|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
28-478 |
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: 786.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 28 VKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEI 107
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 108 GYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTA 187
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 188 YALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDAN 267
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 268 LDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATA 347
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 348 KGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRV 427
Cdd:cd07103 321 KGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 480084072 428 GEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCV 478
Cdd:cd07103 401 AEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
26-478 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 728.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARG 105
Cdd:PLN02278 42 FPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 106 EIGYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPL 185
Cdd:PLN02278 122 EVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 186 TAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDD 265
Cdd:PLN02278 202 TALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDD 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 266 ANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADA 345
Cdd:PLN02278 282 ADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 346 TAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQW 425
Cdd:PLN02278 362 VSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAW 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 480084072 426 RVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCV 478
Cdd:PLN02278 442 RVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
28-474 |
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: 694.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 28 VKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEI 107
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 108 GYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTA 187
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 188 YALEVLALKAGLPADILLNISGD-AIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDA 266
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGSrAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 267 NLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADAT 346
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 347 AKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWR 426
Cdd:TIGR01780 321 EKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 480084072 427 VGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:TIGR01780 401 VAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
26-480 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 648.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARG 105
Cdd:PRK11241 28 IDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 106 EIGYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPL 185
Cdd:PRK11241 108 EISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 186 TAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDD 265
Cdd:PRK11241 188 SALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 266 ANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADA 345
Cdd:PRK11241 268 ADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 346 TAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQW 425
Cdd:PRK11241 348 LEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVF 427
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 480084072 426 RVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVDL 480
Cdd:PRK11241 428 RVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
17-480 |
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: 616.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 17 FAAPAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQ 96
Cdd:COG1012 14 WVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLET 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 97 GKPLAEARGEIGYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSML 176
Cdd:COG1012 94 GKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 177 VKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGG 256
Cdd:COG1012 174 LKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 257 NAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAIT 336
Cdd:COG1012 254 KNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 337 KVQSHIADATAKGATIRIGGQR-SALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAY 415
Cdd:COG1012 334 RVLAYIEDAVAEGAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAAS 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480084072 416 VFTQSAARQWRVGEALEYGMVGINTGAISNEV-APFGGVKQSGLGREGSKFGIEEYLEMKYLCVDL 480
Cdd:COG1012 414 VFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
20-474 |
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: 574.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 20 PAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKP 99
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 100 LAEARGEIGYAASFIRWFAEQARRIDGEVLtPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKP 179
Cdd:pfam00171 83 LAEARGEVDRAIDVLRYYAGLARRLDGETL-PSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 180 AEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAP 259
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 260 VLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQ 339
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 340 SHIADATAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQ 419
Cdd:pfam00171 322 KYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTS 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 480084072 420 SAARQWRVGEALEYGMVGINTGAISN-EVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:pfam00171 402 DLERALRVARRLEAGMVWINDYTTGDaDGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
49-478 |
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: 529.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 49 EAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAASFIRWFAEQARRIDGEV 128
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 129 LTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLALKAGLPADILLNIS 208
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 209 GDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCV 288
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 289 CANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAKGATIRIGGQRSALG-GTFFE 367
Cdd:cd07078 241 AASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkGYFVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 368 PTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAISNEV 447
Cdd:cd07078 321 PTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEP 400
|
410 420 430
....*....|....*....|....*....|..
gi 480084072 448 -APFGGVKQSGLGREGSKFGIEEYLEMKYLCV 478
Cdd:cd07078 401 sAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
17-474 |
2.25e-168 |
|
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: 482.92 E-value: 2.25e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 17 FAAPAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQ 96
Cdd:cd07088 6 FVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 97 GKPLAEARGEIGYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSML 176
Cdd:cd07088 86 GKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 177 VKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGG 256
Cdd:cd07088 166 IKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 257 NAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAIT 336
Cdd:cd07088 246 KAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 337 KVQSHIADATAKGATIRIGGQRSALG-GTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAY 415
Cdd:cd07088 326 KVEEMVERAVEAGATLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSY 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480084072 416 VFTQSAARQWRVGEALEYGMVGINTGaisNEVAPFG---GVKQSGLGREGSKFGIEEYLEMK 474
Cdd:cd07088 406 IYTENLNTAMRATNELEFGETYINRE---NFEAMQGfhaGWKKSGLGGADGKHGLEEYLQTK 464
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
30-474 |
1.81e-154 |
|
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: 447.00 E-value: 1.81e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 30 DAATSETLAWVKSYDRAGVEAAIQRSAQA--QAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEI 107
Cdd:cd07114 3 NPATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 108 GYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTA 187
Cdd:cd07114 83 RYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPAST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 188 YALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDAN 267
Cdd:cd07114 163 LELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 268 LDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATA 347
Cdd:cd07114 243 LDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARARE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 348 KGATIRIGGQRSAL----GGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAAR 423
Cdd:cd07114 323 EGARVLTGGERPSGadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLAR 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 480084072 424 QWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:cd07114 403 AHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
30-478 |
5.73e-149 |
|
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: 432.76 E-value: 5.73e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 30 DAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEAR-GEIG 108
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRDIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 109 YAASFIRWFAEQARRIDGEVLtPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAY 188
Cdd:cd07093 83 RAAANFRFFADYILQLDGESY-PQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 189 ALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANL 268
Cdd:cd07093 162 LLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 269 DQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAK 348
Cdd:cd07093 242 DRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 349 GATIRIGGQRSAL----GGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQ 424
Cdd:cd07093 322 GATILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 480084072 425 WRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCV 478
Cdd:cd07093 402 HRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
26-478 |
3.58e-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: 425.86 E-value: 3.58e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARG 105
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 106 EIGYAASFIRWFAEQARRIDGEVL----TPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAE 181
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIpfdaSPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 182 QTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAptIKKLSLELGGNAPVL 261
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 262 VFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSH 341
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 342 IADATAKGATIRIGGQRSalgGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSA 421
Cdd:cd07149 319 VEEAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 422 ARQWRVGEALEYGMVGINTgaISN---EVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCV 478
Cdd:cd07149 396 QKALKAARELEVGGVMIND--SSTfrvDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
48-478 |
2.53e-144 |
|
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: 420.01 E-value: 2.53e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 48 VEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAASFIRWFAEQARRIDGE 127
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 128 VLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYAL--EVLALkAGLPADILL 205
Cdd:cd07104 82 ILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLiaEIFEE-AGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 206 NISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQ 285
Cdd:cd07104 161 VVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 286 TCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAKGATIRIGGQRSalgGTF 365
Cdd:cd07104 241 ICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE---GLF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 366 FEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAISN 445
Cdd:cd07104 318 YQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVND 397
|
410 420 430
....*....|....*....|....*....|....
gi 480084072 446 E-VAPFGGVKQSGLGREGSKFGIEEYLEMKYLCV 478
Cdd:cd07104 398 EpHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
26-474 |
5.58e-143 |
|
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: 418.54 E-value: 5.58e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVKSYDRAGVEAAIQ--RSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAE- 102
Cdd:cd07091 21 FPTINPATEEVICQVAEADEEDVDAAVKaaRAAFETGWWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEEs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 103 ARGEIGYAASFIRWFAEQARRIDGEVLtPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQ 182
Cdd:cd07091 101 AKGDVALSIKCLRYYAGWADKIQGKTI-PIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 183 TPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPT-IKKLSLELGGNAPVL 261
Cdd:cd07091 180 TPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSnLKKVTLELGGKSPNI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 262 VFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSH 341
Cdd:cd07091 260 VFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 342 IADATAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSA 421
Cdd:cd07091 340 IESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDI 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 480084072 422 ARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:cd07091 420 NKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
53-478 |
1.29e-142 |
|
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: 413.55 E-value: 1.29e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 53 QRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAASFIRWFAEQARRIDGEVLTPT 132
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 133 LPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAI 212
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 213 EVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANR 292
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 293 IYVQDGIYDALADRLVeavaklqvgdgrqetstqgplidedaitkvqshiadatakgatiriggqrsalggtffepTVLT 372
Cdd:cd06534 241 LLVHESIYDEFVEKLV------------------------------------------------------------TVLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 373 NVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAISNEV-APFG 451
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPeAPFG 340
|
410 420
....*....|....*....|....*..
gi 480084072 452 GVKQSGLGREGSKFGIEEYLEMKYLCV 478
Cdd:cd06534 341 GVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
48-469 |
1.88e-140 |
|
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: 410.31 E-value: 1.88e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 48 VEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAASFIRWFAEQARridgE 127
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAE----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 128 VLTPT---LPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLALKAGLPADIL 204
Cdd:cd07100 77 FLADEpieTDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 205 --LNISGDAIEvgkTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRN 282
Cdd:cd07100 157 qnLLIDSDQVE---AIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 283 SGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAKGATIRIGGQRSALG 362
Cdd:cd07100 234 AGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 363 GTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGA 442
Cdd:cd07100 314 GAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMV 393
|
410 420
....*....|....*....|....*..
gi 480084072 443 ISNEVAPFGGVKQSGLGREGSKFGIEE 469
Cdd:cd07100 394 KSDPRLPFGGVKRSGYGRELGRFGIRE 420
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
26-476 |
4.49e-139 |
|
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: 407.89 E-value: 4.49e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARG 105
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 106 EIGYAASFIRWFAEQARRIDGEvltpTLP------NQRLLVI--KQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLV 177
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGE----TIPvdayeyNERRIAFtvREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 178 KPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGN 257
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 258 APVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITK 337
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 338 VQSHIADATAKGATIRIGGQRSalGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVF 417
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 418 TQSAARQWRVGEALEYGMVGIN-TGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYL 476
Cdd:cd07145 395 TNDINRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
27-478 |
2.08e-136 |
|
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: 400.94 E-value: 2.08e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 27 EVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGE 106
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 107 IGYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLT 186
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 187 AYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDA 266
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 267 NLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADAT 346
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 347 AKGATIRIGGQRSalgGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWR 426
Cdd:cd07150 322 AKGAKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFK 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 480084072 427 VGEALEYGMVGINTGAISNE-VAPFGGVKQSGLGREGSKFGIEEYLEMKYLCV 478
Cdd:cd07150 399 LAERLESGMVHINDPTILDEaHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
32-474 |
3.67e-136 |
|
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: 400.44 E-value: 3.67e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 32 ATSETLAWVKSYDRAGVEAAIQ--RSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEAR-GEIG 108
Cdd:cd07112 10 ATGRVLAEVAACDAADVDRAVAaaRRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALaVDVP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 109 YAASFIRWFAEQARRIDGEVlTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAY 188
Cdd:cd07112 90 SAANTFRWYAEAIDKVYGEV-APTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 189 ALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPT-IKKLSLELGGNAPVLVFDDA- 266
Cdd:cd07112 169 RLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKSPNIVFADAp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 267 NLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADAT 346
Cdd:cd07112 249 DLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 347 AKGATIRIGGQR--SALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQ 424
Cdd:cd07112 329 AEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRA 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 480084072 425 WRVGEALEYGMVGINT-GAISNEVaPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:cd07112 409 HRVARRLRAGTVWVNCfDEGDITT-PFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
14-482 |
4.60e-136 |
|
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: 400.92 E-value: 4.60e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 14 DISFAAPAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQ--RSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQI 91
Cdd:cd07119 3 DGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAaaRRAFDSGEWPHLPAQERAALLFRIADKIREDAEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 92 LTAEQGKPLAEARGEIGYAASFIRWFAEQARRIDGEVLtPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAA 171
Cdd:cd07119 83 ETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVY-DVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 172 GCSMLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLS 251
Cdd:cd07119 162 GNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 252 LELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLID 331
Cdd:cd07119 242 LELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 332 EDAITKVQSHIADATAKGATIRIGGQRSALG----GTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMAND 407
Cdd:cd07119 322 AEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLAND 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480084072 408 TEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVDLSE 482
Cdd:cd07119 402 TPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLSP 476
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
19-474 |
4.84e-136 |
|
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: 400.34 E-value: 4.84e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 19 APAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGK 98
Cdd:cd07138 9 APAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 99 PLAEARG-EIGYAASFIRWFAEQARRIDGEvltptLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLV 177
Cdd:cd07138 89 PITLARAaQVGLGIGHLRAAADALKDFEFE-----ERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 178 KPAEQTPLTAYAL-EVLAlKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGG 256
Cdd:cd07138 164 KPSEVAPLSAIILaEILD-EAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 257 NAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAIT 336
Cdd:cd07138 243 KSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 337 KVQSHIADATAKGATIRIGGQRSALG---GTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLA 413
Cdd:cd07138 323 RVQGYIQKGIEEGARLVAGGPGRPEGlerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLA 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480084072 414 AYVFTQSAARQWRVGEALEYGMVGINtGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:cd07138 403 GYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
28-474 |
8.51e-135 |
|
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: 396.51 E-value: 8.51e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 28 VKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEI 107
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 108 GYAASFIRWFAEQarRIDGEVLTPTlPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTA 187
Cdd:cd07106 81 GGAVAWLRYTASL--DLPDEVIEDD-DTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 188 YALEVLALKAgLPADILLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDAN 267
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSGGD-ELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 268 LDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATA 347
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 348 KGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRV 427
Cdd:cd07106 316 KGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAV 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 480084072 428 GEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:cd07106 396 ARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
32-476 |
2.85e-134 |
|
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: 395.44 E-value: 2.85e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 32 ATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAA 111
Cdd:cd07099 4 ATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 112 SFIRWFAEQARRI--DGEVLT-PTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAY 188
Cdd:cd07099 84 EAIDWAARNAPRVlaPRKVPTgLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 189 ALEVLALKAGLPADILLNISGDAiEVGKTLCESdIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANL 268
Cdd:cd07099 164 LLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 269 DQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAK 348
Cdd:cd07099 242 ERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 349 GATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVG 428
Cdd:cd07099 322 GAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 480084072 429 EALEYGMVGIN----TGAISNevAPFGGVKQSGLGREGSKFGIEEYLEMKYL 476
Cdd:cd07099 402 RRLEAGAVSINdvllTAGIPA--LPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
31-481 |
5.30e-132 |
|
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: 390.55 E-value: 5.30e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 31 AATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYA 110
Cdd:cd07131 22 ADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 111 ASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYAL 190
Cdd:cd07131 102 IDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 191 EVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQ 270
Cdd:cd07131 182 VELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 271 AVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAKGA 350
Cdd:cd07131 262 ALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 351 TIRIGGQRSALG----GTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWR 426
Cdd:cd07131 342 TLLLGGERLTGGgyekGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFR 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 480084072 427 VGEALEYGMVGINTGAISNEV-APFGGVKQSGLG-REGSKFGIEEYLEMKYLCVDLS 481
Cdd:cd07131 422 ARRDLEAGITYVNAPTIGAEVhLPFGGVKKSGNGhREAGTTALDAFTEWKAVYVDYS 478
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
28-476 |
9.86e-132 |
|
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: 389.02 E-value: 9.86e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 28 VKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEI 107
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 108 GYAASFIRWFAEQARRID---GEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTP 184
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDakaERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 185 LTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFD 264
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 265 DANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIAD 344
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 345 ATAKGATIRIGGQRSALG--GTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAA 422
Cdd:cd07110 321 GKEEGARLLCGGRRPAHLekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 480084072 423 RQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYL 476
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
26-478 |
2.47e-130 |
|
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: 385.25 E-value: 2.47e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARG 105
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 106 EIGYAASFIRWFAEQARRIDGEVL----TPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAE 181
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIpldaTQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 182 QTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAptIKKLSLELGGNAPVL 261
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 262 VFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSH 341
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 342 IADATAKGATIRIGGQRSalgGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSA 421
Cdd:cd07094 319 VEEAVEAGARLLCGGERD---GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 480084072 422 ARQWRVGEALEYGMVGINTG-AISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCV 478
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSsAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
32-480 |
3.62e-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: 3.62e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 32 ATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARG-EIGYA 110
Cdd:cd07115 5 ATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVPRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 111 ASFIRWFAEQARRIDGEVLtPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYAL 190
Cdd:cd07115 85 ADTFRYYAGWADKIEGEVI-PVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 191 EVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQ 270
Cdd:cd07115 164 AELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 271 AVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAKGA 350
Cdd:cd07115 244 AVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 351 TIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEA 430
Cdd:cd07115 324 RLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAA 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 480084072 431 LEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVDL 480
Cdd:cd07115 404 LKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
48-474 |
4.49e-129 |
|
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: 381.15 E-value: 4.49e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 48 VEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAASFIRWFAEQARRIDGE 127
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 128 VLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLALKAGLPADIL--L 205
Cdd:cd07105 82 SIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLnvV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 206 NIS-GDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNSG 284
Cdd:cd07105 162 THSpEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 285 QTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDgrqetSTQGPLIDEDAITKVQSHIADATAKGATIRIGG-QRSALGG 363
Cdd:cd07105 242 QICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlADESPSG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 364 TFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAI 443
Cdd:cd07105 317 TSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTV 396
|
410 420 430
....*....|....*....|....*....|..
gi 480084072 444 SNE-VAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:cd07105 397 HDEpTLPHGGVKSSGYGRFNGKWGIDEFTETK 428
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
30-478 |
4.56e-129 |
|
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: 382.08 E-value: 4.56e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 30 DAATSETLAWVKSYDRAGVEAAIQRSAQA--QAVWKKQTALvRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEI 107
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAfdETDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 108 GYAASFIRWFAEQARRIDGEVLTPTlPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTA 187
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPE-PGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 188 YAL-EVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDA 266
Cdd:cd07120 161 AAIiRILAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 267 NLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADAT 346
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 347 AKGATIRIGGQRSALG---GTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAAR 423
Cdd:cd07120 321 AAGAEVVLRGGPVTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLAR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 480084072 424 QWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCV 478
Cdd:cd07120 401 AMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
40-474 |
1.78e-128 |
|
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: 380.53 E-value: 1.78e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 40 VKSYDRAGVE---AAIQ--RSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAASFI 114
Cdd:cd07118 10 VARYAEGTVEdvdAAVAaaRKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 115 RWFAEQARRIDGEVLTpTLPNQRL-LVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVL 193
Cdd:cd07118 90 RYAASLARTLHGDSYN-NLGDDMLgLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 194 ALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQ 273
Cdd:cd07118 169 LIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 274 GIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAKGATIR 353
Cdd:cd07118 249 AVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 354 IGGQRSALG-GTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALE 432
Cdd:cd07118 329 LGGERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIR 408
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 480084072 433 YGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:cd07118 409 AGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELK 450
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
28-474 |
4.61e-128 |
|
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: 379.66 E-value: 4.61e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 28 VKDAATSETLAWVKSYDRAGVEAAIQ--RSAQAQAVWKKQTALvRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARG 105
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAaaRRAFDTGDWSTDAEE-RARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 106 -EIGYAASFIRWFAEQARRIDGEV-----LTPTLPNQRLLViKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKP 179
Cdd:cd07089 80 mQVDGPIGHLRYFADLADSFPWEFdlpvpALRGGPGRRVVR-REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 180 AEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAP 259
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 260 VLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQ 339
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 340 SHIADATAKGATIRIGGQRSA--LGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVF 417
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 480084072 418 TQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
31-474 |
2.79e-127 |
|
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: 378.13 E-value: 2.79e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 31 AATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYA 110
Cdd:cd07097 22 SDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 111 ASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYAL 190
Cdd:cd07097 102 GQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWAL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 191 -EVLAlKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLD 269
Cdd:cd07097 182 vEILE-EAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 270 QAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAKG 349
Cdd:cd07097 261 LAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 350 ATIRIGGQR--SALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRV 427
Cdd:cd07097 341 AKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHF 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 480084072 428 GEALEYGMVGINTGAISNEV-APFGGVKQSGLG-REGSKFGIEEYLEMK 474
Cdd:cd07097 421 KRRVEAGVVMVNLPTAGVDYhVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
17-480 |
8.42e-127 |
|
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: 377.52 E-value: 8.42e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 17 FAAPAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQA-QAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAE 95
Cdd:cd07144 16 FVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 96 QGKPL-AEARGEIGYAASFIRWFAEQARRIDGEVLtPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCS 174
Cdd:cd07144 96 SGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTI-PTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 175 MLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLEL 254
Cdd:cd07144 175 VVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLEC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 255 GGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAK-LQVGDGRQETSTQGPLIDED 333
Cdd:cd07144 255 GGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGPQVSKT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 334 AITKVQSHIADATAKGATIRIGGQRSALG---GTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEF 410
Cdd:cd07144 335 QYDRVLSYIEKGKKEGAKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTY 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 411 GLAAYVFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVDL 480
Cdd:cd07144 415 GLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
28-481 |
1.71e-126 |
|
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: 375.49 E-value: 1.71e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 28 VKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEI 107
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 108 GYAASFIRWFAEQARRIDGEVLTptLPNQRLLVIKQA-IGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLT 186
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVP--LPGGSFAYTRREpLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 187 AYAL-EVLAlKAGLPADILLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDD 265
Cdd:cd07090 159 ALLLaEILT-EAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 266 ANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADA 345
Cdd:cd07090 237 ADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 346 TAKGATIRIGGQRSAL-----GGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQS 420
Cdd:cd07090 317 KQEGAKVLCGGERVVPedgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480084072 421 AARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVDLS 481
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
26-476 |
5.10e-126 |
|
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: 374.27 E-value: 5.10e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARG 105
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 106 EIGYAASFIRWFAEQARRIDGEVL----TPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAE 181
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLpldiSARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 182 QTPLTAYAL-EVLAlKAGLPADILlNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPtiKKLSLELGGNAPV 260
Cdd:cd07147 161 RTPLSALILgEVLA-ETGLPKGAF-SVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 261 LVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQS 340
Cdd:cd07147 237 IVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 341 HIADATAKGATIRIGGQRSalgGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQS 420
Cdd:cd07147 317 WVNEAVDAGAKLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 480084072 421 AARQWRVGEALEYGMVGIN---TGAISNevAPFGGVKQSGLGREGSKFGIEEYLEMKYL 476
Cdd:cd07147 394 LEKALRAWDELEVGGVVINdvpTFRVDH--MPYGGVKDSGIGREGVRYAIEEMTEPRLL 450
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
26-474 |
1.85e-125 |
|
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: 372.85 E-value: 1.85e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVksydRAGVEAAIQRSAQAQAVWKKQ-TALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEAR 104
Cdd:cd07146 1 LEVRNPYTGEVVGTV----PAGTEEALREALALAASYRSTlTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 105 GEIGYAASFIRWFAEQARRIDGEV----LTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPA 180
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESfscdLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 181 EQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILmqQCAPTIKKLSLELGGNAPV 260
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 261 LVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQS 340
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 341 HIADATAKGATIRIGGQRSalgGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQS 420
Cdd:cd07146 315 RVEEAIAQGARVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 480084072 421 AARQWRVGEALEYGMVGINTG-AISNEVAPFGGVKQSGLG-REGSKFGIEEYLEMK 474
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNEVpGFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
19-481 |
1.55e-124 |
|
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: 371.51 E-value: 1.55e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 19 APAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGK 98
Cdd:cd07086 8 VGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 99 PLAEARGEIGYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVK 178
Cdd:cd07086 88 ILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 179 PAEQTPLTAYAL-----EVLAlKAGLPADILLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLE 253
Cdd:cd07086 168 PSETTPLTAIAVtkilaEVLE-KNGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 254 LGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDED 333
Cdd:cd07086 246 LGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 334 AITKVQSHIADATAKGATIRIGGQRS--ALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFG 411
Cdd:cd07086 326 AVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQG 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480084072 412 LAAYVFTQS--AARQWRVGEALEYGMVGINTGAISNEV-APFGGVKQSGLGREGSKFGIEEYLEMKYLCVDLS 481
Cdd:cd07086 406 LSSSIFTEDlrEAFRWLGPKGSDCGIVNVNIPTSGAEIgGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
28-478 |
9.47e-124 |
|
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: 368.58 E-value: 9.47e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 28 VKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEAR-GE 106
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 107 IGYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLT 186
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 187 AYALEVLAlKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDA 266
Cdd:cd07092 161 TLLLAELA-AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 267 NLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADAt 346
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERA- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 347 AKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWR 426
Cdd:cd07092 319 PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 480084072 427 VGEALEYGMVGINT-GAISNEvAPFGGVKQSGLGREGSKFGIEEYLEMKYLCV 478
Cdd:cd07092 399 LSARLDFGTVWVNThIPLAAE-MPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
28-474 |
9.19e-123 |
|
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: 366.17 E-value: 9.19e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 28 VKDAATSETLAWVKSYDRAGVEAAIQRSAQA-QAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGE 106
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 107 IGYAASFIRWFAEQARRIDGEVLtPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLT 186
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETI-PLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 187 AYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDA 266
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 267 NLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGrQETSTQGPLIDEDAITKVQSHIADAT 346
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPG-LEDPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 347 AKGATIRIGGQR---SALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAAR 423
Cdd:cd07109 319 ARGARIVAGGRIaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 480084072 424 QWRVGEALEYGMVGINTGAISNEVA-PFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:cd07109 399 ALRVARRLRAGQVFVNNYGAGGGIElPFGGVKKSGHGREKGLEALYNYTQTK 450
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
17-474 |
2.53e-122 |
|
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: 365.36 E-value: 2.53e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 17 FAAPAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQ--RSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTA 94
Cdd:cd07139 7 WVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAaaRRAFDNGPWPRLSPAERAAVLRRLADALEARADELARLWTA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 95 EQGKPLAEAR-GEIGYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGC 173
Cdd:cd07139 87 ENGMPISWSRrAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 174 SMLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLE 253
Cdd:cd07139 167 TVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR-EVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 254 LGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDED 333
Cdd:cd07139 246 LGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASAR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 334 AITKVQSHIADATAKGATIRIGGQRSA--LGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFG 411
Cdd:cd07139 326 QRERVEGYIAKGRAEGARLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYG 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480084072 412 LAAYVFTQSAARQWRVGEALEYGMVGINtGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:cd07139 406 LSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETK 467
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
20-478 |
5.53e-122 |
|
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: 364.32 E-value: 5.53e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 20 PAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKP 99
Cdd:cd07151 6 GTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 100 LAEARGEIGYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKP 179
Cdd:cd07151 86 RIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 180 AEQTPLT-----AYALEvlalKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLEL 254
Cdd:cd07151 166 ASDTPITgglllAKIFE----EAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 255 GGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDA 334
Cdd:cd07151 242 GGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 335 ITKVQSHIADATAKGATIRIGGQRSalgGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAA 414
Cdd:cd07151 322 VDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSG 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480084072 415 YVFTQSAARQWRVGEALEYGMVGINTGAISNE-VAPFGGVKQSGLGREGSKFGIEEYLEMKYLCV 478
Cdd:cd07151 399 AVFTSDLERGVQFARRIDAGMTHINDQPVNDEpHVPFGGEKNSGLGRFNGEWALEEFTTDKWISV 463
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
28-481 |
1.96e-121 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 363.46 E-value: 1.96e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 28 VKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARG-E 106
Cdd:PRK13473 21 VYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNdE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 107 IGYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLT 186
Cdd:PRK13473 101 IPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 187 AYALEVLALKAgLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDA 266
Cdd:PRK13473 181 ALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 267 NLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADAT 346
Cdd:PRK13473 260 DLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 347 AKG-ATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQW 425
Cdd:PRK13473 340 ALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAH 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 480084072 426 RVGEALEYGMVGINT-GAISNEvAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVDLS 481
Cdd:PRK13473 420 RVSARLQYGCTWVNThFMLVSE-MPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKHT 475
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
79-476 |
2.91e-121 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 360.59 E-value: 2.91e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 79 QLVLEHKENLAQILTAEQGKPLAEARGEIGYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPA 158
Cdd:PRK10090 6 AGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 159 AMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRI 238
Cdd:PRK10090 86 FLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 239 LMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGD 318
Cdd:PRK10090 166 IMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 319 -GRQETSTQGPLIDEDAITKVQSHIADATAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKT 397
Cdd:PRK10090 246 pAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 398 EDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK--Y 475
Cdd:PRK10090 326 LEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQvvY 405
|
.
gi 480084072 476 L 476
Cdd:PRK10090 406 L 406
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
19-472 |
6.57e-121 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 363.81 E-value: 6.57e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 19 APAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGK 98
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 99 PLAEARGEIGYAASFIRWFAEQARRIDGE--------VLTptlpnqRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIA 170
Cdd:PRK09407 107 ARRHAFEEVLDVALTARYYARRAPKLLAPrrragalpVLT------KTTELRQPKGVVGVISPWNYPLTLAVSDAIPALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 171 AGCSMLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESdiVRKLSFTGSTQVGRILMQQCAPTIKKL 250
Cdd:PRK09407 181 AGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 251 SLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLI 330
Cdd:PRK09407 259 SLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 331 DEDAITKVQSHIADATAKGATIRIGGQ-RSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTE 409
Cdd:PRK09407 339 SEAQLETVSAHVDDAVAKGATVLAGGKaRPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTP 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480084072 410 FGLAAYVFTQSAARQWRVGEALEYGMVGINTG---AISNEVAPFGGVKQSGLGREGSKFGIEEYLE 472
Cdd:PRK09407 419 YGLNASVWTGDTARGRAIAARIRAGTVNVNEGyaaAWGSVDAPMGGMKDSGLGRRHGAEGLLKYTE 484
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
19-478 |
1.60e-116 |
|
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: 350.97 E-value: 1.60e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 19 APAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQA-QAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQG 97
Cdd:cd07113 10 AGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 98 KPLAEARG-EIGYAASFIRWFAEQARRIDGEVLTPTLPNQR-----LLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAA 171
Cdd:cd07113 90 KSIHLSRAfEVGQSANFLRYFAGWATKINGETLAPSIPSMQgerytAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 172 GCSMLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLS 251
Cdd:cd07113 170 GCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 252 LELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLID 331
Cdd:cd07113 249 LELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLAN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 332 EDAITKVQSHIADATAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFG 411
Cdd:cd07113 329 QPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFG 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480084072 412 LAAYVFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGRE-GSKFgIEEYLEMKYLCV 478
Cdd:cd07113 409 LTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREfGSAF-IDDYTELKSVMI 475
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
17-474 |
2.70e-116 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 351.05 E-value: 2.70e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 17 FAAPAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQA--QAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTA 94
Cdd:PLN02766 29 FVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 95 EQGKPLAEARG-EIGYAASFIRWFAEQARRIDGEVLTPTLPNQRLlVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGC 173
Cdd:PLN02766 109 DAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGY-TLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 174 SMLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPT-IKKLSL 252
Cdd:PLN02766 188 TMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSnLKQVSL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 253 ELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDE 332
Cdd:PLN02766 268 ELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 333 DAITKVQSHIADATAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGL 412
Cdd:PLN02766 348 QQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGL 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480084072 413 AAYVFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:PLN02766 428 AAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVK 489
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
33-472 |
4.88e-116 |
|
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: 348.91 E-value: 4.88e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 33 TSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAAS 112
Cdd:cd07101 5 TGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 113 FIRWFAEQARRidgeVLTP-----TLPN-QRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLT 186
Cdd:cd07101 85 VARYYARRAER----LLKPrrrrgAIPVlTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 187 AYALEVLALKAGLPADILLNISGDAIEVGKTLCE-SDIVrklSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDD 265
Cdd:cd07101 161 ALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDnADYV---MFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 266 ANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADA 345
Cdd:cd07101 238 ADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 346 TAKGATIRIGGQ-RSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQ 424
Cdd:cd07101 318 VAKGATVLAGGRaRPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARG 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 480084072 425 WRVGEALEYGMVGINTG---AISNEVAPFGGVKQSGLGREGSKFGIEEYLE 472
Cdd:cd07101 398 RRIAARLRAGTVNVNEGyaaAWASIDAPMGGMKDSGLGRRHGAEGLLKYTE 448
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
17-480 |
1.34e-115 |
|
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: 348.56 E-value: 1.34e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 17 FAAPAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQ 96
Cdd:cd07559 9 WVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 97 GKPLAEARG-EIGYAASFIRWFAEQARRIDGEVltPTLPNQRL-LVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCS 174
Cdd:cd07559 89 GKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSL--SEIDEDTLsYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 175 MLVKPAEQTPLTAyaLEVLALKAG-LPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLE 253
Cdd:cd07559 167 VVLKPASQTPLSI--LVLMELIGDlLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 254 LGGNAPVLVFDDA-----NLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGP 328
Cdd:cd07559 245 LGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 329 LIDEDAITKVQSHIADATAKGATIRIGGQRSALG----GTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAM 404
Cdd:cd07559 325 QVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480084072 405 ANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVDL 480
Cdd:cd07559 405 ANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILVSY 480
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
26-482 |
3.21e-115 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 348.02 E-value: 3.21e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEAR- 104
Cdd:PRK13252 24 FEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 105 GEIGYAASFIRWFAEQARRIDGEVLtPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTP 184
Cdd:PRK13252 104 VDIVTGADVLEYYAGLAPALEGEQI-PLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 185 LTAYALEVLALKAGLPADILLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFD 264
Cdd:PRK13252 183 LTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 265 DANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIAD 344
Cdd:PRK13252 262 DADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 345 ATAKGATIRIGGQR----SALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQS 420
Cdd:PRK13252 342 GKAEGARLLCGGERltegGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTAD 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480084072 421 AARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVDLSE 482
Cdd:PRK13252 422 LSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMGP 483
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
32-474 |
3.27e-115 |
|
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: 347.80 E-value: 3.27e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 32 ATSETLAWVKSYDRAGVEAAIQRSAQA---QAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEAR-GEI 107
Cdd:cd07141 30 ATGEKICEVQEGDKADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYlVDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 108 GYAASFIRWFAEQARRI-------DGEVLTPTLpnqrllviKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPA 180
Cdd:cd07141 110 PGAIKVLRYYAGWADKIhgktipmDGDFFTYTR--------HEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 181 EQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPT-IKKLSLELGGNAP 259
Cdd:cd07141 182 EQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSnLKRVTLELGGKSP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 260 VLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQ 339
Cdd:cd07141 262 NIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKIL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 340 SHIADATAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQ 419
Cdd:cd07141 342 ELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTK 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 480084072 420 SAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:cd07141 422 DIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVK 476
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
19-474 |
3.74e-115 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 348.26 E-value: 3.74e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 19 APAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQA-----QAVWKKQTALVRADVLLAWYQLVLEHKENLAQILT 93
Cdd:PLN02467 18 EPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLET 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 94 AEQGKPLAEARGEIGYAASFIRWFAEQARRIDGEVLTP-TLP--NQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIA 170
Cdd:PLN02467 98 LDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPvSLPmeTFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 171 AGCSMLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKL 250
Cdd:PLN02467 178 AGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 251 SLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLI 330
Cdd:PLN02467 258 SLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 331 DEDAITKVQSHIADATAKGATIRIGGQRSALG--GTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDT 408
Cdd:PLN02467 338 SEGQYEKVLKFISTAKSEGATILCGGKRPEHLkkGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDS 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480084072 409 EFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:PLN02467 418 HYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
16-474 |
1.89e-114 |
|
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: 345.63 E-value: 1.89e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 16 SFAAPAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQ--RSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILT 93
Cdd:cd07142 11 QFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKaaRKAFDEGPWPRMTGYERSRILLRFADLLEKHADELAALET 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 94 AEQGKPLAEAR-GEIGYAASFIRWFAEQARRIDGEVLtPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAG 172
Cdd:cd07142 91 WDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTL-PADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 173 CSMLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPT-IKKLS 251
Cdd:cd07142 170 NTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSnLKPVT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 252 LELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLID 331
Cdd:cd07142 250 LELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 332 EDAITKVQSHIADATAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFG 411
Cdd:cd07142 330 KEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYG 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480084072 412 LAAYVFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:cd07142 410 LAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
28-474 |
2.46e-113 |
|
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: 342.03 E-value: 2.46e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 28 VKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPL-AEARGE 106
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 107 IGYAASFIRWFAEQARRIDGEVLtPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLT 186
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETL-PFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 187 AYAL-EVLAlkAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDD 265
Cdd:cd07108 160 VLLLaEILA--QVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 266 ANLDQAVQGIMAS-KYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIAD 344
Cdd:cd07108 238 ADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 345 A-TAKGATIRIGGQRSALG----GTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQ 419
Cdd:cd07108 318 GlSTSGATVLRGGPLPGEGpladGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 480084072 420 SAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFG-IEEYLEMK 474
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKK 453
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
17-480 |
1.87e-112 |
|
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: 340.66 E-value: 1.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 17 FAAPAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQA-QAVWKKQ-TALVRADVLLAWYQLVLEHKENLAQILTA 94
Cdd:cd07143 15 FVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLMERNLDYLASIEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 95 EQGKP-LAEARGEIGYAASFIRWFAEQARRIDGEVLTpTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGC 173
Cdd:cd07143 95 DNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIE-TDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 174 SMLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPT-IKKLSL 252
Cdd:cd07143 174 TIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSnLKKVTL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 253 ELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDE 332
Cdd:cd07143 254 ELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 333 DAITKVQSHIADATAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGL 412
Cdd:cd07143 334 IQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGL 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480084072 413 AAYVFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVDL 480
Cdd:cd07143 414 AAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
26-480 |
3.20e-112 |
|
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: 339.82 E-value: 3.20e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARG 105
Cdd:cd07117 18 IDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 106 -EIGYAASFIRWFAEQARRIDGEVltpTLPNQRLL--VIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQ 182
Cdd:cd07117 98 vDIPLAADHFRYFAGVIRAEEGSA---NMIDEDTLsiVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 183 TPLTAyaLEVLAL-KAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVL 261
Cdd:cd07117 175 TSLSL--LELAKIiQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 262 VFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSH 341
Cdd:cd07117 253 IFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 342 IADATAKGATIRIGGQRSALG----GTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVF 417
Cdd:cd07117 333 VDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVF 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480084072 418 TQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVDL 480
Cdd:cd07117 413 TKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
35-478 |
1.17e-110 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 334.65 E-value: 1.17e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 35 ETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAASFI 114
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 115 RWFAEQARRIDGEVLtPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYAL--EV 192
Cdd:cd07152 82 HEAAGLPTQPQGEIL-PSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVViaRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 193 LALkAGLPADILLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAV 272
Cdd:cd07152 161 FEE-AGLPAGVLHVLPGGA-DAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 273 QGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAKGATI 352
Cdd:cd07152 239 SNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 353 RIGGQRSalgGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALE 432
Cdd:cd07152 319 EAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 480084072 433 YGMVGINTGAISNE-VAPFGGVKQSGLG-REGSKFGIEEYLEMKYLCV 478
Cdd:cd07152 396 TGMLHINDQTVNDEpHNPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
36-479 |
9.84e-107 |
|
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: 325.99 E-value: 9.84e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 36 TLAWVKSYDRAgVEAAiqRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEA-RGEIGYAASFI 114
Cdd:cd07140 38 SLATVEDVDRA-VAAA--KEAFENGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLAlKTHVGMSIQTF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 115 RWFAEQARRIDGEVL--TPTLPNQRL-LVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALE 191
Cdd:cd07140 115 RYFAGWCDKIQGKTIpiNQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 192 VLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPT-IKKLSLELGGNAPVLVFDDANLDQ 270
Cdd:cd07140 195 ELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSnLKKVSLELGGKSPLIIFADCDMDK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 271 AVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAKGA 350
Cdd:cd07140 275 AVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 351 TIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTED-EAV-AMANDTEFGLAAYVFTQSAARQWRVG 428
Cdd:cd07140 355 TLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDvDGVlQRANDTEYGLASGVFTKDINKALYVS 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 480084072 429 EALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVD 479
Cdd:cd07140 435 DKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIE 485
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
26-468 |
3.50e-106 |
|
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: 324.14 E-value: 3.50e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALV-RADVLLAWYQLVLEHKENLAQILTAEQGKPLAEAR 104
Cdd:cd07082 18 IEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLEeRIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 105 GEIGYAASFIRWFAEQARRIDGEVLTPTLPNQRL----LVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPA 180
Cdd:cd07082 98 KEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 181 EQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQcAPtIKKLSLELGGNAPV 260
Cdd:cd07082 178 TQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ-HP-MKRLVLELGGKDPA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 261 LVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQS 340
Cdd:cd07082 256 IVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 341 HIADATAKGATIRIGGQRsaLGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQS 420
Cdd:cd07082 336 LIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKD 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 480084072 421 AARQWRVGEALEYGMVGINTG-AISNEVAPFGGVKQSGLGREGSKFGIE 468
Cdd:cd07082 414 INKARKLADALEVGTVNINSKcQRGPDHFPFLGRKDSGIGTQGIGDALR 462
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
44-468 |
2.29e-105 |
|
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: 321.50 E-value: 2.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 44 DRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAASFIRWFAEQARR 123
Cdd:cd07102 16 SLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 124 IDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLALKAGLPADI 203
Cdd:cd07102 96 ALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 204 LLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNS 283
Cdd:cd07102 176 FQVLHLSH-ETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 284 GQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAKGATIRIGGQR---SA 360
Cdd:cd07102 255 GQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALfpeDK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 361 LGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINT 440
Cdd:cd07102 335 AGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNR 414
|
410 420
....*....|....*....|....*...
gi 480084072 441 GAISNEVAPFGGVKQSGLGREGSKFGIE 468
Cdd:cd07102 415 CDYLDPALAWTGVKDSGRGVTLSRLGYD 442
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
17-476 |
1.95e-103 |
|
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: 317.42 E-value: 1.95e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 17 FAAPAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQ 96
Cdd:cd07111 30 WVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 97 GKPLAEAR-GEIGYAASFIRWFAEQARRIDGEvltptLPNQrllvikQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSM 175
Cdd:cd07111 110 GKPIRESRdCDIPLVARHFYHHAGWAQLLDTE-----LAGW------KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 176 LVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELG 255
Cdd:cd07111 179 VLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 256 GNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAI 335
Cdd:cd07111 258 GKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 336 TKVQSHIADATAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAY 415
Cdd:cd07111 338 KRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAAS 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480084072 416 VFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYL 476
Cdd:cd07111 418 VWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWE 478
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
28-480 |
3.80e-103 |
|
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: 315.85 E-value: 3.80e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 28 VKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEI 107
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 108 GYAASFIRWFAEQARRIDGEVLtPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTA 187
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETI-PVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 188 YALEVLALKAgLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDAN 267
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 268 LDQAVQGIMAS-KYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADAT 346
Cdd:cd07107 239 PEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 347 AKGATIRIGGQRS---AL-GGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAA 422
Cdd:cd07107 319 REGARLVTGGGRPegpALeGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 480084072 423 RQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVDL 480
Cdd:cd07107 399 QAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
26-474 |
4.41e-101 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 310.52 E-value: 4.41e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETlawVKSYDRAG---VEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAE 102
Cdd:PRK09406 3 IATINPATGET---VKTFTALTddeVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 103 ARGEIGYAASFIRWFAEQARRI--DGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPA 180
Cdd:PRK09406 80 AKAEALKCAKGFRYYAEHAEALlaDEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 181 EQTPLTAYALEVLALKAGLPADIL--LNISGDAIEvgkTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNA 258
Cdd:PRK09406 160 SNVPQTALYLADLFRRAGFPDGCFqtLLVGSGAVE---AILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 259 PVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKV 338
Cdd:PRK09406 237 PFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 339 QSHIADATAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFT 418
Cdd:PRK09406 317 EKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWT 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 480084072 419 QSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:PRK09406 397 RDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIK 452
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
31-471 |
1.43e-99 |
|
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: 308.38 E-value: 1.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 31 AATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYA 110
Cdd:cd07124 54 ADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 111 ASFIRWFAEQARRIDGEVLTPtLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYAL 190
Cdd:cd07124 134 IDFLEYYAREMLRLRGFPVEM-VPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 191 EVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPT------IKKLSLELGGNAPVLVFD 264
Cdd:cd07124 213 VEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpgqkwLKRVIAEMGGKNAIIVDE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 265 DANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIAD 344
Cdd:cd07124 293 DADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 345 ATaKGATIRIGGQRSAL--GGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAA 422
Cdd:cd07124 373 GK-SEGRLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPE 451
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 480084072 423 RQWRVGEALEYGMVGIN---TGAISnEVAPFGGVKQSGLgreGSKFGIEEYL 471
Cdd:cd07124 452 HLERARREFEVGNLYANrkiTGALV-GRQPFGGFKMSGT---GSKAGGPDYL 499
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
30-474 |
6.38e-99 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 307.50 E-value: 6.38e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 30 DAATSETLAWVKSYDRAGVEAAIQ--RSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARG-E 106
Cdd:PLN02466 79 DPRTGEVIAHVAEGDAEDVNRAVAaaRKAFDEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKaE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 107 IGYAASFIRWFAEQARRIDGEVLtPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLT 186
Cdd:PLN02466 159 LPMFARLFRYYAGWADKIHGLTV-PADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLS 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 187 AYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPT-IKKLSLELGGNAPVLVFDD 265
Cdd:PLN02466 238 ALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSnLKPVTLELGGKSPFIVCED 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 266 ANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADA 345
Cdd:PLN02466 318 ADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSG 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 346 TAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQW 425
Cdd:PLN02466 398 VESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTAN 477
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 480084072 426 RVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:PLN02466 478 TLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
30-479 |
8.57e-99 |
|
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: 304.99 E-value: 8.57e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 30 DAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEAR-GEIG 108
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 109 YAASFIRWFAEQarridGE-VLTP-TLPNQRLLVIKQA------IGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPA 180
Cdd:cd07098 82 VTCEKIRWTLKH-----GEkALRPeSRPGGLLMFYKRArveyepLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 181 EQTPL-TAYALEVL--ALKA-GLPADILLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGG 256
Cdd:cd07098 157 EQVAWsSGFFLSIIreCLAAcGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 257 NAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAIT 336
Cdd:cd07098 236 KDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 337 KVQSHIADATAKGATIRIGGQRSAL----GGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGL 412
Cdd:cd07098 316 RLEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480084072 413 AAYVFTQSAARQWRVGEALEYGMVGINTGAIS--NEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVD 479
Cdd:cd07098 396 GASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTED 464
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
26-459 |
1.17e-92 |
|
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: 289.42 E-value: 1.17e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARG 105
Cdd:cd07085 18 LDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 106 EIGYAASFIrwfaEQARRIDGEVLTPTLPNQR----LLVIKQAIGVTAAITPWNFPAaMITR-KAAPAIAAGCSMLVKPA 180
Cdd:cd07085 98 DVLRGLEVV----EFACSIPHLLKGEYLENVArgidTYSYRQPLGVVAGITPFNFPA-MIPLwMFPMAIACGNTFVLKPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 181 EQTPLTAYALEVLALKAGLPADILLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPV 260
Cdd:cd07085 173 ERVPGAAMRLAELLQEAGLPDGVLNVVHGGK-EAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 261 LVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQS 340
Cdd:cd07085 252 VVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 341 HIADATAKGATIRIGGQRSAL----GGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYV 416
Cdd:cd07085 332 LIESGVEEGAKLVLDGRGVKVpgyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAI 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 480084072 417 FTQS--AARQWRvgEALEYGMVGINTGaISNEVA--PFGGVKQSGLG 459
Cdd:cd07085 412 FTRSgaAARKFQ--REVDAGMVGINVP-IPVPLAffSFGGWKGSFFG 455
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
17-480 |
1.30e-92 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 289.87 E-value: 1.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 17 FAAPAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQ--RSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTA 94
Cdd:PRK09847 28 YTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSaaRGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 95 EQGKPLAEA-RGEIGYAASFIRWFAEQARRIDGEVlTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGC 173
Cdd:PRK09847 108 DTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEV-ATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 174 SMLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPT-IKKLSL 252
Cdd:PRK09847 187 SVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSnMKRVWL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 253 ELGGNAPVLVFDDA-NLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLID 331
Cdd:PRK09847 267 EAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLID 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 332 EDAITKVQSHIADATAKGaTIRIGGQRSALGGtFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFG 411
Cdd:PRK09847 347 CAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYG 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480084072 412 LAAYVFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVDL 480
Cdd:PRK09847 425 LGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
20-470 |
1.08e-91 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 286.37 E-value: 1.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 20 PAAHNdIEVkDAATSETLA---WVKSYDragVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQ 96
Cdd:PRK13968 5 PATHA-ISV-NPATGEQLSvlpWAGADD---IENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 97 GKPLAEARGEIGYAASFIRWFAEQA-RRIDGEvltPTL-PNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCS 174
Cdd:PRK13968 80 GKPINQARAEVAKSANLCDWYAEHGpAMLKAE---PTLvENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 175 MLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVrKLSFTGSTQVGRILMQQCAPTIKKLSLEL 254
Cdd:PRK13968 157 YLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIA-AVTVTGSVRAGAAIGAQAGAALKKCVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 255 GGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDA 334
Cdd:PRK13968 236 GGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 335 ITKVQSHIADATAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAA 414
Cdd:PRK13968 316 RDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 480084072 415 YVFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEY 470
Cdd:PRK13968 396 TIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
31-471 |
1.31e-85 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 272.19 E-value: 1.31e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 31 AATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYA 110
Cdd:PRK03137 58 ANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 111 ASFIRWFAEQARRI-DGEVLTPtLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYA 189
Cdd:PRK03137 138 IDFLEYYARQMLKLaDGKPVES-RPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 190 L-EVLaLKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPT------IKKLSLELGGNAPVLV 262
Cdd:PRK03137 217 FvEVL-EEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVqpgqiwLKRVIAEMGGKDAIVV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 263 FDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGrQETSTQGPLIDEDAITKVQSHI 342
Cdd:PRK03137 296 DEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNAYMGPVINQASFDKIMSYI 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 343 ADATAKGATIrIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAA 422
Cdd:PRK03137 375 EIGKEEGRLV-LGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNRE 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 480084072 423 RQWRVGEALEYGMVGIN---TGAISNeVAPFGGVKQSGlgrEGSKFGIEEYL 471
Cdd:PRK03137 454 HLEKARREFHVGNLYFNrgcTGAIVG-YHPFGGFNMSG---TDSKAGGPDYL 501
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
25-463 |
3.63e-81 |
|
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: 259.45 E-value: 3.63e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 25 DIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEAR 104
Cdd:cd07130 13 VVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 105 GEI-------GYAASfirwfaeQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLV 177
Cdd:cd07130 93 GEVqemidicDFAVG-------LSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 178 KPAEQTPLTAYALEVLALKA----GLPADILLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLE 253
Cdd:cd07130 166 KPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGA-DVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 254 LGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDED 333
Cdd:cd07130 245 LGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 334 AITKVQSHIADATAKGATIRIGGQRSALGGTFFEPTVLTnVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLA 413
Cdd:cd07130 325 AVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLS 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 480084072 414 AYVFTQS--AARQWRVGEALEYGMVGINTGAISNEV-APFGGVKQSGLGRE-GS 463
Cdd:cd07130 404 SSIFTTDlrNAFRWLGPKGSDCGIVNVNIGTSGAEIgGAFGGEKETGGGREsGS 457
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
20-474 |
8.05e-81 |
|
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: 258.93 E-value: 8.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 20 PAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQ--RSAQAQAVWKKQTALvRADVLLAWYQLVLEHKENLAQILTAEQG 97
Cdd:TIGR04284 11 AGSAGTFPTVNPATEEVLGVAADATAADMDAAIAaaRRAFDETDWSRDTAL-RVRCLRQLRDALRAHVEELRELTIAEVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 98 KPL-----AEARGEIGYaasfIRWFAEQARRID-----GEVLTPTLPNQRLLViKQAIGVTAAITPWNFPAAMITRKAAP 167
Cdd:TIGR04284 90 APRmltagAQLEGPVDD----LGFAADLAESYAwttdlGVASPMGIPTRRTLR-REAVGVVGAITPWNFPHQINLAKLGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 168 AIAAGCSMLVKPAEQTPLTAYAL-EVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPT 246
Cdd:TIGR04284 165 ALAAGNTVVLKPAPDTPWCAAVLgELIAEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMADAAAT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 247 IKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQ 326
Cdd:TIGR04284 245 LKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPGTVC 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 327 GPLIDEDAITKVQSHIADATAKGATIRIGGQRSA--LGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAM 404
Cdd:TIGR04284 325 GPVISARQRDRVQSYLDLAVAEGGRFACGGGRPAdrDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 405 ANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMK 474
Cdd:TIGR04284 405 ANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETK 474
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
17-478 |
2.66e-80 |
|
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: 257.38 E-value: 2.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 17 FAAPAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQ 96
Cdd:cd07116 9 WVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 97 GKPLAEARG-EIGYAASFIRWFAEQARRIDGEVltPTLPNQRLLV-IKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCS 174
Cdd:cd07116 89 GKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSI--SEIDENTVAYhFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 175 MLVKPAEQTPLTAYAL-EVLAlkAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLE 253
Cdd:cd07116 167 VVLKPAEQTPASILVLmELIG--DLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 254 LGGNAPVLVF------DDANLDQAVQGIMASKYrNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQG 327
Cdd:cd07116 245 LGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 328 PLIDEDAITKVQSHIADATAKGATIRIGGQRSAL-----GGTFFEPTVLTNvtQDMKVSKEETFGPLAPLFRFKTEDEAV 402
Cdd:cd07116 324 AQASLEQLEKILSYIDIGKEEGAEVLTGGERNELggllgGGYYVPTTFKGG--NKMRIFQEEIFGPVLAVTTFKDEEEAL 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480084072 403 AMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCV 478
Cdd:cd07116 402 EIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
26-462 |
9.90e-80 |
|
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: 255.42 E-value: 9.90e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVKSYDRAGVEAAIQRsaqAQAVWKKQT----ALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLA 101
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDT---AHALFLDRNnwlpAHERIAILERLADLMEERADELALLIAREGGKPLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 102 EARGEIGYAASFIRWFAEQARRIDG-EV---LTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLV 177
Cdd:cd07148 78 DAKVEVTRAIDGVELAADELGQLGGrEIpmgLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 178 KPAEQTPLTAYALEVLALKAGLPADILLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTiKKLSLELGGN 257
Cdd:cd07148 158 KPALATPLSCLAFVDLLHEAGLPEGWCQAVPCEN-AVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 258 APVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITK 337
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 338 VQSHIADATAKGATIRIGGQRsaLGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVF 417
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKR--LSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 480084072 418 TQSAARQWRVGEALEYGMVGINT-GAISNEVAPFGGVKQSGLGREG 462
Cdd:cd07148 394 TKDLDVALKAVRRLDATAVMVNDhTAFRVDWMPFAGRRQSGYGTGG 439
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
48-467 |
2.66e-79 |
|
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: 253.35 E-value: 2.66e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 48 VEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAASFIRWFAEQARRIDGE 127
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 128 VLTPTlPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLALKAGLPADILlNI 207
Cdd:cd07095 82 RATPM-AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVL-NL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 208 SGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCA--PTiKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQ 285
Cdd:cd07095 160 VQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAgrPG-KILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 286 TCVCANRIYVQDGIY-DALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAKGATIRIGGQRSALGGT 364
Cdd:cd07095 239 RCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 365 FFEPTVLtNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGIN---TG 441
Cdd:cd07095 319 FLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNrptTG 397
|
410 420
....*....|....*....|....*.
gi 480084072 442 AISNevAPFGGVKQSGLGREGSKFGI 467
Cdd:cd07095 398 ASST--APFGGVGLSGNHRPSAYYAA 421
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
28-471 |
2.27e-76 |
|
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: 248.24 E-value: 2.27e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 28 VKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEI 107
Cdd:TIGR01237 51 INPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 108 GYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTA 187
Cdd:TIGR01237 131 AEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 188 YALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVG-RI-----LMQQCAPTIKKLSLELGGNAPVL 261
Cdd:TIGR01237 211 AKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGtRIferaaKVQPGQKHLKRVIAEMGGKDTVI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 262 VFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSH 341
Cdd:TIGR01237 291 VDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEY 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 342 IADATAKGATIrIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSA 421
Cdd:TIGR01237 371 IEIGKAEGRLV-SGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNR 449
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 480084072 422 ARQWRVGEALEYGMVGIN---TGAISNeVAPFGGVKQSGLgreGSKFGIEEYL 471
Cdd:TIGR01237 450 DHINRAKAEFEVGNLYFNrniTGAIVG-YQPFGGFKMSGT---DSKAGGPDYL 498
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
28-474 |
2.21e-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: 245.18 E-value: 2.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 28 VKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEI 107
Cdd:cd07083 37 VSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 108 GYAASFIRWFAEQARRIDGE-VLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLT 186
Cdd:cd07083 117 AEAIDFIRYYARAALRLRYPaVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 187 AYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCA------PTIKKLSLELGGNAPV 260
Cdd:cd07083 197 GYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAArlapgqTWFKRLYVETGGKNAI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 261 LVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQS 340
Cdd:cd07083 277 IVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 341 HIADATAKGaTIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTED--EAVAMANDTEFGL-AAYVF 417
Cdd:cd07083 357 YIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLtGGVYS 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480084072 418 TQSAARQWrVGEALEYGMVGIN---TGAISNeVAPFGGVKQSGLG-REGSKFGIEEYLEMK 474
Cdd:cd07083 436 RKREHLEE-ARREFHVGNLYINrkiTGALVG-VQPFGGFKLSGTNaKTGGPHYLRRFLEMK 494
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
70-469 |
1.43e-73 |
|
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: 238.19 E-value: 1.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 70 RADVLLAWYQLVLEHKENLAQILTAEQGKPLAEA--------RGEIGYAASFIRWFAEQaRRIDgevLTPTLPNQRLLVI 141
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteiavvLGEIDHALKHLKKWMKP-RRVS---VPLLLQPAKAYVI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 142 KQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLaLKAGLPADILLNISGDAiEVGKTLCES 221
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKL-IPKYFDPEAVAVVEGGV-EVATALLAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 222 --D-IVrklsFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDG 298
Cdd:cd07087 176 pfDhIF----FTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 299 IYDALADRLVEAVAKLQvGDGRQETSTQGPLIDEDAITKVQSHIadataKGATIRIGGQRSAlGGTFFEPTVLTNVTQDM 378
Cdd:cd07087 252 IKDELIEELKKAIKEFY-GEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQVDK-EERYIAPTILDDVSPDS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 379 KVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAI--SNEVAPFGGVKQS 456
Cdd:cd07087 325 PLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLhaAIPNLPFGGVGNS 404
|
410
....*....|...
gi 480084072 457 GLGREGSKFGIEE 469
Cdd:cd07087 405 GMGAYHGKAGFDT 417
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
31-471 |
1.93e-73 |
|
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: 240.56 E-value: 1.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 31 AATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYA 110
Cdd:cd07125 54 ADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 111 ASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYAL 190
Cdd:cd07125 134 IDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 191 EVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAP---TIKKLSLELGG-NApVLVFDDA 266
Cdd:cd07125 214 VELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAErdgPILPLIAETGGkNA-MIVDSTA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 267 NLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADAT 346
Cdd:cd07125 293 LPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 347 AKgATIRIGGQRSALGGTFFEPTVLTNVTQDmkVSKEETFGPLAPLFRFKTE--DEAVAMANDTEFGLAAYVFT--QSAA 422
Cdd:cd07125 373 GE-AWLIAPAPLDDGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSrdEREI 449
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 480084072 423 RQWRvgEALEYGMVGIN---TGAISnEVAPFGGVKQSGLgreGSKFGIEEYL 471
Cdd:cd07125 450 EYWR--ERVEAGNLYINrniTGAIV-GRQPFGGWGLSGT---GPKAGGPNYL 495
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
46-470 |
2.64e-72 |
|
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: 235.20 E-value: 2.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 46 AGVEAAIQRSAQAqavWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEAR--------GEIGYAASFI-RW 116
Cdd:cd07134 1 RRVFAAQQAHALA---LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilpvlSEINHAIKHLkKW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 117 FAEQarridgEVLTP-TLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLAL 195
Cdd:cd07134 78 MKPK------RVRTPlLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 196 KAGLPADILLnISGDAiEVGKTLcesdivrkLS-------FTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANL 268
Cdd:cd07134 152 EAFDEDEVAV-FEGDA-EVAQAL--------LElpfdhifFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 269 DQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAK-LQVGDGRQETSTQGPLIDEDAITKVQSHIADATA 347
Cdd:cd07134 222 KKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKfYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 348 KGATIRIGGQRSAlGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRV 427
Cdd:cd07134 302 KGAKVEFGGQFDA-AQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKV 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 480084072 428 GEALEYGMVGINTGAI--SNEVAPFGGVKQSGLGREGSKFGIEEY 470
Cdd:cd07134 381 LARTSSGGVVVNDVVLhfLNPNLPFGGVNNSGIGSYHGVYGFKAF 425
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
25-457 |
4.04e-71 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 233.70 E-value: 4.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 25 DIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEAR 104
Cdd:PRK09457 16 AFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 105 GE----IGYAASFIRWFAEQArridGEVLTPTLPNQRLLVIKqAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPA 180
Cdd:PRK09457 96 TEvtamINKIAISIQAYHERT----GEKRSEMADGAAVLRHR-PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 181 EQTPLTAYALEVLALKAGLPADIlLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKK-LSLELGGNAP 259
Cdd:PRK09457 171 ELTPWVAELTVKLWQQAGLPAGV-LNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKiLALEMGGNNP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 260 VLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIY-DALADRLVEAVAKLQVGDGRQETST-QGPLIDEDAITK 337
Cdd:PRK09457 250 LVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDAEPQPfMGAVISEQAAQG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 338 VQSHIADATAKGATIRIGGQRSALGGTFFEPTVLtNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVF 417
Cdd:PRK09457 330 LVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLL 408
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 480084072 418 TQSAARQWRVGEALEYGMVGIN---TGAISNevAPFGGVKQSG 457
Cdd:PRK09457 409 SDDREDYDQFLLEIRAGIVNWNkplTGASSA--APFGGVGASG 449
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
59-460 |
1.25e-64 |
|
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: 215.04 E-value: 1.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 59 QAVWKKQ---TALVRADVLLAWYQLVLEHKENLAQILTAEQGK------PLAE---ARGEIGYAASFI-RWFAEQARRID 125
Cdd:cd07133 8 KAAFLANpppSLEERRDRLDRLKALLLDNQDALAEAISADFGHrsrhetLLAEilpSIAGIKHARKHLkKWMKPSRRHVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 126 gevlTPTLPNqRLLVIKQAIGVTAAITPWNFP-----AAMITrkaapAIAAGCSMLVKPAEQTPLTAyalEVLA--LKAG 198
Cdd:cd07133 88 ----LLFLPA-KAEVEYQPLGVVGIIVPWNYPlylalGPLIA-----ALAAGNRVMIKPSEFTPRTS---ALLAelLAEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 199 LPADILLNISGDAiEVGKTLCES--DivrKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIM 276
Cdd:cd07133 155 FDEDEVAVVTGGA-DVAAAFSSLpfD---HLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 277 ASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKL--QVGDGRQETStqgpLIDEDAITKVQSHIADATAKGAT-IR 353
Cdd:cd07133 231 FGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMypTLADNPDYTS----IINERHYARLQGLLEDARAKGARvIE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 354 IGGQRSALGGT-FFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALE 432
Cdd:cd07133 307 LNPAGEDFAATrKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTH 386
|
410 420 430
....*....|....*....|....*....|
gi 480084072 433 YGMVGINTGA--ISNEVAPFGGVKQSGLGR 460
Cdd:cd07133 387 SGGVTINDTLlhVAQDDLPFGGVGASGMGA 416
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
75-470 |
4.77e-62 |
|
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: 208.61 E-value: 4.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 75 LAWyqLVLEHKENLAQILTAEQGKP-----LAE---ARGEIGYAASFIRWFAEqarriDGEVLTPTLPNQ--RLLVIKQA 144
Cdd:cd07135 36 LYW--AVKDNEEAIVEALKKDLGRPpfetlLTEvsgVKNDILHMLKNLKKWAK-----DEKVKDGPLAFMfgKPRIRKEP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 145 IGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLaLKAGLPADILLNISGDAIEVGKTL-CESDi 223
Cdd:cd07135 109 LGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVVQGGVPETTALLeQKFD- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 224 vrKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDAL 303
Cdd:cd07135 187 --KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 304 ADRLVEAVAKLqVGDGRQETSTQGPLIDEDAITKVQSHIadATAKGaTIRIGGQRSAlGGTFFEPTVLTNVTQDMKVSKE 383
Cdd:cd07135 265 VEELKKVLDEF-YPGGANASPDYTRIVNPRHFNRLKSLL--DTTKG-KVVIGGEMDE-ATRFIPPTIVSDVSWDDSLMSE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 384 ETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAI--SNEVAPFGGVKQSGLGRE 461
Cdd:cd07135 340 ELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPFGGVGDSGYGAY 419
|
....*....
gi 480084072 462 GSKFGIEEY 470
Cdd:cd07135 420 HGKYGFDTF 428
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
21-481 |
4.30e-61 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 207.69 E-value: 4.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 21 AAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPL 100
Cdd:PLN00412 28 SSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 101 AEARGEIGYAASFIRWFAEQARRIDGE---VLTPTLP----NQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGC 173
Cdd:PLN00412 108 KDAVTEVVRSGDLISYTAEEGVRILGEgkfLVSDSFPgnerNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 174 SMLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTG-------STQVGRILMQqcapt 246
Cdd:PLN00412 188 AVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGgdtgiaiSKKAGMVPLQ----- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 247 ikklsLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGrQETSTQ 326
Cdd:PLN00412 263 -----MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 327 GPLIDEDAITKVQSHIADATAKGATIRIGGQRSalgGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMAN 406
Cdd:PLN00412 337 TPVVSESSANFIEGLVMDAKEKGATFCQEWKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCN 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480084072 407 DTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTG-AISNEVAPFGGVKQSGLGREGSKFGIEEYLEMKYLCVDLS 481
Cdd:PLN00412 414 ASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKSTVINLP 489
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
78-460 |
3.75e-60 |
|
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: 203.89 E-value: 3.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 78 YQLVLEHKENLAQILTAEQGKPLAEAR-GEIGYAASFIRWFAE------QARRidgeVLTPtLPNQ--RLLVIKQAIGVT 148
Cdd:cd07136 30 KQAIKKYENEILEALKKDLGKSEFEAYmTEIGFVLSEINYAIKhlkkwmKPKR----VKTP-LLNFpsKSYIYYEPYGVV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 149 AAITPWNFPAAMItrkAAP---AIAAGCSMLVKPAEQTPLTAyalEVLA--LKAGLPADILLNISGDaIEVGKTLCESDi 223
Cdd:cd07136 105 LIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTS---KVIAkiIEETFDEEYVAVVEGG-VEENQELLDQK- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 224 VRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDAL 303
Cdd:cd07136 177 FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 304 ADRLVEAVaKLQVGDGRQETSTQGPLIDEDAITKVQSHIadataKGATIRIGGQRSAlGGTFFEPTVLTNVTQDMKVSKE 383
Cdd:cd07136 257 IKELKEEI-KKFYGEDPLESPDYGRIINEKHFDRLAGLL-----DNGKIVFGGNTDR-ETLYIEPTILDNVTWDDPVMQE 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480084072 384 ETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAI--SNEVAPFGGVKQSGLGR 460
Cdd:cd07136 330 EIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMhlANPYLPFGGVGNSGMGS 408
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
16-439 |
3.78e-56 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 196.89 E-value: 3.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 16 SFAAPAAHNDIEVKDAATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAE 95
Cdd:PLN02419 121 SFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 96 QGKPLAEARGEIGYAASFIRWFAEQARRIDGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSM 175
Cdd:PLN02419 201 QGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 176 LVKPAEQTPLTAYALEVLALKAGLPaDILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELG 255
Cdd:PLN02419 281 ILKPSEKDPGASVILAELAMEAGLP-DGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMG 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 256 GNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVC-ANRIYVQDGiyDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDA 334
Cdd:PLN02419 360 AKNHGLVLPDANIDATLNALLAAGFGAAGQRCMAlSTVVFVGDA--KSWEDKLVERAKALKVTCGSEPDADLGPVISKQA 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 335 ITKVQSHIADATAKGATIRIGGQRSAL----GGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEF 410
Cdd:PLN02419 438 KERICRLIQSGVDDGAKLLLDGRDIVVpgyeKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKY 517
|
410 420
....*....|....*....|....*....
gi 480084072 411 GLAAYVFTQSAARQWRVGEALEYGMVGIN 439
Cdd:PLN02419 518 GNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
70-468 |
4.78e-56 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 194.09 E-value: 4.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 70 RADVLLAWYQLVLEHKENLAQILTAEQGKPLAEA--------RGEIGYAASFIRWFAeQARRIDGEVLTptLPNQRLLvI 141
Cdd:PTZ00381 31 RKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETkmtevlltVAEIEHLLKHLDEYL-KPEKVDTVGVF--GPGKSYI-I 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 142 KQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLALKAgLPADILLNISGDAiEVGKTLCES 221
Cdd:PTZ00381 107 PEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGV-EVTTELLKE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 222 --DIVrklSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGI 299
Cdd:PTZ00381 185 pfDHI---FFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 300 YDALADRLVEAVaKLQVGDGRQETSTQGPLIDEDAITKVQSHIADataKGATIRIGGQRSaLGGTFFEPTVLTNVTQDMK 379
Cdd:PTZ00381 262 KDKFIEALKEAI-KEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVD-IENKYVAPTIIVNPDLDSP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 380 VSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGA--ISNEVAPFGGVKQSG 457
Cdd:PTZ00381 337 LMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVfhLLNPNLPFGGVGNSG 416
|
410
....*....|.
gi 480084072 458 LGREGSKFGIE 468
Cdd:PTZ00381 417 MGAYHGKYGFD 427
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
20-459 |
9.22e-53 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 192.00 E-value: 9.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 20 PAAHNDI--EVKDAATSEtlawvksydragVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQG 97
Cdd:PRK11905 574 PADHDDVvgTVTEASAED------------VERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 98 KPLAEARGEIGYAASFIRWFAEQARRidgevltpTLPNQRLlvikQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLV 177
Cdd:PRK11905 642 KTLANAIAEVREAVDFLRYYAAQARR--------LLNGPGH----KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLA 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 178 KPAEQTPLTA-YALEVLaLKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKK---LSLE 253
Cdd:PRK11905 710 KPAEQTPLIAaRAVRLL-HEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpvpLIAE 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 254 LGG-NApVLVFDDANLDQAVQGIMASKYRNSGQTCvCANRI-YVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLID 331
Cdd:PRK11905 789 TGGqNA-MIVDSSALPEQVVADVIASAFDSAGQRC-SALRVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVID 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 332 EDAITKVQSHIADATAKGATI-RIGGQRSALGGTFFEPTVLTnvTQDMKVSKEETFGPLAPLFRFKTE--DEAVAMANDT 408
Cdd:PRK11905 867 AEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKADelDRVIDDINAT 944
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 480084072 409 EFGLAAYVFTQSAARQWRVGEALEYGMVGIN---TGAISNeVAPFGGVKQSGLG 459
Cdd:PRK11905 945 GYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrniIGAVVG-VQPFGGEGLSGTG 997
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
49-471 |
9.62e-53 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 185.42 E-value: 9.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 49 EAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAASFIRWFAEQARRIDGEV 128
Cdd:PLN02315 59 EEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 129 LTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYAL-----EVLAlKAGLPADI 203
Cdd:PLN02315 139 IPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMtklvaEVLE-KNNLPGAI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 204 LLNISGDAiEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNS 283
Cdd:PLN02315 218 FTSFCGGA-EIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 284 GQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAKGATIRIGGQRSALGG 363
Cdd:PLN02315 297 GQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 364 TFFEPTVLtNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAAR--QWRVGEALEYGMVGINTG 441
Cdd:PLN02315 377 NFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETifKWIGPLGSDCGIVNVNIP 455
|
410 420 430
....*....|....*....|....*....|.
gi 480084072 442 AISNEV-APFGGVKQSGLGREGSKFGIEEYL 471
Cdd:PLN02315 456 TNGAEIgGAFGGEKATGGGREAGSDSWKQYM 486
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
31-471 |
2.54e-52 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 190.41 E-value: 2.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 31 AATSETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYA 110
Cdd:PRK11904 570 ADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREA 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 111 ASFIRWFAEQARRIDGEvlTPTLP------NQRLLvikQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTP 184
Cdd:PRK11904 650 VDFCRYYAAQARRLFGA--PEKLPgptgesNELRL---HGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTP 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 185 LTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCA-------PTIKklslELGG- 256
Cdd:PRK11904 725 LIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAardgpivPLIA----ETGGq 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 257 NApVLVFDDANLDQAVQGIMASKYRNSGQTCvCANRI-YVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAI 335
Cdd:PRK11904 801 NA-MIVDSTALPEQVVDDVVTSAFRSAGQRC-SALRVlFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAK 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 336 TKVQSHIADATAKGATI-RIGGQRSALGGTFFEPTVLTnvTQDMKVSKEETFGPLAPLFRFKTED-EAVAMA-NDTEFGL 412
Cdd:PRK11904 879 ANLDAHIERMKREARLLaQLPLPAGTENGHFVAPTAFE--IDSISQLEREVFGPILHVIRYKASDlDKVIDAiNATGYGL 956
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480084072 413 AAYVFT--QSAARqwRVGEALEYGMVGIN---TGAISNeVAPFGGvkqSGLGREGSKFGIEEYL 471
Cdd:PRK11904 957 TLGIHSriEETAD--RIADRVRVGNVYVNrnqIGAVVG-VQPFGG---QGLSGTGPKAGGPHYL 1014
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
19-471 |
4.11e-52 |
|
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: 183.57 E-value: 4.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 19 APAAHNDIevkdaatsetLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGK 98
Cdd:TIGR01238 57 NPADRRDI----------VGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 99 PLAEARGEIGYAASFIRWFAEQARRidgevltpTLPNQRLlvikQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVK 178
Cdd:TIGR01238 127 TIHNAIAEVREAVDFCRYYAKQVRD--------VLGEFSV----ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 179 PAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAPTIK---KLSLELG 255
Cdd:TIGR01238 195 PAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDapvPLIAETG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 256 GNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAI 335
Cdd:TIGR01238 275 GQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 336 TKVQSHIADATAKGATI---RIGGQRSALGGTFFEPTVLTnvTQDMKVSKEETFGPLAPLFRFKTE--DEAVAMANDTEF 410
Cdd:TIGR01238 355 QNLLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKARelDQIVDQINQTGY 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480084072 411 GLAAYVFTQSAARQWRVGEALEYGMVGIN---TGAISNeVAPFGGvkqSGLGREGSKFGIEEYL 471
Cdd:TIGR01238 433 GLTMGVHSRIETTYRWIEKHARVGNCYVNrnqVGAVVG-VQPFGG---QGLSGTGPKAGGPHYL 492
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
20-459 |
3.93e-51 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 187.07 E-value: 3.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 20 PAAHNDI--EVKDAatsetlawvksyDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQG 97
Cdd:COG4230 577 PADHSDVvgTVVEA------------TAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAG 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 98 KPLAEARGEIGYAASFIRWFAEQARRIDGEvltPTLPnqrllvikQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLV 177
Cdd:COG4230 645 KTLPDAIAEVREAVDFCRYYAAQARRLFAA---PTVL--------RGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLA 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 178 KPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCA---PTIKKLSLEL 254
Cdd:COG4230 714 KPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAardGPIVPLIAET 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 255 GG-NApvLVFDD-ANLDQAVQGIMASKYRNSGQTCvCANRI-YVQDGIYDALADRLVEAVAKLQVGDGRQeTSTQ-GPLI 330
Cdd:COG4230 794 GGqNA--MIVDSsALPEQVVDDVLASAFDSAGQRC-SALRVlCVQEDIADRVLEMLKGAMAELRVGDPAD-LSTDvGPVI 869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 331 DEDAITKVQSHIADATAKGATI-RIGGQRSALGGTFFEPTVLTnvTQDMKVSKEETFGPLAPLFRFKTED-EAVAMA-ND 407
Cdd:COG4230 870 DAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLIE--IDSISDLEREVFGPVLHVVRYKADElDKVIDAiNA 947
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 480084072 408 TEFGLAAYVFTQSAARQWRVGEALEYGMVGIN---TGAISnEVAPFGGVKQSGLG 459
Cdd:COG4230 948 TGYGLTLGVHSRIDETIDRVAARARVGNVYVNrniIGAVV-GVQPFGGEGLSGTG 1001
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
20-459 |
1.55e-48 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 179.40 E-value: 1.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 20 PAAHNDIevkdaatsetLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKP 99
Cdd:PRK11809 666 PADPRDI----------VGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 100 LAEARGEIGYAASFIRWFAEQARR-IDGEVLTPtlpnqrllvikqaIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVK 178
Cdd:PRK11809 736 FSNAIAEVREAVDFLRYYAGQVRDdFDNDTHRP-------------LGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 179 PAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCA--------PTikKL 250
Cdd:PRK11809 803 PAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAgrldpqgrPI--PL 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 251 SLELGG-NApvLVFDDANL-DQAVQGIMASKYRNSGQTCvCANRIY-VQDGIYDALADRLVEAVAKLQVGDGRQETSTQG 327
Cdd:PRK11809 881 IAETGGqNA--MIVDSSALtEQVVADVLASAFDSAGQRC-SALRVLcLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIG 957
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 328 PLIDEDAITKVQSHIADATAKGATI----RIGGQRSALgGTFFEPTV--LTNVTQdmkvSKEETFGPLAPLFRFKTE--D 399
Cdd:PRK11809 958 PVIDAEAKANIERHIQAMRAKGRPVfqaaRENSEDWQS-GTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRNqlD 1032
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480084072 400 EAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGIN---TGAISNeVAPFGGVKQSGLG 459
Cdd:PRK11809 1033 ELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrnmVGAVVG-VQPFGGEGLSGTG 1094
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
45-468 |
4.83e-44 |
|
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: 160.27 E-value: 4.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 45 RAGVEAAIQRSAQaqavWKKQTalvradvLLAWYQLVLEHKENLAQILTAEQGKPLAEA-RGEIGYAASFI--------R 115
Cdd:cd07137 9 RETFRSGRTRSAE----WRKSQ-------LKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCklaikelkK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 116 WFAEQarridgEVLTP--TLPNqRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVL 193
Cdd:cd07137 78 WMAPE------KVKTPltTFPA-KAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 194 aLKAGLPADILLNISGdAIEVGKTLCES--DivrKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQA 271
Cdd:cd07137 151 -IPEYLDTKAIKVIEG-GVPETTALLEQkwD---KIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 272 VQGIMASKY-RNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLqVGDGRQETSTQGPLIDEDAITKVqSHIADATAKGA 350
Cdd:cd07137 226 VRRIAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRL-SRLLDDPSVAD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 351 TIRIGGQRSAlGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEA 430
Cdd:cd07137 304 KIVHGGERDE-KNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAE 382
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 480084072 431 LEYGMVGINTGAI--SNEVAPFGGVKQSGLGREGSKFGIE 468
Cdd:cd07137 383 TSSGGVTFNDTVVqyAIDTLPFGGVGESGFGAYHGKFSFD 422
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
79-468 |
4.62e-43 |
|
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: 157.77 E-value: 4.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 79 QLVLEHKENLAQILTAEQGKPLAEA--------RGEIGYAASFIRWFAEqarridgevltPTLPNQRLLVI-------KQ 143
Cdd:cd07132 31 RMLEENEDEIVEALAKDLRKPKFEAvlseillvKNEIKYAISNLPEWMK-----------PEPVKKNLATLlddvyiyKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 144 AIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLALKAgLPADILLNISGDAIEVGKTLCES-D 222
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKY-LDKECYPVVLGGVEETTELLKQRfD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 223 ivrKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDA 302
Cdd:cd07132 179 ---YIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 303 LADRLVEAVAKLqVGDGRQETSTQGPLIDEDAITKVQSHIadataKGATIRIGGQRSAlGGTFFEPTVLTNVTQDMKVSK 382
Cdd:cd07132 256 FVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVAIGGQTDE-KERYIAPTVLTDVKPSDPVMQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 383 EETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGA--ISNEVAPFGGVKQSGLGR 460
Cdd:cd07132 329 EEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTImhYTLDSLPFGGVGNSGMGA 408
|
....*...
gi 480084072 461 EGSKFGIE 468
Cdd:cd07132 409 YHGKYSFD 416
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
34-457 |
1.01e-38 |
|
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: 147.35 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 34 SETLAWVKSYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLV---LEHKENLAQILTaeQGKPLAEArgEIGYA 110
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLsgkYRYELNAATMLG--QGKNVWQA--EIDAA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 111 AS---FIRWFAEQARRI-DGEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAaGCSMLVKPAEQTPLT 186
Cdd:cd07123 133 CElidFLRFNVKYAEELyAQQPLSSPAGVWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 187 AYALEVLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCAP------TIKKLSLELGGNAPV 260
Cdd:cd07123 212 NYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGEnldryrTYPRIVGETGGKNFH 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 261 LVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQS 340
Cdd:cd07123 292 LVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKG 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 341 HIADA-TAKGATIRIGGQRSALGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTED--EAVAMANDT-EFGLAAYV 416
Cdd:cd07123 372 YIDHAkSDPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDfeETLELVDTTsPYALTGAI 451
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 480084072 417 FTQ--SAARQWRvgEALEY--GMVGIN---TGAISNEvAPFGGVKQSG 457
Cdd:cd07123 452 FAQdrKAIREAT--DALRNaaGNFYINdkpTGAVVGQ-QPFGGARASG 496
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
70-468 |
5.16e-34 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 133.70 E-value: 5.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 70 RADVLLAWYQLVLEHKENLAQILTAEQGKPLAEA-RGEIGYAASFIR--------WFAEQarriDGEVLTPTLPNqRLLV 140
Cdd:PLN02203 30 RKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyRDEVGVLTKSANlalsnlkkWMAPK----KAKLPLVAFPA-TAEV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 141 IKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAyALEVLALKAGLPADILLNISGDAiEVGKTLCE 220
Cdd:PLN02203 105 VPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS-AFLAANIPKYLDSKAVKVIEGGP-AVGEQLLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 221 SDIvRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLV--FDDA-NLDQAVQGIMASKYRN-SGQTCVCANRIYVQ 296
Cdd:PLN02203 183 HKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAIDYVLVE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 297 DGIYDALADrLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIADATAKgATIRIGGQRSAlGGTFFEPTVLTNVTQ 376
Cdd:PLN02203 262 ERFAPILIE-LLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSIDE-KKLFIEPTILLNPPL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 377 DMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAISN--EVAPFGGVK 454
Cdd:PLN02203 339 DSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYacDSLPFGGVG 418
|
410
....*....|....
gi 480084072 455 QSGLGREGSKFGIE 468
Cdd:PLN02203 419 ESGFGRYHGKYSFD 432
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
26-469 |
1.08e-31 |
|
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: 127.39 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 26 IEVKDAATSETLAWVKSyDRAGVEAAIQRSAQ-AQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILT---AEQGKPLA 101
Cdd:cd07128 17 RTLHDAVTGEVVARVSS-EGLDFAAAVAYAREkGGPALRALTFHERAAMLKALAKYLMERKEDLYALSAatgATRRDSWI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 102 EARGEIG---YAASFIRWFAEQARRI-DGEVL----TPTLPNQRLLVIKQaiGVTAAITPWNFPAAMITRKAAPAIAAGC 173
Cdd:cd07128 96 DIDGGIGtlfAYASLGRRELPNAHFLvEGDVEplskDGTFVGQHILTPRR--GVAVHINAFNFPVWGMLEKFAPALLAGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 174 SMLVKPAEQTPLTAYALEVLALKAG-LPADILLNISGDAIEVGKTLCESDIVrklSFTGSTQVGRILmqQCAPTIKKLSL 252
Cdd:cd07128 174 PVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQDVV---AFTGSAATAAKL--RAHPNIVARSI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 253 ELGG-----NAPVL----VFDDANLDQAVQGI---MASKyrnSGQTCVCANRIYVQDGIYDALADRLVEAVAKLQVGDGR 320
Cdd:cd07128 249 RFNAeadslNAAILgpdaTPGTPEFDLFVKEVareMTVK---AGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 321 QETSTQGPLIDEDAITKVQSHIADATAkGATIRIGGQRS-------ALGGTFFEPTVLT--NVTQDMKVSKEETFGPLAP 391
Cdd:cd07128 326 LEGVRMGPLVSREQREDVRAAVATLLA-EAEVVFGGPDRfevvgadAEKGAFFPPTLLLcdDPDAATAVHDVEAFGPVAT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 392 LFRFKTEDEAVAMANDTEFGLAAYVFTQSA--ARQWRVGEALEYGMVGINTGAISNEV----APFGGVKQSGLGREGskf 465
Cdd:cd07128 405 LMPYDSLAEAIELAARGRGSLVASVVTNDPafARELVLGAAPYHGRLLVLNRDSAKEStghgSPLPQLVHGGPGRAG--- 481
|
....
gi 480084072 466 GIEE 469
Cdd:cd07128 482 GGEE 485
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
140-474 |
2.48e-29 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 120.15 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 140 VIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLaLKAGLPADILLNISGDAIEVGKTLC 219
Cdd:PLN02174 108 IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTETTALLE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 220 ESdiVRKLSFTGSTQVGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYR-NSGQTCVCANRIYVQDG 298
Cdd:PLN02174 187 QK--WDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 299 IYDALADRLVEAVAKLqVGDGRQETSTQGPLIDEDAITKVqSHIADATAKGATIRIGGQRSAlGGTFFEPTVLTNVTQDM 378
Cdd:PLN02174 265 YAPKVIDAMKKELETF-YGKNPMESKDMSRIVNSTHFDRL-SKLLDEKEVSDKIVYGGEKDR-ENLKIAPTILLDVPLDS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 379 KVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAARQWRVGEALEYGMVGINTGAI--SNEVAPFGGVKQS 456
Cdd:PLN02174 342 LIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVhlALHTLPFGGVGES 421
|
330
....*....|....*...
gi 480084072 457 GLGREGSKFGIEEYLEMK 474
Cdd:PLN02174 422 GMGAYHGKFSFDAFSHKK 439
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
70-422 |
3.03e-25 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 108.64 E-value: 3.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 70 RADVLLAWYQLVLEHKENLAQILTAEQGKPLAEAR----GEIGYAASFIRWFA---EQARRIDGEVL----TPTLPNQRL 138
Cdd:PRK11903 65 RAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAvdidGGIFTLGYYAKLGAalgDARLLRDGEAVqlgkDPAFQGQHV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 139 LVIKQaiGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLALKAG-LPADILLNISGDAIEVGKT 217
Cdd:PRK11903 145 LVPTR--GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDH 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 218 LCESDIVrklSFTGSTQVGRILmqQCAPTIKKLSLELGG-----NAPVLVFDDA----NLDQAVQGIMASKYRNSGQTCV 288
Cdd:PRK11903 223 LQPFDVV---SFTGSAETAAVL--RSHPAVVQRSVRVNVeadslNSALLGPDAApgseAFDLFVKEVVREMTVKSGQKCT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 289 CANRIYVQDGIYDALADRLVEAVAKLQVGDGRQETSTQGPLIDEDAITKVQSHIAdATAKGATIRIGGQRSAL------G 362
Cdd:PRK11903 298 AIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALvdadpaV 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480084072 363 GTFFEPTVLtnVTQD----MKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGLAAYVFTQSAA 422
Cdd:PRK11903 377 AACVGPTLL--GASDpdaaTAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAA 438
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
48-406 |
3.81e-22 |
|
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: 98.77 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 48 VEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAASFIRWFAEQAR----- 122
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVRegswl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 123 --RID-GEVLTPTLPNQRLLVIKQAIGVTAAITPWNFPAAMITrkA----APAIAAGCSMLVK--PA--EQTPLTAYALE 191
Cdd:cd07129 81 daRIDpADPDRQPLPRPDLRRMLVPLGPVAVFGASNFPLAFSV--AggdtASALAAGCPVVVKahPAhpGTSELVARAIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 192 VLALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCA--PTIKKLSLELGGNAPVLVFDDA--- 266
Cdd:cd07129 159 AALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAarPEPIPFYAELGSVNPVFILPGAlae 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 267 NLDQAVQGIMASKYRNSGQTCVCANRIYVQDGiydALADRLVEAVAKLqVGDgrqetSTQGPLIDE---DAITKVQSHIA 343
Cdd:cd07129 239 RGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAG---PAGDAFIAALAEA-LAA-----APAQTMLTPgiaEAYRQGVEALA 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480084072 344 DATakGATIRIGGQrSALGGTFFEPTVLTNVTQDM---KVSKEETFGPLAPLFRFKTEDEAVAMAN 406
Cdd:cd07129 310 AAP--GVRVLAGGA-AAEGGNQAAPTLFKVDAAAFladPALQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
48-405 |
6.28e-19 |
|
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: 88.83 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 48 VEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEArGEIGYAASFIRWFAEQA-----R 122
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFVIysyriP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 123 RIDGEVLTPTLPNQRLLVIkQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKPAEQTPLTAYALEVLALKAG-LPA 201
Cdd:cd07084 80 HEPGNHLGQGLKQQSHGYR-WPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 202 DILLNISGDAIEVGKTLCESDIvRKLSFTGSTQVGRILMQQcaPTIKKLSLELGGNAPVLVFDDAN-LDQAVQGIMASKY 280
Cdd:cd07084 159 EDVTLINGDGKTMQALLLHPNP-KMVLFTGSSRVAEKLALD--AKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 281 RNSGQTCVCANRIYV-QDGIYDALADRLVEAVAKLQVGDgrqetSTQGPLIDEDAITKVQSHIADATAK---GATIRIGG 356
Cdd:cd07084 236 ACSGQKCTAQSMLFVpENWSKTPLVEKLKALLARRKLED-----LLLGPVQTFTTLAMIAHMENLLGSVllfSGKELKNH 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 480084072 357 QRSALGGTFFEPTVLTNVTQDMKVSK---EETFGPLAPLFRFKTEDEAVAMA 405
Cdd:cd07084 311 SIPSIYGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKKDQLALVLE 362
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
42-458 |
7.21e-13 |
|
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: 70.59 E-value: 7.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 42 SYDRAGVEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQ--ILTAEQ--------GKPLAEARG--EIGY 109
Cdd:cd07127 80 TYPQCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHavMHTTGQafmmafqaGGPHAQDRGleAVAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 110 AA---SFI----RWFAEQARRidgevlTPTLPNQRLLVIKQAIGVT---AAITPWNFPAAMITrkaapAIAAGCSMLVKP 179
Cdd:cd07127 160 AWremSRIpptaEWEKPQGKH------DPLAMEKTFTVVPRGVALVigcSTFPTWNGYPGLFA-----SLATGNPVIVKP 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 180 AEQTPLTA-----YALEVLAlKAGL-PADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQQCapTIKKLSLE 253
Cdd:cd07127 229 HPAAILPLaitvqVAREVLA-EAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANA--RQAQVYTE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 254 LGGNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRIYV-QDGI--------YDALADRLVEAVAKLqVGDGRQETS 324
Cdd:cd07127 306 KAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGL-LADPARAAA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 325 TQGPLIDEDAITKvqshIADATAKGATIRIGGQRSA---LGGTFFEPTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEA 401
Cdd:cd07127 385 LLGAIQSPDTLAR----IAEARQLGEVLLASEAVAHpefPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHS 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480084072 402 VAMANDT--EFG-LAAYVFTQSAA-------RQWRVGEALEYGMVGintGAISNEVAPFGGVKQSGL 458
Cdd:cd07127 461 IELARESvrEHGaMTVGVYSTDPEvvervqeAALDAGVALSINLTG---GVFVNQSAAFSDFHGTGA 524
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
48-309 |
1.41e-12 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 69.22 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 48 VEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGKPLAEARGEIGYAASFIRWFAEQARRIDGe 127
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTCG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 128 VLTPTLPNQrLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKP----AEQTPLTAYALEVLALKAGLPADI 203
Cdd:cd07081 80 VLTGDENGG-TLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 204 LLNISGDAIEVGKTLCESDIVRKLSFTGstqvGRILMQQCAPTIKKLSLELGGNAPVLVFDDANLDQAVQGIMASKYRNS 283
Cdd:cd07081 159 IGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDN 234
|
250 260
....*....|....*....|....*.
gi 480084072 284 GQTCVCANRIYVQDGIYDALADRLVE 309
Cdd:cd07081 235 GVICASEQSVIVVDSVYDEVMRLFEG 260
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
118-316 |
1.45e-12 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 69.17 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 118 AEQARRIDGEVLTPTLP-NQRLLVIKQAIGVTAAITPWNFPAAMITrKAAPAIAAGCSMLVKPAEQTPLTAYALEVL--- 193
Cdd:cd07077 73 ERGITASVGHIQDVLLPdNGETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLfqa 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 194 ALKAGLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRiLMQQCAPTIKKLSLElGGNAPVLVFDDANLDQAVQ 273
Cdd:cd07077 152 ADAAHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVD-AAVKHSPHIPVIGFG-AGNSPVVVDETADEERASG 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 480084072 274 GIMASKYRNsGQTCVCANRIYVQDGIYDALADRLVE--AVAKLQV 316
Cdd:cd07077 230 SVHDSKFFD-QNACASEQNLYVVDDVLDPLYEEFKLklVVEGLKV 273
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
48-412 |
1.73e-09 |
|
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: 59.56 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 48 VEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGkplaeargeIGYAASFIRWFAEQARRIDG- 126
Cdd:cd07121 6 VDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETG---------MGRVEDKIAKNHLAAEKTPGt 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 127 EVLTPTL---PNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKP---AEQTplTAYALEVL---ALKA 197
Cdd:cd07121 77 EDLTTTAwsgDNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKV--SAYAVELInkaIAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 198 GLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQqcapTIKKLSLELGGNAPVLVFDDANLDQAVQGIMA 277
Cdd:cd07121 155 GGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALS----SGKKAIGAGAGNPPVVVDETADIEKAARDIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 278 SKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAkLQVGDGRQETSTQGPLIDEDAITKVQSHI---ADATAKGATIRI 354
Cdd:cd07121 231 GASFDNNLPCIAEKEVIAVDSVADYLIAAMQRNGA-YVLNDEQAEQLLEVVLLTNKGATPNKKWVgkdASKILKAAGIEV 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 480084072 355 GGQRsalggtffePTVLTNVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGL 412
Cdd:cd07121 310 PADI---------RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGN 358
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
98-400 |
1.56e-08 |
|
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: 56.74 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 98 KPLAEARGEIGYAASFIRWFA-EQAR------RIDGEVLTPTLPNQRLlvikqAIGVTAAITPWNFPAAMITRKAAPAIA 170
Cdd:cd07126 94 KSDAQALGEVVVTRKFLENFAgDQVRflarsfNVPGDHQGQQSSGYRW-----PYGPVAIITPFNFPLEIPALQLMGALF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 171 AGCSMLVKPAEQTPLTAYALEVLALKAGLPADILLNISGDAIEVGKTLCESDiVRKLSFTGSTQVGrilmqqcaptiKKL 250
Cdd:cd07126 169 MGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEAN-PRMTLFTGSSKVA-----------ERL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 251 SLELGGNAPVlvfDDANLDQAVQGIMASK------------YRNSGQTCVCANRIYVQDGIYDA-LADRLVEAVAKLQVG 317
Cdd:cd07126 237 ALELHGKVKL---EDAGFDWKILGPDVSDvdyvawqcdqdaYACSGQKCSAQSILFAHENWVQAgILDKLKALAEQRKLE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 318 DgrqetSTQGPLIDEDAiTKVQSHIADATA-KGATIRIGGQ------RSALGGTfFEPTVLTNVTQDMKVSK------EE 384
Cdd:cd07126 314 D-----LTIGPVLTWTT-ERILDHVDKLLAiPGAKVLFGGKpltnhsIPSIYGA-YEPTAVFVPLEEIAIEEnfelvtTE 386
|
330
....*....|....*.
gi 480084072 385 TFGPLAPLFRFKTEDE 400
Cdd:cd07126 387 VFGPFQVVTEYKDEQL 402
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
48-412 |
1.12e-06 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 51.06 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 48 VEAAIQRSAQAQAVWKKQTALVRADVLLAWYQLVLEHKENLAQILTAEQGkplaeargeIGYAASFIRWFAEQARRIDG- 126
Cdd:PRK15398 38 VDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETG---------MGRVEDKIAKNVAAAEKTPGv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 127 EVLTPTL---PNQRLLVIKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKP---AEQTplTAYALEVL---ALKA 197
Cdd:PRK15398 109 EDLTTEAltgDNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgAKKV--SLRAIELLneaIVAA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 198 GLPADILLNISGDAIEVGKTLCESDIVRKLSFTGSTQVGRILMQqcapTIKKLSLELGGNAPVLVFDDANLDQAVQGIMA 277
Cdd:PRK15398 187 GGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMK----SGKKAIGAGAGNPPVVVDETADIEKAARDIVK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 278 SKYRNSGQTCVCANRIYVQDGIYDALADRLVEAVAkLQVGDGRQETSTQGPLIDEDAITK--VQShiaDAT--AKGATIR 353
Cdd:PRK15398 263 GASFDNNLPCIAEKEVIVVDSVADELMRLMEKNGA-VLLTAEQAEKLQKVVLKNGGTVNKkwVGK---DAAkiLEAAGIN 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 354 IGgqrsalggtfFEPTVLT-NVTQDMKVSKEETFGPLAPLFRFKTEDEAVAMANDTEFGL 412
Cdd:PRK15398 339 VP----------KDTRLLIvETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGN 388
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
141-309 |
1.83e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 47.10 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 141 IKQAIGVTAAITPWNFPAAMITRKAAPAIAAGCSMLVKP---AEQTplTAYALEVL---ALKAGLPADILLNISGDAIEV 214
Cdd:cd07122 92 IAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKC--SIEAAKIMreaAVAAGAPEGLIQWIEEPSIEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480084072 215 GKTLCESDIVRKLSFTGSTQvgrilMQQCAPTIKKLSLELG-GNAPVLVFDDANLDQAVQGIMASKYRNSGQTCVCANRI 293
Cdd:cd07122 170 TQELMKHPDVDLILATGGPG-----MVKAAYSSGKPAIGVGpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSV 244
|
170
....*....|....*.
gi 480084072 294 YVQDGIYDALADRLVE 309
Cdd:cd07122 245 IVDDEIYDEVRAELKR 260
|
|
| |
