|
Name |
Accession |
Description |
Interval |
E-value |
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
1-482 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 1002.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 1 MKLNDSNLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWF 80
Cdd:PRK11241 1 MQLNDSTLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 81 NLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPA 160
Cdd:PRK11241 81 NLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 161 AMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQ 240
Cdd:PRK11241 161 AMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 241 LMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
Cdd:PRK11241 241 LMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 321 GLDKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDE 400
Cdd:PRK11241 321 GLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:PRK11241 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
..
gi 15832776 481 GL 482
Cdd:PRK11241 481 GL 482
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
30-480 |
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: 874.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 30 VTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 110 SYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSA 189
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 190 LALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDAD 269
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 270 LDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADALE 349
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 350 KGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRV 429
Cdd:cd07103 321 KGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 15832776 430 GEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07103 401 AEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
30-476 |
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: 843.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 30 VTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 110 SYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSA 189
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 190 LALAELAIRAGIPAGVFNVVTGS-AGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGSrAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 269 DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADAL 348
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 349 EKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFR 428
Cdd:TIGR01780 321 EKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15832776 429 VGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:TIGR01780 401 VAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
2-481 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 826.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 2 KLNDSNLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFN 81
Cdd:PLN02278 16 KLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 82 LMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAA 161
Cdd:PLN02278 96 LIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 162 MITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQL 241
Cdd:PLN02278 176 MITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 242 MEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDG 321
Cdd:PLN02278 256 MAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 322 LDKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEA 401
Cdd:PLN02278 336 FEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 402 DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIG 481
Cdd:PLN02278 416 EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCLG 495
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
7-482 |
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: 711.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 7 NLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEH 86
Cdd:COG1012 2 TTPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 87 QDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRK 166
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 167 AGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCA 246
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 247 KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGV 326
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 327 TIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHER-GGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIA 405
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832776 406 QANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV-APFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
19-476 |
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: 637.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 19 WLDANnGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQ 98
Cdd:pfam00171 1 WVDSE-SETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 99 GKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGhQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMV 178
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 179 LKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGG 258
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 259 NAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVA 338
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 339 KVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYF 418
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15832776 419 YARDLSRVFRVGEALEYGIVGINTGIISN-EVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:pfam00171 399 FTSDLERALRVARRLEAGMVWINDYTTGDaDGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
52-476 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 571.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 52 AAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTI 131
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 132 PGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTG 211
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 212 SAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVC 291
Cdd:cd07078 162 DGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 292 ANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERG-GNFFQP 370
Cdd:cd07078 242 ASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkGYFVPP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 371 TILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV- 449
Cdd:cd07078 322 TVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPs 401
|
410 420
....*....|....*....|....*..
gi 15832776 450 APFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07078 402 APFGGVKQSGIGREGGPYGLEEYTEPK 428
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
15-476 |
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: 542.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLM 94
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 95 TLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAG 174
Cdd:cd07088 82 VEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 175 CTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSL 254
Cdd:cd07088 162 NTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 255 ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDE 334
Cdd:cd07088 242 ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 335 KAVAKVEEHIADALEKGARVVCGGK-AHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFG 413
Cdd:cd07088 322 AALDKVEEMVERAVEAGATLLTGGKrPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832776 414 LAAYFYARDLSRVFRVGEALEYGIVGINTGiisNEVAPFG---GIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07088 402 LTSYIYTENLNTAMRATNELEFGETYINRE---NFEAMQGfhaGWKKSGLGGADGKHGLEEYLQTK 464
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
30-480 |
2.34e-176 |
|
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: 502.48 E-value: 2.34e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 30 VTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAK-GE 108
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 109 ISYAASFIEWFAEEGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS 188
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYP-QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 189 ALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 269 DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADAL 348
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 349 EKGARVVCGGKAHE----RGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLS 424
Cdd:cd07093 320 AEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15832776 425 RVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07093 400 RAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
30-476 |
3.01e-174 |
|
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: 497.46 E-value: 3.01e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 30 VTNPANGDKLGSVPKMGADETRAAIDAANRAL--PVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 108 EISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPF 187
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 188 SALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDD 267
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 268 ADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADA 347
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 348 LEKGARVVCGGKAHE----RGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDL 423
Cdd:cd07114 321 REEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15832776 424 SRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07114 401 ARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
12-476 |
2.13e-169 |
|
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: 485.56 E-value: 2.13e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 12 QALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPV--WRALTAKERANILRNWFNLMMEHQDD 89
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 90 LARLMTLEQGKPLAE-AKGEISYAASFIEWFAEEGKRIYGDTIPghQADKRL-IVIKQPIGVTAAITPWNFPAAMITRKA 167
Cdd:cd07091 85 LAALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIP--IDGNFLaYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 168 GPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 248 -DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGV 326
Cdd:cd07091 243 sNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 327 TIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQ 406
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07091 403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
29-480 |
2.78e-168 |
|
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: 481.83 E-value: 2.78e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 29 DVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGE 108
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 109 ISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS 188
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 189 ALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 269 DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADAL 348
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 349 EKGARVVCGGKaheRGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFR 428
Cdd:cd07150 322 AKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFK 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15832776 429 VGEALEYGIVGINTGIISNE-VAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07150 399 LAERLESGMVHINDPTILDEaHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
28-480 |
1.77e-167 |
|
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: 479.78 E-value: 1.77e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 28 IDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 108 EISYAASFIEWFAEEGKRIYGDTIPGHQA----DKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPAS 183
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFDASpggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 184 QTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAkdIKKVSLELGGNAPFI 263
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 264 VFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEH 343
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 344 IADALEKGARVVCGGKaheRGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDL 423
Cdd:cd07149 319 VEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 424 SRVFRVGEALEYGIVGINTgiISN---EVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07149 396 QKALKAARELEVGGVMIND--SSTfrvDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
30-476 |
1.77e-165 |
|
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: 474.71 E-value: 1.77e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 30 VTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 110 SYAASFIEWFAE---EGKRIYGDtipghqADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTP 186
Cdd:cd07106 81 GGAVAWLRYTASldlPDEVIEDD------DTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 187 FSALALAELaIRAGIPAGVFNVVTGSaGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFD 266
Cdd:cd07106 155 LCTLKLGEL-AQEVLPPGVLNVVSGG-DELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 267 DADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIAD 346
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 347 ALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRV 426
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 15832776 427 FRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
15-482 |
5.43e-162 |
|
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: 467.17 E-value: 5.43e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL--PVWRALTAKERANILRNWFNLMMEHQDDLAR 92
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07119 82 LETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYD-VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLI 332
Cdd:cd07119 241 ALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 333 DEKAVAKVEEHIADALEKGARVVCGGKAHERG----GNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQAN 408
Cdd:cd07119 321 SAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLAN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832776 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINT-GIISNEvAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:cd07119 401 DTPYGLAGAVWTKDIARANRVARRLRAGTVWINDyHPYFAE-APWGGYKQSGIGRELGPTGLEEYQETKHININL 474
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
51-480 |
7.67e-162 |
|
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: 464.70 E-value: 7.67e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 51 RAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDT 130
Cdd:cd07104 3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 131 IPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS-ALALAELAIRAGIPAGVFNVV 209
Cdd:cd07104 83 LPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 210 TGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTC 289
Cdd:cd07104 163 PGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQIC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 290 VCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHergGNFFQ 369
Cdd:cd07104 243 MAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE---GLFYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 370 PTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNE- 448
Cdd:cd07104 320 PTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDEp 399
|
410 420 430
....*....|....*....|....*....|..
gi 15832776 449 VAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07104 400 HVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
28-480 |
2.99e-161 |
|
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: 464.13 E-value: 2.99e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 28 IDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 108 EISYAASFIEWFAEEGKRIYGDTIP---GHQADKRLIVIK-QPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPAS 183
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPvdaYEYNERRIAFTVrEPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 184 QTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFI 263
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 264 VFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEH 343
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 344 IADALEKGARVVCGGKAHErgGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDL 423
Cdd:cd07145 321 VNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDI 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15832776 424 SRVFRVGEALEYGIVGIN-TGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07145 399 NRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
14-476 |
7.62e-160 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 461.33 E-value: 7.62e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 14 LINGEWLDANNGEviDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLAR 92
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLI 332
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 333 DEKAVAKVEEHIADALEKGARVVCGGKAHERG--GNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDT 410
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDT 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832776 411 EFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV-APFGGIKASGLG-REGSKYGIEDYLEIK 476
Cdd:cd07097 402 EFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYhVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
15-476 |
9.59e-159 |
|
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: 458.12 E-value: 9.59e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLM 94
Cdd:cd07138 3 IDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 95 TLEQGKPLAEAK--------GEISYAASFIEWFAEEGKRiyGDTIpghqadkrliVIKQPIGVTAAITPWNFPAAMITRK 166
Cdd:cd07138 83 TLEMGAPITLARaaqvglgiGHLRAAADALKDFEFEERR--GNSL----------VVREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 167 AGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCA 246
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 247 KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGV 326
Cdd:cd07138 231 DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 327 TIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERG---GNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADV 403
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEGlerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832776 404 IAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINtGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
14-478 |
3.64e-156 |
|
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: 452.19 E-value: 3.64e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 14 LINGEWLDANNGEVIDVTNPANGDKL-GSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLAR 92
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVvGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLI 332
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 333 DEKAVAKVEEHIADALEKGARVVCGGKAHERG----GNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQAN 408
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERLTGGgyekGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15832776 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV-APFGGIKASGLG-REGSKYGIEDYLEIKYM 478
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVhLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
25-476 |
2.23e-154 |
|
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: 447.05 E-value: 2.23e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 25 GEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--VWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPL 102
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 103 AEA-KGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIViKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKP 181
Cdd:cd07112 81 SDAlAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALIT-REPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 182 ASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAK-DIKKVSLELGGNA 260
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 261 PFIVFDDA-DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAK 339
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 340 VEEHIADALEKGARVVCGGKAH--ERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAY 417
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15832776 418 FYARDLSRVFRVGEALEYGIVGINT---GIISnevAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCfdeGDIT---TPFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
28-480 |
2.49e-154 |
|
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: 446.49 E-value: 2.49e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 28 IDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 108 EISYAASFIEWFAEEGKRIYGDTIPG----HQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPAS 183
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 184 QTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAkdIKKVSLELGGNAPFI 263
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 264 VFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEH 343
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 344 IADALEKGARVVCGGkahERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDL 423
Cdd:cd07094 319 VEEAVEAGARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15832776 424 SRVFRVGEALEYGIVGINTG-IISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSsAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
55-476 |
3.35e-154 |
|
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: 442.82 E-value: 3.35e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 55 DAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGH 134
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 135 QADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAG 214
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 215 AVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANR 294
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 295 LYVQDGVYDRFAEKLQqavsklhigdgldkgvtigplidekavakveehiadalekgarvvcggkaherggnffqpTILV 374
Cdd:cd06534 241 LLVHESIYDEFVEKLV------------------------------------------------------------TVLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 375 DVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV-APFG 453
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPeAPFG 340
|
410 420
....*....|....*....|...
gi 15832776 454 GIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd06534 341 GVKNSGIGREGGPYGLEEYTRTK 363
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
30-476 |
7.44e-154 |
|
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: 445.26 E-value: 7.44e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 30 VTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 110 SYAASFIEWFAE--EGKRIYGD-TIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTP 186
Cdd:cd07110 81 DDVAGCFEYYADlaEQLDAKAErAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 187 FSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFD 266
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 267 DADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIAD 346
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 347 ALEKGARVVCGGK--AHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLS 424
Cdd:cd07110 321 GKEEGARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15832776 425 RVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
12-476 |
5.83e-153 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 443.97 E-value: 5.83e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 12 QALINGEWlDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLA 91
Cdd:PRK13473 4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 92 RLMTLEQGKPLAEAKG-EISYAASFIEWFAE-----EGKRIyGDTIPGHQADKRliviKQPIGVTAAITPWNFPAAMITR 165
Cdd:PRK13473 83 RLESLNCGKPLHLALNdEIPAIVDVFRFFAGaarclEGKAA-GEYLEGHTSMIR----RDPVGVVASIAPWNYPLMMAAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:PRK13473 158 KLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 246 AKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKG 325
Cdd:PRK13473 237 ADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 326 VTIGPLIDEKAVAKVEEHIADALEKG-ARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVI 404
Cdd:PRK13473 317 TELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832776 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEvAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:PRK13473 397 RWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFmLVSE-MPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
52-476 |
1.84e-152 |
|
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: 440.74 E-value: 1.84e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 52 AAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTi 131
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 132 PGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTG 211
Cdd:cd07100 82 PIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 212 SAGAVgNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVC 291
Cdd:cd07100 162 DSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 292 ANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPT 371
Cdd:cd07100 241 AKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 372 ILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAP 451
Cdd:cd07100 321 VLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLP 400
|
410 420
....*....|....*....|....*
gi 15832776 452 FGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07100 401 FGGVKRSGYGRELGRFGIREFVNIK 425
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
30-476 |
1.43e-149 |
|
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: 434.75 E-value: 1.43e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 30 VTNPANGDKLGSVPKMGADETRAAIDAANRALPVW-RALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAK-- 106
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 107 ------GEISYAASFIEWFAEEgkRIYGDTIPGHQADKRLIViKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLK 180
Cdd:cd07089 81 qvdgpiGHLRYFADLADSFPWE--FDLPVPALRGGPGRRVVR-REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 181 PASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNA 260
Cdd:cd07089 158 PAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 261 PFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKV 340
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 341 EEHIADALEKGARVVCGGK--AHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYF 418
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGrpAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15832776 419 YARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
32-482 |
1.14e-148 |
|
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: 432.25 E-value: 1.14e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 32 NPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKG-EIS 110
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 111 YAASFIEWFAEEGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSAL 190
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 191 ALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADL 270
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 271 DKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADALEK 350
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 351 GARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVG 430
Cdd:cd07115 322 GARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15832776 431 EALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:cd07115 402 AALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
14-463 |
1.15e-147 |
|
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: 430.45 E-value: 1.15e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 14 LINGEWLdANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARL 93
Cdd:cd07086 2 VIGGEWV-GSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAA 173
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 174 GCTMVLKPASQTPFSALALAELAIRA----GIPAGVFNVVTGsAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI 249
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 250 KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIG 329
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 330 PLIDEKAVAKVEEHIADALEKGARVVCGGKAHERG--GNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQA 407
Cdd:cd07086 320 PLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGepGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAIN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15832776 408 NDTEFGLAAYFYARDLSRVFRVGEA--LEYGIVGINTGIISNEV-APFGGIKASGLGRE 463
Cdd:cd07086 400 NDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPTSGAEIgGAFGGEKETGGGRE 458
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
28-480 |
5.24e-145 |
|
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: 422.81 E-value: 5.24e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 28 IDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 108 EISYAASFIEWFAEEGKRIYGDTIP--------GHQAdkrlIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVL 179
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldisargeGRQG----LVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 180 KPASQTPFSALALAELAIRAGIPAGVFNVVTGSAgAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKdiKKVSLELGGN 259
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPCSR-DDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 260 APFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAK 339
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 340 VEEHIADALEKGARVVCGGKaheRGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFY 419
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832776 420 ARDLSRVFRVGEALEYGivgintGIISNEV-------APFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07147 391 TRDLEKALRAWDELEVG------GVVINDVptfrvdhMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
10-482 |
5.54e-145 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 423.91 E-value: 5.54e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 10 RQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDD 89
Cdd:PRK13252 6 LQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 90 LARLMTLEQGKPLAEAK-GEISYAASFIEWFAEEGKRIYGDTIPGHQAD----KRlivikQPIGVTAAITPWNFPAAMIT 164
Cdd:PRK13252 86 LAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSfvytRR-----EPLGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGsAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQ 244
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQG-DGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 245 CAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDK 324
Cdd:PRK13252 240 AAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERG----GNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDE 400
Cdd:PRK13252 320 ATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGgfanGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:PRK13252 400 DEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
..
gi 15832776 481 GL 482
Cdd:PRK13252 480 EM 481
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
30-477 |
2.88e-144 |
|
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: 420.58 E-value: 2.88e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 30 VTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAK-GE 108
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 109 ISYAASFIEWFA-----EEGKRIyGDTIPGHQAdkrlIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPAS 183
Cdd:cd07092 81 LPGAVDNFRFFAgaartLEGPAA-GEYLPGHTS----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 184 QTPFSALALAELAIRaGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFI 263
Cdd:cd07092 156 TTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 264 VFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEH 343
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 344 IADAlEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDL 423
Cdd:cd07092 315 VERA-PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15832776 424 SRVFRVGEALEYGIVGINT-GIISNEvAPFGGIKASGLGREGSKYGIEDYLEIKY 477
Cdd:cd07092 394 GRAMRLSARLDFGTVWVNThIPLAAE-MPHGGFKQSGYGKDLSIYALEDYTRIKH 447
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
33-476 |
3.76e-144 |
|
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: 420.59 E-value: 3.76e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 33 PANGDKLGSVPKMGADETRAAIDAANRALPV--WRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEIS 110
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 111 YAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSAL 190
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 191 ALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADL 270
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 271 DKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADALEK 350
Cdd:cd07118 244 DAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 351 GARVVCGGKAHERG-GNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRV 429
Cdd:cd07118 324 GATLLLGGERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTV 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15832776 430 GEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07118 404 ARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELK 450
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
30-480 |
1.66e-142 |
|
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: 416.71 E-value: 1.66e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 30 VTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 110 SYAASFIEWFAEEGKRIYGDTIP---GHQADKRliviKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTP 186
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPlpgGSFAYTR----REPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 187 FSALALAELAIRAGIPAGVFNVVTGsAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFD 266
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 267 DADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIAD 346
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 347 ALEKGARVVCGG-----KAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYAR 421
Cdd:cd07090 316 AKQEGAKVLCGGervvpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15832776 422 DLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
15-482 |
1.81e-142 |
|
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: 417.58 E-value: 1.81e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP-VWRALTAKERANILRNWFNLMMEHQDDLARL 93
Cdd:cd07144 12 INNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFEsWWSKVTGEERGELLDKLADLVEKNRDLLAAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 94 MTLEQGKPL-AEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQAdKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07144 92 EALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPN-KLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLH-IGDGLDKGVTIGPL 331
Cdd:cd07144 251 TLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkVGSPFDDDTVVGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 332 IDEKAVAKVEEHIADALEKGARVVCGGKAHERG---GNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQAN 408
Cdd:cd07144 331 VSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKAN 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832776 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:cd07144 411 DTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
15-476 |
1.83e-142 |
|
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: 416.98 E-value: 1.83e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL--PVWRALTAKERANILRNWFNLMMEHQDDLAR 92
Cdd:cd07139 3 IGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 93 LMTLEQGKPLAEAK-GEISYAASFIEWFAEEGKRI-YGDTIPGhQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPA 170
Cdd:cd07139 83 LWTAENGMPISWSRrAQGPGPAALLRYYAALARDFpFEERRPG-SGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 171 LAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAgAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIK 250
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR-EVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 251 KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGP 330
Cdd:cd07139 241 RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 331 LIDEKAVAKVEEHIADALEKGARVVCGGK--AHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQAN 408
Cdd:cd07139 321 LASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIAN 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832776 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINtGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07139 401 DSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETK 467
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
31-472 |
2.09e-142 |
|
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: 416.24 E-value: 2.09e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 31 TNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEIS 110
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 111 YAASFIEWFAEEGKRIYGDT-IPGHQ--ADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPF 187
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRkVPTGLlmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 188 SALALAELAIRAGIPAGVFNVVTGsAGAVGNELTSNPlVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDD 267
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTG-DGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 268 ADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADA 347
Cdd:cd07099 239 ADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 348 LEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVF 427
Cdd:cd07099 319 VAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAE 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15832776 428 RVGEALEYGIVGINTGI--ISNEVAPFGGIKASGLGREGSKYGIEDY 472
Cdd:cd07099 399 AIARRLEAGAVSINDVLltAGIPALPFGGVKDSGGGRRHGAEGLREF 445
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
14-482 |
9.15e-142 |
|
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: 415.59 E-value: 9.15e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARL 93
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 94 MTLEQGKPLAEAKG-EISYAASFIEWFA-----EEG--KRIYGDTIPghqadkrlIVIKQPIGVTAAITPWNFPAAMITR 165
Cdd:cd07559 84 ETLDNGKPIRETLAaDIPLAIDHFRYFAgviraQEGslSEIDEDTLS--------YHFHEPLGVVGQIIPWNFPLLMAAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 166 KAGPALAAGCTMVLKPASQTPFSALALAELaIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:cd07559 156 KLAPALAAGNTVVLKPASQTPLSILVLMEL-IGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 246 AKDIKKVSLELGGNAPFIVFDDA-----DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
Cdd:cd07559 235 AENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 321 GLDKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERG----GNFFQPTILVDVPANAKVSKEETFGPLAPLFR 396
Cdd:cd07559 315 PLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVIT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 397 FKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07559 395 FKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
....*.
gi 15832776 477 YMCIGL 482
Cdd:cd07559 475 NILVSY 480
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
30-476 |
2.22e-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: 410.86 E-value: 2.22e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 30 VTNPANGDKLGSVPKMGADETRAAIDAANRALP-VWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGE 108
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFEsGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 109 ISYAASFIEWFAEEGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS 188
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 189 ALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 269 DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDkGVTIGPLIDEKAVAKVEEHIADAL 348
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 349 EKGARVVCGGKAHE---RGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSR 425
Cdd:cd07109 319 ARGARIVAGGRIAEgapAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15832776 426 VFRVGEALEYGIVGINT-----GIisnEVaPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07109 399 ALRVARRLRAGQVFVNNygaggGI---EL-PFGGVKKSGHGREKGLEALYNYTQTK 450
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
17-480 |
6.35e-140 |
|
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: 410.16 E-value: 6.35e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 17 GEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTL 96
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 97 EQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCT 176
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 177 MVLKPASQTPFSA-LALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLE 255
Cdd:cd07151 161 VVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 256 LGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEK 335
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 336 AVAKVEEHIADALEKGARVVCGGKAHergGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLA 415
Cdd:cd07151 321 QVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLS 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832776 416 AYFYARDLSRVFRVGEALEYGIVGINTGIISNE-VAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07151 398 GAVFTSDLERGVQFARRIDAGMTHINDQPVNDEpHVPFGGEKNSGLGRFNGEWALEEFTTDKWISV 463
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
12-476 |
2.18e-139 |
|
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: 409.43 E-value: 2.18e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 12 QALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PVWRALTAKERANILRNWFNLMMEHQD 88
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 89 DLARLMTLEQGKPLAEAK-GEISYAASFIEWFAEEGKRIYGDTIPghqADKRLIVI--KQPIGVTAAITPWNFPAAMITR 165
Cdd:cd07141 88 YLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIP---MDGDFFTYtrHEPVGVCGQIIPWNFPLLMAAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:cd07141 165 KLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 246 AK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDK 324
Cdd:cd07141 245 GKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVI 404
Cdd:cd07141 325 KTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15832776 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07141 405 ERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVK 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
12-476 |
9.19e-139 |
|
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: 407.65 E-value: 9.19e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 12 QALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPV--WRALTAKERANILRNWFNLMMEHQDD 89
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 90 LARLMTLEQGKPLAEAK-GEISYAASFIEWFAEEGKRIYGDTIPG---HQADkrliVIKQPIGVTAAITPWNFPAAMITR 165
Cdd:cd07142 85 LAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPAdgpHHVY----TLHEPIGVVGQIIPWNFPLLMFAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:cd07142 161 KVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 246 AK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDK 324
Cdd:cd07142 241 AKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVI 404
Cdd:cd07142 321 GVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15832776 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
30-476 |
7.58e-137 |
|
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: 402.12 E-value: 7.58e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 30 VTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPL-AEAKGE 108
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 109 ISYAASFIEWFAEEGKRIYGDTIPGHQaDKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS 188
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFGP-DVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 189 ALALAELAIRAgIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 269 DLDKAVEGALAS-KFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADA 347
Cdd:cd07108 239 DLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 348 LE-KGARVVCGGKAHERG----GNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD 422
Cdd:cd07108 319 LStSGATVLRGGPLPGEGpladGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15832776 423 LSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYG-IEDYLEIK 476
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKK 453
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
12-480 |
5.67e-136 |
|
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: 401.10 E-value: 5.67e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 12 QALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPV--WRALTAKERANILRNWFNLMMEHQDD 89
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 90 LARLMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDTIPGHQA--DKRL-IVIKQPIGVTAAITPWNFPAAMITR 165
Cdd:cd07140 87 LATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPINQArpNRNLtLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 246 AK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDK 324
Cdd:cd07140 247 AVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDE--AD 402
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDG 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832776 403 VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
14-482 |
7.11e-136 |
|
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: 400.29 E-value: 7.11e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARL 93
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 94 MTLEQGKPLAEAKG-EISYAASFIEWFAeegKRIYGDTIPGHQADKRL--IVIKQPIGVTAAITPWNFPAAMITRKAGPA 170
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFA---GVIRAEEGSANMIDEDTlsIVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 171 LAAGCTMVLKPASQTPFSALALAELaIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIK 250
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 251 KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGP 330
Cdd:cd07117 240 PATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 331 LIDEKAVAKVEEHIADALEKGARVVCGGK----AHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQ 406
Cdd:cd07117 320 QVNKDQLDKILSYVDIAKEEGAKILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDM 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832776 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:cd07117 400 ANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
10-476 |
8.26e-136 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 401.03 E-value: 8.26e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 10 RQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP-----VWRALTAKERANILRNWFNLMM 84
Cdd:PLN02467 7 RRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnkgkDWARTTGAVRAKYLRAIAAKIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 85 EHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGD-----TIPGHQADKRliVIKQPIGVTAAITPWNFP 159
Cdd:PLN02467 87 ERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKqkapvSLPMETFKGY--VLKEPLGVVGLITPWNYP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 160 AAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGR 239
Cdd:PLN02467 165 LLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 240 QLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIG 319
Cdd:PLN02467 245 KIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKIS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 320 DGLDKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGK--AHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRF 397
Cdd:PLN02467 325 DPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTF 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832776 398 KDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:PLN02467 405 STEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
12-470 |
2.18e-135 |
|
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: 398.87 E-value: 2.18e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 12 QALINGEWLDaNNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRA-LPVWRALTAKERANILRNWFNLMMEHQDDL 90
Cdd:cd07082 3 KYLINGEWKE-SSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 91 ARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRL----IVIKQPIGVTAAITPWNFPAAMITRK 166
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaQVRREPLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 167 AGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCA 246
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 247 kdIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGV 326
Cdd:cd07082 242 --MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 327 TIGPLIDEKAVAKVEEHIADALEKGARVVCGGKahERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQ 406
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832776 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINT----GIisnEVAPFGGIKASGLGREGSKYGIE 470
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINSkcqrGP---DHFPFLGRKDSGIGTQGIGDALR 462
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
52-476 |
4.17e-135 |
|
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: 396.56 E-value: 4.17e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 52 AAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTI 131
Cdd:cd07105 4 QAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 132 PGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTG 211
Cdd:cd07105 84 PSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 212 S---AGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQT 288
Cdd:cd07105 164 SpedAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 289 CVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDgldkgVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKA-HERGGNF 367
Cdd:cd07105 244 CMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLAdESPSGTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 368 FQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISN 447
Cdd:cd07105 319 MPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHD 398
|
410 420 430
....*....|....*....|....*....|
gi 15832776 448 E-VAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07105 399 EpTLPHGGVKSSGYGRFNGKWGIDEFTETK 428
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
32-479 |
3.54e-134 |
|
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: 395.17 E-value: 3.54e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 32 NPANGDKLGSVPKMGADETRAAIDAANRAL--PVWRAlTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 110 SYAASFIEWFAEEGKRIYGDTI---PGHQAdkrlIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTP 186
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIepePGSFS----LVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 187 FSALALAE-LAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVF 265
Cdd:cd07120 158 QINAAIIRiLAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 266 DDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIA 345
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 346 DALEKGARVVC-GGKAHER--GGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD 422
Cdd:cd07120 318 RAIAAGAEVVLrGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15832776 423 LSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMC 479
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
14-473 |
9.27e-134 |
|
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: 396.21 E-value: 9.27e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 14 LINGEWLDAnnGEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLAR 92
Cdd:cd07124 36 VIGGKEVRT--EEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIpGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07124 114 WMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPV-EMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKD---- 248
Cdd:cd07124 193 TGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpgq 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 249 --IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGV 326
Cdd:cd07124 273 kwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 327 TIGPLIDEKAVAKVEEHIADAlEKGARVVCGGK--AHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVI 404
Cdd:cd07124 353 YMGPVIDKGARDRIRRYIEIG-KSEGRLLLGGEvlELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEAL 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15832776 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN---TGIISnEVAPFGGIKASGLgreGSKYGIEDYL 473
Cdd:cd07124 432 EIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkiTGALV-GRQPFGGFKMSGT---GSKAGGPDYL 499
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
25-474 |
3.49e-133 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 395.02 E-value: 3.49e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 25 GEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAE 104
Cdd:PRK09407 31 GPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 105 AKGEISYAASfiewfaeeGKRIYGDTIPGHQADKR----------LIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAG 174
Cdd:PRK09407 111 AFEEVLDVAL--------TARYYARRAPKLLAPRRragalpvltkTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 175 CTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSL 254
Cdd:PRK09407 183 NAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGFSL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 255 ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDE 334
Cdd:PRK09407 261 ELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 335 KAVAKVEEHIADALEKGARVVCGGKAH-ERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFG 413
Cdd:PRK09407 341 AQLETVSAHVDDAVAKGATVLAGGKARpDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYG 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832776 414 LAAYFYARDLSRVFRVGEALEYGIVGINTGIIS---NEVAPFGGIKASGLGREGSKYGIEDYLE 474
Cdd:PRK09407 421 LNASVWTGDTARGRAIAARIRAGTVNVNEGYAAawgSVDAPMGGMKDSGLGRRHGAEGLLKYTE 484
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
28-476 |
6.77e-131 |
|
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: 386.71 E-value: 6.77e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 28 IDVTNPANGDKLGSVPKMGADETRAAID-AANRALPvwraLTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAK 106
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALAlAASYRST----LTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 107 GEISYAASFIEWFAEEGKRIYGDTIP---GHQADKRLIV-IKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPA 182
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFScdlTANGKARKIFtLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 183 SQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAkdIKKVSLELGGNAPF 262
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 263 IVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEE 342
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 343 HIADALEKGARVVCGgkaHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD 422
Cdd:cd07146 315 RVEEAIAQGARVLLG---NQRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15832776 423 LSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLG-REGSKYGIEDYLEIK 476
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNEVPgFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
15-482 |
1.73e-130 |
|
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: 386.88 E-value: 1.73e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL--PVWRALTAKERANILRNWFNLMMEHQDDLAR 92
Cdd:cd07143 11 INGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFetDWGLKVSGSKRGRCLSKLADLMERNLDYLAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 93 LMTLEQGKP-LAEAKGEISYAASFIEWFAEEGKRIYGDTIpgHQADKRLIVIK-QPIGVTAAITPWNFPAAMITRKAGPA 170
Cdd:cd07143 91 IEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVI--ETDIKKLTYTRhEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 171 LAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAK-DI 249
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKsNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 250 KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIG 329
Cdd:cd07143 249 KKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 330 PLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQAND 409
Cdd:cd07143 329 PQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRAND 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832776 410 TEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:cd07143 409 STYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
15-480 |
1.82e-130 |
|
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: 386.41 E-value: 1.82e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRA-LTAKERANILRNWFNLMMEHQDDLARL 93
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAkTTPAERGRILLRLADLIEQHGEELAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 94 MTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDT----IPGHQADK-RLIVIKQPIGVTAAITPWNFPAAMITRKA 167
Cdd:cd07113 84 ETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETlapsIPSMQGERyTAFTRREPVGVVAGIVPWNFSVMIAVWKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 168 GPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSaGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
Cdd:cd07113 164 GAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGK-GAVGAQLISHPDVAKVSFTGSVATGKKIGRQAAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 248 DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVT 327
Cdd:cd07113 243 DLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 328 IGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQA 407
Cdd:cd07113 323 FGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLI 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832776 408 NDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07113 403 NDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
33-475 |
2.32e-127 |
|
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: 377.80 E-value: 2.32e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 33 PANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYA 112
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 113 ASFIEWFAEEGKRIYGD-----TIPGHQadkRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPF 187
Cdd:cd07101 83 AIVARYYARRAERLLKPrrrrgAIPVLT---RTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 188 SALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDD 267
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 268 ADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADA 347
Cdd:cd07101 238 ADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 348 LEKGARVVCGGKAH-ERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRV 426
Cdd:cd07101 318 VAKGATVLAGGRARpDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARG 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15832776 427 FRVGEALEYGIVGINTGIIS---NEVAPFGGIKASGLGREGSKYGIEDYLEI 475
Cdd:cd07101 398 RRIAARLRAGTVNVNEGYAAawaSIDAPMGGMKDSGLGRRHGAEGLLKYTET 449
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
15-478 |
4.42e-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: 375.58 E-value: 4.42e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLM 94
Cdd:cd07111 26 INGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 95 TLEQGKPLAEAK-GEISYAASFIEWFAeeGKRIYGDT-IPGHQadkrlivikqPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07111 106 SLDNGKPIRESRdCDIPLVARHFYHHA--GWAQLLDTeLAGWK----------PVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGsAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLI 332
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 333 DEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPL--APLFRFKDEAdvIAQANDT 410
Cdd:cd07111 333 DPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVlvVLTFRTAKEA--VALANNT 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832776 411 EFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYM 478
Cdd:cd07111 411 PYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWE 478
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
76-476 |
1.36e-125 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 371.76 E-value: 1.36e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 76 LRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITP 155
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 156 WNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGST 235
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 236 EIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSK 315
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 316 LHIGDGLDKG-VTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPL 394
Cdd:PRK10090 241 VQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 395 FRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTgiiSNEVAPFG---GIKASGLGREGSKYGIED 471
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR---ENFEAMQGfhaGWRKSGIGGADGKHGLHE 397
|
....*
gi 15832776 472 YLEIK 476
Cdd:PRK10090 398 YLQTQ 402
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
30-476 |
4.89e-125 |
|
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: 372.09 E-value: 4.89e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 30 VTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 110 SYAASFIEWFAEEGKRIYGDTIP-GHQAdkRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS 188
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPvGGRN--LHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 189 ALALAELaIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
Cdd:cd07107 159 ALRLAEL-AREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 269 DLDKAVEGALAS-KFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADA 347
Cdd:cd07107 238 DPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 348 LEKGARVVCGGKAHE----RGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDL 423
Cdd:cd07107 318 KREGARLVTGGGRPEgpalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15832776 424 SRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEK 450
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
15-476 |
8.26e-125 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 373.00 E-value: 8.26e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--VWRALTAKERANILRNWFNLMMEHQDDLAR 92
Cdd:PLN02766 25 INGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 93 LMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPAL 171
Cdd:PLN02766 105 LDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLK-MSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 172 AAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAK-DIK 250
Cdd:PLN02766 184 AAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 251 KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGP 330
Cdd:PLN02766 264 QVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 331 LIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDT 410
Cdd:PLN02766 344 QVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNT 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832776 411 EFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:PLN02766 424 KYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVK 489
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
12-476 |
2.07e-123 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 370.68 E-value: 2.07e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 12 QALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PvWRALTAKERANILRNWFNLMMEHQD 88
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFdegP-WPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 89 DLARLMTLEQGKPLAE-AKGEISYAASFIEWFAEEGKRIYGDTIPG---HQADkrliVIKQPIGVTAAITPWNFPAAMIT 164
Cdd:PLN02466 138 ELAALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHGLTVPAdgpHHVQ----TLHEPIGVAGQIIPWNFPLLMFA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQ 244
Cdd:PLN02466 214 WKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLEL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 245 CAK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLD 323
Cdd:PLN02466 294 AAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFK 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 324 KGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADV 403
Cdd:PLN02466 374 KGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEV 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832776 404 IAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:PLN02466 454 IRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
28-481 |
2.53e-119 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 357.51 E-value: 2.53e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 28 IDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 108 EISYAASFIEWFAEEGKRIYGDTiPGHQAD---KRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQ 184
Cdd:PRK09406 83 EALKCAKGFRYYAEHAEALLADE-PADAAAvgaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 185 TPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELtSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIV 264
Cdd:PRK09406 162 VPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAIL-RDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 265 FDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHI 344
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 345 ADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLS 424
Cdd:PRK09406 321 DDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15832776 425 RVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIG 481
Cdd:PRK09406 401 EQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
36-474 |
7.75e-117 |
|
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: 350.44 E-value: 7.75e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 36 GDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASF 115
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 116 IEWFAEEGKRIYGDTIPghQADKRL-IVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSA-LALA 193
Cdd:cd07152 81 LHEAAGLPTQPQGEILP--SAPGRLsLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 194 ELAIRAGIPAGVFNVVTGSAGAvGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKA 273
Cdd:cd07152 159 RLFEEAGLPAGVLHVLPGGADA-GEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 274 VEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADALEKGAR 353
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 354 VVCGGkahERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEAL 433
Cdd:cd07152 318 LEAGG---TYDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15832776 434 EYGIVGINTGIISNE-VAPFGGIKASGLG-REGSKYGIEDYLE 474
Cdd:cd07152 395 RTGMLHINDQTVNDEpHNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
12-461 |
3.37e-111 |
|
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: 337.18 E-value: 3.37e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 12 QALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLA 91
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 92 RLMTLEQGKPLAEAKGEISYAASFIEwFA----EEGKriyGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAaMITR-K 166
Cdd:cd07085 82 RLITLEHGKTLADARGDVLRGLEVVE-FAcsipHLLK---GEYLENVARGIDTYSYRQPLGVVAGITPFNFPA-MIPLwM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 167 AGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVgNELTSNPLVRKLSFTGSTEIGRQLMEQCA 246
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 247 KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGV 326
Cdd:cd07085 236 ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 327 TIGPLIDEKAVAKVEEHIADALEKGARVVCGG-----KAHERgGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEA 401
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgvkvPGYEN-GNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832776 402 DVIAQANDTEFGLAAYFYARD--LSRVFRvgEALEYGIVGINTGI-ISNEVAPFGGIKASGLG 461
Cdd:cd07085 395 EAIAIINANPYGNGAAIFTRSgaAARKFQ--REVDAGMVGINVPIpVPLAFFSFGGWKGSFFG 455
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
32-470 |
1.14e-110 |
|
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: 334.98 E-value: 1.14e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 32 NPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISY 111
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 112 AASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALA 191
Cdd:cd07102 82 MLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 192 LAELAIRAGIPAGVFNVVTGSaGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLD 271
Cdd:cd07102 162 FAAAFAEAGLPEGVFQVLHLS-HETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 272 KAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADALEKG 351
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 352 ARVVCGGK---AHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFR 428
Cdd:cd07102 321 ARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15832776 429 VGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIE 470
Cdd:cd07102 401 LGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYD 442
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
32-469 |
2.32e-110 |
|
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: 334.65 E-value: 2.32e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 32 NPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAK-GEIS 110
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 111 YAASFIEWFAEEGKRIY------GDTIPGHqadKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQ 184
Cdd:cd07098 82 VTCEKIRWTLKHGEKALrpesrpGGLLMFY---KRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 185 TPFSA---LALAELAIRA-GIPAGVFNVVTGSAGAvGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNA 260
Cdd:cd07098 159 VAWSSgffLSIIRECLAAcGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 261 PFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKV 340
Cdd:cd07098 238 PAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 341 EEHIADALEKGARVVCGGKAH----ERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAA 416
Cdd:cd07098 318 EELVADAVEKGARLLAGGKRYphpeYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15832776 417 YFYARDLSRVFRVGEALEYGIVGINTGIIS--NEVAPFGGIKASGLGREGSKYGI 469
Cdd:cd07098 398 SVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGL 452
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
14-473 |
9.22e-107 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 326.89 E-value: 9.22e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 14 LINGEWLDAnnGEVIDVTNPANGDKL-GSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLAR 92
Cdd:PRK03137 40 IIGGERITT--EDKIVSINPANKSEVvGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEE------GKRIYgdTIPGHqaDKRLIVIkqPIGVTAAITPWNFPAAMITRK 166
Cdd:PRK03137 118 WLVKEAGKPWAEADADTAEAIDFLEYYARQmlkladGKPVE--SRPGE--HNRYFYI--PLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 167 AGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCA 246
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 247 KD------IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
Cdd:PRK03137 272 KVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 321 GLDKGVtIGPLIDEKAVAKVEEHIADALEKGaRVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDE 400
Cdd:PRK03137 352 PEDNAY-MGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832776 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN---TGIISNeVAPFGGIKASGlgrEGSKYGIEDYL 473
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgcTGAIVG-YHPFGGFNMSG---TDSKAGGPDYL 501
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
15-482 |
2.62e-106 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 325.31 E-value: 2.62e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--VWRALTAKERANILRNWFNLMMEHQDDLAR 92
Cdd:PRK09847 24 INGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 93 LMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIViKQPIGVTAAITPWNFPAAMITRKAGPAL 171
Cdd:PRK09847 104 LETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIV-REPVGVIAAIVPWNFPLLLTCWKLGPAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 172 AAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAK-DIK 250
Cdd:PRK09847 183 AAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 251 KVSLELGGNAPFIVFDDA-DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIG 329
Cdd:PRK09847 263 RVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 330 PLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGgnFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQAND 409
Cdd:PRK09847 343 TLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAA--AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLAND 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832776 410 TEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:PRK09847 421 SQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
16-465 |
1.68e-105 |
|
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: 322.23 E-value: 1.68e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 16 NGEWldANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMT 95
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 96 LEQGKPLAEAKGEISyaasfiEW-----FAEEGKR-IYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGP 169
Cdd:cd07130 82 LEMGKILPEGLGEVQ------EMidicdFAVGLSRqLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 170 ALAAGCTMVLKPASQTPFSALA----LAELAIRAGIPAGVFNVVTGSAgAVGNELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:cd07130 156 ALVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGA-DVGEALVKDPRVPLVSFTGSTAVGRQVGQAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 246 AKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKG 325
Cdd:cd07130 235 AARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 326 VTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTIlVDVPANAKVSKEETFGPLAPLFRFKDEADVIA 405
Cdd:cd07130 315 TLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832776 406 QANDTEFGLAAYFYARDLSRVFRVGEAL--EYGIVGINTGIISNEV-APFGGIKASGLGRE-GS 465
Cdd:cd07130 394 WNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSGAEIgGAFGGEKETGGGREsGS 457
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
15-480 |
3.67e-104 |
|
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: 319.01 E-value: 3.67e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLM 94
Cdd:cd07116 5 IGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 95 TLEQGKPLAEAKG-EISYAASFIEWFA-----EEG--KRIYGDTIPGHqadkrlivIKQPIGVTAAITPWNFPAAMITRK 166
Cdd:cd07116 85 TWDNGKPVRETLAaDIPLAIDHFRYFAgciraQEGsiSEIDENTVAYH--------FHEPLGVVGQIIPWNFPLLMATWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 167 AGPALAAGCTMVLKPASQTPFSALALAELaIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCA 246
Cdd:cd07116 157 LAPALAAGNCVVLKPAEQTPASILVLMEL-IGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 247 KDIKKVSLELGGNAPFIVF------DDADLDKAVEGALASKFrNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
Cdd:cd07116 236 ENIIPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 321 GLDKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGN----FFQPTiLVDVPANAKVSKEETFGPLAPLFR 396
Cdd:cd07116 315 PLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPT-TFKGGNKMRIFQEEIFGPVLAVTT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 397 FKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07116 394 FKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
....
gi 15832776 477 YMCI 480
Cdd:cd07116 474 NLLV 477
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
12-476 |
2.23e-99 |
|
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: 307.08 E-value: 2.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 12 QALINGEWLDANNGeVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPV--WRALTAKeRANILRNWFNLMMEHQDD 89
Cdd:TIGR04284 2 RLLIDGKLVAGSAG-TFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDEtdWSRDTAL-RVRCLRQLRDALRAHVEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 90 LARLMTLEQGKPL-----AEAKGEI---SYAASFIEWFaeEGKRIYGDTIPGHQADKRLIViKQPIGVTAAITPWNFPAA 161
Cdd:TIGR04284 80 LRELTIAEVGAPRmltagAQLEGPVddlGFAADLAESY--AWTTDLGVASPMGIPTRRTLR-REAVGVVGAITPWNFPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 162 MITRKAGPALAAGCTMVLKPASQTPFSALALAEL-AIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQ 240
Cdd:TIGR04284 157 INLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELiAEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 241 LMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
Cdd:TIGR04284 237 VMADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 321 GLDKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGG--KAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFK 398
Cdd:TIGR04284 317 PADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGgrPADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHD 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832776 399 DEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:TIGR04284 397 GDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETK 474
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
14-473 |
1.56e-96 |
|
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: 300.63 E-value: 1.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 14 LINGEWLDANNGevIDVTNPANGDK-LGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLAR 92
Cdd:TIGR01237 36 VINGERVETENK--IVSINPCDKSEvVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:TIGR01237 114 LLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAK----- 247
Cdd:TIGR01237 194 TGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKvqpgq 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 248 -DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGV 326
Cdd:TIGR01237 274 kHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 327 TIGPLIDEKAVAKVEEHIADALEKGaRVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQ 406
Cdd:TIGR01237 354 YVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEI 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN---TGIISNeVAPFGGIKASGLgreGSKYGIEDYL 473
Cdd:TIGR01237 433 ANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrniTGAIVG-YQPFGGFKMSGT---DSKAGGPDYL 498
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
32-476 |
8.96e-96 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 297.16 E-value: 8.96e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 32 NPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISY 111
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 112 AASFIEWFAEEGKRIYgDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALA 191
Cdd:PRK13968 93 SANLCDWYAEHGPAML-KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 192 LAELAIRAGIPAGVFNVVTGSAGAVgNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLD 271
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 272 KAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADALEKG 351
Cdd:PRK13968 251 LAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 352 ARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGE 431
Cdd:PRK13968 331 ARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAA 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 15832776 432 ALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
Cdd:PRK13968 411 RLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQ 455
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
28-480 |
5.15e-95 |
|
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: 294.71 E-value: 5.15e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 28 IDVTNPANGDKLGSVPKMGADETRAAIDAAN-RALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAK 106
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHaLFLDRNNWLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 107 GEISYAASFIEWFAEEGKRIYGDTIP-GHQ---ADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPA 182
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGREIPmGLTpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 183 SQTPFSALALAELAIRAGIPAG-VFNVVTGSAGAvgNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDiKKVSLELGGNAP 261
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGwCQAVPCENAVA--EKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 262 FIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVE 341
Cdd:cd07148 238 VIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 342 EHIADALEKGARVVCGGKahERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYAR 421
Cdd:cd07148 318 EWVNEAVAAGARLLCGGK--RLSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTK 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832776 422 DLSRVFRVGEALEYGIVGINtgiisNEVA------PFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07148 396 DLDVALKAVRRLDATAVMVN-----DHTAfrvdwmPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
1-473 |
3.07e-87 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 276.77 E-value: 3.07e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 1 MKLNDSNLFRQQALINGEwlDANNGEVIDVTNPANGDK-LGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNW 79
Cdd:cd07125 23 LKAFDEKEWEAIPIINGE--ETETGEGAPVIDPADHERtIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 80 FNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFP 159
Cdd:cd07125 101 ADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 160 AAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGR 239
Cdd:cd07125 181 LAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 240 QLMEQCAK---DIKKVSLELGG-NApFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSK 315
Cdd:cd07125 261 LINRALAErdgPILPLIAETGGkNA-MIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMAS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 316 LHIGDGLDKGVTIGPLIDEKAVAKVEEHIaDALEKGARVVCGGKAHERGGNFFQPTILVDVpaNAKVSKEETFGPLAPLF 395
Cdd:cd07125 340 LKVGDPWDLSTDVGPLIDKPAGKLLRAHT-ELMRGEAWLIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVI 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 396 RFKDE--ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISN--EVAPFGGIKASGLgreGSKYGIED 471
Cdd:cd07125 417 RFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAivGRQPFGGWGLSGT---GPKAGGPN 493
|
..
gi 15832776 472 YL 473
Cdd:cd07125 494 YL 495
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
52-472 |
4.82e-86 |
|
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: 270.68 E-value: 4.82e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 52 AAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGD-T 130
Cdd:cd07095 4 AAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTGErA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 131 IPGhqADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVT 210
Cdd:cd07095 84 TPM--AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 211 GsAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV-SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTC 289
Cdd:cd07095 162 G-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKIlALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 290 VCANRLYVQDG-VYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFF 368
Cdd:cd07095 241 TCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 369 QPTILvDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN---TGII 445
Cdd:cd07095 321 SPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNrptTGAS 399
|
410 420
....*....|....*....|....*..
gi 15832776 446 SNevAPFGGIKASGLGREGSKYGIeDY 472
Cdd:cd07095 400 ST--APFGGVGLSGNHRPSAYYAA-DY 423
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
15-472 |
4.98e-84 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 267.21 E-value: 4.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLdANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLM 94
Cdd:PRK09457 5 INGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 95 TLEQGKPLAEAKGE---------ISYAAsfiewFAEEGKRIYGDTipghqADKRLIVIKQPIGVTAAITPWNFPAAMITR 165
Cdd:PRK09457 84 ARETGKPLWEAATEvtaminkiaISIQA-----YHERTGEKRSEM-----ADGAAVLRHRPHGVVAVFGPYNFPGHLPNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAgAVGNELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:PRK09457 154 HIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGR-ETGKALAAHPDIDGLLFTGSANTGYLLHRQF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 246 AKDIKKV-SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVY-DRFAEKLQQAVSKLHIGD-GL 322
Cdd:PRK09457 233 AGQPEKIlALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRwDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 323 DKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILvDVPANAKVSKEETFGPLAPLFRFKDEAD 402
Cdd:PRK09457 313 EPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDE 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832776 403 VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN---TGIISNevAPFGGIKASGLGREgSKYGIEDY 472
Cdd:PRK09457 392 AIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNkplTGASSA--APFGGVGASGNHRP-SAYYAADY 461
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
15-473 |
1.20e-80 |
|
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: 259.05 E-value: 1.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLDAnnGEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARL 93
Cdd:cd07083 23 IGGEWVDT--KERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYG--DTIPGHQADKRLIVIkQPIGVTAAITPWNFPAAMITRKAGPAL 171
Cdd:cd07083 101 LTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFY-VGLGAGVVISPWNFPVAIFTGMIVAPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 172 AAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKD--- 248
Cdd:cd07083 180 AVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLapg 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 249 ---IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKG 325
Cdd:cd07083 260 qtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 326 VTIGPLIDEKAVAKVEEHIADALEKGaRVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDE--ADV 403
Cdd:cd07083 340 TDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDdfAEA 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15832776 404 IAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGlgrEGSKYGIEDYL 473
Cdd:cd07083 419 LEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGvqPFGGFKLSG---TNAKTGGPHYL 487
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
14-482 |
4.55e-77 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 249.67 E-value: 4.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARL 93
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYG-------DTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRK 166
Cdd:PLN00412 99 LVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGegkflvsDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 167 AGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFT-GSTEIGrqlmeqC 245
Cdd:PLN00412 179 IAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIA------I 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 246 AKDIKKVSL--ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLD 323
Cdd:PLN00412 253 SKKAGMVPLqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 324 KgVTIGPLIDEKAVAKVEEHIADALEKGARVVcggKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADV 403
Cdd:PLN00412 333 D-CDITPVVSESSANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 404 IAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISN-EVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:PLN00412 409 IHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGpDHFPFQGLKDSGIGSQGITNSINMMTKVKSTVINL 488
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
12-473 |
7.42e-72 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 245.88 E-value: 7.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 12 QALINGEW----LDANNGEVIDVTNPANGDK-LGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEH 86
Cdd:PRK11904 544 AAFLEKQWqagpIINGEGEARPVVSPADRRRvVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEAN 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 87 QDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGD--TIPGhQADKRLIVIKQPIGVTAAITPWNFPAAMIT 164
Cdd:PRK11904 624 RAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGApeKLPG-PTGESNELRLHGRGVFVCISPWNFPLAIFL 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTE----IGRQ 240
Cdd:PRK11904 703 GQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTEtariINRT 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 241 LmeqCAKDIKKVSL--ELGG-NApFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLH 317
Cdd:PRK11904 783 L---AARDGPIVPLiaETGGqNA-MIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELK 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 318 IGDGLDKGVTIGPLIDEKAVAKVEEHIAdALEKGARVVCGGKAHE--RGGNFFQPTIlVDVPaNAKVSKEETFGPLAPLF 395
Cdd:PRK11904 859 VGDPRLLSTDVGPVIDAEAKANLDAHIE-RMKREARLLAQLPLPAgtENGHFVAPTA-FEID-SISQLEREVFGPILHVI 935
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 396 RFK--DEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISN--EVAPFGGikaSGLGREGSKYGIED 471
Cdd:PRK11904 936 RYKasDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAvvGVQPFGG---QGLSGTGPKAGGPH 1012
|
..
gi 15832776 472 YL 473
Cdd:PRK11904 1013 YL 1014
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
72-470 |
2.16e-70 |
|
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: 230.11 E-value: 2.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 72 RANILRNWFNLMMEHQDDLARLMTLEQGKPLAEA--------KGEISYAASFIEWFAEEgKRIYgdtIPGHQADKRLIVI 143
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteiavvLGEIDHALKHLKKWMKP-RRVS---VPLLLQPAKAYVI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 144 KQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELaIRAGIPAGVFNVVTGsAGAVGNELTSN 223
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKL-IPKYFDPEAVAVVEG-GVEVATALLAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 224 PLvRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYD 303
Cdd:cd07087 176 PF-DHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 304 RFAEKLQQAVSKLHiGDGLDKGVTIGPLIDEKAVAKVEEHIadaleKGARVVCGGKAhERGGNFFQPTILVDVPANAKVS 383
Cdd:cd07087 255 ELIEELKKAIKEFY-GEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQV-DKEERYIAPTILDDVSPDSPLM 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 384 KEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGII--SNEVAPFGGIKASGLG 461
Cdd:cd07087 328 QEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLhaAIPNLPFGGVGNSGMG 407
|
....*....
gi 15832776 462 REGSKYGIE 470
Cdd:cd07087 408 AYHGKAGFD 416
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
51-468 |
4.45e-70 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 229.42 E-value: 4.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 51 RAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAK--------GEISYAASFIE-WFAe 121
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilpvlSEINHAIKHLKkWMK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 122 eGKRIygdTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELaIRAGI 201
Cdd:cd07134 80 -PKRV---RTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKI-IREAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 202 PAGVFNVVTGSAgAVGNELTSNPlVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASK 281
Cdd:cd07134 155 DEDEVAVFEGDA-EVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 282 FRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDK-GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGkA 360
Cdd:cd07134 233 FLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG-Q 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 361 HERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGI 440
Cdd:cd07134 312 FDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVV 391
|
410 420 430
....*....|....*....|....*....|
gi 15832776 441 NTGII--SNEVAPFGGIKASGLGREGSKYG 468
Cdd:cd07134 392 NDVVLhfLNPNLPFGGVNNSGIGSYHGVYG 421
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
13-463 |
4.30e-69 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 228.95 E-value: 4.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 13 ALINGEWldANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLAR 92
Cdd:PLN02315 23 CYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:PLN02315 101 LVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 173 AGCTMVLKPASQTPFSALAL----AELAIRAGIPAGVFNVVTGSAgAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKD 248
Cdd:PLN02315 181 CGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCGGA-EIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 249 IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTI 328
Cdd:PLN02315 260 FGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 329 GPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTIlVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQAN 408
Cdd:PLN02315 340 GPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINN 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15832776 409 DTEFGLAAYFYARDLSRVFR-VG-EALEYGIVGINTGIISNEV-APFGGIKASGLGRE 463
Cdd:PLN02315 419 SVPQGLSSSIFTRNPETIFKwIGpLGSDCGIVNVNIPTNGAEIgGAFGGEKATGGGRE 476
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
9-473 |
1.09e-66 |
|
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: 222.48 E-value: 1.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 9 FRQQALINGEWLDanNGEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQ 87
Cdd:TIGR01238 36 WQAAPIIGHSYKA--DGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 88 DDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKriygDTIPGHQAdkrlivikQPIGVTAAITPWNFPAAMITRKA 167
Cdd:TIGR01238 114 PELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVR----DVLGEFSV--------ESRGVFVCISPWNFPLAIFTGQI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 168 GPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
Cdd:TIGR01238 182 SAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 248 DI-KKVSL--ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDK 324
Cdd:TIGR01238 262 REdAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 325 GVTIGPLIDEKAVAKVEEHIADALEKG---ARVVCGGKAHERGGNFFQPTiLVDVPANAKVsKEETFGPLAPLFRFK-DE 400
Cdd:TIGR01238 342 TTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPT-LFELDDIAEL-SEEVFGPVLHVVRYKaRE 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832776 401 AD-VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYL 473
Cdd:TIGR01238 420 LDqIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGG---QGLSGTGPKAGGPHYL 492
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
21-461 |
1.99e-66 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 231.68 E-value: 1.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 21 DANNGEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQG 99
Cdd:PRK11905 562 GDVDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 100 KPLAEAKGEISYAASFIEWFAEEGKRIYGDtiPGHQadkrlivikqPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVL 179
Cdd:PRK11905 642 KTLANAIAEVREAVDFLRYYAAQARRLLNG--PGHK----------PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLA 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 180 KPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTE----IGRQLMEQCAKDIKKVSlE 255
Cdd:PRK11905 710 KPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEvarlIQRTLAKRSGPPVPLIA-E 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 256 LGG-NApFIVFDDADLDKAVEGALASKFRNAGQTCvCANR-LYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLID 333
Cdd:PRK11905 789 TGGqNA-MIVDSSALPEQVVADVIASAFDSAGQRC-SALRvLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVID 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 334 EKAVAKVEEHIADALEKGARV-VCGGKAHERGGNFFQPTIL-VDvpaNAKVSKEETFGPLAPLFRFK-DEAD-VIAQAND 409
Cdd:PRK11905 867 AEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIeID---SISDLEREVFGPVLHVVRFKaDELDrVIDDINA 943
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15832776 410 TEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGLG 461
Cdd:PRK11905 944 TGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGvqPFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
13-414 |
1.35e-63 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 223.28 E-value: 1.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 13 ALINGEwldANNGEVIDVTNPANG-DKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLA 91
Cdd:COG4230 560 PLIAGE---AASGEARPVRNPADHsDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELM 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 92 RLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHqadkrlivikqPIGVTAAITPWNFPAAMITRKAGPAL 171
Cdd:COG4230 637 ALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTVLR-----------GRGVFVCISPWNFPLAIFTGQVAAAL 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 172 AAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTE----IGRQLMEQCAK 247
Cdd:COG4230 706 AAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTEtarlINRTLAARDGP 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 248 DIKKVSlELGG-NApFIVFDDADLDKAVEGALASKFRNAGQTCvCANR-LYVQDGVYDRFAEKLQQAVSKLHIGDGLDKG 325
Cdd:COG4230 786 IVPLIA-ETGGqNA-MIVDSSALPEQVVDDVLASAFDSAGQRC-SALRvLCVQEDIADRVLEMLKGAMAELRVGDPADLS 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 326 VTIGPLIDEKAVAKVEEHIaDALEKGARVVCGGKAHE--RGGNFFQPTIL-VDvpaNAKVSKEETFGPLAPLFRFK-DEA 401
Cdd:COG4230 863 TDVGPVIDAEARANLEAHI-ERMRAEGRLVHQLPLPEecANGTFVAPTLIeID---SISDLEREVFGPVLHVVRYKaDEL 938
|
410
....*....|....
gi 15832776 402 D-VIAQANDTEFGL 414
Cdd:COG4230 939 DkVIDAINATGYGL 952
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
142-462 |
5.66e-62 |
|
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: 208.11 E-value: 5.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 142 VIKQPIGVTAAITPWNFP-----AAMITrkagpALAAGCTMVLKPASQTPFSALALAELaIRAGIPAGVFNVVTGSAgAV 216
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPlylalGPLIA-----ALAAGNRVMIKPSEFTPRTSALLAEL-LAEYFDEDEVAVVTGGA-DV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 217 GNELTSNPLvRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLY 296
Cdd:cd07133 170 AAAFSSLPF-DHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 297 VQDGVYDRFAEKLQQAVSKLHiGDGLDkGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHER--GGNFFQPTILV 374
Cdd:cd07133 249 VPEDKLEEFVAAAKAAVAKMY-PTLAD-NPDYTSIINERHYARLQGLLEDARAKGARVIELNPAGEDfaATRKLPPTLVL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 375 DVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI--ISNEVAPF 452
Cdd:cd07133 327 NVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLlhVAQDDLPF 406
|
330
....*....|
gi 15832776 453 GGIKASGLGR 462
Cdd:cd07133 407 GGVGASGMGA 416
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
10-476 |
6.14e-62 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 212.30 E-value: 6.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 10 RQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDD 89
Cdd:PLN02419 113 RVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 90 LARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGP 169
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 170 ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVgNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI 249
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 250 KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVC-ANRLYVQDGvyDRFAEKLQQAVSKLHIGDGLDKGVTI 328
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMAlSTVVFVGDA--KSWEDKLVERAKALKVTCGSEPDADL 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 329 GPLIDEKAVAKVEEHIADALEKGARVVCGGK-----AHERgGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADV 403
Cdd:PLN02419 430 GPVISKQAKERICRLIQSGVDDGAKLLLDGRdivvpGYEK-GNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832776 404 IAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLGREG--SKYGIEDYLEIK 476
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIpVPLPFFSFTGNKASFAGDLNfyGKAGVDFFTQIK 584
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
72-472 |
2.14e-59 |
|
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: 201.29 E-value: 2.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 72 RANILRNWFNLMMEHQDDLARLMTLEQGKP-----LAE---AKGEISYAASFIEWFAEEGKRiyGDTIPGHQADKrLIVI 143
Cdd:cd07135 29 RLWQLKQLYWAVKDNEEAIVEALKKDLGRPpfetlLTEvsgVKNDILHMLKNLKKWAKDEKV--KDGPLAFMFGK-PRIR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 144 KQPIGVTAAITPWNFPaamITRKAGP---ALAAGCTMVLKPASQTPFSALALAELaIRAGIPAGVFNVVTGsagavGNEL 220
Cdd:cd07135 106 KEPLGVVLIIGPWNYP---VLLALSPlvgAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVVQG-----GVPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 221 TSNPLVRKLS---FTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYV 297
Cdd:cd07135 177 TTALLEQKFDkifYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 298 QDGVYDRFAEKLQQAVSKLHiGDGLDKGVTIGPLIDEKAVAKVEEHIADAleKGaRVVCGGKaHERGGNFFQPTILVDVP 377
Cdd:cd07135 257 DPSVYDEFVEELKKVLDEFY-PGGANASPDYTRIVNPRHFNRLKSLLDTT--KG-KVVIGGE-MDEATRFIPPTIVSDVS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 378 ANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGII--SNEVAPFGGI 455
Cdd:cd07135 332 WDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPFGGV 411
|
410
....*....|....*..
gi 15832776 456 KASGLGREGSKYGIEDY 472
Cdd:cd07135 412 GDSGYGAYHGKYGFDTF 428
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
142-470 |
4.01e-58 |
|
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: 198.50 E-value: 4.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 142 VIKQPIGVTAAITPWNFP-----AAMItrkaGpALAAGCTMVLKPASQTPFSALALAELaIRAGIPAGVFNVVTGSAgAV 216
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPfqlalAPLI----G-AIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEGGV-EE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 217 GNELTSNPlVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLY 296
Cdd:cd07136 169 NQELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 297 VQDGVYDRFAEKLQQAVsKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIadaleKGARVVCGGKaHERGGNFFQPTILVDV 376
Cdd:cd07136 248 VHESVKEKFIKELKEEI-KKFYGEDPLESPDYGRIINEKHFDRLAGLL-----DNGKIVFGGN-TDRETLYIEPTILDNV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 377 PANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGII--SNEVAPFGG 454
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMhlANPYLPFGG 400
|
330
....*....|....*.
gi 15832776 455 IKASGLGREGSKYGIE 470
Cdd:cd07136 401 VGNSGMGSYHGKYSFD 416
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
70-470 |
4.88e-56 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 194.09 E-value: 4.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 70 KERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAK--------GEISYaasFIEWFAEEGKRIYGDTiPGHQADKRLI 141
Cdd:PTZ00381 29 EFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmtevlltvAEIEH---LLKHLDEYLKPEKVDT-VGVFGPGKSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 142 VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELaIRAGIPAGVFNVVTGSAgAVGNELT 221
Cdd:PTZ00381 105 IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL-LTKYLDPSYVRVIEGGV-EVTTELL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 222 SNPLvRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGV 301
Cdd:PTZ00381 183 KEPF-DHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 302 YDRFAEKLQQAVsKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIADaleKGARVVCGGKAHERgGNFFQPTILVDVPANAK 381
Cdd:PTZ00381 262 KDKFIEALKEAI-KEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVDIE-NKYVAPTIIVNPDLDSP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 382 VSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI--ISNEVAPFGGIKASG 459
Cdd:PTZ00381 337 LMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVfhLLNPNLPFGGVGNSG 416
|
410
....*....|.
gi 15832776 460 LGREGSKYGIE 470
Cdd:PTZ00381 417 MGAYHGKYGFD 427
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
22-461 |
8.19e-55 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 197.89 E-value: 8.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 22 ANNGEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGK 100
Cdd:PRK11809 655 VAAGEMSPVINPADpRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 101 PLAEAKGEISYAASFIEWFAEEGKRIYG-DTipgHQadkrlivikqPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVL 179
Cdd:PRK11809 735 TFSNAIAEVREAVDFLRYYAGQVRDDFDnDT---HR----------PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLA 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 180 KPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI----KKVSL- 254
Cdd:PRK11809 802 KPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqgRPIPLi 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 255 -ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKGVTIGPLID 333
Cdd:PRK11809 882 aETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVID 961
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 334 EKAVAKVEEHIADALEKGARV---VCGGKAHERGGNFFQPTiLVDVPANAKVsKEETFGPLAPLFRFKDEA--DVIAQAN 408
Cdd:PRK11809 962 AEAKANIERHIQAMRAKGRPVfqaARENSEDWQSGTFVPPT-LIELDSFDEL-KREVFGPVLHVVRYNRNQldELIEQIN 1039
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15832776 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGLG 461
Cdd:PRK11809 1040 ASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvqPFGGEGLSGTG 1094
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
13-459 |
1.10e-52 |
|
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: 185.87 E-value: 1.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 13 ALINGEWLDanNGEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMM-EHQDDL 90
Cdd:cd07123 35 LVIGGKEVR--TGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 91 ARLMTLEQGKPLAEAkgEISYAASFIEWF---AEEGKRIYGDTIPGHQADKRLIVIKQPI-GVTAAITPWNFPAAMITRK 166
Cdd:cd07123 113 NAATMLGQGKNVWQA--EIDAACELIDFLrfnVKYAEELYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGGNLA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 167 AGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCA 246
Cdd:cd07123 191 GAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 247 KDIK------KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
Cdd:cd07123 270 ENLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 321 GLDKGVTIGPLIDEKAVAKVEEHIADALE-KGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKD 399
Cdd:cd07123 350 PDDFSNFMGAVIDEKAFDRIKGYIDHAKSdPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPD 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832776 400 E--ADVIAQANDT-EFGLAAYFYARDLSRVFRVGEALEY--GIVGIN---TGIISNEvAPFGGIKASG 459
Cdd:cd07123 430 SdfEETLELVDTTsPYALTGAIFAQDRKAIREATDALRNaaGNFYINdkpTGAVVGQ-QPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
76-470 |
2.06e-46 |
|
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: 167.01 E-value: 2.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 76 LRNWFNLMMEHQDDLARLMTLEQGKPLAEA--------KGEISYAASFI-EWFAEEgkriYGDTIPGHQADKRLIViKQP 146
Cdd:cd07132 26 LEALLRMLEENEDEIVEALAKDLRKPKFEAvlseillvKNEIKYAISNLpEWMKPE----PVKKNLATLLDDVYIY-KEP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 147 IGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELairagIPAGV----FNVVTGSAgAVGNELTS 222
Cdd:cd07132 101 LGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLdkecYPVVLGGV-EETTELLK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 223 NplvR--KLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDG 300
Cdd:cd07132 175 Q---RfdYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 301 VYDRFAEKLQQAVSKLHiGDGLDKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKaHERGGNFFQPTILVDVPANA 380
Cdd:cd07132 252 VQEKFVEALKKTLKEFY-GEDPKESPDYGRIINDRHFQRLK-----KLLSGGKVAIGGQ-TDEKERYIAPTVLTDVKPSD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 381 KVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI--ISNEVAPFGGIKAS 458
Cdd:cd07132 325 PVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTImhYTLDSLPFGGVGNS 404
|
410
....*....|..
gi 15832776 459 GLGREGSKYGIE 470
Cdd:cd07132 405 GMGAYHGKYSFD 416
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
48-470 |
1.68e-40 |
|
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: 150.64 E-value: 1.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 48 DETRAAIDAAnralpvwRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEA-KGEISYAASFI--------EW 118
Cdd:cd07137 6 RELRETFRSG-------RTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCklaikelkKW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 119 FAEEGKRIYGDTIPGHQAdkrliVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELaIR 198
Cdd:cd07137 79 MAPEKVKTPLTTFPAKAE-----IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 199 AGIPAGVFNVVTGSAgAVGNELTSNPLvRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGAL 278
Cdd:cd07137 153 EYLDTKAIKVIEGGV-PETTALLEQKW-DKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 279 ASKF-RNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDKG-----------VTIGPLIDEKAVAkveehiad 346
Cdd:cd07137 231 GGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKdlsrivnshhfQRLSRLLDDPSVA-------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 347 alekgARVVCGGKAHERgGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRV 426
Cdd:cd07137 303 -----DKIVHGGERDEK-NLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELK 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15832776 427 FRVGEALEYGIVGINTGII--SNEVAPFGGIKASGLGREGSKYGIE 470
Cdd:cd07137 377 RRIVAETSSGGVTFNDTVVqyAIDTLPFGGVGESGFGAYHGKFSFD 422
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
142-470 |
5.42e-37 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 142.17 E-value: 5.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 142 VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAElAIRAGIPAGVFNVVTGSAgAVGNELT 221
Cdd:PLN02203 104 VVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAA-NIPKYLDSKAVKVIEGGP-AVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 222 SNPLvRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIV--FDDA-DLDKAVEGALASKFRN-AGQTCVCANRLYV 297
Cdd:PLN02203 182 QHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAIDYVLV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 298 QDGVYDRFAEKLQQAVSKLhIGDGLDKGVTIGPLIDEKAVAKVEEHIADALEKgARVVCGGKAHERGgNFFQPTILVDVP 377
Cdd:PLN02203 261 EERFAPILIELLKSTIKKF-FGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSIDEKK-LFIEPTILLNPP 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 378 ANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISN--EVAPFGGI 455
Cdd:PLN02203 338 LDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYacDSLPFGGV 417
|
330
....*....|....*
gi 15832776 456 KASGLGREGSKYGIE 470
Cdd:PLN02203 418 GESGFGRYHGKYSFD 432
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
12-422 |
2.52e-35 |
|
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: 137.79 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 12 QALINGEWLdANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLA 91
Cdd:cd07128 2 QSYVAGQWH-AGTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 92 RLMTLeQGKPLAEAKGEISYAASFIEWFAEEGKR--------IYGDTIP----GHQADKRLIVIKQpiGVTAAITPWNFP 159
Cdd:cd07128 81 ALSAA-TGATRRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPlskdGTFVGQHILTPRR--GVAVHINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 160 AAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGI-PAGVFNVVTGSAGAVGNELTSNPLVrklSFTGSTEIG 238
Cdd:cd07128 158 VWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHLGEQDVV---AFTGSAATA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 239 RQL--------------MEQcakDikkvSLELGGNAPFIVFDDADLD---KAVEGALASKfrnAGQTCVCANRLYVQDGV 301
Cdd:cd07128 235 AKLrahpnivarsirfnAEA---D----SLNAAILGPDATPGTPEFDlfvKEVAREMTVK---AGQKCTAIRRAFVPEAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 302 YDRFAEKLQQAVSKLHIGDGLDKGVTIGPLIDEKAVAKVEEHIAdALEKGARVVCGGK-------AHERGGNFFQPTILV 374
Cdd:cd07128 305 VDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVA-TLLAEAEVVFGGPdrfevvgADAEKGAFFPPTLLL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 15832776 375 -DVPANAKVSKE-ETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD 422
Cdd:cd07128 384 cDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
15-422 |
3.55e-34 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 134.45 E-value: 3.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 15 INGEWLdANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLM 94
Cdd:PRK11903 9 VAGRWQ-AGSGAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 95 TLEQGKPLAEAKGEISYAASFIEWFAEEGKRIyGDTipGHQADKRLIVI-KQPI-----------GVTAAITPWNFPAAM 162
Cdd:PRK11903 88 TANSGTTRNDSAVDIDGGIFTLGYYAKLGAAL-GDA--RLLRDGEAVQLgKDPAfqgqhvlvptrGVALFINAFNFPAWG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 163 ITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGI-PAGVFNVVTGSAGAVGNELTSNPLVrklSFTGSTEIGRQL 241
Cdd:PRK11903 165 LWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFDVV---SFTGSAETAAVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 242 MEQCA-------KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVS 314
Cdd:PRK11903 242 RSHPAvvqrsvrVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 315 KLHIGDGLDKGVTIGPLIDEKAVAKVEEHIAdALEKGARVVCGGKAHE------RGGNFFQPTILV--DVPANAKVSKEE 386
Cdd:PRK11903 322 KTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLGasDPDAATAVHDVE 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 15832776 387 TFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD 422
Cdd:PRK11903 401 VFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
52-408 |
1.21e-30 |
|
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: 123.42 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 52 AAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEE-------GK 124
Cdd:cd07129 3 AAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLvregswlDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 125 RIygDT-----IPGHQADKRLIviKQPIGVTAAITPWNFPAAMITrkAG----PALAAGCTMVLKPASQTPFSALALAEL 195
Cdd:cd07129 83 RI--DPadpdrQPLPRPDLRRM--LVPLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKAHPAHPGTSELVARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 196 AIRA----GIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAK--DIKKVSLELGGNAPFIVFDDA- 268
Cdd:cd07129 157 IRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGAl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 269 --DLDKAVEGALASKFRNAGQTCVCANRLYVQDGV-YDRFAEKLQQAVSK------LH--IGDGLDKGVtigplidekav 337
Cdd:cd07129 237 aeRGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPaGDAFIAALAEALAAapaqtmLTpgIAEAYRQGV----------- 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832776 338 akveEHIADAleKGARVVCGGKAHErGGNFFQPTILV----DVPANAKVSkEETFGPLAPLFRFKDEADVIAQAN 408
Cdd:cd07129 306 ----EALAAA--PGVRVLAGGAAAE-GGNQAAPTLFKvdaaAFLADPALQ-EEVFGPASLVVRYDDAAELLAVAE 372
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
118-472 |
1.06e-28 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 118.61 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 118 WFAEEGKRIYGDTIPGHQAdkrliVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELaI 197
Cdd:PLN02174 89 WMAPEKAKTSLTTFPASAE-----IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-L 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 198 RAGIPAGVFNVVTGSAGAVGNELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGA 277
Cdd:PLN02174 163 EQYLDSSAVRVVEGAVTETTALLEQK--WDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 278 LASKFR-NAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHiGDGLDKGVTIGPLIDEKAVAKVEEhIADALEKGARVVC 356
Cdd:PLN02174 241 IAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETFY-GKNPMESKDMSRIVNSTHFDRLSK-LLDEKEVSDKIVY 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 357 GGKaHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYG 436
Cdd:PLN02174 319 GGE-KDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAG 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15832776 437 ivgintGIISNEVA--------PFGGIKASGLGREGSKYGIEDY 472
Cdd:PLN02174 398 ------GIVVNDIAvhlalhtlPFGGVGESGMGAYHGKFSFDAF 435
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
52-463 |
3.15e-28 |
|
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: 116.57 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 52 AAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAkGEISYAASFIEWFAeegKRIYGDTI 131
Cdd:cd07084 3 RALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARA---FVIYSYRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 132 PGHQADKRLIVIKQ-------PIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGI-PA 203
Cdd:cd07084 79 PHEPGNHLGQGLKQqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 204 GVFNVVTGSaGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQcAKDIkKVSLELGGNAPFIVFDDADLDKAVEGALA-SKF 282
Cdd:cd07084 159 EDVTLINGD-GKTMQALLLHPNPKMVLFTGSSRVAEKLALD-AKQA-RIYLELAGFNWKVLGPDAQAVDYVAWQCVqDMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 283 RNAGQTCVCANRLYV-QDGVYDRFAEKLQQAVSKLhigdgLDKGVTIGPLIDEKAVAKVEEHIADAlekGARVVCGGK-- 359
Cdd:cd07084 236 ACSGQKCTAQSMLFVpENWSKTPLVEKLKALLARR-----KLEDLLLGPVQTFTTLAMIAHMENLL---GSVLLFSGKel 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 360 ----AHERGGNFFQPTILVDVPANAKVSK---EETFGPLAPLFRFKD--EADVIAQANDTEFGLAAYFYARDLSRVFRVG 430
Cdd:cd07084 308 knhsIPSIYGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKKdqLALVLELLERMHGSLTAAIYSNDPIFLQELI 387
|
410 420 430
....*....|....*....|....*....|....*...
gi 15832776 431 EALE-----YGIVGINTGIISNEVAPFGGiKASGLGRE 463
Cdd:cd07084 388 GNLWvagrtYAILRGRTGVAPNQNHGGGP-AADPRGAG 424
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
14-400 |
2.09e-20 |
|
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: 93.71 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 14 LINGEWLDANNGevIDVTNPANGDKLGSVPKMGADETRAAIDAAnRALP---VWRALTAKERANIlrnWFNLMM------ 84
Cdd:cd07126 2 LVAGKWKGASNY--TTLLDPLNGDKFISVPDTDEDEINEFVDSL-RQCPksgLHNPLKNPERYLL---YGDVSHrvahel 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 85 ---EHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIY--GDTIPGHQADKRLIVIKQPIGVTAAITPWNFP 159
Cdd:cd07126 76 rkpEVEDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLarSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 160 AAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTgSAGAVGNELTSNPLVRKLSFTGSTEIGR 239
Cdd:cd07126 156 LEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIH-SDGPTMNKILLEANPRMTLFTGSSKVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 240 QLmeqcAKDIK-KVSLELGGNAPFIVFDD-ADLDKAVEGALASKFRNAGQTCVCANRLYVQDG-VYDRFAEKLQQAVSKL 316
Cdd:cd07126 235 RL----ALELHgKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALAEQR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 317 HIGDgldkgVTIGPLIdEKAVAKVEEHIADALE-KGARVVCGGKA---HERGGNF--FQPTIlVDVPANAKVSKE----- 385
Cdd:cd07126 311 KLED-----LTIGPVL-TWTTERILDHVDKLLAiPGAKVLFGGKPltnHSIPSIYgaYEPTA-VFVPLEEIAIEEnfelv 383
|
410
....*....|....*..
gi 15832776 386 --ETFGPLAPLFRFKDE 400
Cdd:cd07126 384 ttEVFGPFQVVTEYKDE 400
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
48-442 |
2.47e-12 |
|
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: 68.45 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 48 DETRAAIDAANRALPVWralTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIY 127
Cdd:cd07081 2 DDAVAAAKVAQQGLSCK---SQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 128 GdtIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKP----ASQTPFSALALAELAIRAGIPA 203
Cdd:cd07081 79 G--VLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 204 GVFNVVTGSAGAVGNELTSNPLVRKLSFTGsteiGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFR 283
Cdd:cd07081 157 NLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 284 NAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLD-------KGVTIGPLIDEKAVAKVEEHIADALEKGARVVC 356
Cdd:cd07081 233 DNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQqvqpvilKNGDVNRDIVGQDAYKIAAAAGLKVPQETRILI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 357 GgkaherggnffQPTILVDVPANAkvskEETFGPLAPLFRFKDEADVIAQA----NDTEFGLAAYFYARDLS---RVFRV 429
Cdd:cd07081 313 G-----------EVTSLAEHEPFA----HEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKaieNMNQF 377
|
410
....*....|...
gi 15832776 430 GEALEYGIVGINT 442
Cdd:cd07081 378 ANAMKTSRFVKNG 390
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
55-363 |
1.16e-11 |
|
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: 66.48 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 55 DAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIE------WFAEEGKRIYG 128
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSEsklyknIDTERGITASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 129 DTIPGH--QADKRLIVIKQPIGVTAAITPWNFPAAMITrKAGPALAAGCTMVLKPASQTPFSALALAEL---AIRAGIPA 203
Cdd:cd07077 81 GHIQDVllPDNGETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLfqaADAAHGPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 204 GVFNVVTGSAGAVGNELTSNPLVRKLSFTGsteiGRQLMEQCAKDIKKVSLeLG---GNAPFIVFDDADLDKAVEGALAS 280
Cdd:cd07077 160 ILVLYVPHPSDELAEELLSHPKIDLIVATG----GRDAVDAAVKHSPHIPV-IGfgaGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 281 KFRNaGQTCVCANRLYVQDGVYD----RFAEKLQQAVSKLHIG---------DGLDKGVT--IGPLIDEKAVAKVEEHIA 345
Cdd:cd07077 235 KFFD-QNACASEQNLYVVDDVLDplyeEFKLKLVVEGLKVPQEtkplskettPSFDDEALesMTPLECQFRVLDVISAVE 313
|
330
....*....|....*...
gi 15832776 346 DALekgARVVCGGKAHER 363
Cdd:cd07077 314 NAW---MIIESGGGPHTR 328
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
49-460 |
1.36e-11 |
|
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: 66.73 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 49 ETRAAIDAANRALPVWRALTAKERA----NILRNWFNLMME------HQDDLARLMTLEQGKPLAEAKG--EISYAA--- 113
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAgvclEILQRLNARSFEmahavmHTTGQAFMMAFQAGGPHAQDRGleAVAYAWrem 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 114 SFI----EWFAEEGKRiygdtiPGHQADKRLIVIkqPIGVTAAITPWNFPaamiTRKAGPA----LAAGCTMVLKPAsqt 185
Cdd:cd07127 165 SRIpptaEWEKPQGKH------DPLAMEKTFTVV--PRGVALVIGCSTFP----TWNGYPGlfasLATGNPVIVKPH--- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 186 PFSALALA-------ELAIRAGI-PAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKdiKKVSLELG 257
Cdd:cd07127 230 PAAILPLAitvqvarEVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 258 GNAPFIVfDDADLDKAVEGALASKFR-NAGQTCVCANRLYV-QDGV--------YDRFAEKLQQAVSKLhIGDGLDKGVT 327
Cdd:cd07127 308 GVNTVVV-DSTDDLKAMLRNLAFSLSlYSGQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGL-LADPARAAAL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 328 IGPLIDEKAVAKVEEhiADALekgARVVCGGKAHER----GGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADV 403
Cdd:cd07127 386 LGAIQSPDTLARIAE--ARQL---GEVLLASEAVAHpefpDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHS 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832776 404 IAQANDT--EFG-LAAYFYARDLSRVFRVGE-ALEYGI---VGINTGIISNEVAPFGGIKASGL 460
Cdd:cd07127 461 IELARESvrEHGaMTVGVYSTDPEVVERVQEaALDAGValsINLTGGVFVNQSAAFSDFHGTGA 524
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
146-434 |
4.16e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 55.32 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 146 PIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKP---ASQTpfSALA---LAELAIRAGIPAGVFNVVTGSAGAVGNE 219
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKV--SAYAvelINKAIAEAGGPDNLVVTVEEPTIETTNE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 220 LTSNPLVRKLSFTGSTEIGRQLMeqcaKDIKKVSLELGGNAPFIVFDDADLDKA----VEGAlasKFRNaGQTCVCANRL 295
Cdd:cd07121 175 LMAHPDINLLVVTGGPAVVKAAL----SSGKKAIGAGAGNPPVVVDETADIEKAardiVQGA---SFDN-NLPCIAEKEV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 296 YVQDGVYDRFAEKLQQA-VSKLHIGDGLDKGVTI-----GPLIDEKAVAKVEEHIADAlekgARVVCGGKAherggnffq 369
Cdd:cd07121 247 IAVDSVADYLIAAMQRNgAYVLNDEQAEQLLEVVlltnkGATPNKKWVGKDASKILKA----AGIEVPADI--------- 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15832776 370 PTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGL--AAYFYARDLSRVFRVGEALE 434
Cdd:cd07121 314 RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTKMARAMQ 380
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
29-464 |
4.84e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 55.29 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 29 DVTNPANGDKLGSVPKMGA-DETRAAIDAANRALPVWRALTAKERANILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
Cdd:PRK15398 16 EMLSSQTVSPPAAVGEMGVfASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 108 EISYAASF----IEWfaeegkrIYGDTIPGhqaDKRLIVIK-QPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKP- 181
Cdd:PRK15398 96 AKNVAAAEktpgVED-------LTTEALTG---DNGLTLIEyAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPh 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 182 --ASQTPFSALALAELAI-RAGIPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMeqcaKDIKKVSLELGG 258
Cdd:PRK15398 166 pgAKKVSLRAIELLNEAIvAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAM----KSGKKAIGAGAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 259 NAPFIVFDDADLDKA----VEGAlasKFRNaGQTCVCANRLYVQDGVYDRFAEKLQQA----VSKLHIgDGLDKGVTI-G 329
Cdd:PRK15398 242 NPPVVVDETADIEKAardiVKGA---SFDN-NLPCIAEKEVIVVDSVADELMRLMEKNgavlLTAEQA-EKLQKVVLKnG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 330 PLIDEKAVAKVEEHIADAL----EKGARVvcggkaherggnffqptILVDVPANAKVSKEETFGPLAPLFRFKDEADVIA 405
Cdd:PRK15398 317 GTVNKKWVGKDAAKILEAAginvPKDTRL-----------------LIVETDANHPFVVTELMMPVLPVVRVKDVDEAIA 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832776 406 QANDTEFGL--AAYFYARDLSRVFRVGEAleygivgINTGI-ISNevAP-FGGIkasGLGREG 464
Cdd:PRK15398 380 LAVKLEHGNrhTAIMHSRNVDNLNKMARA-------IQTSIfVKN--GPsYAGL---GLGGEG 430
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
138-311 |
9.68e-08 |
|
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: 54.03 E-value: 9.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 138 KRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKP---ASQTPFSAL-ALAELAIRAGIPAGVFNVVTGSA 213
Cdd:cd07122 87 KGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAkIMREAAVAAGAPEGLIQWIEEPS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832776 214 GAVGNELTSNPLVRKLSFTGSTEigrqlMEQCAKDIKKVSLELG-GNAPFIVFDDADLDKAVEGALASK-FRNAgqtCVC 291
Cdd:cd07122 167 IELTQELMKHPDVDLILATGGPG-----MVKAAYSSGKPAIGVGpGNVPAYIDETADIKRAVKDIILSKtFDNG---TIC 238
|
170 180
....*....|....*....|..
gi 15832776 292 A--NRLYVQDGVYDRFAEKLQQ 311
Cdd:cd07122 239 AseQSVIVDDEIYDEVRAELKR 260
|
|
| |
