTDEEA--IQMANDTNAGLAAYIFSTNIKRAWRVT 468
Cdd:cd07084 308 KNhsIPSIYGACVASALfvpideiLKTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELI 387
|
410 420
....*....|....*....|.
gi 807201085 469 EALEYGIVGVNEGLVSTEVAP 489
Cdd:cd07084 388 GNLWVAGRTYAILRGRTGVAP 408
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
50-458 |
2.05e-26 |
|
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: 112.36 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 50 QALIGGKWVdAYDGKTIKVHNPATGEVITDVPCMG---------GRETNDAissaydafsSWSKLTAAERSRYLRKWYDL 120
Cdd:cd07128 2 QSYVAGQWH-AGTGDGRTLHDAVTGEVVARVSSEGldfaaavayAREKGGP---------ALRALTFHERAAMLKALAKY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 121 IMAHKEELGQLMTLEQGKPLKEAIgEVSYGAGFIEFSAEEGKR--------IYGDIIP----SPLADRRLFVLKQPVGVv 188
Cdd:cd07128 72 LMERKEDLYALSAATGATRRDSWI-DIDGGIGTLFAYASLGRRelpnahflVEGDVEPlskdGTFVGQHILTPRRGVAV- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 189 gAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGI-PPGVVNVVMGNAPDIGDALLASPQVrki 267
Cdd:cd07128 150 -HINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHLGEQDVV--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 268 TFTGSTKVGKKL-------MEGAAATVKKVSLelggNApCIIFDDA-------DL---EVALKgaLATKfrnTGQTCVCA 330
Cdd:cd07128 226 AFTGSAATAAKLrahpnivARSIRFNAEADSL----NA-AILGPDAtpgtpefDLfvkEVARE--MTVK---AGQKCTAI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 331 NRILVQEGIYDKFANAFAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVdEATSKGAKVLVGGKRHSLGM------- 403
Cdd:cd07128 296 RRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRFEVVgadaekg 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 807201085 404 TFYEPTVVTGVN--SEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFS 458
Cdd:cd07128 375 AFFPPTLLLCDDpdAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVT 431
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
53-458 |
1.51e-24 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 107.10 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 53 IGGKWVDAyDGKTIKVHNPATGEVITDVPCMG---------GRETNDAISSAydafsswskLTAAERSRYLRKWYDLIMA 123
Cdd:PRK11903 9 VAGRWQAG-SGAGTPLFDPVTGEELVRVSATGldlaaafafAREQGGAALRA---------LTYAQRAALLAAIVKVLQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 124 HKEELGQLMTLEQGKPLKEAIGEVSYGAGFIEFSAEEGK-----RIYGDIIPSPLADRRLF----VLKQPVGVVGAITPW 194
Cdd:PRK11903 79 NRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAalgdaRLLRDGEAVQLGKDPAFqgqhVLVPTRGVALFINAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 195 NFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGI-PPGVVNVVMGNAPDIGDALLASPQVrkiTFTGST 273
Cdd:PRK11903 159 NFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFDVV---SFTGSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 274 KVGKKLMEGAAATVKKV-------SLELGGNAPCIIFDDADLEVALKGALATKFRNTGQTCVCANRILVQEGIYDKFANA 346
Cdd:PRK11903 236 ETAAVLRSHPAVVQRSVrvnveadSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 347 FAKAVQNMKVGDGFTEGVEQGPLINEAAVQKVEYFVdEATSKGAKVLVGGKRHSL------GMTFYEPT--VVTGVNSEM 418
Cdd:PRK11903 316 LAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFALvdadpaVAACVGPTllGASDPDAAT 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 807201085 419 LLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGLAAYIFS 458
Cdd:PRK11903 395 AVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYS 434
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
52-468 |
1.01e-15 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 79.46 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 52 LIGGKWVDAYDgkTIKVHNPATGEVITDVPCMGGRETNDAISSAYDAFSSWSKLTAAERSRYLRkWYDLIMAHKEELGQ- 130
Cdd:cd07126 2 LVAGKWKGASN--YTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKNPERYLL-YGDVSHRVAHELRKp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 131 -----LMTLEQ---GKPLKEAIGEVSYGAGFIE-FSAEEGKRI-YGDIIPSPLADRRLFVLKQPVGVVGAITPWNFPLAM 200
Cdd:cd07126 79 evedfFARLIQrvaPKSDAQALGEVVVTRKFLEnFAGDQVRFLaRSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 201 ITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGIPPGVVNVVMGNAPDIGDALLASpQVRKITFTGSTKVGKKLm 280
Cdd:cd07126 159 PALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEA-NPRMTLFTGSSKVAERL- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 281 egAAATVKKVSLELGGN-----APCIIFDDADLEVALKGALATkfrnTGQTCvCANRIL------VQEGIYDKFANAFAK 349
Cdd:cd07126 237 --ALELHGKVKLEDAGFdwkilGPDVSDVDYVAWQCDQDAYAC----SGQKC-SAQSILfahenwVQAGILDKLKALAEQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 350 -AVQNMKVGDGFTegveqgpLINEAAVQKVEYFvdeATSKGAKVLVGGK---RHSLGMTF--YEPTVV-----TGVNSEM 418
Cdd:cd07126 310 rKLEDLTIGPVLT-------WTTERILDHVDKL---LAIPGAKVLFGGKpltNHSIPSIYgaYEPTAVfvpleEIAIEEN 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 807201085 419 L-LAKEEVFGPVAPLLKFKTDEE--AIQMANDTNAGLAAYIFSTNIKRAWRVT 468
Cdd:cd07126 380 FeLVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEVL 432
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
89-463 |
4.03e-12 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 68.03 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 89 NDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQG------KPLK-EAIGEVSYGAGFIEFSAEEG 161
Cdd:cd07121 7 DDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGmgrvedKIAKnHLAAEKTPGTEDLTTTAWSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 162 kriygdiipsplaDRRLFVLKQ-PVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAEL----SIQ 236
Cdd:cd07121 87 -------------DNGLTLVEYaPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELinkaIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 237 AGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMegaaATVKKVSLELGGNAPCIIFDDADLEVA----L 312
Cdd:cd07121 154 AGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAAL----SSGKKAIGAGAGNPPVVVDETADIEKAardiV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 313 KGAlatKFRNTgQTCVCANRILVQEGIYDKFANAFAKavqnmkvgdgftegvEQGPLINEAAVQK--VEYFVDEATSKGA 390
Cdd:cd07121 230 QGA---SFDNN-LPCIAEKEVIAVDSVADYLIAAMQR---------------NGAYVLNDEQAEQllEVVLLTNKGATPN 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 391 KVLVGGKRHSL----GMTFYEPT--VVTGVNSEMLLAKEEVFGPVAPLLKFKTDEEAIQMANDTNAGL--AAYIFSTNIK 462
Cdd:cd07121 291 KKWVGKDASKIlkaaGIEVPADIrlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVE 370
|
.
gi 807201085 463 R 463
Cdd:cd07121 371 N 371
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
67-463 |
1.23e-11 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 66.85 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 67 KVHNPATGEVITDVPCMGGRET-NDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQG------KP 139
Cdd:PRK15398 16 EMLSSQTVSPPAAVGEMGVFASvDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedKI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 140 LK-EAIGEVSYGagfIEfsaeegkriygDIIPSPLADRRLFVLKQ--PVGVVGAITPWNFPLAMITRKVGPALACGCTVV 216
Cdd:PRK15398 96 AKnVAAAEKTPG---VE-----------DLTTEALTGDNGLTLIEyaPFGVIGAVTPSTNPTETIINNAISMLAAGNSVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 217 IKPSELTPLTALAAAEL----SIQAGIPPGVVNVVMGNAPDIGDALLASPQVRKITFTGSTKVGKKLMEgaaaTVKKVSL 292
Cdd:PRK15398 162 FSPHPGAKKVSLRAIELlneaIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMK----SGKKAIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 293 ELGGNAPCIIFDDADLEVA----LKGAlatKFRNTgQTCVCANRILVQEGIYDKFANAFAK--AVQ-NMKVGDGFTEGV- 364
Cdd:PRK15398 238 AGAGNPPVVVDETADIEKAardiVKGA---SFDNN-LPCIAEKEVIVVDSVADELMRLMEKngAVLlTAEQAEKLQKVVl 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 365 EQGPLINEAAVQK-VEYFVDEA---TSKGAKVLVG--GKRHslgmtfyePTVVTgvnsEMLLakeevfgPVAPLLKFKTD 438
Cdd:PRK15398 314 KNGGTVNKKWVGKdAAKILEAAginVPKDTRLLIVetDANH--------PFVVT----ELMM-------PVLPVVRVKDV 374
|
410 420
....*....|....*....|....*..
gi 807201085 439 EEAIQMANDTNAGL--AAYIFSTNIKR 463
Cdd:PRK15398 375 DEAIALAVKLEHGNrhTAIMHSRNVDN 401
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
208-479 |
2.42e-10 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 62.88 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 208 ALACGCTVVIKPSELTPL----TALAAAELSIQAGIPPGVVNVVMGNAPD-IGDALLASPQVRKITFTGSTKVGKKLMeg 282
Cdd:cd07127 217 SLATGNPVIVKPHPAAILplaiTVQVAREVLAEAGFDPNLVTLAADTPEEpIAQTLATRPEVRIIDFTGSNAFGDWLE-- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 283 AAATVKKVSLELGGNAPCIIfDDADLEVALKGALATKFR-NTGQTCVCANRILV-QEGI--------YDKFANAFAKAVQ 352
Cdd:cd07127 295 ANARQAQVYTEKAGVNTVVV-DSTDDLKAMLRNLAFSLSlYSGQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAID 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 353 NMkVGDGFTEGVEQGPLINEAAVQKVeyfvdEATSKGAKVLVGGKRHS----LGMTFYEPTVVTGVNSEMLLAKEEVFGP 428
Cdd:cd07127 374 GL-LADPARAAALLGAIQSPDTLARI-----AEARQLGEVLLASEAVAhpefPDARVRTPLLLKLDASDEAAYAEERFGP 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 807201085 429 VAPLLKFKTDEEAIQMAND---TNAGLAAYIFSTNIKRAWRVTEAleYGIVGVN 479
Cdd:cd07127 448 IAFVVATDSTDHSIELAREsvrEHGAMTVGVYSTDPEVVERVQEA--ALDAGVA 499
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
183-349 |
5.07e-09 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 58.27 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 183 QPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAEL----SIQAGIPPGVVNVVmgNAPDI--GD 256
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKImreaAVAAGAPEGLIQWI--EEPSIelTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 257 ALLASPQVRKITFTGSTKvgkklMEGAAATVKKVSLELG-GNAPCIIFDDADLEVALKGALATK-FRNtGQTCVCANRIL 334
Cdd:cd07122 172 ELMKHPDVDLILATGGPG-----MVKAAYSSGKPAIGVGpGNVPAYIDETADIKRAVKDIILSKtFDN-GTICASEQSVI 245
|
170
....*....|....*
gi 807201085 335 VQEGIYDKFANAFAK 349
Cdd:cd07122 246 VDDEIYDEVRAELKR 260
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
89-348 |
7.59e-09 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 58.05 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 89 NDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAHKEELGQLMTLEQGKPLKE-------AIGEVSYGAGFIEFSAE-- 159
Cdd:cd07081 2 DDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEdkviknhFAAEYIYNVYKDEKTCGvl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 160 EGKRIYGDIIpspladrrlfvLKQPVGVVGAITPWNFPLAMITRKVGPALACGCTVVIKPSELTPLTALAAAELSIQAGI 239
Cdd:cd07081 82 TGDENGGTLI-----------IAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 240 PPGVVNVVMG--NAPDI--GDALLASPQVRKITFTGstkvGKKLMEGAAATVKKVSLELGGNAPCIIFDDADLEVALKGA 315
Cdd:cd07081 151 AAGAPENLIGwiDNPSIelAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSI 226
|
250 260 270
....*....|....*....|....*....|...
gi 807201085 316 LATKFRNTGQTCVCANRILVQEGIYDKFANAFA 348
Cdd:cd07081 227 VKSKTFDNGVICASEQSVIVVDSVYDEVMRLFE 259
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
89-393 |
2.91e-06 |
|
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: 49.53 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 89 NDAISSAYDAFSSWSKLTAAERSRYLRKWYDLIMAhkeelgqLMTLEQGKPLKEAIGEvsygagfiEFSAEEGKRIYGDI 168
Cdd:cd07077 23 NAIANALYDTRQRLASEAVSERGAYIRSLIANWIA-------MMGCSESKLYKNIDTE--------RGITASVGHIQDVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 169 IPSPLAdrrLFVLKQPVGVVGAITPWNFPLAMITrKVGPALACGCTVVIKPSELTPLTALAAAeLSIQAGIPPGVVN--V 246
Cdd:cd07077 88 LPDNGE---TYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALA-LLFQAADAAHGPKilV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 247 VMGNAPDI--GDALLASPQVRKITFTGstkvGKKLMEGA--AATVKKVSLELGGNAPCIIFDDADLEVALKGALATKFRN 322
Cdd:cd07077 163 LYVPHPSDelAEELLSHPKIDLIVATG----GRDAVDAAvkHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807201085 323 tGQTCVCANRILVQEGIYDKFANAFAKAVQNMKVgdgfteGVEQGPLIneAAVQKVEYFVDEATSKGAKVL 393
Cdd:cd07077 239 -QNACASEQNLYVVDDVLDPLYEEFKLKLVVEGL------KVPQETKP--LSKETTPSFDDEALESMTPLE 300
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
184-445 |
1.03e-04 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 45.18 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 184 PVGVVGAITPWNFP---------LAMITRkvgpalacgCTVVIKPSELTPLTALAAAEL----SIQAGIPPGVVNVVMGN 250
Cdd:PRK13805 108 PVGVIAGITPTTNPtstaifkalIALKTR---------NPIIFSFHPRAQKSSIAAAKIvldaAVAAGAPKDIIQWIEEP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 251 APDIGDALLASPQVRKITFTGSTKvgkklMEGAAATVKKVSLELG-GNAPCIIFDDADLEVALKGALATK-FRNtGQTCV 328
Cdd:PRK13805 179 SVELTNALMNHPGIALILATGGPG-----MVKAAYSSGKPALGVGaGNVPAYIDKTADIKRAVNDILLSKtFDN-GMICA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807201085 329 CANRILVQEGIYDKFANAFA-------KAVQNMKVGDGFTegVEQGPLINEAAV-QKVEYFVDEA---TSKGAKVLVGgk 397
Cdd:PRK13805 253 SEQAVIVDDEIYDEVKEEFAshgayflNKKELKKLEKFIF--GKENGALNADIVgQSAYKIAEMAgfkVPEDTKILIA-- 328
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 807201085 398 rhslgmtfyeptVVTGVNSEMLLAKEEVFgPVAPLLKFKTDEEAIQMA 445
Cdd:PRK13805 329 ------------EVKGVGESEPLSHEKLS-PVLAMYKAKDFEDAVEKA 363
|
|
| |
