|
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: 981.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 1 MQLNDMTLFRQQALIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWF 80
Cdd:PRK11241 1 MQLNDSTLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 81 DLMMENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPA 160
Cdd:PRK11241 81 NLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 161 AMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQ 240
Cdd:PRK11241 161 AMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 241 LMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGD 320
Cdd:PRK11241 241 LMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 321 GLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDE 400
Cdd:PRK11241 321 GLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:PRK11241 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
..
gi 1458409611 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: 845.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 30 VTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 110 SYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSA 189
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 190 LALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDAD 269
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 270 LDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIA 349
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 350 KGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRV 429
Cdd:cd07103 321 KGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1458409611 430 GEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCI 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: 806.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 30 VTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 110 SYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSA 189
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 190 LALAELANRAGIPAGVFNVVTGS-AGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGSrAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 269 DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAI 348
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 349 AKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFR 428
Cdd:TIGR01780 321 EKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1458409611 429 VGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 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: 801.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 2 QLNDMTLFRQQALIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFD 81
Cdd:PLN02278 16 KLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 82 LMMENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAA 161
Cdd:PLN02278 96 LIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 162 MITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQL 241
Cdd:PLN02278 176 MITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 242 MEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDG 321
Cdd:PLN02278 256 MAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 322 LQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEA 401
Cdd:PLN02278 336 FEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 402 DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCIG 481
Cdd:PLN02278 416 EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCLG 495
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
6-482 |
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: 690.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 6 MTLFRQQALIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMME 85
Cdd:COG1012 1 MTTPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 86 NQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITR 165
Cdd:COG1012 81 RREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 166 KAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:COG1012 161 KLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 246 AKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDG 325
Cdd:COG1012 241 AENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 326 VTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHAL-GGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVI 404
Cdd:COG1012 321 TDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 405 AQANDTEFGLAAYFYARDLSRVFRVGEALE--------YGIIGINTgiistevAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEagmvwindGTTGAVPQ-------APFGGVKQSGIGREGGREGLEEYTETK 473
|
....*.
gi 1458409611 477 YMCIGL 482
Cdd:COG1012 474 TVTIRL 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: 614.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 19 WRDaPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQ 98
Cdd:pfam00171 1 WVD-SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 99 GKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGhQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMV 178
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 179 LKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGG 258
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 259 NAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVA 338
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 339 KVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYF 418
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1458409611 419 YARDLSRVFRVGEALEYGIIGI-NTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 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: 555.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 52 EAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTI 131
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 132 PGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTG 211
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 212 SAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVC 291
Cdd:cd07078 162 DGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 292 ANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGK-PHALGGNFFQP 370
Cdd:cd07078 242 ASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKrLEGGKGYFVPP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 371 TILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEV- 449
Cdd:cd07078 322 TVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPs 401
|
410 420
....*....|....*....|....*..
gi 1458409611 450 APFGGVKASGLGREGSKYGIEDYLEIK 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: 536.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 15 IDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLM 94
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 95 TLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAG 174
Cdd:cd07088 82 VEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 175 CTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSL 254
Cdd:cd07088 162 NTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 255 ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDE 334
Cdd:cd07088 242 ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 335 KAVAKVEEHIADAIAKGAKVVTGGK-PHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFG 413
Cdd:cd07088 322 AALDKVEEMVERAVEAGATLLTGGKrPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYG 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1458409611 414 LAAYFYARDLSRVFRVGEALEYGiigintgiistEV----APF-------GGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07088 402 LTSYIYTENLNTAMRATNELEFG-----------ETyinrENFeamqgfhAGWKKSGLGGADGKHGLEEYLQTK 464
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
30-480 |
3.85e-172 |
|
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: 491.69 E-value: 3.85e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 30 VTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAK-GE 108
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 109 ISYAASFIEWFAEEGKRIYGDTIPgHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS 188
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYP-QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 189 ALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 269 DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAI 348
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 349 AKGAKVVTGGKPHAL----GGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLS 424
Cdd:cd07093 320 AEGATILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1458409611 425 RVFRVGEALEygiigintgiiSTEV-----------APFGGVKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07093 400 RAHRVARRLE-----------AGTVwvncwlvrdlrTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
30-476 |
8.37e-167 |
|
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: 478.20 E-value: 8.37e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 30 VTNPANGEQLGSVPKMGADETREAIEAANRAL--PAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKG 107
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 108 EISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPF 187
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 188 SALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDD 267
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 268 ADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADA 347
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 348 IAKGAKVVTGGKPHAL----GGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDL 423
Cdd:cd07114 321 REEGARVLTGGERPSGadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1458409611 424 SRVFRVGEALE--------YGIIGIntgiisteVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07114 401 ARAHRVARAIEagtvwvntYRALSP--------SSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
30-476 |
5.36e-164 |
|
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: 470.86 E-value: 5.36e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 30 VTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 110 SYAASFIEWFAE---EGKRIYGDtipghqADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTP 186
Cdd:cd07106 81 GGAVAWLRYTASldlPDEVIEDD------DTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 187 FSALALAELANRAgIPAGVFNVVTGSaGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFD 266
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSGG-DELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 267 DADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIAD 346
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 347 AIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRV 426
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1458409611 427 FRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
12-476 |
1.00e-162 |
|
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: 468.61 E-value: 1.00e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 12 QALIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPA--WRALTAKERANILRRWFDLMMENQDD 89
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 90 LARLMTLEQGKPLAE-AKGEISYAASFIEWFAEEGKRIYGDTIPghQADKRL-LVIKQPIGVTAAITPWNFPAAMITRKA 167
Cdd:cd07091 85 LAALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIP--IDGNFLaYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 168 GPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 248 -DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGV 326
Cdd:cd07091 243 sNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 327 TTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQ 406
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07091 403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
28-480 |
2.20e-160 |
|
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: 462.07 E-value: 2.20e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 28 IAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKG 107
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 108 EISYAASFIEWFAEEGKRIYGDTIPGHQA----DKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPAS 183
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFDASpggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 184 QTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAkdIKKVSLELGGNAPFI 263
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 264 VFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEH 343
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 344 IADAIAKGAKVVTGGKPHalgGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDL 423
Cdd:cd07149 319 VEEAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 424 SRVFRVGEALEygIIGINTGIIST---EVAPFGGVKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07149 396 QKALKAARELE--VGGVMINDSSTfrvDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
30-480 |
8.12e-159 |
|
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: 457.95 E-value: 8.12e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 30 VTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:cd07150 3 DLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 110 SYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSA 189
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 190 LALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDAD 269
Cdd:cd07150 163 LKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 270 LDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIA 349
Cdd:cd07150 243 LDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 350 KGAKVVTGGKphaLGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRV 429
Cdd:cd07150 323 KGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1458409611 430 GEALEYGIIGINTGIISTE-VAPFGGVKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07150 400 AERLESGMVHINDPTILDEaHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
28-480 |
1.13e-157 |
|
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: 455.27 E-value: 1.13e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 28 IAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKG 107
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 108 EISYAASFIEWFAEEGKRIYGDTIP--GHQADKRLLVI--KQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPAS 183
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPvdAYEYNERRIAFtvREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 184 QTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFI 263
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 264 VFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEH 343
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 344 IADAIAKGAKVVTGGKphALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDL 423
Cdd:cd07145 321 VNDAVEKGGKILYGGK--RDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDI 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1458409611 424 SRVFRVGEALEYgiiGINTGIISTEV----APFGGVKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07145 399 NRALKVARELEA---GGVVINDSTRFrwdnLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
15-482 |
2.21e-157 |
|
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: 455.23 E-value: 2.21e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 15 IDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRAL--PAWRALTAKERANILRRWFDLMMENQDDLAR 92
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPgHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07119 82 LETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYD-VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 173 AGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLI 332
Cdd:cd07119 241 ALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 333 DEKAVAKVEEHIADAIAKGAKVVTGGK----PHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
Cdd:cd07119 321 SAEHREKVLSYIQLGKEEGARLVCGGKrptgDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLAN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1458409611 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:cd07119 401 DTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININL 474
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
15-476 |
1.92e-155 |
|
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: 449.65 E-value: 1.92e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 15 IDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLM 94
Cdd:cd07138 3 IDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 95 TLEQGKPLAEAK--------GEISYAASFIEWFAEEGKRiyGDTipghqadkrlLVIKQPIGVTAAITPWNFPAAMITRK 166
Cdd:cd07138 83 TLEMGAPITLARaaqvglgiGHLRAAADALKDFEFEERR--GNS----------LVVREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 167 AGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCA 246
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 247 KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGV 326
Cdd:cd07138 231 DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 327 TTGPLIDEKAVAKVEEHIADAIAKGAKVVTGG--KPHAL-GGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADV 403
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgRPEGLeRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1458409611 404 IAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEvAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPG-APFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
51-480 |
5.68e-154 |
|
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: 444.67 E-value: 5.68e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 51 REAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDT 130
Cdd:cd07104 3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 131 IPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS-ALALAELANRAGIPAGVFNVV 209
Cdd:cd07104 83 LPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 210 TGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTC 289
Cdd:cd07104 163 PGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQIC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 290 VCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHalgGNFFQ 369
Cdd:cd07104 243 MAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE---GLFYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 370 PTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTE- 448
Cdd:cd07104 320 PTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDEp 399
|
410 420 430
....*....|....*....|....*....|..
gi 1458409611 449 VAPFGGVKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07104 400 HVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
14-476 |
8.61e-153 |
|
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: 443.23 E-value: 8.61e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 14 LIDGQWRDApnGDVIAVTNPAN-GEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLAR 92
Cdd:cd07097 4 YIDGEWVAG--GDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 173 AGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLI 332
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 333 DEKAVAKVEEHIADAIAKGAKVVTGGKPHALG--GNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDT 410
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDT 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1458409611 411 EFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEV-APFGGVKASGLG-REGSKYGIEDYLEIK 476
Cdd:cd07097 402 EFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYhVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
14-478 |
1.22e-148 |
|
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: 432.93 E-value: 1.22e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 14 LIDGQWRDAPNGDVIAVTNPANGEQL-GSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLAR 92
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVvGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 173 AGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLI 332
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 333 DEKAVAKVEEHIADAIAKGAKVVTGGKP----HALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1458409611 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEV-APFGGVKASGLG-REGSKYGIEDYLEIKYM 478
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVhLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
28-480 |
3.63e-148 |
|
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: 430.70 E-value: 3.63e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 28 IAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKG 107
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 108 EISYAASFIEWFAEEGKRIYGDTIPG----HQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPAS 183
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 184 QTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAkdIKKVSLELGGNAPFI 263
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 264 VFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEH 343
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 344 IADAIAKGAKVVTGGKPHalgGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDL 423
Cdd:cd07094 319 VEEAVEAGARLLCGGERD---GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1458409611 424 SRVFRVGEALEYGIIGINTGII-STEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSSAfRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
55-476 |
1.67e-147 |
|
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: 425.88 E-value: 1.67e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 55 EAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGH 134
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 135 QADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAG 214
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 215 AVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANR 294
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 295 LYVQDGVYDRFAEKLQqaveklrigdglqdgvttgplidekavakveehiadaiakgakvvtggkphalggnffqpTILV 374
Cdd:cd06534 241 LLVHESIYDEFVEKLV------------------------------------------------------------TVLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 375 NVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEV-APFG 453
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPeAPFG 340
|
410 420
....*....|....*....|...
gi 1458409611 454 GVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd06534 341 GVKNSGIGREGGPYGLEEYTRTK 363
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
25-476 |
8.18e-147 |
|
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: 427.79 E-value: 8.18e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 25 GDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPA--WRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPL 102
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 103 AEA-KGEISYAASFIEWFAEEGKRIYGDTIP-GHQADKrlLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLK 180
Cdd:cd07112 81 SDAlAVDVPSAANTFRWYAEAIDKVYGEVAPtGPDALA--LITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 181 PASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK-DIKKVSLELGGN 259
Cdd:cd07112 159 PAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 260 APFIVFDDA-DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVA 338
Cdd:cd07112 239 SPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 339 KVEEHIADAIAKGAKVVTGGKPH--ALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAA 416
Cdd:cd07112 319 KVLGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 417 YFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
30-476 |
4.10e-145 |
|
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: 423.30 E-value: 4.10e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 30 VTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 110 SYAASFIEWFAE--EGKRIYGD-TIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTP 186
Cdd:cd07110 81 DDVAGCFEYYADlaEQLDAKAErAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 187 FSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFD 266
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 267 DADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIAD 346
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 347 AIAKGAKVVTGGK-PHALG-GNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLS 424
Cdd:cd07110 321 GKEEGARLLCGGRrPAHLEkGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1458409611 425 RVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
52-476 |
2.40e-144 |
|
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: 419.94 E-value: 2.40e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 52 EAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTi 131
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 132 PGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTG 211
Cdd:cd07100 82 PIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 212 SAGAVGgELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVC 291
Cdd:cd07100 162 DSDQVE-AIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 292 ANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPT 371
Cdd:cd07100 241 AKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 372 ILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAP 451
Cdd:cd07100 321 VLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLP 400
|
410 420
....*....|....*....|....*
gi 1458409611 452 FGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07100 401 FGGVKRSGYGRELGRFGIREFVNIK 425
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
14-463 |
1.30e-143 |
|
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: 420.05 E-value: 1.30e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 14 LIDGQWRDAPnGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARL 93
Cdd:cd07086 2 VIGGEWVGSG-GETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAA 173
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 174 GCTMVLKPASQTPFSALALAELANRA----GIPAGVFNVVTGsAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI 249
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 250 KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTG 329
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 330 PLIDEKAVAKVEEHIADAIAKGAKVVTGGK--PHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQA 407
Cdd:cd07086 320 PLINQAAVEKYLNAIEIAKSQGGTVLTGGKriDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAIN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1458409611 408 NDTEFGLAAYFYARDLSRVFRVGEA--LEYGIIGINTGIISTEV-APFGGVKASGLGRE 463
Cdd:cd07086 400 NDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPTSGAEIgGAFGGEKETGGGRE 458
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
12-476 |
1.70e-143 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 419.70 E-value: 1.70e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 12 QALIDGQWRDApNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLA 91
Cdd:PRK13473 4 KLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 92 RLMTLEQGKPLAEAKG-EISYAASFIEWFAE-----EGKRIyGDTIPGHQADKRllviKQPIGVTAAITPWNFPAAMITR 165
Cdd:PRK13473 83 RLESLNCGKPLHLALNdEIPAIVDVFRFFAGaarclEGKAA-GEYLEGHTSMIR----RDPVGVVASIAPWNYPLMMAAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 166 KAGPALAAGCTMVLKPASQTPFSALALAELANRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:PRK13473 158 KLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 246 AKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDG 325
Cdd:PRK13473 237 ADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 326 VTTGPLIDEKAVAKVEEHIADAIAKG-AKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVI 404
Cdd:PRK13473 317 TELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1458409611 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:PRK13473 397 RWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
32-482 |
1.72e-142 |
|
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: 416.45 E-value: 1.72e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 32 NPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKG-EIS 110
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 111 YAASFIEWFAEEGKRIYGDTIPghqADKRLL--VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS 188
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIP---VRGPFLnyTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 189 ALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 269 DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAI 348
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 349 AKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFR 428
Cdd:cd07115 320 EEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1458409611 429 VGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:cd07115 400 VAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
30-476 |
1.66e-141 |
|
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: 413.95 E-value: 1.66e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 30 VTNPANGEQLGSVPKMGADETREAIEAANRALPAW-RALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKG- 107
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 108 EISYAASFIEWFAEEGKRIYGDTIPGHQADKRL----LVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPAS 183
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRGGpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 184 QTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFI 263
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 264 VFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEH 343
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 344 IADAIAKGAKVVTGGK--PHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYAR 421
Cdd:cd07089 321 IARGRDEGARLVTGGGrpAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1458409611 422 DLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07089 401 DVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
33-476 |
6.38e-141 |
|
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: 412.50 E-value: 6.38e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 33 PANGEQLGSVPKMGADETREAIEAANRALPA--WRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEIS 110
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 111 YAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSAL 190
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 191 ALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADL 270
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 271 DKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAK 350
Cdd:cd07118 244 DAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 351 GAKVVTGGKPHALG-GNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRV 429
Cdd:cd07118 324 GATLLLGGERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTV 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1458409611 430 GEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07118 404 ARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELK 450
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
31-472 |
7.63e-140 |
|
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: 409.69 E-value: 7.63e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 31 TNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEIS 110
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 111 YAASFIEWFAEEGKRIYGDT-IPGHQ--ADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPF 187
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRkVPTGLlmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 188 SALALAELANRAGIPAGVFNVVTGsAGAVGGELTSNPlVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDD 267
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTG-DGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 268 ADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADA 347
Cdd:cd07099 239 ADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 348 IAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVF 427
Cdd:cd07099 319 VAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAE 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1458409611 428 RVGEALEYGIIGINTGIISTEV--APFGGVKASGLGREGSKYGIEDY 472
Cdd:cd07099 399 AIARRLEAGAVSINDVLLTAGIpaLPFGGVKDSGGGRRHGAEGLREF 445
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
30-477 |
2.82e-139 |
|
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: 407.87 E-value: 2.82e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 30 VTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAK-GE 108
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 109 ISYAASFIEWFA-----EEGKRIyGDTIPGHQADKRllviKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPAS 183
Cdd:cd07092 81 LPGAVDNFRFFAgaartLEGPAA-GEYLPGHTSMIR----REPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 184 QTPFSALALAELANRaGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFI 263
Cdd:cd07092 156 TTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 264 VFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEH 343
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 344 IADAiAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDL 423
Cdd:cd07092 315 VERA-PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1458409611 424 SRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKY 477
Cdd:cd07092 394 GRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKH 447
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
14-482 |
2.59e-137 |
|
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: 404.03 E-value: 2.59e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 14 LIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARL 93
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 94 MTLEQGKPLAEAKG-EISYAASFIEWFA-----EEG--KRIYGDTIPghqadkrlLVIKQPIGVTAAITPWNFPAAMITR 165
Cdd:cd07559 84 ETLDNGKPIRETLAaDIPLAIDHFRYFAgviraQEGslSEIDEDTLS--------YHFHEPLGVVGQIIPWNFPLLMAAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 166 KAGPALAAGCTMVLKPASQTPFSALALAELANRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:cd07559 156 KLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 246 AKDIKKVSLELGGNAPFIVFDDA-----DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGD 320
Cdd:cd07559 235 AENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 321 GLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGK----PHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFR 396
Cdd:cd07559 315 PLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGErltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVIT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 397 FKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07559 395 FKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
....*.
gi 1458409611 477 YMCIGL 482
Cdd:cd07559 475 NILVSY 480
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
6-482 |
2.88e-137 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 404.26 E-value: 2.88e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 6 MTLFRQQALIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMME 85
Cdd:PRK13252 2 SRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 86 NQDDLARLMTLEQGKPLAEAK-GEISYAASFIEWFAEEGKRIYGDTIPGHQAD----KRllvikQPIGVTAAITPWNFPA 160
Cdd:PRK13252 82 RNDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSfvytRR-----EPLGVCAGIGAWNYPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 161 AMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGsAGAVGGELTSNPLVRKLSFTGSTEIGRQ 240
Cdd:PRK13252 157 QIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQG-DGRVGAWLTEHPDIAKVSFTGGVPTGKK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 241 LMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGD 320
Cdd:PRK13252 236 VMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 321 GLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGK----PHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFR 396
Cdd:PRK13252 316 PMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGErlteGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 397 FKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:PRK13252 396 FDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIK 475
|
....*.
gi 1458409611 477 YMCIGL 482
Cdd:PRK13252 476 SVQVEM 481
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
30-480 |
3.07e-137 |
|
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: 403.22 E-value: 3.07e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 30 VTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 110 SYAASFIEWFAEEGKRIYGDTIP---GHQADKRllviKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTP 186
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPlpgGSFAYTR----REPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 187 FSALALAELANRAGIPAGVFNVVTGsAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFD 266
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 267 DADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIAD 346
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 347 AIAKGAKVVTGG-----KPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYAR 421
Cdd:cd07090 316 AKQEGAKVLCGGervvpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1458409611 422 DLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
12-476 |
1.09e-136 |
|
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: 402.50 E-value: 1.09e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 12 QALIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRAL---PAWRALTAKERANILRRWFDLMMENQD 88
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 89 DLARLMTLEQGKPLAEAK-GEISYAASFIEWFAEEGKRIYGDTIPghqADKRLLVI--KQPIGVTAAITPWNFPAAMITR 165
Cdd:cd07141 88 YLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIP---MDGDFFTYtrHEPVGVCGQIIPWNFPLLMAAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 166 KAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:cd07141 165 KLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 246 AK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQD 324
Cdd:cd07141 245 GKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 325 GVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVI 404
Cdd:cd07141 325 KTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1458409611 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07141 405 ERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVK 476
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
30-476 |
2.13e-136 |
|
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: 400.84 E-value: 2.13e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 30 VTNPANGEQLGSVPKMGADETREAIEAANRALPA-WRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGE 108
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 109 ISYAASFIEWFAEEGKRIYGDTIPgHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS 188
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 189 ALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 269 DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDgVTTGPLIDEKAVAKVEEHIADAI 348
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 349 AKGAKVVTGG---KPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSR 425
Cdd:cd07109 319 ARGARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1458409611 426 VFRVGEAL--------EYgiiginTGIISTEVaPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07109 399 ALRVARRLragqvfvnNY------GAGGGIEL-PFGGVKKSGHGREKGLEALYNYTQTK 450
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
15-482 |
2.61e-136 |
|
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: 401.79 E-value: 2.61e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 15 IDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPA-WRALTAKERANILRRWFDLMMENQDDLARL 93
Cdd:cd07144 12 INNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 94 MTLEQGKPL-AEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQAdKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07144 92 EALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPN-KLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 173 AGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAV-EKLRIGDGLQDGVTTGPL 331
Cdd:cd07144 251 TLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 332 IDEKAVAKVEEHIADAIAKGAKVVTGGKPHALG---GNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
Cdd:cd07144 331 VSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKAN 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1458409611 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:cd07144 411 DTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
28-480 |
5.09e-136 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 399.70 E-value: 5.09e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 28 IAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKG 107
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 108 EISYAASFIEWFAEEGKRIYGDTIP--------GHQAdkrlLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVL 179
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldisargeGRQG----LVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 180 KPASQTPFSALALAELANRAGIPAGVFNVVTGS-AGAVggELTSNPLVRKLSFTGSTEIGRQLMEQCAKdiKKVSLELGG 258
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPCSrDDAD--LLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 259 NAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVA 338
Cdd:cd07147 233 NAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 339 KVEEHIADAIAKGAKVVTGGKPHalgGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYF 418
Cdd:cd07147 313 RVEGWVNEAVDAGAKLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1458409611 419 YARDLSRVFRVGEALEyGIIGINTGIISTEV--APFGGVKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07147 390 FTRDLEKALRAWDELE-VGGVVINDVPTFRVdhMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
15-476 |
6.58e-136 |
|
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: 400.03 E-value: 6.58e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 15 IDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRAL--PAWRALTAKERANILRRWFDLMMENQDDLAR 92
Cdd:cd07139 3 IGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 93 LMTLEQGKPLAEAK-GEISYAASFIEWFAEEGKRI-YGDTIPGhQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPA 170
Cdd:cd07139 83 LWTAENGMPISWSRrAQGPGPAALLRYYAALARDFpFEERRPG-SGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 171 LAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIK 250
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR-EVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 251 KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGP 330
Cdd:cd07139 241 RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 331 LIDEKAVAKVEEHIADAIAKGAKVVTGGK--PHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
Cdd:cd07139 321 LASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIAN 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1458409611 409 DTEFGLAAYFYARDLSRVFRVGEALEyGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07139 401 DSDYGLSGSVWTADVERGLAVARRIR-TGTVGVNGFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETK 467
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
12-476 |
1.45e-135 |
|
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: 399.56 E-value: 1.45e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 12 QALIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALP--AWRALTAKERANILRRWFDLMMENQDD 89
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 90 LARLMTLEQGKPLAEAK-GEISYAASFIEWFAEEGKRIYGDTIPGHQAdKRLLVIKQPIGVTAAITPWNFPAAMITRKAG 168
Cdd:cd07142 85 LAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGP-HHVYTLHEPIGVVGQIIPWNFPLLMFAWKVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 169 PALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK- 247
Cdd:cd07142 164 PALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKs 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 248 DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVT 327
Cdd:cd07142 244 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 328 TGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQA 407
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1458409611 408 NDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07142 404 NNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
12-470 |
2.37e-133 |
|
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: 393.86 E-value: 2.37e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 12 QALIDGQWRDApNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAW-RALTAKERANILRRWFDLMMENQDDL 90
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWwPTMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 91 ARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRL----LVIKQPIGVTAAITPWNFPAAMITRK 166
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaQVRREPLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 167 AGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCA 246
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 247 kdIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGV 326
Cdd:cd07082 242 --MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 327 TTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKphALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQ 406
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1458409611 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGI-NTGIISTEVAPFGGVKASGLGREGSKYGIE 470
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNInSKCQRGPDHFPFLGRKDSGIGTQGIGDALR 462
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
14-482 |
4.78e-133 |
|
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: 392.97 E-value: 4.78e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 14 LIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARL 93
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 94 MTLEQGKPLAEAKG-EISYAASFIEWFAeegKRIYGDTIPGHQADKRLL--VIKQPIGVTAAITPWNFPAAMITRKAGPA 170
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFA---GVIRAEEGSANMIDEDTLsiVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 171 LAAGCTMVLKPASQTPFSALALAELANRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIK 250
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 251 KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGP 330
Cdd:cd07117 240 PATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 331 LIDEKAVAKVEEHIADAIAKGAKVVTGGK----PHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQ 406
Cdd:cd07117 320 QVNKDQLDKILSYVDIAKEEGAKILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDM 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1458409611 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:cd07117 400 ANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
17-480 |
4.98e-133 |
|
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: 392.82 E-value: 4.98e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 17 GQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTL 96
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 97 EQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCT 176
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 177 MVLKPASQTPFSA-LALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLE 255
Cdd:cd07151 161 VVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 256 LGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEK 335
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 336 AVAKVEEHIADAIAKGAKVVTGGKPHalgGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLA 415
Cdd:cd07151 321 QVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLS 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1458409611 416 AYFYARDLSRVFRVGEALEYGIIGINTGIISTE-VAPFGGVKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07151 398 GAVFTSDLERGVQFARRIDAGMTHINDQPVNDEpHVPFGGEKNSGLGRFNGEWALEEFTTDKWISV 463
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
30-476 |
2.54e-131 |
|
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: 387.87 E-value: 2.54e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 30 VTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPL-AEAKGE 108
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 109 ISYAASFIEWFAEEGKRIYGDTIPGHQaDKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS 188
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFGP-DVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 189 ALALAELANRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 269 DLDKAVEGALAS-KFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADA 347
Cdd:cd07108 239 DLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 348 IA-KGAKVVTGGKPHALG----GNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD 422
Cdd:cd07108 319 LStSGATVLRGGPLPGEGpladGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1458409611 423 LSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYG-IEDYLEIK 476
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKK 453
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
32-479 |
5.27e-131 |
|
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: 387.08 E-value: 5.27e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 32 NPANGEQLGSVPKMGADETREAIEAANRAL--PAWRAlTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 110 SYAASFIEWFAEEGKRIYGDTI---PGHQAdkrlLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTP 186
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIepePGSFS----LVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 187 FSALALAE-LANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVF 265
Cdd:cd07120 158 QINAAIIRiLAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 266 DDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIA 345
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 346 DAIAKGAKVVTGGKPHALG---GNFFQPTiLVNVPDS-AKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYAR 421
Cdd:cd07120 318 RAIAAGAEVVLRGGPVTEGlakGAFLRPT-LLEVDDPdADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1458409611 422 DLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMC 479
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
25-474 |
2.45e-130 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 387.70 E-value: 2.45e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 25 GDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAE 104
Cdd:PRK09407 31 GPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 105 AKGEISYAASfiewfaeeGKRIYGDTIPGHQADKR------LL----VIKQPIGVTAAITPWNFPAAMITRKAGPALAAG 174
Cdd:PRK09407 111 AFEEVLDVAL--------TARYYARRAPKLLAPRRragalpVLtkttELRQPKGVVGVISPWNYPLTLAVSDAIPALLAG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 175 CTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSL 254
Cdd:PRK09407 183 NAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGFSL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 255 ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDE 334
Cdd:PRK09407 261 ELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 335 KAVAKVEEHIADAIAKGAKVVTGGKPHA-LGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFG 413
Cdd:PRK09407 341 AQLETVSAHVDDAVAKGATVLAGGKARPdLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYG 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 414 LAAYFYARDLSRVFRVGEALE---------YgiigiNTGIISTEvAPFGGVKASGLGREGSKYGIEDYLE 474
Cdd:PRK09407 421 LNASVWTGDTARGRAIAARIRagtvnvnegY-----AAAWGSVD-APMGGMKDSGLGRRHGAEGLLKYTE 484
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
15-482 |
5.33e-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: 385.34 E-value: 5.33e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 15 IDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRAL--PAWRALTAKERANILRRWFDLMMENQDDLAR 92
Cdd:cd07143 11 INGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFetDWGLKVSGSKRGRCLSKLADLMERNLDYLAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 93 LMTLEQGKP-LAEAKGEISYAASFIEWFAEEGKRIYGDTIpgHQADKRLLVIK-QPIGVTAAITPWNFPAAMITRKAGPA 170
Cdd:cd07143 91 IEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVI--ETDIKKLTYTRhEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 171 LAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK-DI 249
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKsNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 250 KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTG 329
Cdd:cd07143 249 KKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 330 PLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQAND 409
Cdd:cd07143 329 PQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRAND 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1458409611 410 TEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:cd07143 409 STYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
10-476 |
1.51e-129 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 385.24 E-value: 1.51e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 10 RQQALIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPA-----WRALTAKERANILRRWFDLMM 84
Cdd:PLN02467 7 RRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 85 ENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGD-----TIPGHQADKRLLviKQPIGVTAAITPWNFP 159
Cdd:PLN02467 87 ERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKqkapvSLPMETFKGYVL--KEPLGVVGLITPWNYP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 160 AAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGR 239
Cdd:PLN02467 165 LLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 240 QLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIG 319
Cdd:PLN02467 245 KIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKIS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 320 DGLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGK--PHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRF 397
Cdd:PLN02467 325 DPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTF 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1458409611 398 KDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:PLN02467 405 STEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
12-480 |
4.70e-129 |
|
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: 383.38 E-value: 4.70e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 12 QALIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPA--WRALTAKERANILRRWFDLMMENQDD 89
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 90 LARLMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDTIPGHQA--DKRL-LVIKQPIGVTAAITPWNFPAAMITR 165
Cdd:cd07140 87 LATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPINQArpNRNLtLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 166 KAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 246 AK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQD 324
Cdd:cd07140 247 AVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 325 GVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDE--AD 402
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDG 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1458409611 403 VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
52-476 |
1.07e-128 |
|
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: 380.38 E-value: 1.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 52 EAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTI 131
Cdd:cd07105 4 QAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 132 PGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTG 211
Cdd:cd07105 84 PSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 212 S---AGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQT 288
Cdd:cd07105 164 SpedAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 289 CVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDglqdgVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKP-HALGGNF 367
Cdd:cd07105 244 CMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLAdESPSGTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 368 FQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIIST 447
Cdd:cd07105 319 MPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHD 398
|
410 420 430
....*....|....*....|....*....|
gi 1458409611 448 E-VAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07105 399 EpTLPHGGVKSSGYGRFNGKWGIDEFTETK 428
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
14-473 |
1.11e-126 |
|
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: 378.10 E-value: 1.11e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 14 LIDGQWRDAPngDVIAVTNPAN-GEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLAR 92
Cdd:cd07124 36 VIGGKEVRTE--EKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIpGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07124 114 WMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPV-EMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 173 AGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKD---- 248
Cdd:cd07124 193 TGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpgq 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 249 --IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGV 326
Cdd:cd07124 273 kwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 327 TTGPLIDEKAVAKVEEHIADAIaKGAKVVTGGKP--HALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVI 404
Cdd:cd07124 353 YMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEVleLAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEAL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 405 AQANDTEFGLAAYFYARDLSRV------FRVGE---------ALeygiigintgiisTEVAPFGGVKASGLgreGSKYGI 469
Cdd:cd07124 432 EIANDTEYGLTGGVFSRSPEHLerarreFEVGNlyanrkitgAL-------------VGRQPFGGFKMSGT---GSKAGG 495
|
....
gi 1458409611 470 EDYL 473
Cdd:cd07124 496 PDYL 499
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
28-476 |
2.28e-126 |
|
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: 375.16 E-value: 2.28e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 28 IAVTNPANGEQLGSVPKMGADETREAIE-AANRALPawraLTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAK 106
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALAlAASYRST----LTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 107 GEISYAASFIEWFAEEGKRIYGDTIP---GHQADKRLLV-IKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPA 182
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFScdlTANGKARKIFtLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 183 SQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAkdIKKVSLELGGNAPF 262
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 263 IVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEE 342
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 343 HIADAIAKGAKVVTGGKPHalgGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD 422
Cdd:cd07146 315 RVEEAIAQGARVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1458409611 423 LSRVFRVGEALEYGIIGINTG-IISTEVAPFGGVKASGLG-REGSKYGIEDYLEIK 476
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNEVpGFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
15-480 |
2.44e-124 |
|
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: 371.00 E-value: 2.44e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 15 IDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRAL-PAWRALTAKERANILRRWFDLMMENQDDLARL 93
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 94 MTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDT----IPGHQADK-RLLVIKQPIGVTAAITPWNFPAAMITRKA 167
Cdd:cd07113 84 ETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETlapsIPSMQGERyTAFTRREPVGVVAGIVPWNFSVMIAVWKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 168 GPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSaGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
Cdd:cd07113 164 GAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGK-GAVGAQLISHPDVAKVSFTGSVATGKKIGRQAAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 248 DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVT 327
Cdd:cd07113 243 DLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 328 TGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQA 407
Cdd:cd07113 323 FGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLI 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1458409611 408 NDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07113 403 NDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
33-475 |
4.99e-124 |
|
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: 369.33 E-value: 4.99e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 33 PANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEISYA 112
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 113 ASfiewfaeeGKRIYGDTIPGHQADKR------LL----VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPA 182
Cdd:cd07101 83 AI--------VARYYARRAERLLKPRRrrgaipVLtrttVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 183 SQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPF 262
Cdd:cd07101 155 SQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 263 IVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEE 342
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 343 HIADAIAKGAKVVTGGKPHA-LGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYAR 421
Cdd:cd07101 313 HVDDAVAKGATVLAGGRARPdLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1458409611 422 DLSRVFRVGEALEYGIIGINTGIISTEV---APFGGVKASGLGREGSKYGIEDYLEI 475
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNEGYAAAWAsidAPMGGMKDSGLGRRHGAEGLLKYTET 449
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
76-476 |
2.11e-123 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 365.98 E-value: 2.11e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 76 LRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITP 155
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 156 WNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGST 235
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 236 EIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEK 315
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 316 LRIGDGLQ-DGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPL 394
Cdd:PRK10090 241 VQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 395 FRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLE 474
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQ 400
|
..
gi 1458409611 475 IK 476
Cdd:PRK10090 401 TQ 402
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
30-476 |
1.42e-121 |
|
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: 363.23 E-value: 1.42e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 30 VTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEI 109
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 110 SYAASFIEWFAEEGKRIYGDTIP-GHQAdkRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS 188
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPvGGRN--LHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 189 ALALAELAnRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
Cdd:cd07107 159 ALRLAELA-REVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 269 DLDKAVEGALAS-KFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADA 347
Cdd:cd07107 238 DPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 348 IAKGAKVVTGGKP---HAL-GGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDL 423
Cdd:cd07107 318 KREGARLVTGGGRpegPALeGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1458409611 424 SRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEK 450
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
15-476 |
4.17e-120 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 361.06 E-value: 4.17e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 15 IDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALP--AWRALTAKERANILRRWFDLMMENQDDLAR 92
Cdd:PLN02766 25 INGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 93 LMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPgHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPAL 171
Cdd:PLN02766 105 LDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLK-MSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 172 AAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK-DIK 250
Cdd:PLN02766 184 AAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 251 KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGP 330
Cdd:PLN02766 264 QVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 331 LIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDT 410
Cdd:PLN02766 344 QVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNT 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1458409611 411 EFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:PLN02766 424 KYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVK 489
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
12-476 |
1.32e-119 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 360.66 E-value: 1.32e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 12 QALIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALP--AWRALTAKERANILRRWFDLMMENQDD 89
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 90 LARLMTLEQGKPLAE-AKGEISYAASFIEWFAEEGKRIYGDTIPG---HQADkrllVIKQPIGVTAAITPWNFPAAMITR 165
Cdd:PLN02466 139 LAALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHGLTVPAdgpHHVQ----TLHEPIGVAGQIIPWNFPLLMFAW 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 166 KAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:PLN02466 215 KVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 246 AK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQD 324
Cdd:PLN02466 295 AKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 325 GVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVI 404
Cdd:PLN02466 375 GVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVI 454
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1458409611 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:PLN02466 455 RRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
15-478 |
9.44e-119 |
|
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: 356.71 E-value: 9.44e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 15 IDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLM 94
Cdd:cd07111 26 INGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 95 TLEQGKPLAEAK-GEISYAASFIEWFAeeGKRIYGDT-IPGHQadkrllvikqPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07111 106 SLDNGKPIRESRdCDIPLVARHFYHHA--GWAQLLDTeLAGWK----------PVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 173 AGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGsAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLI 332
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 333 DEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPL--APLFRFKDEAdvIAQANDT 410
Cdd:cd07111 333 DPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVlvVLTFRTAKEA--VALANNT 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1458409611 411 EFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYM 478
Cdd:cd07111 411 PYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWE 478
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
28-481 |
9.15e-114 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 343.26 E-value: 9.15e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 28 IAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKG 107
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 108 EISYAASFIEWFAEEGKRIYGDTiPGHQAD---KRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQ 184
Cdd:PRK09406 83 EALKCAKGFRYYAEHAEALLADE-PADAAAvgaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 185 TPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELtSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIV 264
Cdd:PRK09406 162 VPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAIL-RDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 265 FDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHI 344
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 345 ADAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLS 424
Cdd:PRK09406 321 DDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1458409611 425 RVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCIG 481
Cdd:PRK09406 401 EQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
36-474 |
1.51e-110 |
|
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: 334.26 E-value: 1.51e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 36 GEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEISYAASF 115
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 116 IEWFAEEGKRIYGDTIPghQADKRL-LVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSA-LALA 193
Cdd:cd07152 81 LHEAAGLPTQPQGEILP--SAPGRLsLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 194 ELANRAGIPAGVFNVVTGSAGAvGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKA 273
Cdd:cd07152 159 RLFEEAGLPAGVLHVLPGGADA-GEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 274 VEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAK 353
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 354 VVTGGKPHALggnFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEAL 433
Cdd:cd07152 318 LEAGGTYDGL---FYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1458409611 434 EYGIIGINTGIISTE-VAPFGGVKASGLG-REGSKYGIEDYLE 474
Cdd:cd07152 395 RTGMLHINDQTVNDEpHNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
32-470 |
2.02e-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: 334.21 E-value: 2.02e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 32 NPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEISY 111
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 112 AASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALA 191
Cdd:cd07102 82 MLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 192 LAELANRAGIPAGVFNVVTGSaGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLD 271
Cdd:cd07102 162 FAAAFAEAGLPEGVFQVLHLS-HETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 272 KAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAKG 351
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 352 AKVVTGGK---PHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFR 428
Cdd:cd07102 321 ARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1458409611 429 VGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIE 470
Cdd:cd07102 401 LGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYD 442
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
32-469 |
1.34e-106 |
|
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: 325.02 E-value: 1.34e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 32 NPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAK-GEIS 110
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 111 YAASFIEWFAEEGKRIY------GDTIPGHqadKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQ 184
Cdd:cd07098 82 VTCEKIRWTLKHGEKALrpesrpGGLLMFY---KRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 185 TPFSALALAELANRA----GIPAGVFNVVTGSAGAvGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNA 260
Cdd:cd07098 159 VAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 261 PFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKV 340
Cdd:cd07098 238 PAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 341 EEHIADAIAKGAKVVTGGKPHAL----GGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAA 416
Cdd:cd07098 318 EELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1458409611 417 YFYARDLSRVFRVGEALEYGIIGINTGIISTEVA--PFGGVKASGLGREGSKYGI 469
Cdd:cd07098 398 SVFGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGRFAGEEGL 452
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
12-422 |
5.61e-105 |
|
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: 321.00 E-value: 5.61e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 12 QALIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLA 91
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 92 RLMTLEQGKPLAEAKGEISYAASFIEwFA----EEGKriyGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAaMITR-K 166
Cdd:cd07085 82 RLITLEHGKTLADARGDVLRGLEVVE-FAcsipHLLK---GEYLENVARGIDTYSYRQPLGVVAGITPFNFPA-MIPLwM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 167 AGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGgELTSNPLVRKLSFTGSTEIGRQLMEQCA 246
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVN-ALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 247 KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGV 326
Cdd:cd07085 236 ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 327 TTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHAL----GGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEAD 402
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVpgyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
|
410 420
....*....|....*....|
gi 1458409611 403 VIAQANDTEFGLAAYFYARD 422
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRS 415
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
14-473 |
2.67e-101 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 313.02 E-value: 2.67e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 14 LIDGQWRDAPngDVIAVTNPAN-GEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLAR 92
Cdd:PRK03137 40 IIGGERITTE--DKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEE------GKRIYgdTIPGHqaDKRLLVIkqPIGVTAAITPWNFPAAMITRK 166
Cdd:PRK03137 118 WLVKEAGKPWAEADADTAEAIDFLEYYARQmlkladGKPVE--SRPGE--HNRYFYI--PLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 167 AGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCA 246
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 247 KD------IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGD 320
Cdd:PRK03137 272 KVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 321 GlQDGVTTGPLIDEKAVAKVEEHIadAIAKG-AKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKD 399
Cdd:PRK03137 352 P-EDNAYMGPVINQASFDKIMSYI--EIGKEeGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 400 EADVIAQANDTEFGLAAYFYARDLSRV------FRVGE---------ALeygiigintgiisTEVAPFGGVKASGlgrEG 464
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNNREHLekarreFHVGNlyfnrgctgAI-------------VGYHPFGGFNMSG---TD 492
|
....*....
gi 1458409611 465 SKYGIEDYL 473
Cdd:PRK03137 493 SKAGGPDYL 501
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
1-482 |
3.03e-101 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 312.22 E-value: 3.03e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 1 MQLNDMTLFRQQAL---------IDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPA--WRALTA 69
Cdd:PRK09847 1 MNFHHLAYWQDKALslaienrlfINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 70 KERANILRRWFDLMMENQDDLARLMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDTIPGhQADKRLLVIKQPIG 148
Cdd:PRK09847 81 AKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATT-SSHELAMIVREPVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 149 VTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRK 228
Cdd:PRK09847 160 VIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 229 LSFTGSTEIGRQLMEQCAK-DIKKVSLELGGNAPFIVFDDA-DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFA 306
Cdd:PRK09847 240 IAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 307 EKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTG---GKPHALGgnffqPTILVNVPDSAKVA 383
Cdd:PRK09847 320 ALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGrnaGLAAAIG-----PTIFVDVDPNASLS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 384 KEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGRE 463
Cdd:PRK09847 395 REEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRD 474
|
490
....*....|....*....
gi 1458409611 464 GSKYGIEDYLEIKYMCIGL 482
Cdd:PRK09847 475 KSLHALEKFTELKTIWISL 493
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
15-480 |
2.10e-99 |
|
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: 307.07 E-value: 2.10e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 15 IDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLM 94
Cdd:cd07116 5 IGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 95 TLEQGKPLAEAKG-EISYAASFIEWFA-----EEG--KRIYGDTIPGHqadkrllvIKQPIGVTAAITPWNFPAAMITRK 166
Cdd:cd07116 85 TWDNGKPVRETLAaDIPLAIDHFRYFAgciraQEGsiSEIDENTVAYH--------FHEPLGVVGQIIPWNFPLLMATWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 167 AGPALAAGCTMVLKPASQTPFSALALAELANRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCA 246
Cdd:cd07116 157 LAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 247 KDIKKVSLELGGNAPFIVF------DDADLDKAVEGALASKFrNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGD 320
Cdd:cd07116 236 ENIIPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 321 GLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGN----FFQPTiLVNVPDSAKVAKEETFGPLAPLFR 396
Cdd:cd07116 315 PLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPT-TFKGGNKMRIFQEEIFGPVLAVTT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 397 FKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:cd07116 394 FKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
....
gi 1458409611 477 YMCI 480
Cdd:cd07116 474 NLLV 477
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
16-465 |
3.72e-98 |
|
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: 303.36 E-value: 3.72e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 16 DGQWRdaPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMT 95
Cdd:cd07130 4 DGEWG--GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 96 LEQGKPLAEAKGEISyaasfiEW-----FAEEGKR-IYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGP 169
Cdd:cd07130 82 LEMGKILPEGLGEVQ------EMidicdFAVGLSRqLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 170 ALAAGCTMVLKPASQTPFSALALAELANRA----GIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
Cdd:cd07130 156 ALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGA-DVGEALVKDPRVPLVSFTGSTAVGRQVGQAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 246 AKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDG 325
Cdd:cd07130 235 AARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 326 VTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTIlVNVPDSAKVAKEETFGPLAPLFRFKDEADVIA 405
Cdd:cd07130 315 TLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 406 QANDTEFGLAAYFYARDLSRVFR----------------------VGEAleygiigintgiistevapFGGVKASGLGRE 463
Cdd:cd07130 394 WNNEVPQGLSSSIFTTDLRNAFRwlgpkgsdcgivnvnigtsgaeIGGA-------------------FGGEKETGGGRE 454
|
...
gi 1458409611 464 -GS 465
Cdd:cd07130 455 sGS 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
28-480 |
3.29e-93 |
|
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: 290.09 E-value: 3.29e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 28 IAVTNPANGEQLGSVPKMGADETREAIEAAnRALPAWRA--LTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEA 105
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTA-HALFLDRNnwLPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 106 KGEISYAASFIEWFAEEGKRIYGDTIP-GH---QADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKP 181
Cdd:cd07148 80 KVEVTRAIDGVELAADELGQLGGREIPmGLtpaSAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 182 ASQTPFSALALAELANRAGIPAG-VFNVVTGSAGAvgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDiKKVSLELGGNA 260
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEGwCQAVPCENAVA--EKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 261 PFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKV 340
Cdd:cd07148 237 PVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 341 EEHIADAIAKGAKVVTGGKPhaLGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYA 420
Cdd:cd07148 317 EEWVNEAVAAGARLLCGGKR--LSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1458409611 421 RDLSRVFRVGEALEYGIIGINTGII-STEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCI 480
Cdd:cd07148 395 KDLDVALKAVRRLDATAVMVNDHTAfRVDWMPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
14-473 |
2.93e-92 |
|
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: 289.46 E-value: 2.93e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 14 LIDGQWRDAPNGdvIAVTNPANGEQ-LGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLAR 92
Cdd:TIGR01237 36 VINGERVETENK--IVSINPCDKSEvVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:TIGR01237 114 LLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 173 AGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK----- 247
Cdd:TIGR01237 194 TGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKvqpgq 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 248 -DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGV 326
Cdd:TIGR01237 274 kHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 327 TTGPLIDEKAVAKVEEHIADAIAKGaKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQ 406
Cdd:TIGR01237 354 YVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEI 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1458409611 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVA--PFGGVKASGLgreGSKYGIEDYL 473
Cdd:TIGR01237 433 ANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGyqPFGGFKMSGT---DSKAGGPDYL 498
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
12-476 |
3.08e-91 |
|
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: 285.89 E-value: 3.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 12 QALIDGQWRDAPNGdVIAVTNPANGEQLGSVPKMGADETREAIEAANRAL--PAWRALTAKeRANILRRWFDLMMENQDD 89
Cdd:TIGR04284 2 RLLIDGKLVAGSAG-TFPTVNPATEEVLGVAADATAADMDAAIAAARRAFdeTDWSRDTAL-RVRCLRQLRDALRAHVEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 90 LARLMTLEQGKPL-----AEAKGEI---SYAASFIEWFaeEGKRIYGDTIPGHQADKRLLViKQPIGVTAAITPWNFPAA 161
Cdd:TIGR04284 80 LRELTIAEVGAPRmltagAQLEGPVddlGFAADLAESY--AWTTDLGVASPMGIPTRRTLR-REAVGVVGAITPWNFPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 162 MITRKAGPALAAGCTMVLKPASQTPFSALALAEL-ANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQ 240
Cdd:TIGR04284 157 INLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELiAEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 241 LMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGD 320
Cdd:TIGR04284 237 VMADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 321 GLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGG-KPHALGGNFF-QPTILVNVPDSAKVAKEETFGPLAPLFRFK 398
Cdd:TIGR04284 317 PADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGgRPADRDRGFFvEPTVIAGLDNNARVAREEIFGPVLTVIAHD 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1458409611 399 DEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:TIGR04284 397 GDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETK 474
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
32-476 |
2.16e-89 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 280.59 E-value: 2.16e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 32 NPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEISY 111
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 112 AASFIEWFAEEGKRIYgDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALA 191
Cdd:PRK13968 93 SANLCDWYAEHGPAML-KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 192 LAELANRAGIPAGVFNVVTGSAGAVGgELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLD 271
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGVS-QMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 272 KAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAKG 351
Cdd:PRK13968 251 LAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 352 AKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGE 431
Cdd:PRK13968 331 ARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAA 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1458409611 432 ALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDYLEIK 476
Cdd:PRK13968 411 RLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQ 455
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
52-472 |
1.52e-83 |
|
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: 264.52 E-value: 1.52e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 52 EAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGD-T 130
Cdd:cd07095 4 AAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTGErA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 131 IPGhqADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVT 210
Cdd:cd07095 84 TPM--AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 211 GsAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV-SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTC 289
Cdd:cd07095 162 G-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKIlALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 290 VCANRLYVQDG-VYDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFF 368
Cdd:cd07095 241 TCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 369 QPTILvNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYF-------YARDLSRVfRVGealeyGIIGIN 441
Cdd:cd07095 321 SPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLlsddealFERFLARI-RAG-----IVNWNR 393
|
410 420 430
....*....|....*....|....*....|.
gi 1458409611 442 TGIISTEVAPFGGVKASGLGREGSKYGIeDY 472
Cdd:cd07095 394 PTTGASSTAPFGGVGLSGNHRPSAYYAA-DY 423
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
15-473 |
2.87e-79 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 255.58 E-value: 2.87e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 15 IDGQWRDApnGDVIAVTNPAN-GEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARL 93
Cdd:cd07083 23 IGGEWVDT--KERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYG--DTIPGHQADKRLLVIkQPIGVTAAITPWNFPAAMITRKAGPAL 171
Cdd:cd07083 101 LTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFY-VGLGAGVVISPWNFPVAIFTGMIVAPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 172 AAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKD--- 248
Cdd:cd07083 180 AVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLapg 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 249 ---IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDG 325
Cdd:cd07083 260 qtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 326 VTTGPLIDEKAVAKVEEHIaDAIAKGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDE--ADV 403
Cdd:cd07083 340 TDLGPVIDAEQEAKVLSYI-EHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDdfAEA 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1458409611 404 IAQANDTEFGL--AAYFYARD----LSRVFRVGEAleYGIIGINTGIISteVAPFGGVKASGlgrEGSKYGIEDYL 473
Cdd:cd07083 419 LEVANSTPYGLtgGVYSRKREhleeARREFHVGNL--YINRKITGALVG--VQPFGGFKLSG---TNAKTGGPHYL 487
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
6-472 |
1.55e-78 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 252.96 E-value: 1.55e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 6 MTLFrqqalIDGQWRdAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMME 85
Cdd:PRK09457 1 MTLW-----INGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 86 NQDDLARLMTLEQGKPLAEAKGE---------ISYAAsfiewFAEEGKRIYGDTipghqADKRLLVIKQPIGVTAAITPW 156
Cdd:PRK09457 75 NKEELAEVIARETGKPLWEAATEvtaminkiaISIQA-----YHERTGEKRSEM-----ADGAAVLRHRPHGVVAVFGPY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 157 NFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTE 236
Cdd:PRK09457 145 NFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGR-ETGKALAAHPDIDGLLFTGSAN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 237 IGRQLMEQCAKDIKKV-SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVY-DRFAEKLQQAVE 314
Cdd:PRK09457 224 TGYLLHRQFAGQPEKIlALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 315 KLRIGDGLQDGVT-TGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTILvNVPDSAKVAKEETFGPLAP 393
Cdd:PRK09457 304 RLTVGRWDAEPQPfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 394 LFRFKDEADVIAQANDTEFGLAA-----------YFYARdlSRVFRV-------GEAleygiigintgiiSTevAPFGGV 455
Cdd:PRK09457 383 VVRYDDFDEAIRLANNTRFGLSAgllsddredydQFLLE--IRAGIVnwnkpltGAS-------------SA--APFGGV 445
|
490
....*....|....*..
gi 1458409611 456 KASGLGREgSKYGIEDY 472
Cdd:PRK09457 446 GASGNHRP-SAYYAADY 461
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
14-473 |
2.79e-78 |
|
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: 253.27 E-value: 2.79e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 14 LIDGQwrDAPNGDVIAVTNPANGE-QLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLAR 92
Cdd:cd07125 36 IINGE--ETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07125 114 LAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 173 AGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK---DI 249
Cdd:cd07125 194 AGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAErdgPI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 250 KKVSLELGG-NApFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTT 328
Cdd:cd07125 274 LPLIAETGGkNA-MIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 329 GPLIDEKAVAKVEEHIaDAIAKGAKVVTGGKPHALGGNFFQPTILVNVpdSAKVAKEETFGPLAPLFRFKDE--ADVIAQ 406
Cdd:cd07125 353 GPLIDKPAGKLLRAHT-ELMRGEAWLIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKAEdlDEAIED 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 407 ANDTEFGL-----------AAYFYARdlsrvFRVGE---------ALeygiigintgiisTEVAPFGGVKASGLgreGSK 466
Cdd:cd07125 430 INATGYGLtlgihsrdereIEYWRER-----VEAGNlyinrnitgAI-------------VGRQPFGGWGLSGT---GPK 488
|
....*..
gi 1458409611 467 YGIEDYL 473
Cdd:cd07125 489 AGGPNYL 495
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
14-482 |
1.59e-76 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 248.13 E-value: 1.59e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 14 LIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARL 93
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYG-------DTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRK 166
Cdd:PLN00412 99 LVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGegkflvsDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 167 AGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFT-GSTEIGrqlmeqC 245
Cdd:PLN00412 179 IAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIA------I 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 246 AKDIKKVSL--ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQ 323
Cdd:PLN00412 253 SKKAGMVPLqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 324 DGVTTgPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHalgGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADV 403
Cdd:PLN00412 333 DCDIT-PVVSESSANFIEGLVMDAKEKGATFCQEWKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 404 IAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTG-IISTEVAPFGGVKASGLGREGSKYGIEDYLEIKYMCIGL 482
Cdd:PLN00412 409 IHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKSTVINL 488
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
12-414 |
1.97e-70 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 242.03 E-value: 1.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 12 QALIDGQWRDAP----NGDVIAVTNPANGEQ-LGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMEN 86
Cdd:PRK11904 544 AAFLEKQWQAGPiingEGEARPVVSPADRRRvVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEAN 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 87 QDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGD--TIPGHQADKRLLVIkQPIGVTAAITPWNFPAAMIT 164
Cdd:PRK11904 624 RAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGApeKLPGPTGESNELRL-HGRGVFVCISPWNFPLAIFL 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 165 RKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTE----IGRQ 240
Cdd:PRK11904 703 GQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTEtariINRT 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 241 LmeqCAKDIKKVSL--ELGG-NApFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLR 317
Cdd:PRK11904 783 L---AARDGPIVPLiaETGGqNA-MIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELK 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 318 IGDGLQDGVTTGPLIDEKAVAKVEEHIAdAIAKGAKVVTGGK--PHALGGNFFQPTIlVNVpDSAKVAKEETFGPLAPLF 395
Cdd:PRK11904 859 VGDPRLLSTDVGPVIDAEAKANLDAHIE-RMKREARLLAQLPlpAGTENGHFVAPTA-FEI-DSISQLEREVFGPILHVI 935
|
410 420
....*....|....*....|.
gi 1458409611 396 RFK--DEADVIAQANDTEFGL 414
Cdd:PRK11904 936 RYKasDLDKVIDAINATGYGL 956
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
51-468 |
2.43e-67 |
|
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: 222.10 E-value: 2.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 51 REAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAK--------GEISYAASFIE-WFAe 121
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilpvlSEINHAIKHLKkWMK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 122 eGKRIygdTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGI 201
Cdd:cd07134 80 -PKRV---RTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 202 PAGVFnVVTGSAgAVGGELTSNPlVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASK 281
Cdd:cd07134 156 EDEVA-VFEGDA-EVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 282 FRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEK-LRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKP 360
Cdd:cd07134 233 FLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKfYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 361 HAlGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRV----------- 429
Cdd:cd07134 313 DA-AQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVlartssggvvv 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1458409611 430 -GEALEYGIIGIntgiistevaPFGGVKASGLGREGSKYG 468
Cdd:cd07134 392 nDVVLHFLNPNL----------PFGGVNNSGIGSYHGVYG 421
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
13-463 |
4.28e-67 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 223.94 E-value: 4.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 13 ALIDGQWRdaPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLAR 92
Cdd:PLN02315 23 CYVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
Cdd:PLN02315 101 LVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 173 AGCTMVLKPASQTPFSALAL----AELANRAGIPAGVFNVVTGSA--GAVGGELTSNPLVrklSFTGSTEIGRQLMEQCA 246
Cdd:PLN02315 181 CGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCGGAeiGEAIAKDTRIPLV---SFTGSSKVGLMVQQTVN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 247 KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGV 326
Cdd:PLN02315 258 ARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 327 TTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALGGNFFQPTIlVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQ 406
Cdd:PLN02315 338 LLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEI 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 407 ANDTEFGLAAYFYARDLSRVFR-VG-EALEYGIIGINTGIISTEV-APFGGVKASGLGRE 463
Cdd:PLN02315 417 NNSVPQGLSSSIFTRNPETIFKwIGpLGSDCGIVNVNIPTNGAEIgGAFGGEKATGGGRE 476
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
12-414 |
3.02e-66 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 231.29 E-value: 3.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 12 QALIDGQWRDAP-------NGDVIAVTNPAN-GEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLM 83
Cdd:PRK11905 546 NAFAAKTWHAAPllaggdvDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLM 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 84 MENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDtiPGHQadkrllvikqPIGVTAAITPWNFPAAMI 163
Cdd:PRK11905 626 EAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNG--PGHK----------PLGPVVCISPWNFPLAIF 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 164 TRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTE----IGR 239
Cdd:PRK11905 694 TGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEvarlIQR 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 240 QLMEQCAKDIKKVSlELGG-NApFIVFDDADLDKAVEGALASKFRNAGQTCvCANR-LYVQDGVYDRFAEKLQQAVEKLR 317
Cdd:PRK11905 774 TLAKRSGPPVPLIA-ETGGqNA-MIVDSSALPEQVVADVIASAFDSAGQRC-SALRvLCLQEDVADRVLTMLKGAMDELR 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 318 IGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHAL-GGNFFQPTIL-VnvpDSAKVAKEETFGPLAPLF 395
Cdd:PRK11905 851 IGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETeKGTFVAPTLIeI---DSISDLEREVFGPVLHVV 927
|
410 420
....*....|....*....|.
gi 1458409611 396 RFK-DEAD-VIAQANDTEFGL 414
Cdd:PRK11905 928 RFKaDELDrVIDDINATGYGL 948
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
63-470 |
8.94e-65 |
|
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: 215.47 E-value: 8.94e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 63 AWRaltaKERANILRRwfdLMMENQDDLARLMTLEQGKPLAEA--------KGEISYAASFIEWFAEEgKRIYgdtIPGH 134
Cdd:cd07087 20 EWR----KAQLKALKR---MLTENEEEIAAALYADLGKPPAEAylteiavvLGEIDHALKHLKKWMKP-RRVS---VPLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 135 QADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAgIPAGVFNVVTGsAG 214
Cdd:cd07087 89 LQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-GV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 215 AVGGELTSNPLvRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANR 294
Cdd:cd07087 167 EVATALLAEPF-DHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 295 LYVQDGVYDRFAEKLQQAVEKLrIGDGLQDGVTTGPLIDEKAVAKVEEHIadaiaKGAKVVTGGKpHALGGNFFQPTILV 374
Cdd:cd07087 246 VLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQ-VDKEERYIAPTILD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 375 NVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD-------LSR-----------VFRVG-EALey 435
Cdd:cd07087 319 DVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDkavqervLAEtssggvcvndvLLHAAiPNL-- 396
|
410 420 430
....*....|....*....|....*....|....*
gi 1458409611 436 giigintgiistevaPFGGVKASGLGREGSKYGIE 470
Cdd:cd07087 397 ---------------PFGGVGNSGMGAYHGKAGFD 416
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
2-473 |
7.20e-64 |
|
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: 215.16 E-value: 7.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 2 QLNDMTLFRQQAL--IDGQWRDapNGDVIAVTNPAN-GEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRR 78
Cdd:TIGR01238 27 QIHAWADKTWQAApiIGHSYKA--DGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 79 WFDLMMENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKriygDTIPGHQAdkrllvikQPIGVTAAITPWNF 158
Cdd:TIGR01238 105 LADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVR----DVLGEFSV--------ESRGVFVCISPWNF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 159 PAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIG 238
Cdd:TIGR01238 173 PLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 239 RQLMEQCAKDI-KKVSL--ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEK 315
Cdd:TIGR01238 253 QLINQTLAQREdAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 316 LRIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAKG---AKVVTGGKPHALGGNFFQPTILvnVPDSAKVAKEETFGPLA 392
Cdd:TIGR01238 333 LKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLF--ELDDIAELSEEVFGPVL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 393 PLFRFK-DEAD-VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTEVA--PFGGvkaSGLGREGSKYG 468
Cdd:TIGR01238 411 HVVRYKaRELDqIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGG---QGLSGTGPKAG 487
|
....*
gi 1458409611 469 IEDYL 473
Cdd:TIGR01238 488 GPHYL 492
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
13-414 |
1.17e-63 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 223.66 E-value: 1.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 13 ALIDGQwrdAPNGDVIAVTNPANGEQ-LGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLA 91
Cdd:COG4230 560 PLIAGE---AASGEARPVRNPADHSDvVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELM 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 92 RLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHqadkrllvikqPIGVTAAITPWNFPAAMITRKAGPAL 171
Cdd:COG4230 637 ALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTVLR-----------GRGVFVCISPWNFPLAIFTGQVAAAL 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 172 AAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTE----IGRQLMEQCAK 247
Cdd:COG4230 706 AAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTEtarlINRTLAARDGP 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 248 DIKKVSlELGG-NApFIVFDDADLDKAVEGALASKFRNAGQTCvCANR-LYVQDGVYDRFAEKLQQAVEKLRIGDGLQDG 325
Cdd:COG4230 786 IVPLIA-ETGGqNA-MIVDSSALPEQVVDDVLASAFDSAGQRC-SALRvLCVQEDIADRVLEMLKGAMAELRVGDPADLS 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 326 VTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKP-HALGGNFFQPTI--LvnvpDSAKVAKEETFGPLAPLFRFK-DEA 401
Cdd:COG4230 863 TDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPeECANGTFVAPTLieI----DSISDLEREVFGPVLHVVRYKaDEL 938
|
410
....*....|....
gi 1458409611 402 D-VIAQANDTEFGL 414
Cdd:COG4230 939 DkVIDAINATGYGL 952
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
72-472 |
6.79e-57 |
|
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: 194.75 E-value: 6.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 72 RANILRRWFDLMMENQDDLARLMTLEQGKP-----LAE---AKGEISYAASFIEWFAEEGKRiyGDTIPGHQADKrLLVI 143
Cdd:cd07135 29 RLWQLKQLYWAVKDNEEAIVEALKKDLGRPpfetlLTEvsgVKNDILHMLKNLKKWAKDEKV--KDGPLAFMFGK-PRIR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 144 KQPIGVTAAITPWNFPaamITRKAGP---ALAAGCTMVLKPASQTPFSALALAELANRAgIPAGVFNVVTGsagavGGEL 220
Cdd:cd07135 106 KEPLGVVLIIGPWNYP---VLLALSPlvgAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQG-----GVPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 221 TSNPLVRKLS---FTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYV 297
Cdd:cd07135 177 TTALLEQKFDkifYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 298 QDGVYDRFAEKLQQAVEKLrIGDGLQDGVTTGPLIDEKAVAKVEEHIADaiAKGaKVVTGGKpHALGGNFFQPTILVNVP 377
Cdd:cd07135 257 DPSVYDEFVEELKKVLDEF-YPGGANASPDYTRIVNPRHFNRLKSLLDT--TKG-KVVIGGE-MDEATRFIPPTIVSDVS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 378 DSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFR-----------VGEALEYgiigintgiIS 446
Cdd:cd07135 332 WDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHiltrtrsggvvINDTLIH---------VG 402
|
410 420
....*....|....*....|....*.
gi 1458409611 447 TEVAPFGGVKASGLGREGSKYGIEDY 472
Cdd:cd07135 403 VDNAPFGGVGDSGYGAYHGKYGFDTF 428
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
56-462 |
1.08e-56 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 194.24 E-value: 1.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 56 AANRALPAwraLTAKERANILRRWFDLMMENQDDLA-----------RLMTLeqgkpLAE---AKGEISYAASFI-EWFA 120
Cdd:cd07133 9 AAFLANPP---PSLEERRDRLDRLKALLLDNQDALAeaisadfghrsRHETL-----LAEilpSIAGIKHARKHLkKWMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 121 EEgKRIYGDTIPGHQADkrllVIKQPIGVTAAITPWNFP-----AAMITrkagpALAAGCTMVLKPASQTPFSALALAEL 195
Cdd:cd07133 81 PS-RRHVGLLFLPAKAE----VEYQPLGVVGIIVPWNYPlylalGPLIA-----ALAAGNRVMIKPSEFTPRTSALLAEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 196 ANRAgIPAGVFNVVTGSAgAVGGELTSNPLvRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVE 275
Cdd:cd07133 151 LAEY-FDEDEVAVVTGGA-DVAAAFSSLPF-DHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 276 GALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKlRIGDGLQDGVTTGpLIDEKAVAKVEEHIADAIAKGAKVV 355
Cdd:cd07133 228 RIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAK-MYPTLADNPDYTS-IINERHYARLQGLLEDARAKGARVI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 356 T--GGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEal 433
Cdd:cd07133 306 ElnPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLR-- 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1458409611 434 eygiigintgiiST----------------EVAPFGGVKASGLGR 462
Cdd:cd07133 384 ------------RThsggvtindtllhvaqDDLPFGGVGASGMGA 416
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
10-419 |
5.98e-56 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 196.12 E-value: 5.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 10 RQQALIDGQWRDAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDD 89
Cdd:PLN02419 113 RVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 90 LARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGP 169
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 170 ALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGeLTSNPLVRKLSFTGSTEIGRQLMEQCAKDI 249
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 250 KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVC-ANRLYVQDGvyDRFAEKLQQAVEKLRIGDGLQDGVTT 328
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMAlSTVVFVGDA--KSWEDKLVERAKALKVTCGSEPDADL 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 329 GPLIDEKAVAKVEEHIADAIAKGAKVVTGGK----PHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVI 404
Cdd:PLN02419 430 GPVISKQAKERICRLIQSGVDDGAKLLLDGRdivvPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAI 509
|
410
....*....|....*
gi 1458409611 405 AQANDTEFGLAAYFY 419
Cdd:PLN02419 510 SIINKNKYGNGAAIF 524
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
19-414 |
3.61e-54 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 195.96 E-value: 3.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 19 WRDAP-------NGDVIAVTNPAN-GEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDL 90
Cdd:PRK11809 645 WQAAPmledpvaAGEMSPVINPADpRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTL 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 91 ARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYG-DTipgHQadkrllvikqPIGVTAAITPWNFPAAMITRKAGP 169
Cdd:PRK11809 725 MGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDnDT---HR----------PLGPVVCISPWNFPLAIFTGQVAA 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 170 ALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI 249
Cdd:PRK11809 792 ALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRL 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 250 ----KKVSL--ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQ 323
Cdd:PRK11809 872 dpqgRPIPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDR 951
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 324 DGVTTGPLIDEKAVAKVEEHIADAIAKGAKVVTGGKPHALG---GNFFQPTiLVNVpDSAKVAKEETFGPLAPLFRFKDE 400
Cdd:PRK11809 952 LSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEDwqsGTFVPPT-LIEL-DSFDELKREVFGPVLHVVRYNRN 1029
|
410
....*....|....*.
gi 1458409611 401 A--DVIAQANDTEFGL 414
Cdd:PRK11809 1030 QldELIEQINASGYGL 1045
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
142-470 |
1.45e-50 |
|
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: 178.08 E-value: 1.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 142 VIKQPIGVTAAITPWNFP-----AAMItrkaGpALAAGCTMVLKPASQTPFSALALAELANRAgIPAGVFNVVTGSAgAV 216
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPfqlalAPLI----G-AIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGV-EE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 217 GGELTSNPlVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLY 296
Cdd:cd07136 169 NQELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 297 VQDGVYDRFAEKLQQAVEKLrIGDGLQDGVTTGPLIDEKAVAKVEEHIadaiaKGAKVVTGGKPHAlGGNFFQPTILVNV 376
Cdd:cd07136 248 VHESVKEKFIKELKEEIKKF-YGEDPLESPDYGRIINEKHFDRLAGLL-----DNGKIVFGGNTDR-ETLYIEPTILDNV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 377 PDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIIGI--NTGIISTEVAPFGG 454
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIndTIMHLANPYLPFGG 400
|
330
....*....|....*.
gi 1458409611 455 VKASGLGREGSKYGIE 470
Cdd:cd07136 401 VGNSGMGSYHGKYSFD 416
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
24-459 |
6.81e-50 |
|
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: 178.16 E-value: 6.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 24 NGDVIAVTNPAN-GEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMME--NQDDLARLMtLEQGK 100
Cdd:cd07123 44 TGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGkyRYELNAATM-LGQGK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 101 PLAEAkgEISYAASFIEWF---AEEGKRIYGDTIPGHQADKRLLVIKQPI-GVTAAITPWNFPAAMITRKAGPALAaGCT 176
Cdd:cd07123 123 NVWQA--EIDAACELIDFLrfnVKYAEELYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 177 MVLKPASQTPFSALALAELANRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIK------ 250
Cdd:cd07123 200 VLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtyp 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 251 KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTTGP 330
Cdd:cd07123 280 RIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 331 LIDEKAVAKVEEHIADAIA-KGAKVVTGGKPHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDE--ADVIAQA 407
Cdd:cd07123 360 VIDEKAFDRIKGYIDHAKSdPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSdfEETLELV 439
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1458409611 408 NDT-EFGLAAYFYARDLSRVFRVGEALEYGIIGINTGIISTE--VA--PFGGVKASG 459
Cdd:cd07123 440 DTTsPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKPTGavVGqqPFGGARASG 496
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
70-470 |
2.02e-48 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 173.68 E-value: 2.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 70 KERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAK--------GEISYaasFIEWFAEEGKRIYGDTiPGHQADKRLL 141
Cdd:PTZ00381 29 EFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmtevlltvAEIEH---LLKHLDEYLKPEKVDT-VGVFGPGKSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 142 VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAgIPAGVFNVVTGSAgAVGGELT 221
Cdd:PTZ00381 105 IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGV-EVTTELL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 222 SNPLvRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGV 301
Cdd:PTZ00381 183 KEPF-DHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 302 YDRFAEKLQQAVEKLrIGDGLQDGVTTGPLIDEKAVAKVEEHIADaiaKGAKVVTGGKPHaLGGNFFQPTILVNV-PDSa 380
Cdd:PTZ00381 262 KDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVD-IENKYVAPTIIVNPdLDS- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 381 KVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEaleygiigintGIISTEVA---------- 450
Cdd:PTZ00381 336 PLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLE-----------NTSSGAVVindcvfhlln 404
|
410 420
....*....|....*....|...
gi 1458409611 451 ---PFGGVKASGLGREGSKYGIE 470
Cdd:PTZ00381 405 pnlPFGGVGNSGMGAYHGKYGFD 427
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
52-470 |
1.72e-42 |
|
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: 156.23 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 52 EAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEA--------KGEISYAASFI-EWFAEE 122
Cdd:cd07132 2 EAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAvlseillvKNEIKYAISNLpEWMKPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 123 gkriYGDTIPGHQADkRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELanragIP 202
Cdd:cd07132 82 ----PVKKNLATLLD-DVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 203 AGV----FNVVTGsagavGGELTSNPLVRKLS---FTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVE 275
Cdd:cd07132 152 KYLdkecYPVVLG-----GVEETTELLKQRFDyifYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 276 GALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLrIGDGLQDGVTTGPLIDEKAVAKVEEHIadaiaKGAKVV 355
Cdd:cd07132 227 RIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 356 TGGKpHALGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD-------LSRV-- 426
Cdd:cd07132 301 IGGQ-TDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNkkvinkiLSNTss 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1458409611 427 --FRVGEALEYgiigintgiISTEVAPFGGVKASGLGREGSKYGIE 470
Cdd:cd07132 380 ggVCVNDTIMH---------YTLDSLPFGGVGNSGMGAYHGKYSFD 416
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
12-422 |
5.45e-37 |
|
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: 142.41 E-value: 5.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 12 QALIDGQWRdAPNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLA 91
Cdd:cd07128 2 QSYVAGQWH-AGTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 92 RLMTLeQGKPLAEAKGEISYAASFIEWFAEEGKR--------IYGDTIP----GHQADKRLLVIKQpiGVTAAITPWNFP 159
Cdd:cd07128 81 ALSAA-TGATRRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPlskdGTFVGQHILTPRR--GVAVHINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 160 AAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGI-PAGVFNVVTGSAGAVGGELTSNPLVrklSFTGSTEIG 238
Cdd:cd07128 158 VWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHLGEQDVV---AFTGSAATA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 239 RQL--------------MEQcakDikkvSLELGGNAPFIVFDDADLD---KAVEGALASKfrnAGQTCVCANRLYVQDGV 301
Cdd:cd07128 235 AKLrahpnivarsirfnAEA---D----SLNAAILGPDATPGTPEFDlfvKEVAREMTVK---AGQKCTAIRRAFVPEAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 302 YDRFAEKLQQAVEKLRIGDGLQDGVTTGPLIDEKAVAKVEEHIAdAIAKGAKVVTGGKP-------HALGGNFFQPTILV 374
Cdd:cd07128 305 VDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVA-TLLAEAEVVFGGPDrfevvgaDAEKGAFFPPTLLL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1458409611 375 -NVPDSAKVAKE-ETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD 422
Cdd:cd07128 384 cDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
17-422 |
2.58e-36 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 140.61 E-value: 2.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 17 GQWRDApNGDVIAVTNPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTL 96
Cdd:PRK11903 11 GRWQAG-SGAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 97 EQGKPLAEAKGEISYAASFIEWFAEEGKRIyGDTI-----PGHQADKRLLVIKQPI-----GVTAAITPWNFPAAMITRK 166
Cdd:PRK11903 90 NSGTTRNDSAVDIDGGIFTLGYYAKLGAAL-GDARllrdgEAVQLGKDPAFQGQHVlvptrGVALFINAFNFPAWGLWEK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 167 AGPALAAGCTMVLKPASQTPFSALALAELANRAGI-PAGVFNVVTGSAGAVGGELTSNPLVrklSFTGSTEIGRQLMEQC 245
Cdd:PRK11903 169 AAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFDVV---SFTGSAETAAVLRSHP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 246 A-------KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRI 318
Cdd:PRK11903 246 AvvqrsvrVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 319 GDGLQDGVTTGPLIDEKAVAKVEEHIAdAIAKGAKVVTGGKPHAL------GGNFFQPTIL-VNVPDSAKVAKE-ETFGP 390
Cdd:PRK11903 326 GNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALvdadpaVAACVGPTLLgASDPDAATAVHDvEVFGP 404
|
410 420 430
....*....|....*....|....*....|..
gi 1458409611 391 LAPLFRFKDEADVIAQANDTEFGLAAYFYARD 422
Cdd:PRK11903 405 VATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
48-470 |
2.81e-36 |
|
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: 139.08 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 48 DETREAIEAANRALPAWRALTAKeraNILRrwfdLMMENQDDLARLMTLEQGKPLAEA-KGEISYAASFI--------EW 118
Cdd:cd07137 6 RELRETFRSGRTRSAEWRKSQLK---GLLR----LVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCklaikelkKW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 119 FAEEGKRIYGDTIPGHQAdkrllVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELanr 198
Cdd:cd07137 79 MAPEKVKTPLTTFPAKAE-----IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 199 agIP----AGVFNVVTGSAgAVGGELTSNPLvRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAV 274
Cdd:cd07137 151 --IPeyldTKAIKVIEGGV-PETTALLEQKW-DKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 275 EGALASKF-RNAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLrIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAKgAK 353
Cdd:cd07137 227 RRIAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVA-DK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 354 VVTGGKPHAlGGNFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD--LSRVFRVGE 431
Cdd:cd07137 305 IVHGGERDE-KNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNkeLKRRIVAET 383
|
410 420 430
....*....|....*....|....*....|....*....
gi 1458409611 432 ALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIE 470
Cdd:cd07137 384 SSGGVTFNDTVVQYAIDTLPFGGVGESGFGAYHGKFSFD 422
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
49-470 |
1.95e-32 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 129.08 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 49 ETREAIEAANRALPAWRAltakeraNILRRWFDLMMENQDDLARLMTLEQGKPLAEA--------KGEISYAASFI-EWF 119
Cdd:PLN02203 14 ELRETYESGRTRSLEWRK-------SQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyrdevgvlTKSANLALSNLkKWM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 120 AEEGKRIYGDTIPGhqadkRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAelanrA 199
Cdd:PLN02203 87 APKKAKLPLVAFPA-----TAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA-----A 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 200 GIP----AGVFNVVTGSAgAVGGELTSNPLvRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIV--FDDA-DLDK 272
Cdd:PLN02203 157 NIPkyldSKAVKVIEGGP-AVGEQLLQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 273 AVEGALASKFRN-AGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLrIGDGLQDGVTTGPLIDEKAVAKVEEHIADAIAKg 351
Cdd:PLN02203 235 AVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKF-FGENPRESKSMARILNKKHFQRLSNLLKDPRVA- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 352 AKVVTGG--KPHALggnFFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDlsrvfrv 429
Cdd:PLN02203 313 ASIVHGGsiDEKKL---FIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNN------- 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1458409611 430 gEALEYGIIGINTGIIST----------EVAPFGGVKASGLGREGSKYGIE 470
Cdd:PLN02203 383 -EKLKRRILSETSSGSVTfndaiiqyacDSLPFGGVGESGFGRYHGKYSFD 432
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
52-408 |
4.03e-31 |
|
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: 124.96 E-value: 4.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 52 EAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEE-------GK 124
Cdd:cd07129 3 AAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLvregswlDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 125 RIygDT-----IPGHQADKRLLviKQPIGVTAAITPWNFPAAMITrkAG----PALAAGCTMVLKPASQTPFSALALAEL 195
Cdd:cd07129 83 RI--DPadpdrQPLPRPDLRRM--LVPLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKAHPAHPGTSELVARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 196 ANRA----GIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK--DIKKVSLELGGNAPFIVFDDA- 268
Cdd:cd07129 157 IRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGAl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 269 --DLDKAVEGALASKFRNAGQTCVCANRLYVQDGV-YDRFAEKLQQAVEKL--------RIGDGLQDGVttgplidekav 337
Cdd:cd07129 237 aeRGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPaGDAFIAALAEALAAApaqtmltpGIAEAYRQGV----------- 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1458409611 338 akveEHIADaiAKGAKVVTGGKPhALGGNFFQPTILvnVPDSAKVAK-----EETFGPLAPLFRFKDEADVIAQAN 408
Cdd:cd07129 306 ----EALAA--APGVRVLAGGAA-AEGGNQAAPTLF--KVDAAAFLAdpalqEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
53-463 |
1.31e-27 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 114.64 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 53 AIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAkGEISYAASFIEWFAeegKRIYGDTIP 132
Cdd:cd07084 4 ALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARA---FVIYSYRIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 133 GHQADKRLLVIKQ-------PIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGI-PAG 204
Cdd:cd07084 80 HEPGNHLGQGLKQqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 205 VFNVVTGSaGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQcAKDIkKVSLELGGNAPFIVFDDADLDKAVEGALA-SKFR 283
Cdd:cd07084 160 DVTLINGD-GKTMQALLLHPNPKMVLFTGSSRVAEKLALD-AKQA-RIYLELAGFNWKVLGPDAQAVDYVAWQCVqDMTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 284 NAGQTCVCANRLYV-QDGVYDRFAEKLQQAVEKLRIGDglqdgVTTGPLIDEKAVAKVEEHIADAiakGAKVVTGGK--- 359
Cdd:cd07084 237 CSGQKCTAQSMLFVpENWSKTPLVEKLKALLARRKLED-----LLLGPVQTFTTLAMIAHMENLL---GSVLLFSGKelk 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 360 ----PHALGGNFFQPTILVNVPDSAK--VAKEETFGPLAPLFRFKD--EADVIAQANDTEFGLAAYFYARDLSRVFRVGE 431
Cdd:cd07084 309 nhsiPSIYGACVASALFVPIDEILKTyeLVTEEIFGPFAIVVEYKKdqLALVLELLERMHGSLTAAIYSNDPIFLQELIG 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 1458409611 432 ALEYGIIGINTGIISTEVAPF----GGVKASGLGRE 463
Cdd:cd07084 389 NLWVAGRTYAILRGRTGVAPNqnhgGGPAADPRGAG 424
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
118-472 |
1.36e-24 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 106.28 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 118 WFAEEGKRIYGDTIPGHQAdkrllVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAN 197
Cdd:PLN02174 89 WMAPEKAKTSLTTFPASAE-----IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 198 RAGIPAGVfNVVTGSAGAVGGELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGA 277
Cdd:PLN02174 164 QYLDSSAV-RVVEGAVTETTALLEQK--WDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 278 LASKFR-NAGQTCVCANRLYVQDGVYDRFAEKLQQAVEKLRIGDGLQDGVTT-----------GPLIDEKAVAKveehia 345
Cdd:PLN02174 241 IAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSrivnsthfdrlSKLLDEKEVSD------ 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 346 daiakgaKVVTGGKPHALGGNfFQPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYA--RDL 423
Cdd:PLN02174 315 -------KIVYGGEKDRENLK-IAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFThnKKL 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1458409611 424 SRVFRVGEALEYGIIGINTGIISTEVAPFGGVKASGLGREGSKYGIEDY 472
Cdd:PLN02174 387 KERFAATVSAGGIVVNDIAVHLALHTLPFGGVGESGMGAYHGKFSFDAF 435
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
14-400 |
3.01e-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: 93.33 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 14 LIDGQWRDAPNGdvIAVTNPANGEQLGSVPKMGADETREAIEAAnRALPA---WRALTAKERANIlrrWFDLMM------ 84
Cdd:cd07126 2 LVAGKWKGASNY--TTLLDPLNGDKFISVPDTDEDEINEFVDSL-RQCPKsglHNPLKNPERYLL---YGDVSHrvahel 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 85 ---ENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIY--GDTIPGHQADKRLLVIKQPIGVTAAITPWNFP 159
Cdd:cd07126 76 rkpEVEDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLarSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 160 AAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTgSAGAVGGELTSNPLVRKLSFTGSTEIGR 239
Cdd:cd07126 156 LEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIH-SDGPTMNKILLEANPRMTLFTGSSKVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 240 QLmeqcAKDIK-KVSLELGGNAPFIVFDD-ADLDKAVEGALASKFRNAGQTCVCANRLYVQDG-VYDRFAEKLQQAVEKL 316
Cdd:cd07126 235 RL----ALELHgKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALAEQR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 317 RIGDglqdgVTTGPLIdEKAVAKVEEHIADAIA-KGAKVVTGGKP---HALGGNF--FQPTIL------VNVPDSAKVAK 384
Cdd:cd07126 311 KLED-----LTIGPVL-TWTTERILDHVDKLLAiPGAKVLFGGKPltnHSIPSIYgaYEPTAVfvpleeIAIEENFELVT 384
|
410
....*....|....*.
gi 1458409611 385 EETFGPLAPLFRFKDE 400
Cdd:cd07126 385 TEVFGPFQVVTEYKDE 400
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
32-361 |
1.95e-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: 65.71 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 32 NPANGEQLGSVPKMGADETREAIEAANRALPAWRALTAKERANILRR----WFDLMMENQDDLARLMTLEQGKPLAEAKg 107
Cdd:cd07077 4 KNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSlianWIAMMGCSESKLYKNIDTERGITASVGH- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 108 eisyaaSFIEWFAEEGKriygdtipghqadkrLLVIKQPIGVTAAITPWNFPAAMITrKAGPALAAGCTMVLKPASQTPF 187
Cdd:cd07077 83 ------IQDVLLPDNGE---------------TYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 188 SALALAeLANRAGIPAG-----VFNVVTGSAGAVgGELTSNPLVRKLSFTGsteiGRQLMEQCAKDIKKVSLeLG---GN 259
Cdd:cd07077 141 TNRALA-LLFQAADAAHgpkilVLYVPHPSDELA-EELLSHPKIDLIVATG----GRDAVDAAVKHSPHIPV-IGfgaGN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 260 APFIVFDDADLDKAVEGALASKFRNaGQTCVCANRLYVQDGVYDRFAE--KLQQAVEKLRIGDG--LQDGVTT------- 328
Cdd:cd07077 214 SPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYVVDDVLDPLYEefKLKLVVEGLKVPQEtkPLSKETTpsfddea 292
|
330 340 350
....*....|....*....|....*....|....*..
gi 1458409611 329 ----GPLIDEKAVAKVEEHIADAIAKGAKvvtGGKPH 361
Cdd:cd07077 293 lesmTPLECQFRVLDVISAVENAWMIIES---GGGPH 326
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
52-407 |
2.06e-11 |
|
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: 65.75 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 52 EAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGdtI 131
Cdd:cd07081 3 DAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTCG--V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 132 PGHQADKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRAGIPAGVFNVVTG 211
Cdd:cd07081 81 LTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 212 SAGAVGGELTsNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELG-GNAPFIVFDDADLDKAVEGALASKFRNAGQTCV 290
Cdd:cd07081 161 WIDNPSIELA-QRLMKFPGIGLLLATGGPAVVKAAYSSGKPAIGVGaGNTPVVIDETADIKRAVQSIVKSKTFDNGVICA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 291 CANRLYVQDGVYDRFAEKLQQaveklrigdglQDGVttgpLIDEKAVAKVEEHIADAIAKGAKVV--TGGKPHALGGNFF 368
Cdd:cd07081 240 SEQSVIVVDSVYDEVMRLFEG-----------QGAY----KLTAEELQQVQPVILKNGDVNRDIVgqDAYKIAAAAGLKV 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1458409611 369 QPTILVNVPDSAKVAKEETFG-----PLAPLFRFKDEADVIAQA 407
Cdd:cd07081 305 PQETRILIGEVTSLAEHEPFAheklsPVLAMYRAANFADADAKA 348
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
49-432 |
9.82e-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: 64.04 E-value: 9.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 49 ETREAIEAANRALPAWRALTAKERA----NILRRWFDLMMENQDDL------ARLMTLEQGKPLAEAKG--EISYAA--- 113
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAgvclEILQRLNARSFEMAHAVmhttgqAFMMAFQAGGPHAQDRGleAVAYAWrem 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 114 SFI----EWFAEEGKRiygdtiPGHQADKRLLVIkqPIGVTAAITPWNFPaamiTRKAGPA----LAAGCTMVLKPAsqt 185
Cdd:cd07127 165 SRIpptaEWEKPQGKH------DPLAMEKTFTVV--PRGVALVIGCSTFP----TWNGYPGlfasLATGNPVIVKPH--- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 186 PFSALALA-------ELANRAGI-PAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKdiKKVSLELG 257
Cdd:cd07127 230 PAAILPLAitvqvarEVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 258 GNAPFIVfDDADLDKAVEGALASKFR-NAGQTCVCANRLYV-QDGV--------YDRFAEKLQQAVEKLrIGDGLQDGVT 327
Cdd:cd07127 308 GVNTVVV-DSTDDLKAMLRNLAFSLSlYSGQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGL-LADPARAAAL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 328 TGPLIDEKAVAKVEEhiadaIAKGAKVVTGGKPHA----LGGNFFQPTIL-VNVPDSAKVAkEETFGPLAPLFRFKDEAD 402
Cdd:cd07127 386 LGAIQSPDTLARIAE-----ARQLGEVLLASEAVAhpefPDARVRTPLLLkLDASDEAAYA-EERFGPIAFVVATDSTDH 459
|
410 420 430
....*....|....*....|....*....|...
gi 1458409611 403 VIAQANDT--EFG-LAAYFYARDLSRVFRVGEA 432
Cdd:cd07127 460 SIELARESvrEHGaMTVGVYSTDPEVVERVQEA 492
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
26-434 |
8.66e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 57.60 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 26 DVIA-VTNPANGEQLGSVPKMGA-DETREAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLA 103
Cdd:PRK15398 12 AVLAeMLSSQTVSPPAAVGEMGVfASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 104 EAKGEISYAASF----IEWFAEEGkrIYGDtipghqaDKRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVL 179
Cdd:PRK15398 92 EDKIAKNVAAAEktpgVEDLTTEA--LTGD-------NGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 180 KPASQTPFSALALAELANRAGIPA-GVFNVVTGSAGAV---GGELTSNPLVRKLSFTGSTEIGRQLMeqcaKDIKKVSLE 255
Cdd:PRK15398 163 SPHPGAKKVSLRAIELLNEAIVAAgGPENLVVTVAEPTietAQRLMKHPGIALLVVTGGPAVVKAAM----KSGKKAIGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 256 LGGNAPFIVFDDADLDKA----VEGAlasKFRNaGQTCVCANRLYVQDGVYDRFAEKLQQAvEKLRIGDGLQDGVTTGPL 331
Cdd:PRK15398 239 GAGNPPVVVDETADIEKAardiVKGA---SFDN-NLPCIAEKEVIVVDSVADELMRLMEKN-GAVLLTAEQAEKLQKVVL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 332 IDEKAVAKveEHI---ADAIAKGAKVVTGGKPhalggnffqPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
Cdd:PRK15398 314 KNGGTVNK--KWVgkdAAKILEAAGINVPKDT---------RLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAV 382
|
410 420
....*....|....*....|....*...
gi 1458409611 409 DTEFGL--AAYFYARDLSRVFRVGEALE 434
Cdd:PRK15398 383 KLEHGNrhTAIMHSRNVDNLNKMARAIQ 410
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
52-434 |
1.95e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 56.48 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 52 EAIEAANRALPAWRALTAKERANILRRWFDLMMENQDDLARLMTLEQGKPLAEAK-------GEISYAASFIEWFAEEGK 124
Cdd:cd07121 8 DAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKiaknhlaAEKTPGTEDLTTTAWSGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 125 RiyGDTipghqadkrlLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELANRA----G 200
Cdd:cd07121 88 N--GLT----------LVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAiaeaG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 201 IPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMeqcaKDIKKVSLELGGNAPFIVFDDADLDKA----VEG 276
Cdd:cd07121 156 GPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAAL----SSGKKAIGAGAGNPPVVVDETADIEKAardiVQG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 277 AlasKFRNaGQTCVCANRLYVQDGVYDRFAEKLQ---------QAVEKLrigdgLQDGVTT--GPLIDEKAVAKVeehiA 345
Cdd:cd07121 232 A---SFDN-NLPCIAEKEVIAVDSVADYLIAAMQrngayvlndEQAEQL-----LEVVLLTnkGATPNKKWVGKD----A 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 346 DAIAKGAKVVTGGKPhalggnffqPTILVNVPDSAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGL--AAYFYARDL 423
Cdd:cd07121 299 SKILKAAGIEVPADI---------RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNV 369
|
410
....*....|.
gi 1458409611 424 SRVFRVGEALE 434
Cdd:cd07121 370 ENLTKMARAMQ 380
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
138-354 |
2.30e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 49.80 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 138 KRLLVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKP---ASQTPFSAL-ALAELANRAGIPAGVFNVVTGSA 213
Cdd:cd07122 87 KGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAkIMREAAVAAGAPEGLIQWIEEPS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1458409611 214 GAVGGELTSNPLVRKLSFTGSTEigrqlMEQCAKDIKKVSLELG-GNAPFIVFDDADLDKAVEGALASK-FRNAgqtCVC 291
Cdd:cd07122 167 IELTQELMKHPDVDLILATGGPG-----MVKAAYSSGKPAIGVGpGNVPAYIDETADIKRAVKDIILSKtFDNG---TIC 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1458409611 292 A--NRLYVQDGVYDRFAEKLQQ-------AVEKLRIGDGLQDGvttGPLIDEKAVAKVEEHIADA----IAKGAKV 354
Cdd:cd07122 239 AseQSVIVDDEIYDEVRAELKRrgayflnEEEKEKLEKALFDD---GGTLNPDIVGKSAQKIAELagieVPEDTKV 311
|
|
| |
