|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 791.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 30 VSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 110 AYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTA 189
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 190 LAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDAD 269
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 270 IDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMS 349
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 350 RGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRV 429
Cdd:cd07103 321 KGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1513169189 430 SEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLCQ 480
Cdd:cd07103 401 AEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
6-481 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 745.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 6 SNLFRQQALIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILE 85
Cdd:PLN02278 20 AGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 86 NKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITR 165
Cdd:PLN02278 100 NKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 166 KAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQC 245
Cdd:PLN02278 180 KVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 246 AESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESD 325
Cdd:PLN02278 260 AATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 326 VQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIE 405
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIA 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1513169189 406 QANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLCQG 481
Cdd:PLN02278 420 IANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCLG 495
|
|
| 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: 689.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 1 MSVFHSNLFRQQALIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWH 80
Cdd:PRK11241 1 MQLNDSTLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 81 RLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPA 160
Cdd:PRK11241 81 NLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 161 AMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRV 240
Cdd:PRK11241 161 AMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 241 LMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGD 320
Cdd:PRK11241 241 LMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 321 GSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDE 400
Cdd:PRK11241 321 GLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 401 QEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLCQ 480
Cdd:PRK11241 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
..
gi 1513169189 481 GL 482
Cdd:PRK11241 481 GL 482
|
|
| 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: 667.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 30 VSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 110 AYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTA 189
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 190 LAMAELANQAGIPQGVINVVTG-QSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDA 268
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 269 DIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAM 348
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 349 SRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWR 428
Cdd:TIGR01780 321 EKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1513169189 429 VSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:TIGR01780 401 VAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
7-482 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 637.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 7 NLFRQQALIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILEN 86
Cdd:COG1012 2 TTPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 87 KTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRK 166
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 167 AGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCA 246
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 247 ESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDV 326
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 327 QIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPL-GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIE 405
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513169189 406 QANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEV-APFGGVKQSGLGREGSEHGIEDYLEMKYLCQGL 482
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
19-476 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 570.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 19 WRDAaDGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQ 98
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 99 GKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPgADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMV 178
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSD-PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 179 IKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGG 258
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 259 NAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGR 338
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 339 KVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYF 418
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1513169189 419 YSNDAARIWRVSEQLEYGMVGINTGLISN-EVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:pfam00171 399 FTSDLERALRVARRLEAGMVWINDYTTGDaDGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
67-476 |
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: 529.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 67 LTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQG 146
Cdd:cd07078 17 LPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGELAIVRREP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 147 VGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERV 226
Cdd:cd07078 97 LGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALASHPRV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 227 RKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFC 306
Cdd:cd07078 177 DKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 307 DKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLG-GNFFTPTVIGDVQPGSLLLQE 385
Cdd:cd07078 257 ERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkGYFVPPTVLTDVDPDMPIAQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 386 EIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEV-APFGGVKQSGLGREG 464
Cdd:cd07078 337 EIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPsAPFGGVKQSGIGREG 416
|
410
....*....|..
gi 1513169189 465 SEHGIEDYLEMK 476
Cdd:cd07078 417 GPYGLEEYTEPK 428
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
15-476 |
1.08e-169 |
|
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: 486.00 E-value: 1.08e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIM 94
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 95 TAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAG 174
Cdd:cd07088 82 VEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 175 CTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSL 254
Cdd:cd07088 162 NTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 255 ELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINA 334
Cdd:cd07088 242 ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 335 DAGRKVQSLLDDAMSRGATLLTGGKAHPLG-GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYG 413
Cdd:cd07088 322 AALDKVEEMVERAVEAGATLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1513169189 414 LASYFYSNDAARIWRVSEQLEYGMVGINTGlisNEVAPFG---GVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07088 402 LTSYIYTENLNTAMRATNELEFGETYINRE---NFEAMQGfhaGWKKSGLGGADGKHGLEEYLQTK 464
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
67-476 |
2.09e-157 |
|
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: 454.32 E-value: 2.09e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 67 LTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQG 146
Cdd:cd07114 40 LTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 147 VGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERV 226
Cdd:cd07114 120 LGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 227 RKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFC 306
Cdd:cd07114 200 AKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 307 DKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPL----GGNFFTPTVIGDVQPGSLL 382
Cdd:cd07114 280 ERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSGadlgAGYFFEPTILADVTNDMRI 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 383 LQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGR 462
Cdd:cd07114 360 AQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGR 439
|
410
....*....|....
gi 1513169189 463 EGSEHGIEDYLEMK 476
Cdd:cd07114 440 ENGIEAIREYTQTK 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
32-479 |
4.33e-157 |
|
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: 453.56 E-value: 4.33e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 32 NPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAE-GEIA 110
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRDIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 111 YAASFIEWFAEQGKRANGEIIPSPGaDKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTAL 190
Cdd:cd07093 83 RAAANFRFFADYILQLDGESYPQDG-GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 191 AMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADI 270
Cdd:cd07093 162 LLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 271 DKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSR 350
Cdd:cd07093 242 DRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 351 GATLLTGGKAHPL----GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARI 426
Cdd:cd07093 322 GATILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1513169189 427 WRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLC 479
Cdd:cd07093 402 HRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
3-476 |
2.66e-152 |
|
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: 442.03 E-value: 2.66e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 3 VFHSNLFrqqalIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRA--EAQQAVDAAAAALPAWRALTAAQRAALLKNWH 80
Cdd:cd07091 1 EQPTGLF-----INNEFVDSVSGKTFPTINPATEEVICQVAEADEEdvDAAVKAARAAFETGWWRKMDPRERGRLLNKLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 81 RLILENKTALAQIMTAEQGKPLAE-AEGEIAYAASFIEWFAEQGKRANGEIIPSPGaDKRLMVIRQGVGVCAAITPWNFP 159
Cdd:cd07091 76 DLIERDRDELAALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIPIDG-NFLAYTRREPIGVCGQIIPWNFP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 160 AAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGR 239
Cdd:cd07091 155 LLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 240 VLMRQCAES-IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKV 318
Cdd:cd07091 235 TIMEAAAKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 319 GDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFE 398
Cdd:cd07091 315 GDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFK 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513169189 399 DEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07091 395 TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
30-476 |
1.39e-151 |
|
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: 439.27 E-value: 1.39e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 30 VSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 110 AYAASFIEWFAEQgkRANGEIIPSpGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTA 189
Cdd:cd07106 81 GGAVAWLRYTASL--DLPDEVIED-DDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 190 LAMAELANQAgIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDAD 269
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 270 IDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMS 349
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 350 RGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRV 429
Cdd:cd07106 316 KGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAV 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1513169189 430 SEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07106 396 ARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
67-478 |
6.38e-151 |
|
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: 436.96 E-value: 6.38e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 67 LTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQG 146
Cdd:cd07104 19 TPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDVPGKESMVRRVP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 147 VGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFT-ALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDER 225
Cdd:cd07104 99 LGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGGGSEIGDALVEHPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 226 VRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQF 305
Cdd:cd07104 179 VRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 306 CDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQE 385
Cdd:cd07104 259 VEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE---GLFYQPTVLSDVTPDMPIFRE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 386 EIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNE-VAPFGGVKQSGLGREG 464
Cdd:cd07104 336 EIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDEpHVPFGGVKASGGGRFG 415
|
410
....*....|....
gi 1513169189 465 SEHGIEDYLEMKYL 478
Cdd:cd07104 416 GPASLEEFTEWQWI 429
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
32-478 |
4.31e-147 |
|
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: 427.90 E-value: 4.31e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 32 NPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAY 111
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 112 AASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALA 191
Cdd:cd07150 85 TPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 192 MAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADID 271
Cdd:cd07150 165 IAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 272 KAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRG 351
Cdd:cd07150 245 YAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 352 ATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSE 431
Cdd:cd07150 325 AKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAE 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1513169189 432 QLEYGMVGINTGLISNE-VAPFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07150 402 RLESGMVHINDPTILDEaHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
30-479 |
1.04e-146 |
|
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: 427.01 E-value: 1.04e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 30 VSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 110 AYAASFIEWFAEQGKRANGEIIP---SPGADKRL-MVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANET 185
Cdd:cd07149 83 DRAIETLRLSAEEAKRLAGETIPfdaSPGGEGRIgFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 186 PFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAesIKKLSLELGGNAPFIVF 265
Cdd:cd07149 163 PLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 266 DDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLD 345
Cdd:cd07149 241 ADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 346 DAMSRGATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAAR 425
Cdd:cd07149 321 EAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQK 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1513169189 426 IWRVSEQLEYGMVGINTglISN---EVAPFGGVKQSGLGREGSEHGIEDYLEMKYLC 479
Cdd:cd07149 398 ALKAARELEVGGVMIND--SSTfrvDHMPYGGVKESGTGREGPRYAIEEMTEIKLVC 452
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
15-476 |
2.62e-144 |
|
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: 421.53 E-value: 2.62e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIM 94
Cdd:cd07138 3 IDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 95 TAEQGKPLAEAE--------GEIAYAASFIEWFAEQGKRANGeiipspgadkrlMVIRQGVGVCAAITPWNFPAAMITRK 166
Cdd:cd07138 83 TLEMGAPITLARaaqvglgiGHLRAAADALKDFEFEERRGNS------------LVVREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 167 AGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCA 246
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 247 ESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDV 326
Cdd:cd07138 231 DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 327 QIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLG---GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEA 403
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEGlerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513169189 404 IEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINtGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
15-476 |
2.77e-143 |
|
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: 419.41 E-value: 2.77e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAA--LPAWRALTAAQRAALLKNWHRLILENKTALAQ 92
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 93 IMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRlMVIRQGVGVCAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07119 82 LETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVIS-RTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 173 AGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKL 252
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 253 SLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLI 332
Cdd:cd07119 241 ALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 333 NADAGRKVQSLLDDAMSRGATLLTGGKAhPLG-----GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQA 407
Cdd:cd07119 321 SAEHREKVLSYIQLGKEEGARLVCGGKR-PTGdelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 408 NNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINT-GLISNEvAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07119 400 NDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDyHPYFAE-APWGGYKQSGIGRELGPTGLEEYQETK 468
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
67-479 |
5.74e-140 |
|
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: 406.62 E-value: 5.74e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 67 LTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQG 146
Cdd:cd06534 13 LPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEAYVRREP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 147 VGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERV 226
Cdd:cd06534 93 LGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLSHPRV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 227 RKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFC 306
Cdd:cd06534 173 DKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDEFV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 307 DKFVarvaalkvgdgsesdvqigplinadagrkvqsllddamsrgatlltggkahplggnfftpTVIGDVQPGSLLLQEE 386
Cdd:cd06534 253 EKLV------------------------------------------------------------TVLVDVDPDMPIAQEE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 387 IFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEV-APFGGVKQSGLGREGS 465
Cdd:cd06534 273 IFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPeAPFGGVKNSGIGREGG 352
|
410
....*....|....
gi 1513169189 466 EHGIEDYLEMKYLC 479
Cdd:cd06534 353 PYGLEEYTRTKTVV 366
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
70-469 |
2.36e-139 |
|
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: 407.23 E-value: 2.36e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 70 AQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRAN-GEIIPSPGadKRLMVIRQGVG 148
Cdd:cd07100 21 AERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLaDEPIETDA--GKAYVRYEPLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 149 VCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFtGDERVRK 228
Cdd:cd07100 99 VVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEAII-ADPRVRG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 229 LSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDK 308
Cdd:cd07100 178 VTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 309 FVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIF 388
Cdd:cd07100 258 FVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELF 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 389 GPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHG 468
Cdd:cd07100 338 GPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVKRSGYGRELGRFG 417
|
.
gi 1513169189 469 I 469
Cdd:cd07100 418 I 418
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
14-476 |
1.46e-138 |
|
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: 407.12 E-value: 1.46e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 14 LIAGSWRDAADGTTLAVSNPSTGATL-GQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQ 92
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVvGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 93 IMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 173 AGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKL 252
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 253 SLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLI 332
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 333 NADAGRKVQSLLDDAMSRGATLLTGGKA----HPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQAN 408
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 409 NTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEV-APFGGVKQSGLG-REGSEHGIEDYLEMK 476
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVhLPFGGVKKSGNGhREAGTTALDAFTEWK 471
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
28-478 |
3.21e-138 |
|
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: 405.58 E-value: 3.21e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 28 LAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEG 107
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 108 EIAYAASFIEWFAEQGKRANGEIIPSPGAD--KRLMVI--RQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPAN 183
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEynERRIAFtvREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 184 ETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFI 263
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 264 VFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSL 343
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 344 LDDAMSRGATLLTGGKAHPlgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDA 423
Cdd:cd07145 321 VNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDI 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1513169189 424 ARIWRVSEQLEYGMVGIN-TGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07145 399 NRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
15-476 |
1.85e-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: 401.57 E-value: 1.85e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAA--LPAWRALTAAQRAALLKNWHRLILENKTALAQ 92
Cdd:cd07139 3 IGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 93 IMTAEQGKPLAEAE-GEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPAL 171
Cdd:cd07139 83 LWTAENGMPISWSRrAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 172 AAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKK 251
Cdd:cd07139 163 AAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 252 LSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPL 331
Cdd:cd07139 242 VTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 332 INADAGRKVQSLLDDAMSRGATLLTGGK--AHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANN 409
Cdd:cd07139 322 ASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIAND 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513169189 410 TIYGLASYFYSNDAARIWRVSEQLEYGMVGINtGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07139 402 SDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETK 467
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
67-476 |
4.73e-136 |
|
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: 400.08 E-value: 4.73e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 67 LTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEG-EIAYAASFIEWFAEQGKRANGEII----PSPGADKRLM 141
Cdd:cd07089 39 TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAmQVDGPIGHLRYFADLADSFPWEFDlpvpALRGGPGRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 142 VIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFT 221
Cdd:cd07089 119 VRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 222 GDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAV 301
Cdd:cd07089 199 TDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 302 YDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGK--AHPLGGNFFTPTVIGDVQPG 379
Cdd:cd07089 279 YDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGrpAGLDKGFYVEPTLFADVDND 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 380 SLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSG 459
Cdd:cd07089 359 MRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSG 438
|
410
....*....|....*..
gi 1513169189 460 LGREGSEHGIEDYLEMK 476
Cdd:cd07089 439 LGRENGIEGLEEFLETK 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
17-477 |
2.17e-135 |
|
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: 398.60 E-value: 2.17e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 17 GSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTA 96
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 97 EQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCT 176
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 177 MVIKPANETPFTA-LAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLE 255
Cdd:cd07151 161 VVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 256 LGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINAD 335
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 336 AGRKVQSLLDDAMSRGATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLA 415
Cdd:cd07151 321 QVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLS 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513169189 416 SYFYSNDAARIWRVSEQLEYGMVGINTGLISNE-VAPFGGVKQSGLGREGSEHGIEDYLEMKY 477
Cdd:cd07151 398 GAVFTSDLERGVQFARRIDAGMTHINDQPVNDEpHVPFGGEKNSGLGRFNGEWALEEFTTDKW 460
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
67-476 |
2.17e-133 |
|
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: 393.51 E-value: 2.17e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 67 LTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEA-EGEIAYAASFIEWFAEQGKRANGEIIPSpGADKRLMVIRQ 145
Cdd:cd07112 45 LSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAlAVDVPSAANTFRWYAEAIDKVYGEVAPT-GPDALALITRE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 146 GVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDER 225
Cdd:cd07112 124 PLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 226 VRKLSFTGSTEVGRVLMRQCAES-IKKLSLELGGNAPFIVFDDA-DIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYD 303
Cdd:cd07112 204 VDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 304 QFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPL--GGNFFTPTVIGDVQPGSL 381
Cdd:cd07112 284 EFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRVLTetGGFFVEPTVFDGVTPDMR 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 382 LLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINT---GLISnevAPFGGVKQS 458
Cdd:cd07112 364 IAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCfdeGDIT---TPFGGFKQS 440
|
410
....*....|....*...
gi 1513169189 459 GLGREGSEHGIEDYLEMK 476
Cdd:cd07112 441 GNGRDKSLHALDKYTELK 458
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
12-476 |
4.84e-133 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 393.12 E-value: 4.84e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 12 QALIAGSWrDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALA 91
Cdd:PRK13473 4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 92 QIMTAEQGKPL-AEAEGEIAYAASFIEWFAE-----QGKRAnGEIIPspgaDKRLMVIRQGVGVCAAITPWNFPAAMITR 165
Cdd:PRK13473 83 RLESLNCGKPLhLALNDEIPAIVDVFRFFAGaarclEGKAA-GEYLE----GHTSMIRRDPVGVVASIAPWNYPLMMAAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 166 KAGPALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQC 245
Cdd:PRK13473 158 KLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 246 AESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESD 325
Cdd:PRK13473 237 ADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 326 VQIGPLINADAGRKVQSLLDDAMSRG-ATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAI 404
Cdd:PRK13473 317 TELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513169189 405 EQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINT-GLISNEvAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:PRK13473 397 RWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNThFMLVSE-MPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
30-478 |
7.05e-133 |
|
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: 392.10 E-value: 7.05e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 30 VSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 110 AYAASFIEWFA---EQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETP 186
Cdd:cd07110 81 DDVAGCFEYYAdlaEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 187 FTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFD 266
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 267 DADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDD 346
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 347 AMSRGATLLTGGK--AHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAA 424
Cdd:cd07110 321 GKEEGARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1513169189 425 RIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
28-478 |
1.57e-132 |
|
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: 390.84 E-value: 1.57e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 28 LAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEG 107
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 108 EIAYAASFIEWFAEQGKRANGEIIP---SPGADKRL-MVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPAN 183
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldiSARGEGRQgLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 184 ETPFTALAMAELANQAGIPQGVINVVTgQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAEsiKKLSLELGGNAPFI 263
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLP-CSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 264 VFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSL 343
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 344 LDDAMSRGATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDA 423
Cdd:cd07147 318 VNEAVDAGAKLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513169189 424 ARIWRVSEQLEYGmvgintGLISNEV-------APFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07147 395 EKALRAWDELEVG------GVVINDVptfrvdhMPYGGVKDSGIGREGVRYAIEEMTEPRLL 450
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
28-479 |
2.89e-132 |
|
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: 390.26 E-value: 2.89e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 28 LAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEG 107
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 108 EIAYAASFIEWFAEQGKRANGEIIPSP---GADKRL-MVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPAN 183
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDatqGSDNRLaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 184 ETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAesIKKLSLELGGNAPFI 263
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 264 VFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSL 343
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 344 LDDAMSRGATLLTGGKahpLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDA 423
Cdd:cd07094 319 VEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1513169189 424 ARIWRVSEQLEYGMVGINTG-LISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLC 479
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSsAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVV 452
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
67-476 |
1.97e-131 |
|
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: 388.23 E-value: 1.97e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 67 LTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQG 146
Cdd:cd07118 40 MSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 147 VGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERV 226
Cdd:cd07118 120 IGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 227 RKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFC 306
Cdd:cd07118 200 DMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 307 DKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLG-GNFFTPTVIGDVQPGSLLLQE 385
Cdd:cd07118 280 AAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAaGLFYQPTIFTDVTPDMAIARE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 386 EIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGS 465
Cdd:cd07118 360 EIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELG 439
|
410
....*....|.
gi 1513169189 466 EHGIEDYLEMK 476
Cdd:cd07118 440 RYGVEEYTELK 450
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
32-478 |
1.11e-130 |
|
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: 386.19 E-value: 1.11e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 32 NPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAY 111
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 112 AASFIEWFAEQGKR--ANGEIIPSPG-ADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFT 188
Cdd:cd07099 82 ALEAIDWAARNAPRvlAPRKVPTGLLmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 189 ALAMAELANQAGIPQGVINVVTGqSREIGAVFTgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDA 268
Cdd:cd07099 162 GELLAEAWAAAGPPQGVLQVVTG-DGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 269 DIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAM 348
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 349 SRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWR 428
Cdd:cd07099 320 AKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1513169189 429 VSEQLEYGMVGIN----TGLISNevAPFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07099 400 IARRLEAGAVSINdvllTAGIPA--LPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
14-476 |
2.90e-129 |
|
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: 383.14 E-value: 2.90e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 14 LIAGSWRDAADGttLAVSNPS-TGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQ 92
Cdd:cd07097 4 YIDGEWVAGGDG--EENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 93 IMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 173 AGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKL 252
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 253 SLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLI 332
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 333 NADAGRKVQSLLDDAMSRGATLLTGGKAHPLG--GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNT 410
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDT 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513169189 411 IYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEV-APFGGVKQSGLG-REGSEHGIEDYLEMK 476
Cdd:cd07097 402 EFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYhVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
32-482 |
3.47e-129 |
|
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: 382.56 E-value: 3.47e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 32 NPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEG-EIA 110
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 111 YAASFIEWFAEQGKRANGEIIPSPGaDKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTAL 190
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRG-PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 191 AMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADI 270
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 271 DKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSR 350
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 351 GATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVS 430
Cdd:cd07115 322 GARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1513169189 431 EQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLCQGL 482
Cdd:cd07115 402 AALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
30-476 |
5.40e-128 |
|
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: 379.27 E-value: 5.40e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 30 VSNPSTGATLGQIPNMGRA-EAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGE 108
Cdd:cd07109 1 VFDPSTGEVFARIARGGAAdVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 109 IAYAASFIEWFAEQGKRANGEIIPsPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFT 188
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 189 ALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDA 268
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 269 DIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSEsDVQIGPLINADAGRKVQSLLDDAM 348
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 349 SRGATLLTGGKA---HPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAAR 425
Cdd:cd07109 319 ARGARIVAGGRIaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1513169189 426 IWRVSEQLEYGMVGINTGLISNEVA-PFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07109 399 ALRVARRLRAGQVFVNNYGAGGGIElPFGGVKKSGHGREKGLEALYNYTQTK 450
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
14-466 |
1.32e-127 |
|
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: 379.22 E-value: 1.32e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 14 LIAGSWRDAAdGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQI 93
Cdd:cd07086 2 VIGGEWVGSG-GETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 94 MTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAA 173
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 174 GCTMVIKPANETPFTALAMAELANQA----GIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESI 249
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 250 KKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIG 329
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 330 PLINADAGRKVQSLLDDAMSRGATLLTGGKA--HPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQA 407
Cdd:cd07086 320 PLINQAAVEKYLNAIEIAKSQGGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAIN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513169189 408 NNTIYGLASYFYSNDAARI--WRVSEQLEYGMVGINTGLISNEV-APFGGVKQSGLGRE-GSE 466
Cdd:cd07086 400 NDVPQGLSSSIFTEDLREAfrWLGPKGSDCGIVNVNIPTSGAEIgGAFGGEKETGGGREsGSD 462
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
30-477 |
6.56e-127 |
|
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: 376.28 E-value: 6.56e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 30 VSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAE-AEGE 108
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 109 IAYAASFIEWFA----EQGKRANGEIIPSPGAdkrlMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANE 184
Cdd:cd07092 81 LPGAVDNFRFFAgaarTLEGPAAGEYLPGHTS----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 185 TPFTALAMAELAnQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIV 264
Cdd:cd07092 157 TPLTTLLLAELA-AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 265 FDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLL 344
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 345 DDAmSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAA 424
Cdd:cd07092 316 ERA-PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1513169189 425 RIWRVSEQLEYGMVGINT-GLISNEvAPFGGVKQSGLGREGSEHGIEDYLEMKY 477
Cdd:cd07092 395 RAMRLSARLDFGTVWVNThIPLAAE-MPHGGFKQSGYGKDLSIYALEDYTRIKH 447
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
10-480 |
8.80e-127 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 377.92 E-value: 8.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 10 RQQALIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRA-----LTAAQRAALLKNWHRLIL 84
Cdd:PLN02467 7 RRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRNKGkdwarTTGAVRAKYLRAIAAKIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 85 ENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQG---KRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAA 161
Cdd:PLN02467 87 ERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAealDAKQKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 162 MITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVL 241
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 242 MRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDG 321
Cdd:PLN02467 247 MTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 322 SESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKA-HPLGGNFFT-PTVIGDVQPGSLLLQEEIFGPVAALVKFED 399
Cdd:PLN02467 327 LEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRpEHLKKGFFIePTIITDVTTSMQIWREEVFGPVLCVKTFST 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 400 EQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLC 479
Cdd:PLN02467 407 EDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQVT 486
|
.
gi 1513169189 480 Q 480
Cdd:PLN02467 487 K 487
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
15-476 |
1.39e-126 |
|
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: 376.75 E-value: 1.39e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAA-LPAWRALTAAQRAALLKNWHRLILENKTALAQI 93
Cdd:cd07144 12 INNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 94 MTAEQGKPL-AEAEGEIAYAASFIEWFAEQGKRANGEIIPSpGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALA 172
Cdd:cd07144 92 EALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPT-SPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 173 AGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKL 252
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 253 SLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVA-ALKVGDGSESDVQIGPL 331
Cdd:cd07144 251 TLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 332 INADAGRKVQSLLDDAMSRGATLLTGGKAHPLG---GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQAN 408
Cdd:cd07144 331 VSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKAN 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513169189 409 NTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07144 411 DTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
3-476 |
1.28e-123 |
|
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: 368.98 E-value: 1.28e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 3 VFHSNLFrqqalIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWR---ALTAAQRAALLKNW 79
Cdd:cd07141 4 IKYTKIF-----INNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSpwrTMDASERGRLLNKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 80 HRLILENKTALAQIMTAEQGKPLAEA-EGEIAYAASFIEWFAEQGKRANGEIIPSPGaDKRLMVIRQGVGVCAAITPWNF 158
Cdd:cd07141 79 ADLIERDRAYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPMDG-DFFTYTRHEPVGVCGQIIPWNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 159 PAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVG 238
Cdd:cd07141 158 PLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 239 RVLMRQCAES-IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALK 317
Cdd:cd07141 238 KLIQQAAGKSnLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 318 VGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKF 397
Cdd:cd07141 318 VGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKF 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513169189 398 EDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07141 398 KTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVK 476
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
32-480 |
8.79e-123 |
|
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: 366.28 E-value: 8.79e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 32 NPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQ-RAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIA 110
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDPRlRARVLLELADAFEANAERLARLLALENGKILGEARFEIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 111 YAASFIEWFAEQGKRANGEII-PSPGADKrlMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTA 189
Cdd:cd07120 83 GAISELRYYAGLARTEAGRMIePEPGSFS--LVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 190 LAMAE-LANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDA 268
Cdd:cd07120 161 AAIIRiLAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 269 DIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAM 348
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 349 SRGATLLTGGKAHPLG---GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAAR 425
Cdd:cd07120 321 AAGAEVVLRGGPVTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLAR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1513169189 426 IWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLCQ 480
Cdd:cd07120 401 AMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
15-476 |
9.19e-123 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 366.44 E-value: 9.19e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIM 94
Cdd:TIGR01804 2 IDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 95 TAEQGKPLAEAE-GEIAYAASFIEWFAEQGKRANGEIIPSPGADKrLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAA 173
Cdd:TIGR01804 82 TLDTGKTLQETIvADMDSGADVFEFFAGLAPALNGEIIPLGGPSF-AYTIREPLGVCVGIGAWNYPLQIASWKIAPALAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 174 GCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLS 253
Cdd:TIGR01804 161 GNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 254 LELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLIN 333
Cdd:TIGR01804 241 MELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLIS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 334 ADAGRKVQSLLDDAMSRGATLLTGGKAHPL----GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANN 409
Cdd:TIGR01804 321 AAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARAND 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513169189 410 TIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:TIGR01804 401 TEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
10-476 |
1.50e-121 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 364.20 E-value: 1.50e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 10 RQQALIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTA 89
Cdd:PRK13252 6 LQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 90 LAQIMTAEQGKPLAEAE-GEIAYAASFIEWFAEQGKRANGEIIPSPGADkRLMVIRQGVGVCAAITPWNFPAAMITRKAG 168
Cdd:PRK13252 86 LAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGS-FVYTRREPLGVCAGIGAWNYPIQIACWKSA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 169 PALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES 248
Cdd:PRK13252 165 PALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQG-DGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 249 IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQtcVCVN--RFYIHRAVYDQFCDKFVARVAALKVGDGSESDV 326
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQ--VCTNgtRVFVQKSIKAAFEARLLERVERIRIGDPMDPAT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 327 QIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLG----GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQE 402
Cdd:PRK13252 322 NFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGgfanGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513169189 403 AIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:PRK13252 402 VIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIK 475
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
30-479 |
1.85e-121 |
|
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: 362.78 E-value: 1.85e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 30 VSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 110 AYAASFIEWFAEQGKRANGEIIPSPG---ADKRlmviRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETP 186
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPGgsfAYTR----REPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 187 FTALAMAELANQAGIPQGVINVVTGQSrEIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFD 266
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 267 DADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDD 346
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 347 AMSRGATLLTGG-KAHPL----GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSN 421
Cdd:cd07090 316 AKQEGAKVLCGGeRVVPEdgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1513169189 422 DAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLC 479
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
15-476 |
7.36e-121 |
|
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: 362.23 E-value: 7.36e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRAL--TAAQRAALLKNWHRLILENKTALAQ 92
Cdd:cd07143 11 INGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLkvSGSKRGRCLSKLADLMERNLDYLAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 93 IMTAEQGKP-LAEAEGEIAYAASFIEWFAEQGKRANGEIIPSpgADKRLMVIR-QGVGVCAAITPWNFPAAMITRKAGPA 170
Cdd:cd07143 91 IEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIET--DIKKLTYTRhEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 171 LAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES-I 249
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSnL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 250 KKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIG 329
Cdd:cd07143 249 KKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 330 PLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANN 409
Cdd:cd07143 329 PQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRAND 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513169189 410 TIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07143 409 STYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIK 475
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
15-479 |
1.31e-120 |
|
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: 361.37 E-value: 1.31e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAA-LPAWRALTAAQRAALLKNWHRLILENKTALAQI 93
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 94 MTAEQGKPLAEAEG-EIAYAASFIEWFAEQGKRANGEI----IPSPGADK-RLMVIRQGVGVCAAITPWNFPAAMITRKA 167
Cdd:cd07113 84 ETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETlapsIPSMQGERyTAFTRREPVGVVAGIVPWNFSVMIAVWKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 168 GPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAE 247
Cdd:cd07113 164 GAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNG-KGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 248 SIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQ 327
Cdd:cd07113 243 DLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 328 IGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQA 407
Cdd:cd07113 323 FGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLI 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513169189 408 NNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYLC 479
Cdd:cd07113 403 NDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
21-474 |
1.53e-120 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 362.66 E-value: 1.53e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 21 DAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGK 100
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 101 PLAEAEGEIAYAASFIEWFAEQG------KRANGEIipsPGAdKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAG 174
Cdd:PRK09407 107 ARRHAFEEVLDVALTARYYARRApkllapRRRAGAL---PVL-TKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 175 CTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTgdERVRKLSFTGSTEVGRVLMRQCAESIKKLSL 254
Cdd:PRK09407 183 NAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRLIGFSL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 255 ELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINA 334
Cdd:PRK09407 261 ELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 335 DAGRKVQSLLDDAMSRGATLLTGGKAHP-LGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYG 413
Cdd:PRK09407 341 AQLETVSAHVDDAVAKGATVLAGGKARPdLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYG 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513169189 414 LASYFYSNDAARIWRVSEQLEYGMVGINTGLIS---NEVAPFGGVKQSGLGREGSEHGIEDYLE 474
Cdd:PRK09407 421 LNASVWTGDTARGRAIAARIRAGTVNVNEGYAAawgSVDAPMGGMKDSGLGRRHGAEGLLKYTE 484
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
67-476 |
4.86e-120 |
|
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: 358.04 E-value: 4.86e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 67 LTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQG 146
Cdd:cd07105 19 TPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIPSDKPGTLAMVVKEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 147 VGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTgQSREIGAVFT----G 222
Cdd:cd07105 99 VGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVT-HSPEDAPEVVealiA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 223 DERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVY 302
Cdd:cd07105 178 HPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 303 DQFCDKFVARVAALKVGdgsesDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKA-HPLGGNFFTPTVIGDVQPGSL 381
Cdd:cd07105 258 DEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLAdESPSGTSMPPTILDNVTPDMD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 382 LLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNE-VAPFGGVKQSGL 460
Cdd:cd07105 333 IYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDEpTLPHGGVKSSGY 412
|
410
....*....|....*.
gi 1513169189 461 GREGSEHGIEDYLEMK 476
Cdd:cd07105 413 GRFNGKWGIDEFTETK 428
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
33-474 |
1.02e-119 |
|
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: 358.16 E-value: 1.02e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 33 PSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYA 112
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 113 ASFIEWFAEQG------KRANGEIipsPGAdKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETP 186
Cdd:cd07101 83 AIVARYYARRAerllkpRRRRGAI---PVL-TRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 187 FTALAMAELANQAGIPQGVINVVTGQSREIGAVFTgdERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFD 266
Cdd:cd07101 159 LTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 267 DADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDD 346
Cdd:cd07101 237 DADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 347 AMSRGATLLTGGKAHP-LGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAAR 425
Cdd:cd07101 317 AVAKGATVLAGGRARPdLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1513169189 426 IWRVSEQLEYGMVGINTGLIS---NEVAPFGGVKQSGLGREGSEHGIEDYLE 474
Cdd:cd07101 397 GRRIAARLRAGTVNVNEGYAAawaSIDAPMGGMKDSGLGRRHGAEGLLKYTE 448
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
12-476 |
8.49e-119 |
|
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: 356.80 E-value: 8.49e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 12 QALIAGSWRDAADGTTLAVSNPSTGATLGQI-----PNMGRAEAQQAVDAAAAALPAwraLTAAQRAALLKNWHRLILEN 86
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVaegdaEDVDRAVKAARKAFDEGPWPR---MTGYERSRILLRFADLLEKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 87 KTALAQIMTAEQGKPLAEAE-GEIAYAASFIEWFAEQGKRANGEIIPSPGAdKRLMVIRQGVGVCAAITPWNFPAAMITR 165
Cdd:cd07142 82 ADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGP-HHVYTLHEPIGVVGQIIPWNFPLLMFAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 166 KAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQC 245
Cdd:cd07142 161 KVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 246 AES-IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSES 324
Cdd:cd07142 241 AKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 325 DVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAI 404
Cdd:cd07142 321 GVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513169189 405 EQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
28-476 |
1.65e-118 |
|
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: 355.13 E-value: 1.65e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 28 LAVSNPSTGATLGQIPnmgRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEG 107
Cdd:cd07146 1 LEVRNPYTGEVVGTVP---AGTEEALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 108 EIAYAASFIEWFAEQGKRANGEIIP---SPGADKRLMV-IRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPAN 183
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFScdlTANGKARKIFtLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 184 ETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLmrQCAESIKKLSLELGGNAPFI 263
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 264 VFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSL 343
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 344 LDDAMSRGATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDA 423
Cdd:cd07146 316 VEEAIAQGARVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDL 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1513169189 424 ARIWRVSEQLEYGMVGINTGL-ISNEVAPFGGVKQSGLG-REGSEHGIEDYLEMK 476
Cdd:cd07146 393 DTIKRLVERLDVGTVNVNEVPgFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
83-478 |
6.68e-118 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 352.12 E-value: 6.68e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 83 ILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAM 162
Cdd:PRK10090 8 IRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 163 ITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLM 242
Cdd:PRK10090 88 IARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 243 RQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGD-G 321
Cdd:PRK10090 168 AAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNpA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 322 SESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQ 401
Cdd:PRK10090 248 ERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 402 EAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTgliSNEVAPFG---GVKQSGLGREGSEHGIEDYLEMK-- 476
Cdd:PRK10090 328 EAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR---ENFEAMQGfhaGWRKSGIGGADGKHGLHEYLQTQvv 404
|
..
gi 1513169189 477 YL 478
Cdd:PRK10090 405 YL 406
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
30-476 |
2.50e-117 |
|
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: 352.05 E-value: 2.50e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 30 VSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPL-AEAEGE 108
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 109 IAYAASFIEWFAEQGKRANGEIIPsPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFT 188
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 189 ALAMAELANQAgIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDA 268
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 269 DIDKAVEGALIA-KFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDA 347
Cdd:cd07108 239 DLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 348 MSR-GATLLTGGKAHPLG----GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSND 422
Cdd:cd07108 319 LSTsGATVLRGGPLPGEGpladGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1513169189 423 AARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGS-EHGIEDYLEMK 476
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKK 453
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
14-478 |
4.00e-117 |
|
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: 352.42 E-value: 4.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 14 LIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQI 93
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 94 MTAEQGKPLAEAEG-EIAYAASFIEWFAeqgkranGEIIPSPGA----DKRLM--VIRQGVGVCAAITPWNFPAAMITRK 166
Cdd:cd07559 84 ETLDNGKPIRETLAaDIPLAIDHFRYFA-------GVIRAQEGSlseiDEDTLsyHFHEPLGVVGQIIPWNFPLLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 167 AGPALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCA 246
Cdd:cd07559 157 LAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 247 ESIKKLSLELGGNAPFIVFDDA-----DIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDG 321
Cdd:cd07559 236 ENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 322 SESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLG----GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKF 397
Cdd:cd07559 316 LDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 398 EDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKY 477
Cdd:cd07559 396 KDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKN 475
|
.
gi 1513169189 478 L 478
Cdd:cd07559 476 I 476
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
12-475 |
8.99e-113 |
|
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: 341.09 E-value: 8.99e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 12 QALIAGSWRDAaDGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAA-AAALPAWRALTAAQRAALLKNWHRLILENKTAL 90
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAyDAGRGWWPTMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 91 AQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIP---SPGADKRLMVIRQG-VGVCAAITPWNFPAAMITRK 166
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPgdwFPGTKGKIAQVRREpLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 167 AGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQca 246
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 247 ESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDV 326
Cdd:cd07082 240 HPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 327 QIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAhpLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQ 406
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513169189 407 ANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINT----GLisnEVAPFGGVKQSGLGREgsehGIEDYLEM 475
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINSkcqrGP---DHFPFLGRKDSGIGTQ----GIGDALRS 463
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
15-476 |
2.53e-112 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 341.03 E-value: 2.53e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWR--ALTAAQRAALLKNWHRLILENKTALAQ 92
Cdd:PLN02766 25 INGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPwpRMSGFERGRIMMKFADLIEEHIEELAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 93 IMTAEQGKPLAEAEG-EIAYAASFIEWFAEQGKRANGEIIPSPGADKRlMVIRQGVGVCAAITPWNFPAAMITRKAGPAL 171
Cdd:PLN02766 105 LDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQG-YTLKEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 172 AAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES-IK 250
Cdd:PLN02766 184 AAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSnLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 251 KLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGP 330
Cdd:PLN02766 264 QVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 331 LINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNT 410
Cdd:PLN02766 344 QVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNT 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1513169189 411 IYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:PLN02766 424 KYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVK 489
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
14-476 |
5.47e-111 |
|
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: 336.73 E-value: 5.47e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 14 LIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQI 93
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 94 MTAEQGKPLAEAEG-EIAYAASFIEWFAeqgkranGEIIPSPGA----DKRLM--VIRQGVGVCAAITPWNFPAAMITRK 166
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFA-------GVIRAEEGSanmiDEDTLsiVLREPIGVVGQIIPWNFPFLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 167 AGPALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCA 246
Cdd:cd07117 157 LAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 247 ESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDV 326
Cdd:cd07117 236 KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 327 QIGPLINADAGRKVQSLLDDAMSRGATLLTGGK----AHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQE 402
Cdd:cd07117 316 QMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513169189 403 AIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07117 396 VIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMK 469
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
30-476 |
6.70e-109 |
|
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: 330.49 E-value: 6.70e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 30 VSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEI 109
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 110 AYAASFIEWFAEQGKRANGEIIPSPGADkRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTA 189
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRN-LHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 190 LAMAELANQAgIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDAD 269
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 270 IDKAVEGALIA-KFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAM 348
Cdd:cd07107 239 PEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 349 SRGATLLTGGKaHPLG-----GNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDA 423
Cdd:cd07107 319 REGARLVTGGG-RPEGpalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1513169189 424 ARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEK 450
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
15-478 |
2.93e-107 |
|
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: 327.05 E-value: 2.93e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIM 94
Cdd:cd07111 26 INGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 95 TAEQGKPLAEA-EGEIAYAASFIEWFAEQGKRANGEIipsPGadkrlmviRQGVGVCAAITPWNFPAAMITRKAGPALAA 173
Cdd:cd07111 106 SLDNGKPIRESrDCDIPLVARHFYHHAGWAQLLDTEL---AG--------WKPVGVVGQIVPWNFPLLMLAWKICPALAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 174 GCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSrEIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLS 253
Cdd:cd07111 175 GNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 254 LELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLIN 333
Cdd:cd07111 254 LELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 334 ADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYG 413
Cdd:cd07111 334 PAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYG 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1513169189 414 LASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07111 414 LAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWE 478
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
28-476 |
5.02e-106 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 323.23 E-value: 5.02e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 28 LAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEG 107
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 108 EIAYAASFIEWFAEQGKrangEIIPSPGAD------KRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKP 181
Cdd:PRK09406 83 EALKCAKGFRYYAEHAE----ALLADEPADaaavgaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 182 ANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAP 261
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILR-DPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 262 FIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQ 341
Cdd:PRK09406 238 FIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 342 SLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSN 421
Cdd:PRK09406 318 KQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1513169189 422 DAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:PRK09406 398 DEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIK 452
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
14-473 |
7.12e-105 |
|
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: 321.86 E-value: 7.12e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 14 LIAGSWRDAADgtTLAVSNPS-TGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQ 92
Cdd:cd07124 36 VIGGKEVRTEE--KIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 93 IMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPS-PGADKRLMVIRQGVGVcaAITPWNFPAAMITRKAGPAL 171
Cdd:cd07124 114 WMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMvPGEDNRYVYRPLGVGA--VISPWNFPLAILAGMTTAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 172 AAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES--- 248
Cdd:cd07124 192 VTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 249 ---IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESD 325
Cdd:cd07124 272 qkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 326 VQIGPLINADAGRKVQSLLDDAMSRGaTLLTGGK--AHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEA 403
Cdd:cd07124 352 VYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEvlELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEA 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513169189 404 IEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN---TGLISnEVAPFGGVKQSGLgreGSEHGIEDYL 473
Cdd:cd07124 431 LEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkiTGALV-GRQPFGGFKMSGT---GSKAGGPDYL 499
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
12-476 |
6.63e-104 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 320.60 E-value: 6.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 12 QALIAGSWRDAADGTTLAVSNPSTGATL-----GQIPNMGRAEAQQAVDAAAAALPAwraLTAAQRAALLKNWHRLILEN 86
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIahvaeGDAEDVNRAVAAARKAFDEGPWPK---MTAYERSRILLRFADLLEKH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 87 KTALAQIMTAEQGKPLAEAEG-EIAYAASFIEWFAEQGKRANGEIIPSPGaDKRLMVIRQGVGVCAAITPWNFPAAMITR 165
Cdd:PLN02466 136 NDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADG-PHHVQTLHEPIGVAGQIIPWNFPLLMFAW 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 166 KAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQC 245
Cdd:PLN02466 215 KVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 246 AES-IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSES 324
Cdd:PLN02466 295 AKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 325 DVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAI 404
Cdd:PLN02466 375 GVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVI 454
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513169189 405 EQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:PLN02466 455 RRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
67-474 |
2.46e-103 |
|
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: 315.77 E-value: 2.46e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 67 LTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSpgADKRL-MVIRQ 145
Cdd:cd07152 32 TPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQGEILPS--APGRLsLARRV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 146 GVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTA-LAMAELANQAGIPQGVINVVTGQSrEIGAVFTGDE 224
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPGGA-DAGEALVEDP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 225 RVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQ 304
Cdd:cd07152 189 NVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 305 FCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQ 384
Cdd:cd07152 269 YTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTYD---GLFYRPTVLSGVKPGMPAFD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 385 EEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNE-VAPFGGVKQSGLG-R 462
Cdd:cd07152 346 EEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDEpHNPFGGMGASGNGsR 425
|
410
....*....|..
gi 1513169189 463 EGSEHGIEDYLE 474
Cdd:cd07152 426 FGGPANWEEFTQ 437
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
12-476 |
1.09e-102 |
|
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: 315.59 E-value: 1.09e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 12 QALIAGSWRDAADGTTLAVSNPSTGATLGQIP--NMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTA 89
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSlaTVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 90 LAQIMTAEQGKPLAEA-EGEIAYAASFIEWFAEQGKRANGEIIPSPGA--DKRL-MVIRQGVGVCAAITPWNFPAAMITR 165
Cdd:cd07140 87 LATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPINQArpNRNLtLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 166 KAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQC 245
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 246 AES-IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSES 324
Cdd:cd07140 247 AVSnLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 325 DVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDE--QE 402
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDG 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513169189 403 AIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
70-470 |
2.53e-98 |
|
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: 303.40 E-value: 2.53e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 70 AQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGV 149
Cdd:cd07102 40 EERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 150 CAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGqSREIGAVFTGDERVRKL 229
Cdd:cd07102 120 VLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHL-SHETSAALIADPRIDHV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 230 SFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKF 309
Cdd:cd07102 199 SFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 310 VARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPL---GGNFFTPTVIGDVQPGSLLLQEE 386
Cdd:cd07102 279 VAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 387 IFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSE 466
Cdd:cd07102 359 TFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSR 438
|
....
gi 1513169189 467 HGIE 470
Cdd:cd07102 439 LGYD 442
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
15-476 |
7.96e-95 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 295.65 E-value: 7.96e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTA--AQRAALLKNWHRLILENKTALAQ 92
Cdd:PRK09847 24 INGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSspAKRKAVLNKLADLMEAHAEELAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 93 IMTAEQGKPLAEA-EGEIAYAASFIEWFAEQGKRANGEIIPSpGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPAL 171
Cdd:PRK09847 104 LETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATT-SSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 172 AAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES-IK 250
Cdd:PRK09847 183 AAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSnMK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 251 KLSLELGGNAPFIVFDDA-DIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIG 329
Cdd:PRK09847 263 RVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 330 PLINADAGRKVQSLLDDAMSRGaTLLTGGKAHPLGGnFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANN 409
Cdd:PRK09847 343 TLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLAND 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513169189 410 TIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:PRK09847 421 SQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
22-476 |
1.38e-94 |
|
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: 294.37 E-value: 1.38e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 22 AADGTTLAVSNPSTGATLGQIPN-----MGRAEAQQAVDAAAAALPAWRALtaaqRAALLKNWHRLILENKTALAQIMTA 96
Cdd:TIGR04284 11 AGSAGTFPTVNPATEEVLGVAADataadMDAAIAAARRAFDETDWSRDTAL----RVRCLRQLRDALRAHVEELRELTIA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 97 EQGKPL-----AEAEGEI---AYAASFIEWFAeqGKRANGEIIPSpGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAG 168
Cdd:TIGR04284 87 EVGAPRmltagAQLEGPVddlGFAADLAESYA--WTTDLGVASPM-GIPTRRTLRREAVGVVGAITPWNFPHQINLAKLG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 169 PALAAGCTMVIKPANETPFTALAMAEL-ANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAE 247
Cdd:TIGR04284 164 PALAAGNTVVLKPAPDTPWCAAVLGELiAEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMADAAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 248 SIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQ 327
Cdd:TIGR04284 244 TLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPGTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 328 IGPLINADAGRKVQSLLDDAMSRGATLLTGG--KAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIE 405
Cdd:TIGR04284 324 CGPVISARQRDRVQSYLDLAVAEGGRFACGGgrPADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVR 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1513169189 406 QANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMK 476
Cdd:TIGR04284 404 IANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETK 474
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
69-473 |
6.91e-94 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 293.76 E-value: 6.91e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 69 AAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQG-KRANGE-IIPSPGADKRLMVIRQG 146
Cdd:PRK03137 94 PEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMlKLADGKpVESRPGEHNRYFYIPLG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 147 VGVcaAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERV 226
Cdd:PRK03137 174 VGV--VISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 227 RKLSFTGSTEVGRVLMRQCAES------IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRA 300
Cdd:PRK03137 252 RFITFTGSREVGLRIYERAAKVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHED 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 301 VYDQFCDKFVARVAALKVGDGSESDVqIGPLINADAGRKVQSLLDDAMSRGaTLLTGGKAHPLGGNFFTPTVIGDVQPGS 380
Cdd:PRK03137 332 VYDEVLEKVVELTKELTVGNPEDNAY-MGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKA 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 381 LLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN---TGLISNeVAPFGGVKQ 457
Cdd:PRK03137 410 RIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgcTGAIVG-YHPFGGFNM 488
|
410
....*....|....*.
gi 1513169189 458 SGlgrEGSEHGIEDYL 473
Cdd:PRK03137 489 SG---TDSKAGGPDYL 501
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
32-469 |
3.42e-93 |
|
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: 290.36 E-value: 3.42e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 32 NPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAE-GEIA 110
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 111 YAASFIEWFAEQGKRAngeIIPSPGADKRLMVIRQG------VGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANE 184
Cdd:cd07098 82 VTCEKIRWTLKHGEKA---LRPESRPGGLLMFYKRArveyepLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 185 T-----PFTALAMAELANqAGIPQGVINVVTGQSrEIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGN 259
Cdd:cd07098 159 VawssgFFLSIIRECLAA-CGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 260 APFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRK 339
Cdd:cd07098 237 DPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 340 VQSLLDDAMSRGATLLTGGKAHPL----GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLA 415
Cdd:cd07098 317 LEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1513169189 416 SYFYSNDAARIWRVSEQLEYGMVGINTGLIS--NEVAPFGGVKQSGLGREGSEHGI 469
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGL 452
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
71-473 |
2.05e-88 |
|
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: 279.44 E-value: 2.05e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 71 QRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKR--ANGEIIPSPGADKRLMVIRQGVG 148
Cdd:TIGR01237 92 ERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIElaKGKPVNSREGETNQYVYTPTGVT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 149 VcaAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRK 228
Cdd:TIGR01237 172 V--VISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 229 LSFTGSTEVGRVLMRQCA------ESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVY 302
Cdd:TIGR01237 250 ITFTGSREVGTRIFERAAkvqpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVY 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 303 DQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGaTLLTGGKAHPLGGNFFTPTVIGDVQPGSLL 382
Cdd:TIGR01237 330 DEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARL 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 383 LQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN---TGLISNeVAPFGGVKQSG 459
Cdd:TIGR01237 409 AQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrniTGAIVG-YQPFGGFKMSG 487
|
410
....*....|....
gi 1513169189 460 LgreGSEHGIEDYL 473
Cdd:TIGR01237 488 T---DSKAGGPDYL 498
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
15-478 |
7.57e-88 |
|
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: 277.03 E-value: 7.57e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIM 94
Cdd:cd07116 5 IGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 95 TAEQGKPLAEAEG-EIAYAASFIEWFAeQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAA 173
Cdd:cd07116 85 TWDNGKPVRETLAaDIPLAIDHFRYFA-GCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 174 GCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKKLS 253
Cdd:cd07116 164 GNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 254 LELGGNAPFIVF------DDADIDKAVEGALIAKFrNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQ 327
Cdd:cd07116 243 LELGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 328 IGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGN----FFTPTVIGDVQPGSlLLQEEIFGPVAALVKFEDEQEA 403
Cdd:cd07116 322 IGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKGGNKMR-IFQEEIFGPVLAVTTFKDEEEA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1513169189 404 IEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDYLEMKYL 478
Cdd:cd07116 401 LEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 475
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
12-461 |
8.43e-88 |
|
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: 276.71 E-value: 8.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 12 QALIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALA 91
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 92 QIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPaAMITR-KAGPA 170
Cdd:cd07085 82 RLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFP-AMIPLwMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 171 LAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTgDERVRKLSFTGSTEVGRVLMRQCAESIK 250
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEYIYERAAANGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 251 KLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTC------VCVNrfyihrAVYDQFCDKFVARVAALKVGDGSES 324
Cdd:cd07085 240 RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCmalsvaVAVG------DEADEWIPKLVERAKKLKVGAGDDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 325 DVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPL----GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDE 400
Cdd:cd07085 314 GADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVpgyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1513169189 401 QEAIEQANNTIYGLASYFYSND--AARiwRVSEQLEYGMVGINTGlISNEVA--PFGGVKQSGLG 461
Cdd:cd07085 394 DEAIAIINANPYGNGAAIFTRSgaAAR--KFQREVDAGMVGINVP-IPVPLAffSFGGWKGSFFG 455
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
27-472 |
2.14e-87 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 275.59 E-value: 2.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 27 TLAVS-NPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEA 105
Cdd:PRK13968 7 THAISvNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 106 EGEIAYAASFIEWFAEQGKrANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANET 185
Cdd:PRK13968 87 RAEVAKSANLCDWYAEHGP-AMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 186 PFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVF 265
Cdd:PRK13968 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIN-DSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 266 DDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLD 345
Cdd:PRK13968 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 346 DAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAAR 425
Cdd:PRK13968 325 ATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQ 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1513169189 426 IWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHGIEDY 472
Cdd:PRK13968 405 ARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
70-470 |
1.05e-76 |
|
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: 246.28 E-value: 1.05e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 70 AQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAE--------GEIAYAASFIEWFAEQgKRANGEIIPSPGadkRLM 141
Cdd:cd07087 20 EWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlteiavvlGEIDHALKHLKKWMKP-RRVSVPLLLQPA---KAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 142 VIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFt 221
Cdd:cd07087 96 VIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVATALL- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 222 gDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAV 301
Cdd:cd07087 174 -AEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 302 YDQFCDKFVARVAALKVGDGSESDvQIGPLINADAGRKVQSLLDDamsrgATLLTGGKAHPlGGNFFTPTVIGDVQPGSL 381
Cdd:cd07087 253 KDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLLDD-----GKVVIGGQVDK-EERYIAPTILDDVSPDSP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 382 LLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLI--SNEVAPFGGVKQSG 459
Cdd:cd07087 326 LMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLhaAIPNLPFGGVGNSG 405
|
410
....*....|.
gi 1513169189 460 LGREGSEHGIE 470
Cdd:cd07087 406 MGAYHGKAGFD 416
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
70-472 |
4.01e-76 |
|
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: 245.26 E-value: 4.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 70 AQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEiIPSPGADKRLMVIRQGVGV 149
Cdd:cd07095 22 EERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTGE-RATPMAQGRAVLRHRPHGV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 150 CAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGqSREIGAVFTGDERVRKL 229
Cdd:cd07095 101 MAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG-GRETGEALAAHEGIDGL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 230 SFTGSTEVGRVLMRQCAESIKK-LSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHR-AVYDQFCD 307
Cdd:cd07095 180 LFTGSAATGLLLHRQFAGRPGKiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDgAVGDAFLE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 308 KFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIgDVQPGSLLLQEEI 387
Cdd:cd07095 260 RLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLSPGII-DVTDAADVPDEEI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 388 FGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN---TGLISNevAPFGGVKQSGLGREg 464
Cdd:cd07095 339 FGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNrptTGASST--APFGGVGLSGNHRP- 415
|
....*...
gi 1513169189 465 SEHGIEDY 472
Cdd:cd07095 416 SAYYAADY 423
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
4-461 |
2.00e-75 |
|
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: 245.95 E-value: 2.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 4 FHSNLFRQQALIAGswRDAADGTTLAVSNPS-TGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRL 82
Cdd:cd07125 26 FDEKEWEAIPIING--EETETGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 83 ILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGE-IIPSP-GADKRLMVIRQGVGVCaaITPWNFPA 160
Cdd:cd07125 104 LEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDpELPGPtGELNGLELHGRGVFVC--ISPWNFPL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 161 AMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRV 240
Cdd:cd07125 182 AIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 241 LMRQCAE---SIKKLSLELGG-NApFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAAL 316
Cdd:cd07125 262 INRALAErdgPILPLIAETGGkNA-MIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 317 KVGDGSESDVQIGPLINADAGRKVQSlLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVqpGSLLLQEEIFGPVAALVK 396
Cdd:cd07125 341 KVGDPWDLSTDVGPLIDKPAGKLLRA-HTELMRGEAWLIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIR 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 397 FEDEQ--EAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN---TGLISnEVAPFGGVKQSGLG 461
Cdd:cd07125 418 FKAEDldEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrniTGAIV-GRQPFGGWGLSGTG 486
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
16-465 |
2.53e-75 |
|
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: 244.42 E-value: 2.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 16 AGSWRdaADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLknwhRLI----LENKTALA 91
Cdd:cd07130 4 DGEWG--GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIV----RQIgdalRKKKEALG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 92 QIMTAEQGKPLAEAEGEIAyaasfiEW-----FA-EQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITR 165
Cdd:cd07130 78 KLVSLEMGKILPEGLGEVQ------EMidicdFAvGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 166 KAGPALAAGCTMVIKPANETPFTALAMAELANQA----GIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVL 241
Cdd:cd07130 152 NAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 242 MRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDG 321
Cdd:cd07130 231 GQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 322 SESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIgDVQPGSLLLQEEIFGPVAALVKFEDEQ 401
Cdd:cd07130 311 LDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLE 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513169189 402 EAIEQANNTIYGLASYFYSNDAARIWRVSEQL--EYGMVGINTGLISNEV-APFGGVKQSGLGRE-GS 465
Cdd:cd07130 390 EAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSGAEIgGAFGGEKETGGGREsGS 457
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
15-476 |
5.16e-75 |
|
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: 244.41 E-value: 5.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRDAADGTTlAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIM 94
Cdd:cd07083 23 IGGEWVDTKERMV-SVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 95 TAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANG---EIIPSPGADKRLMVirQGVGVCAAITPWNFPAAMITRKAGPAL 171
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpavEVVPYPGEDNESFY--VGLGAGVVISPWNFPVAIFTGMIVAPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 172 AAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAE---- 247
Cdd:cd07083 180 AVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARlapg 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 248 --SIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESD 325
Cdd:cd07083 260 qtWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 326 VQIGPLINADAGRKVQSLLDDAMSRGaTLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQ--EA 403
Cdd:cd07083 340 TDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEA 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513169189 404 IEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN---TGLISNeVAPFGGVKQSGLG-REGSEHGIEDYLEMK 476
Cdd:cd07083 419 LEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkiTGALVG-VQPFGGFKLSGTNaKTGGPHYLRRFLEMK 494
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
67-471 |
1.83e-74 |
|
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: 241.55 E-value: 1.83e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 67 LTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIP----SPGADKRLMV 142
Cdd:cd07148 41 LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIPmgltPASAGRIAFT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 143 IRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTgQSREIGAVFTG 222
Cdd:cd07148 121 TREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 223 DERVRKLSFTGSTEVGRVLMRQCAESiKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVY 302
Cdd:cd07148 200 DPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 303 DQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKahPLGGNFFTPTVIGDVQPGSLL 382
Cdd:cd07148 279 DDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGK--RLSDTTYAPTVLLDPPRDAKV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 383 LQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINtglisNEVA------PFGGVK 456
Cdd:cd07148 357 STQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVN-----DHTAfrvdwmPFAGRR 431
|
410
....*....|....*
gi 1513169189 457 QSGLGREGSEHGIED 471
Cdd:cd07148 432 QSGYGTGGIPYTMHD 446
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
68-468 |
1.41e-71 |
|
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: 233.27 E-value: 1.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 68 TAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAE--------GEIAYAASFIE-WFAEQGKRAngeiiPSPGADK 138
Cdd:cd07134 18 TAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilpvlSEINHAIKHLKkWMKPKRVRT-----PLLLFGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 139 RLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVinvvtgqsreigA 218
Cdd:cd07134 93 KSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV------------A 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 219 VFTGDERVRK--LS-------FTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTC 289
Cdd:cd07134 161 VFEGDAEVAQalLElpfdhifFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 290 VCVNRFYIHRAVYDQFCDKFvarVAALKVGDGSESDVQIGP----LINADAGRKVQSLLDDAMSRGATLLTGGKAHPlGG 365
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHL---KAEIEKFYGKDAARKASPdlarIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDA-AQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 366 NFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLI 445
Cdd:cd07134 317 RYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVL 396
|
410 420
....*....|....*....|....*
gi 1513169189 446 --SNEVAPFGGVKQSGLGREGSEHG 468
Cdd:cd07134 397 hfLNPNLPFGGVNNSGIGSYHGVYG 421
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
68-475 |
3.15e-69 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 227.37 E-value: 3.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 68 TAAQRAALLKNWHRLILENKTALAQIMTAEQG-KPLAE---AE-----GEIAYAASFI-EWFAEQgKRANGeiIPSPGAd 137
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHEtllAEilpsiAGIKHARKHLkKWMKPS-RRHVG--LLFLPA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 138 kRLMVIRQGVGVCAAITPWNFP-----AAMITrkagpALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGq 212
Cdd:cd07133 94 -KAEVEYQPLGVVGIIVPWNYPlylalGPLIA-----ALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTG- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 213 SREIGAVFTG---DervrKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTC 289
Cdd:cd07133 166 GADVAAAFSSlpfD----HLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 290 VCVNRFYIHRAVYDQFCDKFVARVAALkVGDGSESDvQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPL--GGNF 367
Cdd:cd07133 242 VAPDYVLVPEDKLEEFVAAAKAAVAKM-YPTLADNP-DYTSIINERHYARLQGLLEDARAKGARVIELNPAGEDfaATRK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 368 FTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGL--I 445
Cdd:cd07133 320 LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLlhV 399
|
410 420 430
....*....|....*....|....*....|
gi 1513169189 446 SNEVAPFGGVKQSGLGRegsEHGIEDYLEM 475
Cdd:cd07133 400 AQDDLPFGGVGASGMGA---YHGKEGFLTF 426
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
14-476 |
4.91e-67 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 222.83 E-value: 4.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 14 LIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQI 93
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 94 MTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPaAMITRKAGP-ALA 172
Cdd:TIGR01722 84 ITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFP-AMIPLWMFPiAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 173 AGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDErVRKLSFTGSTEVGRVLMRQCAESIKKL 252
Cdd:TIGR01722 163 CGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPD-VKAVSFVGSTPIGRYIHTTGSAHGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 253 SLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVyDQFCDKFVARVAALKVGDGSESDVQIGPLI 332
Cdd:TIGR01722 242 QALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGAEMGPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 333 NADAGRKVQSLLDDAMSRGATLLTGG-----KAHPlGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQA 407
Cdd:TIGR01722 321 TPQAKDRVASLIAGGAAEGAEVLLDGrgykvDGYE-EGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513169189 408 NNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGL-ISNEVAPFGGVKQSGLGREG--SEHGIEDYLEMK 476
Cdd:TIGR01722 400 NASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIpVPLPYFSFTGWKDSFFGDHHiyGKQGTHFYTRGK 471
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
76-472 |
1.16e-65 |
|
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: 217.86 E-value: 1.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 76 LKNWHRLILENKTALAQIMTAEQGKP-----LAE---AEGEIAYAASFIEwfaeqgKRANGEIIPSPGADKRLMVIR--- 144
Cdd:cd07135 33 LKQLYWAVKDNEEAIVEALKKDLGRPpfetlLTEvsgVKNDILHMLKNLK------KWAKDEKVKDGPLAFMFGKPRirk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 145 QGVGVCAAITPWNFPaamITRKAGP---ALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFt 221
Cdd:cd07135 107 EPLGVVLIIGPWNYP---VLLALSPlvgAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALL- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 222 gDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAV 301
Cdd:cd07135 182 -EQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 302 YDQFcdkfvarVAALK------VGDGSESDVQIGPLINADAGRKVQSLLDDAmsrGATLLTGGKAHPlGGNFFTPTVIGD 375
Cdd:cd07135 261 YDEF-------VEELKkvldefYPGGANASPDYTRIVNPRHFNRLKSLLDTT---KGKVVIGGEMDE-ATRFIPPTIVSD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 376 VQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLI--SNEVAPFG 453
Cdd:cd07135 330 VSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPFG 409
|
410
....*....|....*....
gi 1513169189 454 GVKQSGLGREGSEHGIEDY 472
Cdd:cd07135 410 GVGDSGYGAYHGKYGFDTF 428
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
14-470 |
2.40e-64 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 216.16 E-value: 2.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 14 LIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQI 93
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 94 MTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGE-------IIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRK 166
Cdd:PLN00412 99 LVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkflvsdSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 167 AGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGStEVGRVLMRQCa 246
Cdd:PLN00412 179 IAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKKA- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 247 eSIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDgSESDV 326
Cdd:PLN00412 257 -GMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGP-PEDDC 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 327 QIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHplgGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQ 406
Cdd:PLN00412 335 DITPVVSESSANFIEGLVMDAKEKGATFCQEWKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHH 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1513169189 407 ANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISN-EVAPFGGVKQSGLGREGSEHGIE 470
Cdd:PLN00412 412 CNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGpDHFPFQGLKDSGIGSQGITNSIN 476
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
15-459 |
2.71e-60 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 205.19 E-value: 2.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRdAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQIM 94
Cdd:PRK09457 5 INGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 95 TAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIpSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAG 174
Cdd:PRK09457 84 ARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKR-SEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 175 CTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGqSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIKK-LS 253
Cdd:PRK09457 163 NTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKiLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 254 LELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVY-DQFCDKFVARVAALKVGDgSESDVQ--IGP 330
Cdd:PRK09457 242 LEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGR-WDAEPQpfMGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 331 LINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIgDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNT 410
Cdd:PRK09457 321 VISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1513169189 411 IYGLASYFYSNDAARIWRVSEQLEYGMVGIN---TGLISNevAPFGGVKQSG 459
Cdd:PRK09457 400 RFGLSAGLLSDDREDYDQFLLEIRAGIVNWNkplTGASSA--APFGGVGASG 449
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
70-469 |
1.06e-59 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 203.72 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 70 AQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAE--------GEIAYAASFIEWFAEQgKRANGEIIPSPGADKrlm 141
Cdd:PTZ00381 29 EFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmtevlltvAEIEHLLKHLDEYLKP-EKVDTVGVFGPGKSY--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 142 VIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFT 221
Cdd:PTZ00381 105 IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTELLK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 222 gdERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAV 301
Cdd:PTZ00381 184 --EPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 302 YDQFCDKFvARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDamsRGATLLTGGKAHpLGGNFFTPTVIGDVQPGSL 381
Cdd:PTZ00381 262 KDKFIEAL-KEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVD-IENKYVAPTIIVNPDLDSP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 382 LLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGL--ISNEVAPFGGVKQSG 459
Cdd:PTZ00381 337 LMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVfhLLNPNLPFGGVGNSG 416
|
410
....*....|
gi 1513169189 460 LgreGSEHGI 469
Cdd:PTZ00381 417 M---GAYHGK 423
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
10-441 |
1.54e-59 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 206.14 E-value: 1.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 10 RQQALIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTA 89
Cdd:PLN02419 113 RVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 90 LAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGP 169
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 170 ALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVfTGDERVRKLSFTGSTEVGRVLMRQCAESI 249
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAI-CDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 250 KKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFyIHRAVYDQFCDKFVARVAALKVGDGSESDVQIG 329
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV-VFVGDAKSWEDKLVERAKALKVTCGSEPDADLG 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 330 PLINADAGRKVQSLLDDAMSRGATLLTGGKAHPL----GGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIE 405
Cdd:PLN02419 431 PVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVpgyeKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAIS 510
|
410 420 430
....*....|....*....|....*....|....*.
gi 1513169189 406 QANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN 441
Cdd:PLN02419 511 IINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
13-473 |
2.18e-56 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 195.44 E-value: 2.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 13 ALIAGSWRdaADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQ 92
Cdd:PLN02315 23 CYVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 93 IMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALA 172
Cdd:PLN02315 101 LVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 173 AGCTMVIKPANETPFTALAM----AELANQAGIPQGVINVVTGQSrEIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAES 248
Cdd:PLN02315 181 CGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCGGA-EIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 249 IKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQI 328
Cdd:PLN02315 260 FGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 329 GPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIgDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQAN 408
Cdd:PLN02315 340 GPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINN 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513169189 409 NTIYGLASYFYSNDAARI--WRVSEQLEYGMVGINTGLISNEV-APFGGVKQSGLGREGSEHGIEDYL 473
Cdd:PLN02315 419 SVPQGLSSSIFTRNPETIfkWIGPLGSDCGIVNVNIPTNGAEIgGAFGGEKATGGGREAGSDSWKQYM 486
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
148-468 |
2.09e-55 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 191.18 E-value: 2.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 148 GVCAAITPWNFP-----AAMItrkaGpALAAGCTMVIKPANETPFTALAMAELANQAgIPQGVINVVTGQSREIGAVFtg 222
Cdd:cd07136 102 GVVLIIAPWNYPfqlalAPLI----G-AIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELL-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 223 DERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVY 302
Cdd:cd07136 174 DQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 303 DQFCDKFVARVAALKVGDGSESDvQIGPLINADAGRKVQSLLDDamsrgATLLTGGKAHPlGGNFFTPTVIGDVQPGSLL 382
Cdd:cd07136 254 EKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDN-----GKIVFGGNTDR-ETLYIEPTILDNVTWDDPV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 383 LQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLI--SNEVAPFGGVKQSGL 460
Cdd:cd07136 327 MQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMhlANPYLPFGGVGNSGM 406
|
....*...
gi 1513169189 461 greGSEHG 468
Cdd:cd07136 407 ---GSYHG 411
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
69-461 |
1.37e-50 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 185.40 E-value: 1.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 69 AAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKR--ANGEIIPSP-GADKRLMviRQ 145
Cdd:PRK11904 606 VEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRlfGAPEKLPGPtGESNELR--LH 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 146 GVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDER 225
Cdd:PRK11904 684 GRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPR 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 226 VRKLSFTGSTEVGRVLMRQCAE---SIKKLSLELGG-NApFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAV 301
Cdd:PRK11904 764 IAGVAFTGSTETARIINRTLAArdgPIVPLIAETGGqNA-MIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDI 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 302 YDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKvqsLLD--DAMSRGATLLTGGKAHPLG--GNFFTPTV--IGD 375
Cdd:PRK11904 843 ADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKAN---LDAhiERMKREARLLAQLPLPAGTenGHFVAPTAfeIDS 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 376 VQpgslLLQEEIFGPVAALVKFEDEQ--EAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISN--EVAP 451
Cdd:PRK11904 920 IS----QLEREVFGPILHVIRYKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAvvGVQP 995
|
410
....*....|
gi 1513169189 452 FGGVKQSGLG 461
Cdd:PRK11904 996 FGGQGLSGTG 1005
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
72-462 |
5.48e-48 |
|
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: 171.25 E-value: 5.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 72 RAALLKNWHRLILENKTALAQIMTAEQGKPLAEAE--------GEIAYAASFIEWFAEqgkrangeiiPSPgADKRLMVI 143
Cdd:cd07132 22 RIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVlseillvkNEIKYAISNLPEWMK----------PEP-VKKNLATL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 144 RQGV-------GVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELanqagIPQGVIN----VVTGQ 212
Cdd:cd07132 91 LDDVyiykeplGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLDKecypVVLGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 213 SREIGAVFtgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCV 292
Cdd:cd07132 166 VEETTELL--KQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 293 NrfYI--HRAVYDQFCDKfvARvAALK--VGDGSESDVQIGPLINADAGRKVQSLLDdamsrGATLLTGGKAHPlGGNFF 368
Cdd:cd07132 244 D--YVlcTPEVQEKFVEA--LK-KTLKefYGEDPKESPDYGRIINDRHFQRLKKLLS-----GGKVAIGGQTDE-KERYI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 369 TPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGL--IS 446
Cdd:cd07132 313 APTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTImhYT 392
|
410
....*....|....*.
gi 1513169189 447 NEVAPFGGVKQSGLGR 462
Cdd:cd07132 393 LDSLPFGGVGNSGMGA 408
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
67-477 |
1.82e-45 |
|
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: 165.85 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 67 LTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPgadkrlmvirqg 146
Cdd:TIGR01238 93 TPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVES------------ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 147 VGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERV 226
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 227 RKLSFTGSTEVGRVLMRQCAESIK---KLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYD 303
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDapvPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVAD 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 304 QFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGAT---LLTGGKAHPLGGNFFTPTV--IGDVQP 378
Cdd:TIGR01238 321 RVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKiaqLTLDDSRACQHGTFVAPTLfeLDDIAE 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 379 gsllLQEEIFGPVAALVKFEDEQ--EAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVA--PFGG 454
Cdd:TIGR01238 401 ----LSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGG 476
|
410 420
....*....|....*....|....
gi 1513169189 455 VKQSGLG-REGSEHGIEDYLEMKY 477
Cdd:TIGR01238 477 QGLSGTGpKAGGPHYLYRLTQVQY 500
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
69-461 |
3.82e-45 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 169.66 E-value: 3.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 69 AAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPgadkrlmvirQGVG 148
Cdd:PRK11905 611 AAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKP----------LGPV 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 149 VCaaITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRK 228
Cdd:PRK11905 681 VC--ISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAG 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 229 LSFTGSTEVGRVLMRQCAESIKK---LSLELGG-NApFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQ 304
Cdd:PRK11905 759 VMFTGSTEVARLIQRTLAKRSGPpvpLIAETGGqNA-MIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADR 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 305 FCDKFVARVAALKVGDGSESDVQIGPLINADAgrkVQSLLD--DAMSRGATLLtggKAHPL-----GGNFFTPTVIgdvQ 377
Cdd:PRK11905 838 VLTMLKGAMDELRIGDPWRLSTDVGPVIDAEA---QANIEAhiEAMRAAGRLV---HQLPLpaeteKGTFVAPTLI---E 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 378 PGSL-LLQEEIFGPVAALVKFE-DEQEA-IEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVA--PF 452
Cdd:PRK11905 909 IDSIsDLEREVFGPVLHVVRFKaDELDRvIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGvqPF 988
|
....*....
gi 1513169189 453 GGVKQSGLG 461
Cdd:PRK11905 989 GGEGLSGTG 997
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
70-461 |
7.94e-42 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 159.75 E-value: 7.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 70 AQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKR--ANGEIIPspgadkrlmvirQGV 147
Cdd:PRK11809 704 AERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDdfDNDTHRP------------LGP 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 148 GVCaaITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVR 227
Cdd:PRK11809 772 VVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVR 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 228 KLSFTGSTEVGRVLMRQCAESIKK------LSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAV 301
Cdd:PRK11809 850 GVMFTGSTEVARLLQRNLAGRLDPqgrpipLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDV 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 302 YDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAMSRGATLLTGGKAHPLG---GNFFTPTVI--GDV 376
Cdd:PRK11809 930 ADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEDwqsGTFVPPTLIelDSF 1009
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 377 QPgsllLQEEIFGPVAALVKFEDEQ--EAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYG-------MVGINTGlisn 447
Cdd:PRK11809 1010 DE----LKREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGnlyvnrnMVGAVVG---- 1081
|
410
....*....|....
gi 1513169189 448 eVAPFGGVKQSGLG 461
Cdd:PRK11809 1082 -VQPFGGEGLSGTG 1094
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
148-459 |
5.08e-41 |
|
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: 153.90 E-value: 5.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 148 GVCAAITPWNFPAAMITRKAGPALAaGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVR 227
Cdd:cd07123 172 GFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 228 KLSFTGSTEVGRVLMRQCAESIK------KLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAV 301
Cdd:cd07123 251 GLHFTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 302 YDQFCDKFVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLDDAM-SRGATLLTGGKAHPLGGNFFTPTVIGDVQPGS 380
Cdd:cd07123 331 WPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKsDPEAEIIAGGKCDDSVGYFVEPTVIETTDPKH 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 381 LLLQEEIFGPVAALVKFEDEQ--EAIEQANNT-IYGLASYFYSNDAARIWRVSEQLEY--GMVGIN---TGLISNEvAPF 452
Cdd:cd07123 411 KLMTEEIFGPVLTVYVYPDSDfeETLELVDTTsPYALTGAIFAQDRKAIREATDALRNaaGNFYINdkpTGAVVGQ-QPF 489
|
....*..
gi 1513169189 453 GGVKQSG 459
Cdd:cd07123 490 GGARASG 496
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
69-461 |
3.11e-40 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 155.10 E-value: 3.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 69 AAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRangeiipSPGADKRLmvirQGVG 148
Cdd:COG4230 614 VEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARR-------LFAAPTVL----RGRG 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 149 VCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRK 228
Cdd:COG4230 683 VFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAG 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 229 LSFTGSTEVGRVLMRQCAE---SIKKLSLELGG-NApFIVFDDADIDKAVEGALIAKFRNAGQTC-----VCVNrfyihr 299
Cdd:COG4230 763 VAFTGSTETARLINRTLAArdgPIVPLIAETGGqNA-MIVDSSALPEQVVDDVLASAFDSAGQRCsalrvLCVQ------ 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 300 avyDQFCDKFVARV----AALKVGDGSESDVQIGPLINADAgrkVQSLLD--DAMSRGATLLTGGK--AHPLGGNFFTPT 371
Cdd:COG4230 836 ---EDIADRVLEMLkgamAELRVGDPADLSTDVGPVIDAEA---RANLEAhiERMRAEGRLVHQLPlpEECANGTFVAPT 909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 372 VIgdvQPGSL-LLQEEIFGPVAALVKFEDEQ--EAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINtgliSNE 448
Cdd:COG4230 910 LI---EIDSIsDLEREVFGPVLHVVRYKADEldKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN----RNI 982
|
410
....*....|....*....
gi 1513169189 449 VA------PFGGVKQSGLG 461
Cdd:COG4230 983 IGavvgvqPFGGEGLSGTG 1001
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
69-462 |
2.85e-38 |
|
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: 144.48 E-value: 2.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 69 AAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEA-EGEIAYAASFI--------EWFAEQGKR-------ANGEIIP 132
Cdd:cd07137 20 AEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCklaikelkKWMAPEKVKtplttfpAKAEIVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 133 SPgadkrlmvirqgVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELanqagIPQ----GVINV 208
Cdd:cd07137 100 EP------------LGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-----IPEyldtKAIKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 209 VTGQSREIGAVFtgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKF-RNAGQ 287
Cdd:cd07137 163 IEGGVPETTALL--EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 288 TCVCVNrfYIhrAVYDQFCDKFvarVAALK------VGDGSESDVQIGPLINADAGRKVQSLLDDAmSRGATLLTGGK-- 359
Cdd:cd07137 241 ACIAPD--YV--LVEESFAPTL---IDALKntlekfFGENPKESKDLSRIVNSHHFQRLSRLLDDP-SVADKIVHGGErd 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 360 AHPLggnFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVG 439
Cdd:cd07137 313 EKNL---YIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVT 389
|
410 420
....*....|....*....|....*
gi 1513169189 440 INTGLI--SNEVAPFGGVKQSGLGR 462
Cdd:cd07137 390 FNDTVVqyAIDTLPFGGVGESGFGA 414
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
15-424 |
1.92e-34 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 135.22 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 15 IAGSWRD-AADGTTLavSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTALAQI 93
Cdd:PRK11903 9 VAGRWQAgSGAGTPL--FDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 94 MTAEQGKPLAEA----EGEIAYAASFIEWFAEQGKR---ANGEIIpSPGADKR-----LMVIRQGVGVcaAITPWNFPAA 161
Cdd:PRK11903 87 ATANSGTTRNDSavdiDGGIFTLGYYAKLGAALGDArllRDGEAV-QLGKDPAfqgqhVLVPTRGVAL--FINAFNFPAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 162 MITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGI-PQGVINVVTGQSREIGAVFTGDERVrklSFTGSTEVGRV 240
Cdd:PRK11903 164 GLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFDVV---SFTGSAETAAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 241 L-------MRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARV 313
Cdd:PRK11903 241 LrshpavvQRSVRVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 314 AALKVGDGSESDVQIGPLINADAGRKVQSLLdDAMSRGATLLTGGKAHPL------GGNFFTPTVIG--DVQPGSLLLQE 385
Cdd:PRK11903 321 AKTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFALvdadpaVAACVGPTLLGasDPDAATAVHDV 399
|
410 420 430
....*....|....*....|....*....|....*....
gi 1513169189 386 EIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAA 424
Cdd:PRK11903 400 EVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAA 438
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
12-424 |
2.14e-30 |
|
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: 123.53 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 12 QALIAGSWRD-AADGTTLAvsNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTAL 90
Cdd:cd07128 2 QSYVAGQWHAgTGDGRTLH--DAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 91 AQIMT---AEQGKPLAEAEGEIAYAASFIEWFAEQGKRAN----GEIIP-SPG---ADKRLMVIRQGVGVcaAITPWNFP 159
Cdd:cd07128 80 YALSAatgATRRDSWIDIDGGIGTLFAYASLGRRELPNAHflveGDVEPlSKDgtfVGQHILTPRRGVAV--HINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 160 AAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGI-PQGVINVVTGQSREIGAVFTGDERVrklSFTGSTEVG 238
Cdd:cd07128 158 VWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHLGEQDVV---AFTGSAATA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 239 RVLMRQ---CAESIK----KLSLELGGNAPFIVFDDADID---KAVEGALIAKfrnAGQTCVCVNRFYIHRAVYDQFCDK 308
Cdd:cd07128 235 AKLRAHpniVARSIRfnaeADSLNAAILGPDATPGTPEFDlfvKEVAREMTVK---AGQKCTAIRRAFVPEARVDAVIEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 309 FVARVAALKVGDGSESDVQIGPLINADAGRKVQSLLdDAMSRGATLLTGGK-------AHPLGGNFFTPTVIGDVQP--G 379
Cdd:cd07128 312 LKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPdrfevvgADAEKGAFFPPTLLLCDDPdaA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1513169189 380 SLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAA 424
Cdd:cd07128 391 TAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPA 435
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
69-462 |
1.18e-27 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 115.21 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 69 AAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEA--------EGEIAYAASFI-EWFAEqgKRANGEIIPSPGadkR 139
Cdd:PLN02203 27 LEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyrdevgvlTKSANLALSNLkKWMAP--KKAKLPLVAFPA---T 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 140 LMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAelanqAGIPQ----GVINVVTGQSrE 215
Cdd:PLN02203 102 AEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA-----ANIPKyldsKAVKVIEGGP-A 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 216 IGAVFTgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIV--FDDA-DIDKAVEGALIAKFRN-AGQTCVC 291
Cdd:PLN02203 176 VGEQLL-QHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 292 VNrfYIhrAVYDQFCDKFvarVAALKV------GDGSESDVQIGPLINADAGRKVQSLLDDAMSRgATLLTGGKAHPlGG 365
Cdd:PLN02203 255 ID--YV--LVEERFAPIL---IELLKStikkffGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSIDE-KK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 366 NFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLI 445
Cdd:PLN02203 326 LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAII 405
|
410
....*....|....*....
gi 1513169189 446 SN--EVAPFGGVKQSGLGR 462
Cdd:PLN02203 406 QYacDSLPFGGVGESGFGR 424
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
118-461 |
6.06e-27 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 113.22 E-value: 6.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 118 WFAEQGKRANGEIIPSPGAdkrlmVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELAN 197
Cdd:PLN02174 89 WMAPEKAKTSLTTFPASAE-----IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 198 QAgIPQGVINVVTGQSREIGAVFtgDERVRKLSFTGSTEVGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGA 277
Cdd:PLN02174 164 QY-LDSSAVRVVEGAVTETTALL--EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 278 LIAKFR-NAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDvQIGPLINADAGRKVQSLLDDAMSRGATLLT 356
Cdd:PLN02174 241 IAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLDEKEVSDKIVYG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 357 GGKAHPlggNF-FTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIYGLASYFYSNDAARIWRVSEQLEY 435
Cdd:PLN02174 320 GEKDRE---NLkIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSA 396
|
330 340 350
....*....|....*....|....*....|....
gi 1513169189 436 GmvgintGLISNEVA--------PFGGVKQSGLG 461
Cdd:PLN02174 397 G------GIVVNDIAvhlalhtlPFGGVGESGMG 424
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
67-408 |
1.20e-26 |
|
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: 111.86 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 67 LTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEGEIAYAASFIEWFA---EQGK-------RANGEIIPSPGA 136
Cdd:cd07129 18 LSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFAdlvREGSwldaridPADPDRQPLPRP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 137 DKRLMviRQGVGVCAAITPWNFPAAMITrkAG----PALAAGCTMVIKPANETPFTALAMAELANQA----GIPQGVINV 208
Cdd:cd07129 98 DLRRM--LVPLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLPAGVFSL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 209 VTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESI--KKLSLELGGNAPFIVFDDADIDKAVE--GALIAKFR- 283
Cdd:cd07129 174 LQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPepIPFYAELGSVNPVFILPGALAERGEAiaQGFVGSLTl 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 284 NAGQTCVC---VnrFYIHRAVYDQFCDKFVARVAAlkvgdgSESDVQIGPLINADAGRKVQSLLDDAmsrGATLLTGGKA 360
Cdd:cd07129 254 GAGQFCTNpglV--LVPAGPAGDAFIAALAEALAA------APAQTMLTPGIAEAYRQGVEALAAAP---GVRVLAGGAA 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1513169189 361 HPlGGNFFTPTVI---GDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQAN 408
Cdd:cd07129 323 AE-GGNQAAPTLFkvdAAAFLADPALQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
67-451 |
1.86e-25 |
|
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: 108.48 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 67 LTAAQRAALLKNWHRLILENKTALAQIMTAEQGKPLAEAEgEIAYAASFIEWFAEQGK--RANGEIIPSPGADKRLMVIR 144
Cdd:cd07084 18 LALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE-NICGDQVQLRARAFVIYsyRIPHEPGNHLGQGLKQQSHG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 145 Q--GVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQAGI-PQGVINVVTGQSREIGAVFT 221
Cdd:cd07084 97 YrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLINGDGKTMQALLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 222 gDERVRKLSFTGSTEVGRVLMRQCAESikKLSLELGGNAPFIVFDDADIDKAVEGALIAK-FRNAGQTCVCVNRFYIH-- 298
Cdd:cd07084 177 -HPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVAWQCVQDmTACSGQKCTAQSMLFVPen 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 299 ---RAVYDQFCDKFVARvaalkvgdgSESDVQIGPLINADAGRKVQSLLDDAmsrGATLLTGGKAHPlggNFFTPTVIGD 375
Cdd:cd07084 254 wskTPLVEKLKALLARR---------KLEDLLLGPVQTFTTLAMIAHMENLL---GSVLLFSGKELK---NHSIPSIYGA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 376 VQPGSLLL------------QEEIFGPVAALVKFEDEQEA--IEQANNTIYGLASYFYSNDAARIWRVSEQLEYGMVGIN 441
Cdd:cd07084 319 CVASALFVpideilktyelvTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAGRTYA 398
|
410
....*....|
gi 1513169189 442 TGLISNEVAP 451
Cdd:cd07084 399 ILRGRTGVAP 408
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
11-468 |
6.41e-12 |
|
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440272 [Multi-domain] Cd Length: 975 Bit Score: 68.15 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 11 QQALIAGSWRDAADGTTLAVSNPSTGATLGQIPNMGRAEAQQAVDAAAAALPAWRALTAAQRAALLKNWHRLILENKTAL 90
Cdd:COG0506 490 LAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLL 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 91 AQIMTAEQGKPLAEAEGEIAYAASFIEWFAEQGKRANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPA 170
Cdd:COG0506 570 AAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAA 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 171 LAAGCTMVIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGDERVRKLSFTGSTEVGRVLMRQCAESIK 250
Cdd:COG0506 650 AAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAA 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 251 KLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFYIHRAVYDQFCDKFVARVAALKVGDGSESDVQIGP 330
Cdd:COG0506 730 AAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALAL 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 331 LINADAGRKVQSLLDDAMSRGATLLTGGKAHPLGGNFFTPTVIGDVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNT 410
Cdd:COG0506 810 GIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGL 889
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1513169189 411 IYGLASYFYSNDAARIWRVSEQLEYGMVGINTGLISNEVAPFGGVKQSGLGREGSEHG 468
Cdd:COG0506 890 TGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 947
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
88-431 |
8.55e-12 |
|
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: 67.12 E-value: 8.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 88 TALAQIMTAEQGKPLAEAEG--EIAYAA---SFI----EWFAEQGKRangeiiPSPGADKRLMVIRQGVGV---CAAITP 155
Cdd:cd07127 134 TGQAFMMAFQAGGPHAQDRGleAVAYAWremSRIpptaEWEKPQGKH------DPLAMEKTFTVVPRGVALvigCSTFPT 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 156 WNFPAAMITrkagpALAAGCTMVIKPAnetPFTALAMA-------ELANQAGI-PQGVINVVTGQSREIGAVFTGDERVR 227
Cdd:cd07127 208 WNGYPGLFA-----SLATGNPVIVKPH---PAAILPLAitvqvarEVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVR 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 228 KLSFTGSTEVGRVLMRQCAEsiKKLSLELGGNAPFIVfDDADIDKAVEGALIAKFR-NAGQTCVCVNRFYIHR------- 299
Cdd:cd07127 280 IIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVV-DSTDDLKAMLRNLAFSLSlYSGQMCTTPQNIYVPRdgiqtdd 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 300 --AVYDQFCDKFVARVAALkVGDGSESDVQIGPLINADAGRKVQslldDAMSRGATLLTGGK-AHP--LGGNFFTPTVIG 374
Cdd:cd07127 357 grKSFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIA----EARQLGEVLLASEAvAHPefPDARVRTPLLLK 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 375 DVQPGSLLLQEEIFGPVAALVKFEDEQEAIEQANNTIY---GLASYFYSNDAARIWRVSE 431
Cdd:cd07127 432 LDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVRehgAMTVGVYSTDPEVVERVQE 491
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
100-429 |
8.93e-11 |
|
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: 64.05 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 100 KPLAEAEGEIAYAASFIEWFAEQGKR--ANGEIIPSPGADKRLMVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTM 177
Cdd:cd07126 94 KSDAQALGEVVVTRKFLENFAGDQVRflARSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 178 VIKPANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTgDERVRKLSFTGSTEVgrvlmrqcAEsikKLSLELG 257
Cdd:cd07126 174 LLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILL-EANPRMTLFTGSSKV--------AE---RLALELH 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 258 GNapfIVFDDADIDKAVEGALIAKF--------RNA----GQTCVCVNRFYIHRAVYDQfcdKFVARVAALkVGDGSESD 325
Cdd:cd07126 242 GK---VKLEDAGFDWKILGPDVSDVdyvawqcdQDAyacsGQKCSAQSILFAHENWVQA---GILDKLKAL-AEQRKLED 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 326 VQIGPLINADAgRKVQSLLDDAMS-RGATLLTGGKahPLGgNFFTPTVIGDVQPGSL--------------LLQEEIFGP 390
Cdd:cd07126 315 LTIGPVLTWTT-ERILDHVDKLLAiPGAKVLFGGK--PLT-NHSIPSIYGAYEPTAVfvpleeiaieenfeLVTTEVFGP 390
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1513169189 391 VAALVKFEDEQE--AIEQANNTIYGLASYFYSNDAARIWRV 429
Cdd:cd07126 391 FQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEV 431
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
148-407 |
1.71e-05 |
|
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: 47.23 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 148 GVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQA----GIPQGVINVVTGQSREIGAVFTGD 223
Cdd:cd07121 99 GVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAiaeaGGPDNLVVTVEEPTIETTNELMAH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 224 ERVRKLSFTGSTEVGRVLMRqcaeSIKKLSLELGGNAPFIVFDDADIDKAVEGALI-AKFRNaGQTCVCVNRFYIHRAVY 302
Cdd:cd07121 179 PDINLLVVTGGPAVVKAALS----SGKKAIGAGAGNPPVVVDETADIEKAARDIVQgASFDN-NLPCIAEKEVIAVDSVA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 303 DQFCDKFVaRVAALKVGDgsESDVQIGPLInadagrkvqsLLDDAMSRGATLLTGGKAHPL----GGN--FFTPTVIGDV 376
Cdd:cd07121 254 DYLIAAMQ-RNGAYVLND--EQAEQLLEVV----------LLTNKGATPNKKWVGKDASKIlkaaGIEvpADIRLIIVET 320
|
250 260 270
....*....|....*....|....*....|.
gi 1513169189 377 QPGSLLLQEEIFGPVAALVKFEDEQEAIEQA 407
Cdd:cd07121 321 DKDHPFVVEEQMMPILPVVRVKNFDEAIELA 351
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
141-316 |
5.10e-05 |
|
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: 45.72 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 141 MVIRQGVGVCAAITPWNFPAAMITRKAGPALAAGCTMVIKPANETPFTALAMAELANQA----GIPQGVINVVTGQSREI 216
Cdd:cd07081 90 LIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGWIDNPSIEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 217 GAVFTGDERVRKLSFTGstevGRVLMRQCAESIKKLSLELGGNAPFIVFDDADIDKAVEGALIAKFRNAGQTCVCVNRFY 296
Cdd:cd07081 170 AQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVI 245
|
170 180
....*....|....*....|
gi 1513169189 297 IHRAVYDQFCDKFVARVAAL 316
Cdd:cd07081 246 VVDSVYDEVMRLFEGQGAYK 265
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
148-277 |
1.33e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 44.12 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513169189 148 GVCAAITPWNFPAAMITRKAGPALAAGCTMVIKP----ANETPFTALAMAELANQAGIPQGVINVVTGQSREIGAVFTGD 223
Cdd:PRK15398 131 GVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgaKKVSLRAIELLNEAIVAAGGPENLVVTVAEPTIETAQRLMKH 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1513169189 224 ERVRKLSFTGSTEVGRVLMRqcaeSIKKLSLELGGNAPFIVFDDADIDKA----VEGA 277
Cdd:PRK15398 211 PGIALLVVTGGPAVVKAAMK----SGKKAIGAGAGNPPVVVDETADIEKAardiVKGA 264
|
|
| |
