|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
23-472 |
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: 801.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEV 102
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 103 VYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSA 182
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 183 FAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDA 262
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAE-IGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 263 DIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAI 342
Cdd:cd07103 240 DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 343 EQGAQPVT--PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWK 420
Cdd:cd07103 320 AKGAKVLTggKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 515625329 421 VAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIKYLCF 472
Cdd:cd07103 400 VAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
1-474 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 712.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 1 MLEINNQRLLSF--------MVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAW 72
Cdd:PLN02278 14 LVKLRNAGLLRTqgliggkwTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 73 HQLILENKDDLAHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFP 152
Cdd:PLN02278 94 YDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 153 IAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVG 232
Cdd:PLN02278 174 LAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPE-IGDALLASPKVRKITFTGSTAVG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 233 SILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKI 312
Cdd:PLN02278 253 KKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 313 GNGLDEGINIGPVISERAKQNIQGLIDRAIEQGAQPVT--PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFD 390
Cdd:PLN02278 333 GDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLggKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFK 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 391 SDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIKYL 470
Cdd:PLN02278 413 TEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
....
gi 515625329 471 CFGG 474
Cdd:PLN02278 493 CLGN 496
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
23-468 |
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: 672.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEV 102
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 103 VYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSA 182
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 183 FAVVELAYQAGIPKNLLQVVLGDSPEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDA 262
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGSRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 263 DIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAI 342
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 343 EQGAQPVTPTQ--ELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWK 420
Cdd:TIGR01780 321 EKGAKVVTGGKrhELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 515625329 421 VAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:TIGR01780 401 VAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
17-472 |
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: 647.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 17 ADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLE 96
Cdd:COG1012 19 SGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 97 EATGEVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSD 176
Cdd:COG1012 99 EARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 177 ETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPF 256
Cdd:COG1012 179 QTPLSALLLAELLEEAGLPAGVLNVVTGDGSE-VGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 257 IVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQG 336
Cdd:COG1012 258 IVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 337 LIDRAIEQGAQPVT---PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQ 413
Cdd:COG1012 338 YIEDAVAEGAELLTggrRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTR 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 414 NIHRVWKVAEALEYGMVGINDGLISTEV-APFGGVKQSGIGREGAKEGIDEYMDIKYLCF 472
Cdd:COG1012 418 DLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
19-473 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 611.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 19 KAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEA 98
Cdd:PRK11241 26 EVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 99 TGEVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDET 178
Cdd:PRK11241 106 KGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 179 PLSAFAVVELAYQAGIPKNLLQVVLGDSPEQIGELfTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIV 258
Cdd:PRK11241 186 PFSALALAELAIRAGIPAGVFNVVTGSAGAVGGEL-TSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 259 FDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLI 338
Cdd:PRK11241 265 FDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 339 DRAIEQGAQPVT--PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIH 416
Cdd:PRK11241 345 ADALEKGARVVCggKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLS 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 515625329 417 RVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIKYLCFG 473
Cdd:PRK11241 425 RVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIG 481
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
14-468 |
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: 600.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 14 VTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGK 93
Cdd:pfam00171 2 VDSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 94 PLEEATGEVVYGASFIEWFAEEAKRTYGDSIPSTvAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVK 173
Cdd:pfam00171 82 PLAEARGEVDRAIDVLRYYAGLARRLDGETLPSD-PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 174 PSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGN 253
Cdd:pfam00171 161 PSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAE-VGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 254 APFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQN 333
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 334 IQGLIDRAIEQGAQPVT--PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFY 411
Cdd:pfam00171 320 VLKYVEDAKEEGAKLLTggEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVF 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 515625329 412 SQNIHRVWKVAEALEYGMVGINDGLIST-EVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:pfam00171 400 TSDLERALRVARRLEAGMVWINDYTTGDaDGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
44-472 |
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: 552.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 44 DRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRTYGDS 123
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 124 IPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVL 203
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 204 GDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTC 283
Cdd:cd07078 161 GDGDE-VGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 284 VCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQEL---AGLFI 360
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeggKGYFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 361 QPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTE 440
Cdd:cd07078 320 PPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAE 399
|
410 420 430
....*....|....*....|....*....|...
gi 515625329 441 V-APFGGVKQSGIGREGAKEGIDEYMDIKYLCF 472
Cdd:cd07078 400 PsAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
4-468 |
1.08e-175 |
|
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: 501.02 E-value: 1.08e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 4 INNQrllsFMVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDL 83
Cdd:cd07088 2 INGE----FVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 84 AHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPA 163
Cdd:cd07088 78 AKLIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 164 LAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGI 243
Cdd:cd07088 158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSV-VGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 244 KRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIG 323
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 324 PVISERAKQNIQGLIDRAIEQGAQPVT----PTQElAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMA 399
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTggkrPEGE-KGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515625329 400 NDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGliSTEVAP--FGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRE--NFEAMQgfHAGWKKSGLGGADGKHGLEEYLQTK 464
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
23-468 |
1.18e-170 |
|
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: 487.83 E-value: 1.18e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIA--QKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATG 100
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 101 EVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPL 180
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 181 SAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFD 260
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPE-TGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 261 DADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDR 340
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 341 AIEQGAQ------PVTPTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQN 414
Cdd:cd07114 320 AREEGARvltggeRPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 515625329 415 IHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
23-471 |
7.24e-163 |
|
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: 467.81 E-value: 7.24e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEA-TGE 101
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLArTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 102 VVYGASFIEWFAEEAKRTYGDSIPStvAGKHL-VTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPL 180
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQ--DGGALnYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 181 SAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFD 260
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPE-AGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 261 DADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDR 340
Cdd:cd07093 238 DADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 341 AIEQGAQPVT-----PTQELA-GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQN 414
Cdd:cd07093 318 ARAEGATILTgggrpELPDLEgGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 515625329 415 IHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIKYLC 471
Cdd:cd07093 398 LGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
23-468 |
4.67e-156 |
|
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: 450.44 E-value: 4.67e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEV 102
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 103 VYGASfieWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSA 182
Cdd:cd07106 81 GGAVA---WLRYTASLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 183 FAVVELAYQAgIPKNLLQVVLGDspEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDA 262
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSGG--DELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 263 DIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAI 342
Cdd:cd07106 235 DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 343 EQGAQPVTPTQ--ELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWK 420
Cdd:cd07106 315 AKGAKVLAGGEplDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEA 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 515625329 421 VAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07106 395 VARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
48-472 |
1.06e-152 |
|
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: 438.97 E-value: 1.06e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 48 ERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRTYGDSIPST 127
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 128 VAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSP 207
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 208 EqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCAN 287
Cdd:cd06534 161 E-VGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 288 RFYIHSKVHDEFVAKFdqavqqlkigngldeginigpviserakqniqglidraieqgaqpVTptqelaglfiqpvILKD 367
Cdd:cd06534 240 RLLVHESIYDEFVEKL---------------------------------------------VT-------------VLVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 368 VKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEV-APFGG 446
Cdd:cd06534 262 VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPeAPFGG 341
|
410 420
....*....|....*....|....*.
gi 515625329 447 VKQSGIGREGAKEGIDEYMDIKYLCF 472
Cdd:cd06534 342 VKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
23-472 |
2.19e-152 |
|
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: 441.26 E-value: 2.19e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEV 102
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 103 VYGASFIEWFAEEAKRTYGDSIP--STVAGKHLV--TIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDET 178
Cdd:cd07149 83 DRAIETLRLSAEEAKRLAGETIPfdASPGGEGRIgfTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 179 PLSAFAVVELAYQAGIPKNLLQVVLGdSPEQIGELFTSHPLIKKISFTGSTRVGSILMAQAakGIKRTSMELGGNAPFIV 258
Cdd:cd07149 163 PLSALKLAELLLEAGLPKGALNVVTG-SGETVGDALVTDPRVRMISFTGSPAVGEAIARKA--GLKKVTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 259 FDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLI 338
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 339 DRAIEQGAQPVTPTQElAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRV 418
Cdd:cd07149 320 EEAVEGGARLLTGGKR-DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 515625329 419 WKVAEALEYGMVGINDglIST---EVAPFGGVKQSGIGREGAKEGIDEYMDIKYLCF 472
Cdd:cd07149 399 LKAARELEVGGVMIND--SSTfrvDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
42-470 |
1.13e-150 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 436.19 E-value: 1.13e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 42 ELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRTYG 121
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 122 DSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLS-AFAVVELAYQAGIPKNLLQ 200
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 201 VVLGDsPEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAG 280
Cdd:cd07104 161 VVPGG-GSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 281 QTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAIEQGAQPVTpTQELAGLFI 360
Cdd:cd07104 240 QICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLT-GGTYEGLFY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 361 QPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTE 440
Cdd:cd07104 319 QPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDE 398
|
410 420 430
....*....|....*....|....*....|.
gi 515625329 441 -VAPFGGVKQSGIGREGAKEGIDEYMDIKYL 470
Cdd:cd07104 399 pHVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
21-468 |
4.92e-149 |
|
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: 433.08 E-value: 4.92e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 21 VAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATG 100
Cdd:cd07138 16 IDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 101 -EVVYGASFIEWFAEEAKrtygdSIP-STVAGKHLVtIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDET 178
Cdd:cd07138 96 aQVGLGIGHLRAAADALK-----DFEfEERRGNSLV-VREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 179 PLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIV 258
Cdd:cd07138 170 PLSAIILAEILDEAGLPAGVFNLVNGDGPV-VGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANII 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 259 FDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLI 338
Cdd:cd07138 249 LDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 339 DRAIEQGAQPVT----PTQELA-GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQ 413
Cdd:cd07138 329 QKGIEEGARLVAggpgRPEGLErGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSA 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 515625329 414 NIHRVWKVAEALEYGMVGINDGLISTEvAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07138 409 DPERARAVARRLRAGQVHINGAAFNPG-APFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
43-468 |
6.93e-149 |
|
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: 431.50 E-value: 6.93e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 43 LDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRTYGD 122
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 123 SIPSTVAGKHLVTiKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVV 202
Cdd:cd07100 81 EPIETDAGKAYVR-YEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 203 LGDSpEQIGELFtSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQT 282
Cdd:cd07100 160 LIDS-DQVEAII-ADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 283 CVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAIEQGAQPVT--PTQELAGLFI 360
Cdd:cd07100 238 CIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLggKRPDGPGAFY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 361 QPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTE 440
Cdd:cd07100 318 PPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDP 397
|
410 420
....*....|....*....|....*...
gi 515625329 441 VAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07100 398 RLPFGGVKRSGYGRELGRFGIREFVNIK 425
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
2-468 |
4.14e-148 |
|
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: 431.25 E-value: 4.14e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 2 LEINNQrllsFMVTEADKAVAVTNPATGELIGHAPISSETELDRAIE--RSHIAQKEWAKIPAKSRAAILKAWHQLILEN 79
Cdd:cd07091 6 LFINNE----FVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKaaRAAFETGWWRKMDPRERGRLLNKLADLIERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 80 KDDLAHLMTIEQGKPLEE-ATGEVVYGASFIEWFAEEAKRTYGDSIPStvAGKHLV-TIKQPIGVACAITPWNFPIAMIT 157
Cdd:cd07091 82 RDELAALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIPI--DGNFLAyTRREPIGVCGQIIPWNFPLLMLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 158 RKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPeQIGELFTSHPLIKKISFTGSTRVGSILMA 237
Cdd:cd07091 160 WKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGP-TAGAAISSHMDVDKIAFTGSTAVGRTIME 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 238 QAAK-GIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGL 316
Cdd:cd07091 239 AAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 317 DEGINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQEL--AGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEE 394
Cdd:cd07091 319 DPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHgsKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515625329 395 LIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07091 399 VIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
23-470 |
1.19e-146 |
|
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: 426.75 E-value: 1.19e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEV 102
Cdd:cd07150 3 DLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 103 VYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSA 182
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 183 FAVVELAYQAGIPKNLLQVVLGdSPEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDA 262
Cdd:cd07150 163 LKIAEIMEEAGLPKGVFNVVTG-GGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 263 DIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAI 342
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 343 EQGAQPVTPTQElAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVA 422
Cdd:cd07150 322 AKGAKLLTGGKY-DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 515625329 423 EALEYGMVGINDGLISTE-VAPFGGVKQSGIGREGAKEGIDEYMDIKYL 470
Cdd:cd07150 401 ERLESGMVHINDPTILDEaHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
25-468 |
1.57e-145 |
|
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: 424.84 E-value: 1.57e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 25 NPATG-ELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVV 103
Cdd:cd07131 20 NPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 104 YGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAF 183
Cdd:cd07131 100 EAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 184 AVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDAD 263
Cdd:cd07131 180 KLVELFAEAGLPPGVVNVVHGRGEE-VGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 264 IDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAIE 343
Cdd:cd07131 259 LDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 344 QGAQ------PVTPTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHR 417
Cdd:cd07131 339 EGATlllggeRLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNK 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 515625329 418 VWKVAEALEYGMVGINDGLISTEV-APFGGVKQSGIG-REGAKEGIDEYMDIK 468
Cdd:cd07131 419 AFRARRDLEAGITYVNAPTIGAEVhLPFGGVKKSGNGhREAGTTALDAFTEWK 471
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
21-470 |
1.43e-143 |
|
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: 419.06 E-value: 1.43e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 21 VAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATG 100
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 101 EVVYGASFIEWFAEEAKRTYGDSIPS----TVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSD 176
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVdayeYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 177 ETPLSAFAVVELAYQAGIPKNLLQVVLGDSpEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPF 256
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYG-SEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 257 IVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQG 336
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 337 LIDRAIEQGAQPVTPTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIH 416
Cdd:cd07145 320 LVNDAVEKGGKILYGGKRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDIN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 515625329 417 RVWKVAEALEYGMVGIND-GLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIKYL 470
Cdd:cd07145 400 RALKVARELEAGGVVINDsTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
22-468 |
3.30e-143 |
|
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: 418.16 E-value: 3.30e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 22 AVTNPATGELIGHAPISSETELDRAIERSHIAQKE--WAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEAT 99
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 100 GEVVYG-ASFIEWFAEEAKRTYGDSIPSTVAGKHLVTiKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDET 178
Cdd:cd07112 85 AVDVPSaANTFRWYAEAIDKVYGEVAPTGPDALALIT-REPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 179 PLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKG-IKRTSMELGGNAPFI 257
Cdd:cd07112 164 PLTALRLAELALEAGLPAGVLNVVPGFGHT-AGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKSPNI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 258 VFDDA-DIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQG 336
Cdd:cd07112 243 VFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 337 LIDRAIEQGAQPVT----PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYS 412
Cdd:cd07112 323 YIESGKAEGARLVAggkrVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWT 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 515625329 413 QNIHRVWKVAEALEYGMVGIN---DGLISTevaPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07112 403 SDLSRAHRVARRLRAGTVWVNcfdEGDITT---PFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
23-468 |
1.84e-142 |
|
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: 416.26 E-value: 1.84e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWA-KIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGE 101
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 102 VVYG-ASFIEWFAEEAKRTY-----GDSIPSTVAGKHLVtIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPS 175
Cdd:cd07089 81 QVDGpIGHLRYFADLADSFPwefdlPVPALRGGPGRRVV-RREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 176 DETPLSAFAVVELAYQAGIPKNLLQVVLGdSPEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAP 255
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTG-SDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 256 FIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQ 335
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 336 GLIDRAIEQGAQPVTPTQELAGL----FIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFY 411
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAGLdkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 515625329 412 SQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
23-471 |
9.02e-141 |
|
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: 411.70 E-value: 9.02e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEV 102
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 103 VYGASFIEWFAEEAKRTYGDSIPSTvAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSA 182
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLP-GGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 183 FAVVELAYQAGIPKNLLQVVLGDSpeQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDA 262
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGG--ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 263 DIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAI 342
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 343 EQGAQ------PVTPTQELA-GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNI 415
Cdd:cd07090 318 QEGAKvlcggeRVVPEDGLEnGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 515625329 416 HRVWKVAEALEYGMVGIND-GLISTEVaPFGGVKQSGIGREGAKEGIDEYMDIKYLC 471
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINTyNISPVEV-PFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
22-468 |
1.39e-140 |
|
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: 412.09 E-value: 1.39e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 22 AVTNPATGELIGHAPISSETELDRAIE--RSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEAT 99
Cdd:cd07119 16 DIINPANGEVIATVPEGTAEDAKRAIAaaRRAFDSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 100 GEVVYGASFIEWFAEEAKRTYGDSIPSTvAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETP 179
Cdd:cd07119 96 IDIDDVANCFRYYAGLATKETGEVYDVP-PHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 180 LSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVF 259
Cdd:cd07119 175 LTTIALFELIEEAGLPAGVVNLVTGSGAT-VGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 260 DDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLID 339
Cdd:cd07119 254 ADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 340 RAIEQGAQPVT----PTQ-ELA-GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQ 413
Cdd:cd07119 334 LGKEEGARLVCggkrPTGdELAkGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTK 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 515625329 414 NIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07119 414 DIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETK 468
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
14-465 |
8.05e-140 |
|
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: 410.03 E-value: 8.05e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 14 VTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGK 93
Cdd:cd07086 8 VGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 94 PLEEATGEVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVK 173
Cdd:cd07086 88 ILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 174 PSDETPLSAFAVVELAYQA----GIPKNLLQVVLGDSPeqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSME 249
Cdd:cd07086 168 PSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD--GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 250 LGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISER 329
Cdd:cd07086 246 LGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 330 AKQNIQGLIDRAIEQGAQPVT----PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYG 405
Cdd:cd07086 326 AVEKYLNAIEIAKSQGGTVLTggkrIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQG 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515625329 406 LASYFYSQNIHRV--WKVAEALEYGMVGINDGLISTEV-APFGGVKQSGIGREGAKEGIDEYM 465
Cdd:cd07086 406 LSSSIFTEDLREAfrWLGPKGSDCGIVNVNIPTSGAEIgGAFGGEKETGGGRESGSDAWKQYM 468
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
23-469 |
1.42e-137 |
|
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: 403.99 E-value: 1.42e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEV 102
Cdd:cd07151 14 VLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 103 VYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSA 182
Cdd:cd07151 94 GAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 183 -FAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDD 261
Cdd:cd07151 174 gLLLAKIFEEAGLPKGVLNVVVGAGSE-IGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLED 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 262 ADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRA 341
Cdd:cd07151 253 ADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 342 IEQGAQPVTpTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKV 421
Cdd:cd07151 333 VEEGATLLV-GGEAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQF 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 515625329 422 AEALEYGMVGINDGLISTE-VAPFGGVKQSGIGREGAKEGIDEYMDIKY 469
Cdd:cd07151 412 ARRIDAGMTHINDQPVNDEpHVPFGGEKNSGLGRFNGEWALEEFTTDKW 460
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
24-470 |
8.79e-137 |
|
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: 401.60 E-value: 8.79e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 24 TNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVV 103
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 104 YGASFIEWFAEEAKRTYGD---SIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPL 180
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPrkvPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 181 SAFAVVELAYQAGIPKNLLQVVLGDSPeqigelfTSHPLIK----KISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPF 256
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGA-------TGAALIDagvdKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 257 IVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQG 336
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 337 LIDRAIEQGAQPVT--PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQN 414
Cdd:cd07099 314 HVDDAVAKGAKALTggARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 515625329 415 IHRVWKVAEALEYGMVGINDGLISTEV--APFGGVKQSGIGREGAKEGIDEYMDIKYL 470
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGIpaLPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
15-468 |
1.95e-136 |
|
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: 401.24 E-value: 1.95e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 15 TEADKAVAVTNPA-TGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGK 93
Cdd:cd07097 10 VAGGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 94 PLEEATGEVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVK 173
Cdd:cd07097 90 TLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 174 PSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGN 253
Cdd:cd07097 170 PAELTPASAWALVEILEEAGLPAGVFNLVMGSGSE-VGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 254 APFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQN 333
Cdd:cd07097 249 NPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 334 IQGLIDRAIEQGAQPVTPTQELA----GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASY 409
Cdd:cd07097 329 DLRYIEIARSEGAKLVYGGERLKrpdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAG 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515625329 410 FYSQNIHRVWKVAEALEYGMVGINdgLISTEV---APFGGVKQSGIG-REGAKEGIDEYMDIK 468
Cdd:cd07097 409 IVTTSLKHATHFKRRVEAGVVMVN--LPTAGVdyhVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
23-468 |
3.31e-136 |
|
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: 399.81 E-value: 3.31e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIErSHIAQKEwaKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEV 102
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALA-LAASYRS--TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 103 VYGASFIEWFAEEAKRTYGDSIPSTVA----GKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDET 178
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGESFSCDLTangkARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 179 PLSAFAVVELAYQAGIPKNLLQVVLGDsPEQIGELFTSHPLIKKISFTGSTRVGSILMAQAakGIKRTSMELGGNAPFIV 258
Cdd:cd07146 160 PLSAIYLADLLYEAGLPPDMLSVVTGE-PGEIGDELITHPDVDLVTFTGGVAVGKAIAATA--GYKRQLLELGGNDPLIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 259 FDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLI 338
Cdd:cd07146 237 MDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 339 DRAIEQGAQPVTPTQElAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRV 418
Cdd:cd07146 317 EEAIAQGARVLLGNQR-QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 515625329 419 WKVAEALEYGMVGINDGL-ISTEVAPFGGVKQSGIG-REGAKEGIDEYMDIK 468
Cdd:cd07146 396 KRLVERLDVGTVNVNEVPgFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
21-472 |
4.76e-136 |
|
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: 399.50 E-value: 4.76e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 21 VAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATG 100
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 101 EVVYGASFIEWFAEEAKRTYGDSIPSTVA----GKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSD 176
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDATqgsdNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 177 ETPLSAFAVVELAYQAGIPKNLLQVVLGDsPEQIGELFTSHPLIKKISFTGSTRVGSILMAQAakGIKRTSMELGGNAPF 256
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGE-REVLGDAFAADERVAMLSFTGSAAVGEALRANA--GGKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 257 IVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQG 336
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 337 LIDRAIEQGAQPVTpTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIH 416
Cdd:cd07094 318 WVEEAVEAGARLLC-GGERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLN 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 515625329 417 RVWKVAEALEYGMVGINDG-LISTEVAPFGGVKQSGIGREGAKEGIDEYMDIKYLCF 472
Cdd:cd07094 397 VAFKAAEKLEVGGVMVNDSsAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
23-468 |
1.80e-135 |
|
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: 398.15 E-value: 1.80e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWA-KIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGE 101
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 102 VVYGASFIEWFAEEAKRTYGDSIPStVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLS 181
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPL-GPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 182 AFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDD 261
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAE-AGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 262 ADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEgINIGPVISERAKQNIQGLIDRA 341
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 342 IEQGAQPVT-----PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIH 416
Cdd:cd07109 318 RARGARIVAggriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 515625329 417 RVWKVAEALEYGMVGIND----GLISTevaPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07109 398 RALRVARRLRAGQVFVNNygagGGIEL---PFGGVKKSGHGREKGLEALYNYTQTK 450
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
25-471 |
2.17e-135 |
|
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: 397.97 E-value: 2.17e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 25 NPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATG-EVV 103
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 104 YGASFIEWFAEEAKRTYGDSIPstVAGKHL-VTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSA 182
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIP--VRGPFLnYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 183 FAVVELAYQAGIPKNLLQVVLGDSpEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDA 262
Cdd:cd07115 161 LRIAELMAEAGFPAGVLNVVTGFG-EVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 263 DIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAI 342
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 343 EQGAQPVTPTQELA--GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWK 420
Cdd:cd07115 320 EEGARLLTGGKRPGarGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 515625329 421 VAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIKYLC 471
Cdd:cd07115 400 VAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVW 450
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
23-470 |
3.16e-134 |
|
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: 395.18 E-value: 3.16e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEV 102
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 103 VYGASFIEWFAEEA---KRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETP 179
Cdd:cd07110 81 DDVAGCFEYYADLAeqlDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 180 LSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVF 259
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDE-AGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 260 DDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLID 339
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 340 RAIEQGAQPVT----PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNI 415
Cdd:cd07110 320 RGKEEGARLLCggrrPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 515625329 416 HRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIKYL 470
Cdd:cd07110 400 ERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
26-468 |
4.65e-132 |
|
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: 389.39 E-value: 4.65e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 26 PATGELIGHAPISSETELDRAIERSHIA--QKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVV 103
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 104 YGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAF 183
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 184 AVVELAYQAGIPKNLLQVVLGDSpEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDAD 263
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYG-ATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 264 IDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAIE 343
Cdd:cd07118 243 LDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 344 QGAQPVT---PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWK 420
Cdd:cd07118 323 EGATLLLggeRLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALT 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 515625329 421 VAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07118 403 VARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELK 450
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
23-468 |
2.99e-131 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 388.47 E-value: 2.99e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEA-TGE 101
Cdd:PRK13252 26 VINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETsVVD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 102 VVYGASFIEWFAEEAKRTYGDSIPstVAGKHLV-TIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPL 180
Cdd:PRK13252 106 IVTGADVLEYYAGLAPALEGEQIP--LRGGSFVyTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 181 SAFAVVELAYQAGIPKNLLQVVLGDSpeQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFD 260
Cdd:PRK13252 184 TALKLAEIYTEAGLPDGVFNVVQGDG--RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 261 DADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDR 340
Cdd:PRK13252 262 DADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 341 AIEQGA------QPVTPTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQN 414
Cdd:PRK13252 342 GKAEGArllcggERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTAD 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 515625329 415 IHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:PRK13252 422 LSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIK 475
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
20-468 |
7.84e-131 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 386.96 E-value: 7.84e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 20 AVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEAT 99
Cdd:PRK13473 18 KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 100 GEVVYG-ASFIEWFAEEAKRTYGDSIPSTVAGkHLVTI-KQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDE 177
Cdd:PRK13473 98 NDEIPAiVDVFRFFAGAARCLEGKAAGEYLEG-HTSMIrRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 178 TPLSAFAVVELAYQAgIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFI 257
Cdd:PRK13473 177 TPLTALKLAELAADI-LPPGVLNVVTGRGAT-VGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 258 VFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGL 337
Cdd:PRK13473 255 VFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGF 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 338 IDRAIEQGAQPVT---PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQN 414
Cdd:PRK13473 335 VERAKALGHIRVVtggEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRD 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 515625329 415 IHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:PRK13473 415 VGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
23-468 |
1.79e-130 |
|
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: 385.56 E-value: 1.79e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLE-EATGE 101
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 102 VVYGASFIEWFAEEAKRTYGDSIPstvAGKHLV--TIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETP 179
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP---FGPDVLtyTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 180 LSAFAVVELAYQAgIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVF 259
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEE-CGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 260 DDADIDAAVQGAMAS-KFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLI 338
Cdd:cd07108 236 PDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 339 D--------RAIEQGAQPVTPTQElAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYF 410
Cdd:cd07108 316 DlglstsgaTVLRGGPLPGEGPLA-DGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 515625329 411 YSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEG-IDEYMDIK 468
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKK 453
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
21-468 |
3.50e-130 |
|
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: 385.39 E-value: 3.50e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 21 VAVTNPATGELIGHAPISSETELDRAIE--RSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLE-E 97
Cdd:cd07139 16 IDVVSPATEEVVGRVPEATPADVDAAVAaaRRAFDNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISwS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 98 ATGEVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDE 177
Cdd:cd07139 96 RRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 178 TPLSAFAVVELAYQAGIPKNLLQVVLGDSpeQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFI 257
Cdd:cd07139 176 TPLDAYLLAEAAEEAGLPPGVVNVVPADR--EVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 258 VFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGL 337
Cdd:cd07139 254 VLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 338 IDRAIEQGAQPVT----PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQ 413
Cdd:cd07139 334 IAKGRAEGARLVTgggrPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTA 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 515625329 414 NIHRVWKVAEALEYGMVGINdGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07139 414 DVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETK 467
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
23-469 |
1.00e-129 |
|
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: 383.22 E-value: 1.00e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEE-ATGE 101
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 102 VVYGASFIEWFAEEAKRTYGDSIPSTVAGkHLVTI-KQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPL 180
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPG-HTSMIrREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 181 SAFAVVELAyQAGIPKNLLQVVLGDSpEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFD 260
Cdd:cd07092 160 TTLLLAELA-AEVLPPGVVNVVCGGG-ASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 261 DADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDR 340
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 341 A-----IEQGAQPVtptqELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNI 415
Cdd:cd07092 318 ApaharVLTGGRRA----EGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 515625329 416 HRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIKY 469
Cdd:cd07092 394 GRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKH 447
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
44-468 |
5.65e-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: 380.77 E-value: 5.65e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 44 DRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRTYGDS 123
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 124 IPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVL 203
Cdd:cd07105 83 IPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 204 gDSPE---QIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAG 280
Cdd:cd07105 163 -HSPEdapEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 281 QTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLdeginIGPVISERAKQNIQGLIDRAIEQGAQPV---TPTQELAG 357
Cdd:cd07105 242 QICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVV-----LGSLVSAAAADRVKELVDDALSKGAKLVvggLADESPSG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 358 LFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLI 437
Cdd:cd07105 317 TSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTV 396
|
410 420 430
....*....|....*....|....*....|..
gi 515625329 438 STE-VAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07105 397 HDEpTLPHGGVKSSGYGRFNGKWGIDEFTETK 428
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
2-468 |
8.24e-129 |
|
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: 382.14 E-value: 8.24e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 2 LEINNQrllsFMVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIA-QKEWAKIPAKSRAAILKAWHQLILENK 80
Cdd:cd07144 10 LFINNE----FVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 81 DDLAHLMTIEQGKPLEE-ATGEVVYGASFIEWFAEEAKRTYGDSIPSTVAgKHLVTIKQPIGVACAITPWNFPIAMITRK 159
Cdd:cd07144 86 DLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPTSPN-KLAYTLHEPYGVCGQIIPWNYPLAMAAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 160 AAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQA 239
Cdd:cd07144 165 LAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAV-AGSALAEHPDVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 240 AKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQ-LKIGNGLDE 318
Cdd:cd07144 244 AQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 319 GINIGPVISERAKQNIQGLIDRAIEQGA-----QPVTPTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDE 393
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAklvygGEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYE 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515625329 394 ELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07144 404 EAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
23-472 |
1.20e-127 |
|
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: 378.13 E-value: 1.20e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEV 102
Cdd:cd07147 3 VTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 103 VYGASFIEWFAEEAKRTYG-----DSIPSTvAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDE 177
Cdd:cd07147 83 ARAIDTFRIAAEEATRIYGevlplDISARG-EGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 178 TPLSAFAVVELAYQAGIPKNLLQVVLGDSPeqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKgiKRTSMELGGNAPFI 257
Cdd:cd07147 162 TPLSALILGEVLAETGLPKGAFSVLPCSRD--DADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 258 VFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGL 337
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 338 IDRAIEQGAQPVTPTqELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHR 417
Cdd:cd07147 318 VNEAVDAGAKLLTGG-KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEK 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 515625329 418 VWKVAEALEYGMVGINDglIST---EVAPFGGVKQSGIGREGAKEGIDEYMDIKYLCF 472
Cdd:cd07147 397 ALRAWDELEVGGVVIND--VPTfrvDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
25-471 |
2.48e-125 |
|
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: 372.45 E-value: 2.48e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 25 NPATGELIGHAPISSETELDRAIERSHIAQKE--WAKIPAKsRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEV 102
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 103 VYGASFIEWFAEEAKRTYGDSIPSTvAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSA 182
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPE-PGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 183 FAVVE-LAYQAGIPKNLLQVVLgDSPEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDD 261
Cdd:cd07120 161 AAIIRiLAEIPSLPAGVVNLFT-ESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 262 ADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRA 341
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 342 IEQGAQPV----TPTQELA-GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIH 416
Cdd:cd07120 320 IAAGAEVVlrggPVTEGLAkGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 515625329 417 RVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIKYLC 471
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
7-466 |
5.14e-124 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 371.52 E-value: 5.14e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 7 QRLLSFMVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHL 86
Cdd:PRK09407 20 RRLTARVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 87 MTIEQGKPLEEATGEVVYGASFIEWFAEEAKRTYGdsiPSTVAG-----KHLVTIKQPIGVACAITPWNFPIAMITRKAA 161
Cdd:PRK09407 100 VQLETGKARRHAFEEVLDVALTARYYARRAPKLLA---PRRRAGalpvlTKTTELRQPKGVVGVISPWNYPLTLAVSDAI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 162 PALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGElftshPLIKK---ISFTGSTRVGSILMAQ 238
Cdd:PRK09407 177 PALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPV-VGT-----ALVDNadyLMFTGSTATGRVLAEQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 239 AAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDE 318
Cdd:PRK09407 251 AGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 319 GINIGPVISERAKQNIQGLIDRAIEQGAQPVT---PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEEL 395
Cdd:PRK09407 331 SADMGSLISEAQLETVSAHVDDAVAKGATVLAggkARPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEA 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515625329 396 IEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLI----STEvAPFGGVKQSGIGREGAKEGIDEYMD 466
Cdd:PRK09407 411 VERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAaawgSVD-APMGGMKDSGLGRRHGAEGLLKYTE 484
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
26-467 |
5.09e-123 |
|
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: 366.25 E-value: 5.09e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 26 PATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVVYG 105
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 106 ASFIEWFAEEAKRTYGD-----SIPstVAGKHLVTiKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPL 180
Cdd:cd07101 83 AIVARYYARRAERLLKPrrrrgAIP--VLTRTTVN-RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 181 SAFAVVELAYQAGIPKNLLQVVLGDSPEqIGElftshPLIKK---ISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFI 257
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGPGSE-VGG-----AIVDNadyVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 258 VFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGL 337
Cdd:cd07101 234 VLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 338 IDRAIEQGAQPVT---PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQN 414
Cdd:cd07101 314 VDDAVAKGATVLAggrARPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 515625329 415 IHRVWKVAEALEYGMVGINDGLISTEV---APFGGVKQSGIGREGAKEGIDEYMDI 467
Cdd:cd07101 394 GARGRRIAARLRAGTVNVNEGYAAAWAsidAPMGGMKDSGLGRRHGAEGLLKYTET 449
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
2-468 |
6.12e-122 |
|
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: 364.51 E-value: 6.12e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 2 LEINNQrllsFMVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKE--WAKIPAKSRAAILKAWHQLILEN 79
Cdd:cd07142 6 LFINGQ----FVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 80 KDDLAHLMTIEQGKPLEEA-TGEVVYGASFIEWFAEEAKRTYGDSIPSTvaGKHLV-TIKQPIGVACAITPWNFPIAMIT 157
Cdd:cd07142 82 ADELAALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPAD--GPHHVyTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 158 RKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPeQIGELFTSHPLIKKISFTGSTRVGSILMA 237
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGP-TAGAAIASHMDVDKVAFTGSTEVGKIIMQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 238 QAAKG-IKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGL 316
Cdd:cd07142 239 LAAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 317 DEGINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQELA--GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEE 394
Cdd:cd07142 319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGskGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515625329 395 LIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07142 399 VIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
19-468 |
2.55e-121 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 363.67 E-value: 2.55e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 19 KAVAVTNPATGELIGHAPISSETELDRAIERSHIA-----QKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGK 93
Cdd:PLN02467 23 KRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 94 PLEEATGEVVYGASFIEWFAEEA----KRTYGD-SIPSTVAGKHLVtiKQPIGVACAITPWNFPIAMITRKAAPALAAGC 168
Cdd:PLN02467 103 PLDEAAWDMDDVAGCFEYYADLAealdAKQKAPvSLPMETFKGYVL--KEPLGVVGLITPWNYPLLMATWKVAPALAAGC 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 169 SFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEQiGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSM 248
Cdd:PLN02467 181 TAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEA-GAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 249 ELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISE 328
Cdd:PLN02467 260 ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 329 RAKQNIQGLIDRAIEQGAQPVT----PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIY 404
Cdd:PLN02467 340 GQYEKVLKFISTAKSEGATILCggkrPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHY 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515625329 405 GLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:PLN02467 420 GLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
16-471 |
4.71e-120 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 359.83 E-value: 4.71e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 16 EADKAVAVTNPATGELIGHAPISSETELDRAIERSHIA-QKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKP 94
Cdd:cd07113 12 QSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 95 LEEATG-EVVYGASFIEWFAEEAKRTYGD----SIPSTVAGKHLV-TIKQPIGVACAITPWNFPIAMITRKAAPALAAGC 168
Cdd:cd07113 92 IHLSRAfEVGQSANFLRYFAGWATKINGEtlapSIPSMQGERYTAfTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGC 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 169 SFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSpeQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSM 248
Cdd:cd07113 172 TIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG--AVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 249 ELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISE 328
Cdd:cd07113 250 ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 329 RAKQNIQGLIDRAIEQGAQPVTPTQELA--GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGL 406
Cdd:cd07113 330 PHFDKVCSYLDDARAEGDEIVRGGEALAgeGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGL 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515625329 407 ASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIKYLC 471
Cdd:cd07113 410 TASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
69-465 |
3.38e-119 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 355.20 E-value: 3.38e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 69 LKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITP 148
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 149 WNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGS 228
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGET-VGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 229 TRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQ 308
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 309 QLKIGNGLDEG-INIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQ--ELAGLFIQPVILKDVKHDMDIVQQEIFGPVAP 385
Cdd:PRK10090 240 AVQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEGARVALGGKavEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 386 VMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYM 465
Cdd:PRK10090 320 VVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYL 399
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
4-468 |
1.07e-117 |
|
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: 353.58 E-value: 1.07e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 4 INNQrllsFMVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQK---EWAKIPAKSRAAILKAWHQLILENK 80
Cdd:cd07141 11 INNE----WHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 81 DDLAHLMTIEQGKPLEEA-TGEVVYGASFIEWFAEEAKRTYGDSIPstVAGKHLV-TIKQPIGVACAITPWNFPIAMITR 158
Cdd:cd07141 87 AYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIP--MDGDFFTyTRHEPVGVCGQIIPWNFPLLMAAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 159 KAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEQiGELFTSHPLIKKISFTGSTRVGSILMAQ 238
Cdd:cd07141 165 KLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTA-GAAISSHPDIDKVAFTGSTEVGKLIQQA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 239 AAK-GIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLD 317
Cdd:cd07141 244 AGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 318 EGINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQELA--GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEEL 395
Cdd:cd07141 324 PKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGdkGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEV 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515625329 396 IEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07141 404 IERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVK 476
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
4-470 |
1.17e-117 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 353.57 E-value: 1.17e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 4 INNQrllsFMVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDL 83
Cdd:cd07559 5 INGE----WVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 84 AHLMTIEQGKPLEEATGEVV--------YGASFIEwfAEEAKRTYGDSipSTVAgkhlVTIKQPIGVACAITPWNFPIAM 155
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIplaidhfrYFAGVIR--AQEGSLSEIDE--DTLS----YHFHEPLGVVGQIIPWNFPLLM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 156 ITRKAAPALAAGCSFIVKPSDETPLSAFAVVELaYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSIL 235
Cdd:cd07559 153 AAWKLAPALAAGNTVVLKPASQTPLSILVLMEL-IGDLLPKGVVNVVTGFGSE-AGKPLASHPRIAKLAFTGSTTVGRLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 236 MAQAAKGIKRTSMELGGNAPFIVFDDA-----DIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQL 310
Cdd:cd07559 231 MQYAAENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 311 KIGNGLDEGINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQ------ELAGLFIQPVILKDVKHDMDIVQQEIFGPVA 384
Cdd:cd07559 311 KVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGErltlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 385 PVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEY 464
Cdd:cd07559 391 AVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHY 470
|
....*.
gi 515625329 465 MDIKYL 470
Cdd:cd07559 471 QQTKNI 476
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
2-468 |
1.44e-116 |
|
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: 351.06 E-value: 1.44e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 2 LEINNQrllsFMVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIA-QKEWA-KIPAKSRAAILKAWHQLILEN 79
Cdd:cd07143 9 LFINGE----FVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 80 KDDLAHLMTIEQGKP-LEEATGEVVYGASFIEWFAEEAKRTYGDSIpSTVAGKHLVTIKQPIGVACAITPWNFPIAMITR 158
Cdd:cd07143 85 LDYLASIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVI-ETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 159 KAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSpEQIGELFTSHPLIKKISFTGSTRVGSILMAQ 238
Cdd:cd07143 164 KIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYG-RTCGNAISSHMDIDKVAFTGSTLVGRKVMEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 239 AAKG-IKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLD 317
Cdd:cd07143 243 AAKSnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 318 EGINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQELA--GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEEL 395
Cdd:cd07143 323 EDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGneGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEA 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515625329 396 IEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGIND-GLISTEVaPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07143 403 IKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCyNLLHHQV-PFGGYKQSGIGRELGEYALENYTQIK 475
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
23-463 |
6.48e-116 |
|
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: 348.21 E-value: 6.48e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEV 102
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 103 VYGASFIEWFAEEAKRTYGDSIPSTVAGKHLvTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSA 182
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLHY-TLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 183 FAVVELAyQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDA 262
Cdd:cd07107 160 LRLAELA-REVLPPGVFNILPGDGAT-AGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 263 DIDAAVQGAMAS-KFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRA 341
Cdd:cd07107 238 DPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 342 IEQGAQPVT-----PTQELA-GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNI 415
Cdd:cd07107 318 KREGARLVTgggrpEGPALEgGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 515625329 416 HRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREgakEGIDE 463
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGRE---ECLEE 442
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
4-467 |
3.25e-115 |
|
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: 346.87 E-value: 3.25e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 4 INNQrllsfMVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKI-PAKSRAAILKAWHQLILENKDD 82
Cdd:cd07082 6 INGE-----WKESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 83 LAHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTI----KQPIGVACAITPWNFPIAMITR 158
Cdd:cd07082 81 VANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIaqvrREPLGVVLAIGPFNYPLNLTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 159 KAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQ 238
Cdd:cd07082 161 KLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGRE-IGDPLVTHGRIDVISFTGSTEVGNRLKKQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 239 AakGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDE 318
Cdd:cd07082 240 H--PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 319 GINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEM 398
Cdd:cd07082 318 GVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515625329 399 ANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDgliSTE----VAPFGGVKQSGIGREGAKEGIdEYMDI 467
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINS---KCQrgpdHFPFLGRKDSGIGTQGIGDAL-RSMTR 466
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
25-472 |
4.29e-115 |
|
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: 346.59 E-value: 4.29e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 25 NPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEAT-GEVV 103
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 104 YGASFIEWFAEEAKRTYGdsiPSTVAGKHLVTIK------QPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDE 177
Cdd:cd07098 82 VTCEKIRWTLKHGEKALR---PESRPGGLLMFYKrarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 178 TPLSA---FAVVELAYQA-GIPKNLLQVVLGdSPEQiGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGN 253
Cdd:cd07098 159 VAWSSgffLSIIRECLAAcGHDPDLVQLVTC-LPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 254 APFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQN 333
Cdd:cd07098 237 DPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 334 IQGLIDRAIEQGAQ------PVTPTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLA 407
Cdd:cd07098 317 LEELVADAVEKGARllaggkRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515625329 408 SYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVA--PFGGVKQSGIGREGAKEGIDEYMDIKYLCF 472
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
25-462 |
8.30e-115 |
|
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: 345.39 E-value: 8.30e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 25 NPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVVY 104
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 105 GASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFA 184
Cdd:cd07102 82 MLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 185 VVELAYQAGIPKNLLQVVLGDSPeqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADI 264
Cdd:cd07102 162 FAAAFAEAGLPEGVFQVLHLSHE--TSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 265 DAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAIEQ 344
Cdd:cd07102 240 DAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 345 GAQPVTPTQELA-----GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVW 419
Cdd:cd07102 320 GARALIDGALFPedkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAE 399
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 515625329 420 KVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGID 462
Cdd:cd07102 400 ALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYD 442
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
2-468 |
4.10e-113 |
|
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: 341.74 E-value: 4.10e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 2 LEINNQrllsFMVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKD 81
Cdd:cd07117 3 LFINGE----WVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 82 DLAHLMTIEQGKPLEEATG-EVVYGASFIEWFAEEAKrtyGDSIPSTVAGKHLVTI--KQPIGVACAITPWNFPIAMITR 158
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIR---AEEGSANMIDEDTLSIvlREPIGVVGQIIPWNFPFLMAAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 159 KAAPALAAGCSFIVKPSDETPLSAFAVVELaYQAGIPKNLLQVVLGDSPEQiGELFTSHPLIKKISFTGSTRVGSILMAQ 238
Cdd:cd07117 156 KLAPALAAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKS-GEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 239 AAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDE 318
Cdd:cd07117 234 AAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 319 GINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQEL------AGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSD 392
Cdd:cd07117 314 DTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLtengldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515625329 393 EELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07117 394 DEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMK 469
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
29-465 |
1.30e-111 |
|
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: 336.96 E-value: 1.30e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 29 GELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVVYGASF 108
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 109 IEWFAEEAKRTYGDSIPSTvAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSA-FAVVE 187
Cdd:cd07152 81 LHEAAGLPTQPQGEILPSA-PGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 188 LAYQAGIPKNLLQVVLGDSpeQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAA 267
Cdd:cd07152 160 LFEEAGLPAGVLHVLPGGA--DAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 268 VQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAIEQGAQ 347
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 348 PVT-PTQElaGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALE 426
Cdd:cd07152 318 LEAgGTYD--GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 515625329 427 YGMVGINDGLISTE-VAPFGGVKQSGIG-REGAKEGIDEYM 465
Cdd:cd07152 396 TGMLHINDQTVNDEpHNPFGGMGASGNGsRFGGPANWEEFT 436
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
4-453 |
1.44e-110 |
|
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: 336.50 E-value: 1.44e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 4 INNQRLlsfmvtEADKAVAVTNPA-TGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDD 82
Cdd:cd07124 37 IGGKEV------RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 83 LAHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRtYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAP 162
Cdd:cd07124 111 LAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLR-LRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 163 ALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDsPEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKG 242
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGP-GEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 243 ------IKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGL 316
Cdd:cd07124 269 qpgqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 317 DEGINIGPVISERAKQNIQGLIDRAIEQG---AQPVTPTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDE 393
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEGrllLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFD 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515625329 394 ELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGliST----EVAPFGGVKQSGIG 453
Cdd:cd07124 429 EALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRK--ITgalvGRQPFGGFKMSGTG 490
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
4-468 |
1.94e-108 |
|
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: 329.86 E-value: 1.94e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 4 INNQRLLSfmvtEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDL 83
Cdd:cd07085 5 INGEWVES----KTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 84 AHLMTIEQGKPLEEATGEVVYGASFIEwFAEeakrtygdSIPSTVAGKHL---------VTIKQPIGVACAITPWNFPiA 154
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVE-FAC--------SIPHLLKGEYLenvargidtYSYRQPLGVVAGITPFNFP-A 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 155 MITR-KAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqiGELFTSHPLIKKISFTGSTRVGS 233
Cdd:cd07085 151 MIPLwMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEA--VNALLDHPDIKAVSFVGSTPVGE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 234 ILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIG 313
Cdd:cd07085 229 YIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 314 NGLDEGINIGPVISERAKQNIQGLIDRAIEQGAQ-------PVTPTQElAGLFIQPVILKDVKHDMDIVQQEIFGPVAPV 386
Cdd:cd07085 309 AGDDPGADMGPVISPAAKERIEGLIESGVEEGAKlvldgrgVKVPGYE-NGNFVGPTILDNVTPDMKIYKEEIFGPVLSI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 387 MKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGlISTEVA--PFGGVKQSGIGREGA--KEGID 462
Cdd:cd07085 388 VRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVP-IPVPLAffSFGGWKGSFFGDLHFygKDGVR 466
|
....*.
gi 515625329 463 EYMDIK 468
Cdd:cd07085 467 FYTQTK 472
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
2-468 |
3.08e-108 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 331.39 E-value: 3.08e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 2 LEINNQRLL---SFMVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKE--WAKIPAKSRAAILKAWHQLI 76
Cdd:PLN02466 53 VQVSYTQLLingQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 77 LENKDDLAHLMTIEQGKPLEEATG-EVVYGASFIEWFAEEAKRTYGDSIPSTvaGKHLV-TIKQPIGVACAITPWNFPIA 154
Cdd:PLN02466 133 EKHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPAD--GPHHVqTLHEPIGVAGQIIPWNFPLL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 155 MITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEQiGELFTSHPLIKKISFTGSTRVGSI 234
Cdd:PLN02466 211 MFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTA-GAALASHMDVDKLAFTGSTDTGKI 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 235 LMAQAAKG-IKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIG 313
Cdd:PLN02466 290 VLELAAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 314 NGLDEGINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQELA--GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDS 391
Cdd:PLN02466 370 DPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGskGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKD 449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515625329 392 DEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:PLN02466 450 LDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
2-468 |
6.29e-106 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 324.08 E-value: 6.29e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 2 LEINNQrllsFMVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIA--QKEWAKIPAKSRAAILKAWHQLILEN 79
Cdd:PLN02766 23 LFINGE----FVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 80 KDDLAHLMTIEQGKPLeeATGEVV---YGASFIEWFAEEAKRTYGDSIpsTVAGK-HLVTIKQPIGVACAITPWNFPIAM 155
Cdd:PLN02766 99 IEELAALDTIDAGKLF--ALGKAVdipAAAGLLRYYAGAADKIHGETL--KMSRQlQGYTLKEPIGVVGHIIPWNFPSTM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 156 ITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEQiGELFTSHPLIKKISFTGSTRVGSIL 235
Cdd:PLN02766 175 FFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTA-GAAIASHMDVDKVSFTGSTEVGRKI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 236 MAQAAKG-IKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGN 314
Cdd:PLN02766 254 MQAAATSnLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 315 GLDEGINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQELA--GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSD 392
Cdd:PLN02766 334 PFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGdkGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515625329 393 EELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVK 489
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
4-468 |
6.63e-103 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 315.97 E-value: 6.63e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 4 INNQrllsFMVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIA--QKEWAKIPAKSRAAILKAWHQLILENKD 81
Cdd:cd07140 10 INGE----FVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 82 DLAHLMTIEQGKPLEEATGEVVyGASFIEW--FAEEAKRTYGDSIPSTVA--GKHL-VTIKQPIGVACAITPWNFPIAMI 156
Cdd:cd07140 86 ELATIESLDSGAVYTLALKTHV-GMSIQTFryFAGWCDKIQGKTIPINQArpNRNLtLTKREPIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 157 TRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGdSPEQIGELFTSHPLIKKISFTGSTRVGSILM 236
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPG-SGSLVGQRLSDHPDVRKLGFTGSTPIGKHIM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 237 AQAAKG-IKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNG 315
Cdd:cd07140 244 KSCAVSnLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 316 LDEGINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQEL--AGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSD- 392
Cdd:cd07140 324 LDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVdrPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGd 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515625329 393 -EELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:cd07140 404 vDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
20-468 |
5.22e-101 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 310.13 E-value: 5.22e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 20 AVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEAT 99
Cdd:PRK09406 2 PIATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 100 GEVVYGASFIEWFAEEAKRTYGD--SIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDE 177
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLADepADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 178 TPLSAFAVVELAYQAGIPKNLLQVVL--GDSPEQIgelfTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAP 255
Cdd:PRK09406 162 VPQTALYLADLFRRAGFPDGCFQTLLvgSGAVEAI----LRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 256 FIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQ 335
Cdd:PRK09406 238 FIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 336 GLIDRAIEQGAQPVTPTQELA--GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQ 413
Cdd:PRK09406 318 KQVDDAVAAGATILCGGKRPDgpGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 515625329 414 NIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:PRK09406 398 DEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIK 452
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
16-465 |
1.47e-99 |
|
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: 307.01 E-value: 1.47e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 16 EADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPL 95
Cdd:cd07111 34 ENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 96 EEA-TGEVVYGASFIEWFAEEAkrtygDSIPSTVAGKhlvtikQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKP 174
Cdd:cd07111 114 RESrDCDIPLVARHFYHHAGWA-----QLLDTELAGW------KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 175 SDETPLSAFAVVELAYQAGIPKNLLQVVLGDSpeQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNA 254
Cdd:cd07111 183 AEYTPLTALLFAEICAEAGLPPGVLNIVTGNG--SFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 255 PFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNI 334
Cdd:cd07111 261 PFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 335 QGLIDRAIEQGAQPVTPTQELA--GLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYS 412
Cdd:cd07111 341 RELVEEGRAEGADVFQPGADLPskGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWS 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 515625329 413 QNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYM 465
Cdd:cd07111 421 ENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYL 473
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
2-451 |
1.26e-94 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 295.31 E-value: 1.26e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 2 LEINNQRllsfmVTEADKAVaVTNPA-TGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENK 80
Cdd:PRK03137 39 LIIGGER-----ITTEDKIV-SINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 81 DDLAHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRtYGDSIP-STVAGKHLVTIKQPIGVACAITPWNFPIAMITRK 159
Cdd:PRK03137 113 HEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLK-LADGKPvESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 160 AAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGdSPEQIGELFTSHPLIKKISFTGSTRVGSILMAQA 239
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPG-SGSEVGDYLVDHPKTRFITFTGSREVGLRIYERA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 240 AK---G---IKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIG 313
Cdd:PRK03137 271 AKvqpGqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 314 NGLDEGiNIGPVISERAKQNIQGLIDRAIEQGaQPVT--PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDS 391
Cdd:PRK03137 351 NPEDNA-YMGPVINQASFDKIMSYIEIGKEEG-RLVLggEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515625329 392 DEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVA--PFGGVKQSG 451
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGyhPFGGFNMSG 490
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
19-465 |
3.79e-92 |
|
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: 287.57 E-value: 3.79e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 19 KAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEA 98
Cdd:cd07130 12 GVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 99 TGEVvygASFIEW--FAEEAKRT-YGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPS 175
Cdd:cd07130 92 LGEV---QEMIDIcdFAVGLSRQlYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 176 DETPLSAFAV----VELAYQAGIPKNLLQVVLGDSpeQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELG 251
Cdd:cd07130 169 PTTPLTAIAVtkivARVLEKNGLPGAIASLVCGGA--DVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 252 GNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAK 331
Cdd:cd07130 247 GNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 332 QNIQGLIDRAIEQGAQPVT--PTQELAGLFIQPVILkDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASY 409
Cdd:cd07130 327 DNYLAAIEEAKSQGGTVLFggKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSS 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 515625329 410 FYSQNIHRV--WKVAEALEYGMVGINDGLISTEV-APFGGVKQSGIGREGAKEGIDEYM 465
Cdd:cd07130 406 IFTTDLRNAfrWLGPKGSDCGIVNVNIGTSGAEIgGAFGGEKETGGGRESGSDAWKQYM 464
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
22-468 |
8.94e-90 |
|
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: 282.04 E-value: 8.94e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 22 AVTNPATGELIGHAPISSETELDRAIE--RSHIAQKEWAKIPAkSRAAILKAWHQLILENKDDLAHLMTIEQGKP----- 94
Cdd:TIGR04284 18 PTVNPATEEVLGVAADATAADMDAAIAaaRRAFDETDWSRDTA-LRVRCLRQLRDALRAHVEELRELTIAEVGAPrmlta 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 95 ---LEEATGEVVYGASFIEWFaeEAKRTYGDSIPSTVAGKHLVTiKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFI 171
Cdd:TIGR04284 97 gaqLEGPVDDLGFAADLAESY--AWTTDLGVASPMGIPTRRTLR-REAVGVVGAITPWNFPHQINLAKLGPALAAGNTVV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 172 VKPSDETPLSAFAVVEL-AYQAGIPKNLLQVVLgDSPEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMEL 250
Cdd:TIGR04284 174 LKPAPDTPWCAAVLGELiAEHTDFPPGVVNIVT-SSDHRLGALLAKDPRVDMVSFTGSTATGRAVMADAAATLKKVFLEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 251 GGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERA 330
Cdd:TIGR04284 253 GGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPGTVCGPVISARQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 331 KQNIQGLIDRAIEQGAQPVT----PTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGL 406
Cdd:TIGR04284 333 RDRVQSYLDLAVAEGGRFACgggrPADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGL 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515625329 407 ASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:TIGR04284 413 SGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETK 474
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
24-470 |
7.29e-89 |
|
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: 279.34 E-value: 7.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 24 TNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVV 103
Cdd:cd07116 21 ITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAADI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 104 --------YGASFIEwfAEEAKRTYGDSipSTVAgkhlVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPS 175
Cdd:cd07116 101 plaidhfrYFAGCIR--AQEGSISEIDE--NTVA----YHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 176 DETPLSAFAVVELAYQAgIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAP 255
Cdd:cd07116 173 EQTPASILVLMELIGDL-LPPGVVNVVNGFGLE-AGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 256 FIVF------DDADIDAAVQGAMASKFrNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISER 329
Cdd:cd07116 251 NIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 330 AKQNIQGLIDRAIEQGAQPVTPTQ------ELAGLFIQPVILKDvKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTI 403
Cdd:cd07116 330 QLEKILSYIDIGKEEGAEVLTGGErnelggLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTL 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515625329 404 YGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIKYL 470
Cdd:cd07116 409 YGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 475
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
13-468 |
8.54e-89 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 278.67 E-value: 8.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 13 MVTEADKAVAVtNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQG 92
Cdd:PRK13968 2 TITPATHAISV-NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 93 KPLEEATGEVVYGASFIEWFAEEAKRTYGDSiPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIV 172
Cdd:PRK13968 81 KPINQARAEVAKSANLCDWYAEHGPAMLKAE-PTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 173 KPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSpEQIGELFTShPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGG 252
Cdd:PRK13968 160 KHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADN-DGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 253 NAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQ 332
Cdd:PRK13968 238 SDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 333 NIQGLIDRAIEQGAQPVTPTQELAGL--FIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYF 410
Cdd:PRK13968 318 ELHHQVEATLAEGARLLLGGEKIAGAgnYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 515625329 411 YSQNIHRVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:PRK13968 398 FTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQ 455
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
2-465 |
5.66e-87 |
|
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: 275.59 E-value: 5.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 2 LEINNQRllsfmVTEADKAVAVtNPA-TGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENK 80
Cdd:TIGR01237 35 LVINGER-----VETENKIVSI-NPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 81 DDLAHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKA 160
Cdd:TIGR01237 109 HEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 161 APALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAA 240
Cdd:TIGR01237 189 VAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSE-VGDYLVDHPKTSLITFTGSREVGTRIFERAA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 241 K------GIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGN 314
Cdd:TIGR01237 268 KvqpgqkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 315 GLDEGINIGPVISERAKQNIQGLIDRAIEQG----AQPVTPTQelaGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFD 390
Cdd:TIGR01237 348 PDSADVYVGPVIDQKSFNKIMEYIEIGKAEGrlvsGGCGDDSK---GYFIGPTIFADVDRKARLAQEEIFGPVVAFIRAS 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515625329 391 SDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVA--PFGGVKQSGIgreGAKEGIDEYM 465
Cdd:TIGR01237 425 DFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGyqPFGGFKMSGT---DSKAGGPDYL 498
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
23-456 |
9.36e-86 |
|
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: 270.83 E-value: 9.36e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 23 VTNPATGELIGHAPISSETELDRAIERSHIAQKEWAK-IPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGE 101
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNwLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 102 VVYGASFIEWFAEEAKRTYGDSIP----STVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDE 177
Cdd:cd07148 83 VTRAIDGVELAADELGQLGGREIPmgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 178 TPLSAFAVVELAYQAGIPKNLLQVVLGDSpeQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGiKRTSMELGGNAPFI 257
Cdd:cd07148 163 TPLSCLAFVDLLHEAGLPEGWCQAVPCEN--AVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 258 VFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGL 337
Cdd:cd07148 240 VDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 338 IDRAIEQGAQPVTPTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHR 417
Cdd:cd07148 320 VNEAVAAGARLLCGGKRLSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDV 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 515625329 418 VWKVAEALEYGMVGIND-GLISTEVAPFGGVKQSGIGREG 456
Cdd:cd07148 400 ALKAVRRLDATAVMVNDhTAFRVDWMPFAGRRQSGYGTGG 439
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
15-465 |
1.14e-85 |
|
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: 272.15 E-value: 1.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 15 TEADKAVAVTNPATGE-LIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGK 93
Cdd:cd07125 42 TETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 94 PLEEATGEVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVK 173
Cdd:cd07125 122 TLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 174 PSDETPLSAFAVVELAYQAGIPKNLLQVVLGDsPEQIGELFTSHPLIKKISFTGSTRVGS-ILMAQAAKGIKRT--SMEL 250
Cdd:cd07125 202 PAEQTPLIAARAVELLHEAGVPRDVLQLVPGD-GEEIGEALVAHPRIDGVIFTGSTETAKlINRALAERDGPILplIAET 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 251 GG-NApFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISER 329
Cdd:cd07125 281 GGkNA-MIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 330 AKQNIQGLID------RAIEQgaqpvTPTQELAGLFIQPVIlKDVKHDMDIvQQEIFGPVAPVMKFDSD--EELIEMAND 401
Cdd:cd07125 360 AGKLLRAHTElmrgeaWLIAP-----APLDDGNGYFVAPGI-IEIVGIFDL-TTEVFGPILHVIRFKAEdlDEAIEDINA 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515625329 402 TIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLIS--TEVAPFGGVKQSGIgreGAKEGIDEYM 465
Cdd:cd07125 433 TGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGaiVGRQPFGGWGLSGT---GPKAGGPNYL 495
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
22-468 |
1.28e-85 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 271.38 E-value: 1.28e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 22 AVTNPATGELIGHAPISSETELDRAIE--RSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEAT 99
Cdd:PRK09847 38 ETVDPVTQAPLAKIARGKSVDIDRAVSaaRGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 100 GEVVYGAS-FIEWFAEEAKRTYGDSIPsTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDET 178
Cdd:PRK09847 118 RDDIPGAArAIRWYAEAIDKVYGEVAT-TSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 179 PLSAFAVVELAYQAGIPKNLLQVVLGDSPEQiGELFTSHPLIKKISFTGSTRVGSILMAQAAKG-IKRTSMELGGNAPFI 257
Cdd:PRK09847 197 PLSAIRLAGLAKEAGLPDGVLNVVTGFGHEA-GQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSnMKRVWLEAGGKSANI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 258 VFDDA-DIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQG 336
Cdd:PRK09847 276 VFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 337 LIDRAIEQGAQPVTPTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIH 416
Cdd:PRK09847 356 FIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLS 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 515625329 417 RVWKVAEALEYGMVGINDGLISTEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:PRK09847 436 RAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
19-468 |
1.72e-84 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 268.55 E-value: 1.72e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 19 KAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEA 98
Cdd:PLN00412 31 KSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 99 TGEVVYGASFIEWFAEEAKRTYG-------DSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFI 171
Cdd:PLN00412 111 VTEVVRSGDLISYTAEEGVRILGegkflvsDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 172 VKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGstrvGSILMAQAAK-GIKRTSMEL 250
Cdd:PLN00412 191 LKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSE-IGDFLTMHPGVNCISFTG----GDTGIAISKKaGMVPLQMEL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 251 GGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEgINIGPVISERA 330
Cdd:PLN00412 266 GGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDD-CDITPVVSESS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 331 KQNIQGLIDRAIEQGAQPVTPTQELAGLfIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYF 410
Cdd:PLN00412 345 ANFIEGLVMDAKEKGATFCQEWKREGNL-IWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCV 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 515625329 411 YSQNIHRVWKVAEALEYGMVGINDGLI-STEVAPFGGVKQSGIGREGAKEGIDEYMDIK 468
Cdd:PLN00412 424 FTRDINKAILISDAMETGTVQINSAPArGPDHFPFQGLKDSGIGSQGITNSINMMTKVK 482
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
42-462 |
1.22e-76 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 246.41 E-value: 1.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 42 ELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVVYGASFIEwFAEEAKRTYG 121
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKID-ISIKAYHERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 122 DSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQV 201
Cdd:cd07095 80 GERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 202 VLGDSPEqiGELFTSHPLIKKISFTGSTRVGSILMAQ-AAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAG 280
Cdd:cd07095 160 VQGGRET--GEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 281 QTCVCANRFYIHSK-VHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQ--ELAG 357
Cdd:cd07095 238 QRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMErlVAGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 358 LFIQPVILkDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQN---IHRVWKVAEAleyGMVGIN- 433
Cdd:cd07095 318 AFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDealFERFLARIRA---GIVNWNr 393
|
410 420 430
....*....|....*....|....*....|.
gi 515625329 434 --DGLISTevAPFGGVKQSGIGREGAKEGID 462
Cdd:cd07095 394 ptTGASST--APFGGVGLSGNHRPSAYYAAD 422
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
14-465 |
2.42e-76 |
|
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: 247.49 E-value: 2.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 14 VTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGK 93
Cdd:cd07083 28 VDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 94 PLEEATGEVVYGASFIEWFAEEAKR-TYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIV 172
Cdd:cd07083 108 NWVEAIDDVAEAIDFIRYYARAALRlRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 173 KPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAK------GIKRT 246
Cdd:cd07083 188 KPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEE-VGAYLTEHERIRGINFTGSLETGKKIYEAAARlapgqtWFKRL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 247 SMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVI 326
Cdd:cd07083 267 YVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 327 SERAKQNIQGLIDRA------IEQGAQPvtptqELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDE--ELIEM 398
Cdd:cd07083 347 DAEQEAKVLSYIEHGknegqlVLGGKRL-----EGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEV 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515625329 399 ANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVA--PFGGVKQSGIgreGAKEGIDEYM 465
Cdd:cd07083 422 ANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGvqPFGGFKLSGT---NAKTGGPHYL 487
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
69-464 |
1.18e-71 |
|
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: 233.27 E-value: 1.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 69 LKAWHQLILENKDDLAHLMTIEQGKPLEEAT--------GEVVYGASFIEWFAEEAKRTygDSIPSTVAGKhlVTI-KQP 139
Cdd:cd07135 33 LKQLYWAVKDNEEAIVEALKKDLGRPPFETLltevsgvkNDILHMLKNLKKWAKDEKVK--DGPLAFMFGK--PRIrKEP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 140 IGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELayqagIPKNL----LQVVLGDSPEqIGELFT 215
Cdd:cd07135 109 LGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-----VPKYLdpdaFQVVQGGVPE-TTALLE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 216 SHplIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKV 295
Cdd:cd07135 183 QK--FDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 296 HDEFVAKFDQAVQQLkIGNGLDEGINIGPVISERAKQNIQGLIDRAieqGAQPVTP-TQELAGLFIQPVILKDVKHDMDI 374
Cdd:cd07135 261 YDEFVEELKKVLDEF-YPGGANASPDYTRIVNPRHFNRLKSLLDTT---KGKVVIGgEMDEATRFIPPTIVSDVSWDDSL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 375 VQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEV--APFGGVKQSGI 452
Cdd:cd07135 337 MSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVdnAPFGGVGDSGY 416
|
410
....*....|..
gi 515625329 453 GREGAKEGIDEY 464
Cdd:cd07135 417 GAYHGKYGFDTF 428
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
19-457 |
3.85e-70 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 231.00 E-value: 3.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 19 KAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEA 98
Cdd:PRK09457 15 EAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 99 TGEVvygASFIEWFA----EEAKRTyGDSIPSTVAGKHLVTIKqPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKP 174
Cdd:PRK09457 95 ATEV---TAMINKIAisiqAYHERT-GEKRSEMADGAAVLRHR-PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 175 SDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqiGELFTSHPLIKKISFTGSTRVGSILMAQ-AAKGIKRTSMELGGN 253
Cdd:PRK09457 170 SELTPWVAELTVKLWQQAGLPAGVLNLVQGGRET--GKALAAHPDIDGLLFTGSANTGYLLHRQfAGQPEKILALEMGGN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 254 APFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVH-DEFVAKFDQAVQQLKIGNGLDEGIN-IGPVISERAK 331
Cdd:PRK09457 248 NPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDAEPQPfMGAVISEQAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 332 QNIQGLIDRAIEQGAQP-VTPTQELAGL-FIQPVILkDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASY 409
Cdd:PRK09457 328 QGLVAAQAQLLALGGKSlLEMTQLQAGTgLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAG 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 515625329 410 FYS---QNIHRVWKVAEAleyGMVGIN---DGLISTevAPFGGVKQSGIGREGA 457
Cdd:PRK09457 407 LLSddrEDYDQFLLEIRA---GIVNWNkplTGASSA--APFGGVGASGNHRPSA 455
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
61-463 |
4.98e-69 |
|
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: 226.25 E-value: 4.98e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 61 PAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEA----TGEVVYGASFI-----EWFAEEAKRTygdsiPSTVAGK 131
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteIAVVLGEIDHAlkhlkKWMKPRRVSV-----PLLLQPA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 132 HLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAgIPKNLLQVVLGDsPEQIG 211
Cdd:cd07087 93 KAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGG-VEVAT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 212 ELfTSHPLiKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYI 291
Cdd:cd07087 171 AL-LAEPF-DHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 292 HSKVHDEFVAKFDQAVQQLkIGNGLDEGINIGPVISERAKQNIQGLIDRA-IEQGAQpvtptQELAGLFIQPVILKDVKH 370
Cdd:cd07087 249 HESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDGkVVIGGQ-----VDKEERYIAPTILDDVSP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 371 DMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLI--STEVAPFGGVK 448
Cdd:cd07087 323 DSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLhaAIPNLPFGGVG 402
|
410
....*....|....*
gi 515625329 449 QSGIGREGAKEGIDE 463
Cdd:cd07087 403 NSGMGAYHGKAGFDT 417
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
44-464 |
2.94e-68 |
|
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: 224.41 E-value: 2.94e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 44 DRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVVYG---------ASFIEWFAE 114
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPvlseinhaiKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 115 EAKRTygdsiPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAgI 194
Cdd:cd07134 81 KRVRT-----PLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-F 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 195 PKNLLQVVLGDsPEqigelfTSHPLIKK----ISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQG 270
Cdd:cd07134 155 DEDEVAVFEGD-AE------VAQALLELpfdhIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 271 AMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQ-LKIGNGLDEGINIGPVISERAKQNIQGLIDRAIEQGAQPV 349
Cdd:cd07134 228 IAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKfYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 350 TPTQ-ELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYG 428
Cdd:cd07134 308 FGGQfDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 515625329 429 MVGINDGLIstEVA----PFGGVKQSGIGREGAKEGIDEY 464
Cdd:cd07134 388 GVVVNDVVL--HFLnpnlPFGGVNNSGIGSYHGVYGFKAF 425
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
17-453 |
1.32e-64 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 226.28 E-value: 1.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 17 ADKAVAVTNPA-TGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPL 95
Cdd:PRK11905 565 DGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTL 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 96 EEATGEVVYGASFIEWFAEEAKRTYGDSIPstvagkhlvtikQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPS 175
Cdd:PRK11905 645 ANAIAEVREAVDFLRYYAAQARRLLNGPGH------------KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPA 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 176 DETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKgikrtsmELGGNAP 255
Cdd:PRK11905 713 EQTPLIAARAVRLLHEAGVPKDALQLLPGDGRT-VGAALVADPRIAGVMFTGSTEVARLIQRTLAK-------RSGPPVP 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 256 FI----------VFDDADIDAAVQGAMASKFRNAGQTCvCANR-FYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGP 324
Cdd:PRK11905 785 LIaetggqnamiVDSSALPEQVVADVIASAFDSAGQRC-SALRvLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGP 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 325 VISERAKQNIQGLIDRAIEQG---AQPVTPTQELAGLFIQPVILKdVKHdMDIVQQEIFGPVAPVMKFDSDE--ELIEMA 399
Cdd:PRK11905 864 VIDAEAQANIEAHIEAMRAAGrlvHQLPLPAETEKGTFVAPTLIE-IDS-ISDLEREVFGPVLHVVRFKADEldRVIDDI 941
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 515625329 400 NDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVA--PFGGVKQSGIG 453
Cdd:PRK11905 942 NATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGvqPFGGEGLSGTG 997
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
11-468 |
1.53e-64 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 219.23 E-value: 1.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 11 SFMVTEADKAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIE 90
Cdd:PLN02419 121 SFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 91 QGKPLEEATGEVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPiAMITRKAAP-ALAAGCS 169
Cdd:PLN02419 201 QGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFP-AMIPLWMFPvAVTCGNT 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 170 FIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSpEQIGELFTSHPlIKKISFTGSTRVGSILMAQAAKGIKRTSME 249
Cdd:PLN02419 280 FILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTN-DTVNAICDDED-IRAVSFVGSNTAGMHIYARAAAKGKRIQSN 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 250 LGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANR--FYIHSKVHDEfvaKFDQAVQQLKIGNGLDEGINIGPVIS 327
Cdd:PLN02419 358 MGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvvFVGDAKSWED---KLVERAKALKVTCGSEPDADLGPVIS 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 328 ERAKQNIQGLIDRAIEQGAQ-------PVTPTQElAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMAN 400
Cdd:PLN02419 435 KQAKERICRLIQSGVDDGAKllldgrdIVVPGYE-KGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIIN 513
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515625329 401 DTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGL-ISTEVAPFGGVKQSGIGREG--AKEGIDEYMDIK 468
Cdd:PLN02419 514 KNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIpVPLPFFSFTGNKASFAGDLNfyGKAGVDFFTQIK 584
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
138-463 |
7.07e-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: 213.12 E-value: 7.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 138 QPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAgIPKNLLQVVLGDSpeQIGELFTSH 217
Cdd:cd07133 100 QPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTGGA--DVAAAFSSL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 218 P---LIkkisFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSK 294
Cdd:cd07133 177 PfdhLL----FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPED 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 295 VHDEFVAKFDQAVQQL--KIGNGLDeginIGPVISERAKQNIQGLIDRAIEQGAQ--PVTPTQELAGL--FIQPVILKDV 368
Cdd:cd07133 253 KLEEFVAAAKAAVAKMypTLADNPD----YTSIINERHYARLQGLLEDARAKGARviELNPAGEDFAAtrKLPPTLVLNV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 369 KHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGL--ISTEVAPFGG 446
Cdd:cd07133 329 TDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLlhVAQDDLPFGG 408
|
330
....*....|....*..
gi 515625329 447 VKQSGIGREGAKEGIDE 463
Cdd:cd07133 409 VGASGMGAYHGKEGFLT 425
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
5-453 |
1.17e-61 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 216.99 E-value: 1.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 5 NNQRLLSFMVTEADKAVAVTNPA-TGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDL 83
Cdd:PRK11904 548 EKQWQAGPIINGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAEL 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 84 AHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRTYGDSI--PSTVaGKHLVTIKQPIGVACAITPWNFPIAMITRKAA 161
Cdd:PRK11904 628 IALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEklPGPT-GESNELRLHGRGVFVCISPWNFPLAIFLGQVA 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 162 PALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVG-SILMAQAA 240
Cdd:PRK11904 707 AALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGAT-VGAALTADPRIAGVAFTGSTETArIINRTLAA 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 241 KG------IKRTsmelGG-NApFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIG 313
Cdd:PRK11904 786 RDgpivplIAET----GGqNA-MIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVG 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 314 NGLDEGINIGPVISERAKQNIQGLIDRAIEQG---AQPVTPTQELAGLFIQPVI--LKDVkhdmDIVQQEIFGPVAPVMK 388
Cdd:PRK11904 861 DPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLPAGTENGHFVAPTAfeIDSI----SQLEREVFGPILHVIR 936
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515625329 389 FDSDE--ELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLIST--EVAPFGGVKQSGIG 453
Cdd:PRK11904 937 YKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAvvGVQPFGGQGLSGTG 1005
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
19-465 |
9.75e-61 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 206.61 E-value: 9.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 19 KAVAVTNPATGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEA 98
Cdd:PLN02315 34 PLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 99 TGEVVYGASFIEWFAEEAKRTYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDET 178
Cdd:PLN02315 114 IGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 179 PLSAFA----VVELAYQAGIPKNLLQVVLGDSpeQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNA 254
Cdd:PLN02315 194 PLITIAmtklVAEVLEKNNLPGAIFTSFCGGA--EIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNN 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 255 PFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNI 334
Cdd:PLN02315 272 AIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 335 QGLIDRAIEQGAQPVT--PTQELAGLFIQPVILkDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYS 412
Cdd:PLN02315 352 EKGIEIIKSQGGKILTggSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFT 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 515625329 413 QNIHRV--WKVAEALEYGMVGINDGLISTEV-APFGGVKQSGIGREGAKEGIDEYM 465
Cdd:PLN02315 431 RNPETIfkWIGPLGSDCGIVNVNIPTNGAEIgGAFGGEKATGGGREAGSDSWKQYM 486
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
13-453 |
1.66e-60 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 214.03 E-value: 1.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 13 MVTEADKAVAVTNPA-TGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQ 91
Cdd:COG4230 564 GEAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREA 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 92 GKPLEEATGEVVYGASFIEWFAEEAKRTYGDSipstvagkhlvTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFI 171
Cdd:COG4230 644 GKTLPDAIAEVREAVDFCRYYAAQARRLFAAP-----------TVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVL 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 172 VKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDsPEQIGELFTSHPLIKKISFTGSTRVgsilmaqaAKGIKRT-SMEL 250
Cdd:COG4230 713 AKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGD-GETVGAALVADPRIAGVAFTGSTET--------ARLINRTlAARD 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 251 GGNAPFIvfddAD--------IDA------AVQGAMASKFRNAGQTCvCANR-FYIHSKVHDEFVAKFDQAVQQLKIGNG 315
Cdd:COG4230 784 GPIVPLI----AEtggqnamiVDSsalpeqVVDDVLASAFDSAGQRC-SALRvLCVQEDIADRVLEMLKGAMAELRVGDP 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 316 LDEGINIGPVISERAKQNIQGLIDRAIEQG---AQPVTPTQELAGLFIQPVI--LKDVKHdmdiVQQEIFGPVAPVMKFD 390
Cdd:COG4230 859 ADLSTDVGPVIDAEARANLEAHIERMRAEGrlvHQLPLPEECANGTFVAPTLieIDSISD----LEREVFGPVLHVVRYK 934
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515625329 391 SDE--ELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLIS--TEVAPFGGVKQSGIG 453
Cdd:COG4230 935 ADEldKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGavVGVQPFGGEGLSGTG 1001
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
61-462 |
8.15e-60 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 203.72 E-value: 8.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 61 PAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEA----TGEVVYGASFI-----EWFAEEAKRTYGDSIPstvaGK 131
Cdd:PTZ00381 27 PLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETkmteVLLTVAEIEHLlkhldEYLKPEKVDTVGVFGP----GK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 132 HLVtIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVEL--AYqagIPKNLLQVVLGDSPEQ 209
Cdd:PTZ00381 103 SYI-IPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLltKY---LDPSYVRVIEGGVEVT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 210 IgELfTSHPLiKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRF 289
Cdd:PTZ00381 179 T-EL-LKEPF-DHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 290 YIHSKVHDEFVAKFDQAVQQLkIGNGLDEGINIGPVISERAKQNIQGLIDRaiEQGAQPVTPTQELAGLFIQPVILKDVK 369
Cdd:PTZ00381 256 LVHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKD--HGGKVVYGGEVDIENKYVAPTIIVNPD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 370 HDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGL--ISTEVAPFGGV 447
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVfhLLNPNLPFGGV 412
|
410
....*....|....*
gi 515625329 448 KQSGIGREGAKEGID 462
Cdd:PTZ00381 413 GNSGMGAYHGKYGFD 427
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
136-462 |
1.01e-57 |
|
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: 197.34 E-value: 1.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 136 IKQPIGVACAITPWNFPIAMItrkAAP---ALAAGCSFIVKPSDETPLSAfAVVELAYQAGIPKNLLQVVLGDSPEqige 212
Cdd:cd07136 97 YYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTS-KVIAKIIEETFDEEYVAVVEGGVEE---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 213 lftSHPLIK----KISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANR 288
Cdd:cd07136 169 ---NQELLDqkfdYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 289 FYIHSKVHDEFVAKFDQAVQQLkIGNGLDEGINIGPVISERAKQNIQGLIDRA-IEQGAQpvtpTQElAGLFIQPVILKD 367
Cdd:cd07136 246 VLVHESVKEKFIKELKEEIKKF-YGEDPLESPDYGRIINEKHFDRLAGLLDNGkIVFGGN----TDR-ETLYIEPTILDN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 368 VKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLI--STEVAPFG 445
Cdd:cd07136 320 VTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMhlANPYLPFG 399
|
330
....*....|....*..
gi 515625329 446 GVKQSGIGREGAKEGID 462
Cdd:cd07136 400 GVGNSGMGSYHGKYSFD 416
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
13-453 |
1.34e-57 |
|
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: 198.21 E-value: 1.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 13 MVTEADKAVA----VTNPAT-GELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLM 87
Cdd:TIGR01238 41 IIGHSYKADGeaqpVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALC 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 88 TIEQGKPLEEATGEVVYGASFIEWFAEEAKRTYGDSIpstvagkhlvtiKQPIGVACAITPWNFPIAMITRKAAPALAAG 167
Cdd:TIGR01238 121 VREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFS------------VESRGVFVCISPWNFPLAIFTGQISAALAAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 168 CSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSpEQIGELFTSHPLIKKISFTGSTRVGSIL---MAQAAKGIK 244
Cdd:TIGR01238 189 NTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRG-ADVGAALTSDPRIAGVAFTGSTEVAQLInqtLAQREDAPV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 245 RTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGP 324
Cdd:TIGR01238 268 PLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 325 VISERAKQNIQGLID--RAIEQGAQPVTPTQELA---GLFIQPVILKdvKHDMDIVQQEIFGPVAPVMKFDSDE--ELIE 397
Cdd:TIGR01238 348 VIDAEAKQNLLAHIEhmSQTQKKIAQLTLDDSRAcqhGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAREldQIVD 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 515625329 398 MANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTEVA--PFGGVKQSGIG 453
Cdd:TIGR01238 426 QINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGGQGLSGTG 483
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
61-462 |
8.30e-53 |
|
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: 183.96 E-value: 8.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 61 PAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEAT--------GEVVYGASFI-EWFAEEAkrtygdsipstvAGK 131
Cdd:cd07132 18 PLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVlseillvkNEIKYAISNLpEWMKPEP------------VKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 132 HLVTI-------KQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELayqagIPKNL----LQ 200
Cdd:cd07132 86 NLATLlddvyiyKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLdkecYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 201 VVLGDSPEqIGEL----FtshpliKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKF 276
Cdd:cd07132 161 VVLGGVEE-TTELlkqrF------DYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 277 RNAGQTCVCANrfYI--HSKVHDEFVAKFDQAVQQLkIGNGLDEGINIGPVISERAKQNIQGLIDraieqGAQPVTPTQ- 353
Cdd:cd07132 234 INAGQTCIAPD--YVlcTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLS-----GGKVAIGGQt 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 354 ELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGIN 433
Cdd:cd07132 306 DEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVN 385
|
410 420 430
....*....|....*....|....*....|.
gi 515625329 434 DGL--ISTEVAPFGGVKQSGIGREGAKEGID 462
Cdd:cd07132 386 DTImhYTLDSLPFGGVGNSGMGAYHGKYSFD 416
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
16-453 |
1.92e-48 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 179.01 E-value: 1.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 16 EADKAVAVTNPA-TGELIGHAPISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKP 94
Cdd:PRK11809 656 AAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 95 LEEATGEVVYGASFIEWFAEEAKRTYGDSipstvagKHlvtikQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKP 174
Cdd:PRK11809 736 FSNAIAEVREAVDFLRYYAGQVRDDFDND-------TH-----RPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKP 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 175 SDETPLSAFAVVELAYQAGIPKNLLQVVLGDSpEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIK---RTS---M 248
Cdd:PRK11809 804 AEQTPLIAAQAVRILLEAGVPAGVVQLLPGRG-ETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDpqgRPIpliA 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 249 ELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISE 328
Cdd:PRK11809 883 ETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDA 962
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 329 RAKQNIQGLID------RAIEQGAQPvTPTQELAGLFIQP-VILKDvkhDMDIVQQEIFGPVAPVMKFDSDE--ELIEMA 399
Cdd:PRK11809 963 EAKANIERHIQamrakgRPVFQAARE-NSEDWQSGTFVPPtLIELD---SFDELKREVFGPVLHVVRYNRNQldELIEQI 1038
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515625329 400 NDTIYGLASYFYS---QNIHRVWKVAEALEY----GMVGINDGlisteVAPFGGVKQSGIG 453
Cdd:PRK11809 1039 NASGYGLTLGVHTridETIAQVTGSAHVGNLyvnrNMVGAVVG-----VQPFGGEGLSGTG 1094
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
39-451 |
5.96e-44 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 161.60 E-value: 5.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 39 SETELDRAIERSHIAQKEWAKIPAKSRAAI-LKAWHQLILENKDDLAHLMTIEQGKPLEEAtgEVVYGASFIEWF---AE 114
Cdd:cd07123 67 DAALVEKAIEAALEARKEWARMPFEDRAAIfLKAADLLSGKYRYELNAATMLGQGKNVWQA--EIDAACELIDFLrfnVK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 115 EAKRTYGDSIPSTVAGKHLVTIKQPI-GVACAITPWNFPIAMITRKAAPALAaGCSFIVKPSDETPLSAFAVVELAYQAG 193
Cdd:cd07123 145 YAEELYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 194 IPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIK------RTSMELGGNAPFIVFDDADIDAA 267
Cdd:cd07123 224 LPPGVINFVPGDGPV-VGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKNFHLVHPSADVDSL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 268 VQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGINIGPVISERAKQNIQGLIDRAIEQGAQ 347
Cdd:cd07123 303 VTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 348 PVtptqeLA--------GLFIQPVIL--KDVKHdmDIVQQEIFGPVAPVMKF-DSD-EELIEMANDT-IYGLASYFYSQN 414
Cdd:cd07123 383 EI-----IAggkcddsvGYFVEPTVIetTDPKH--KLMTEEIFGPVLTVYVYpDSDfEETLELVDTTsPYALTGAIFAQD 455
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 515625329 415 IHRVWKVAEALEY--GMVGINDGLISTEVA--PFGGVKQSG 451
Cdd:cd07123 456 RKAIREATDALRNaaGNFYINDKPTGAVVGqqPFGGARASG 496
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
61-454 |
6.92e-40 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 148.71 E-value: 6.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 61 PAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEA----TGEVVYGA-----SFIEWFAEEAKRTYGDSIPSTVAgk 131
Cdd:cd07137 19 SAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfrdeVSVLVSSCklaikELKKWMAPEKVKTPLTTFPAKAE-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 132 hlvTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELayqagIPKNL----LQVVLGDSP 207
Cdd:cd07137 97 ---IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-----IPEYLdtkaIKVIEGGVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 208 EqigelfTSHPLIK---KISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKF-RNAGQTC 283
Cdd:cd07137 169 E------TTALLEQkwdKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQAC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 284 VCANrfYIhsKVHDEFVAKF-DQAVQQLK--IGNGLDEGINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQELAGLFI 360
Cdd:cd07137 243 IAPD--YV--LVEESFAPTLiDALKNTLEkfFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLYI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 361 QPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLISTE 440
Cdd:cd07137 319 EPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYA 398
|
410
....*....|....*.
gi 515625329 441 VA--PFGGVKQSGIGR 454
Cdd:cd07137 399 IDtlPFGGVGESGFGA 414
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
65-454 |
7.09e-34 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 132.93 E-value: 7.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 65 RAAILKAWHQLILENKDDLAHLMTIEQGKPLEEA----TGEVVYGASFI-----EWFAEEAKRTYGDSIPSTVAgkhlvT 135
Cdd:PLN02203 30 RKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyrdeVGVLTKSANLAlsnlkKWMAPKKAKLPLVAFPATAE-----V 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 136 IKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETP-LSAFavveLAyqAGIPKNL----LQVVLGdSPEqI 210
Cdd:PLN02203 105 VPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPaTSAF----LA--ANIPKYLdskaVKVIEG-GPA-V 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 211 GELFTSHPLiKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIV--FDDA-DIDAAVQGAMASKFRN-AGQTCVCA 286
Cdd:PLN02203 177 GEQLLQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 287 NRFYIHSKVHDEFVAKFDQAVQQLkIGNGLDEGINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQELAGLFIQPVILK 366
Cdd:PLN02203 256 DYVLVEERFAPILIELLKSTIKKF-FGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKKLFIEPTILL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 367 DVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGMVGINDGLI--STEVAPF 444
Cdd:PLN02203 335 NPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIqyACDSLPF 414
|
410
....*....|
gi 515625329 445 GGVKQSGIGR 454
Cdd:PLN02203 415 GGVGESGFGR 424
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
111-464 |
2.40e-30 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 123.23 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 111 WFAEEAKRTYGDSIPSTVAgkhlvTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAY 190
Cdd:PLN02174 89 WMAPEKAKTSLTTFPASAE-----IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 191 QAgIPKNLLQVVLGDSPEQIGELftsHPLIKKISFTGSTRVGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQG 270
Cdd:PLN02174 164 QY-LDSSAVRVVEGAVTETTALL---EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 271 AMASKFR-NAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGLdEGINIGPVISERAKQNIQGLIDRAIEQGAQPV 349
Cdd:PLN02174 240 IIAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPM-ESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVY 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 350 TPTQELAGLFIQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGLASYFYSQNIHRVWKVAEALEYGM 429
Cdd:PLN02174 319 GGEKDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGG 398
|
330 340 350
....*....|....*....|....*....|....*....
gi 515625329 430 VGINDglISTEVA----PFGGVKQSGIGREGAKEGIDEY 464
Cdd:PLN02174 399 IVVND--IAVHLAlhtlPFGGVGESGMGAYHGKFSFDAF 435
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
43-443 |
2.14e-29 |
|
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: 119.65 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 43 LDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPlEEATGEVVYGASFIEWFAEEAkrtYGD 122
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG-WMFAENICGDQVQLRARAFVI---YSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 123 SIPSTVAGKHLVTIKQ-------PIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGI- 194
Cdd:cd07084 77 RIPHEPGNHLGQGLKQqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 195 PKNLLQVVLGDspEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGikRTSMELGGNAPFIVFDDAD-IDAAVQGAMA 273
Cdd:cd07084 157 PPEDVTLINGD--GKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQaVDYVAWQCVQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 274 SKFRNAGQTCVCANRFYIHSkvhDEFVAKFDQAVQQLkIGNGLDEGINIGPVISERAKQNI-----QGLIDRAIEQGAQP 348
Cdd:cd07084 233 DMTACSGQKCTAQSMLFVPE---NWSKTPLVEKLKAL-LARRKLEDLLLGPVQTFTTLAMIahmenLLGSVLLFSGKELK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 349 VTPTQELAGLFIQPVIL-----KDVKHDMdiVQQEIFGPVAPVMKFDSDE-----ELIEMANDTiygLASYFYSQNIHRV 418
Cdd:cd07084 309 NHSIPSIYGACVASALFvpideILKTYEL--VTEEIFGPFAIVVEYKKDQlalvlELLERMHGS---LTAAIYSNDPIFL 383
|
410 420
....*....|....*....|....*
gi 515625329 419 WKVAEALEYGMVGINDGLISTEVAP 443
Cdd:cd07084 384 QELIGNLWVAGRTYAILRGRTGVAP 408
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
20-400 |
2.04e-27 |
|
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: 114.67 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 20 AVAVTNPATGELIGHapISSETeLDRAIERSHIAQKEWAKIPAKS---RAAILKAWHQLILENKDDLaHLMTIEQGKPLE 96
Cdd:cd07128 16 GRTLHDAVTGEVVAR--VSSEG-LDFAAAVAYAREKGGPALRALTfheRAAMLKALAKYLMERKEDL-YALSAATGATRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 97 EATGEVVYGASFIEWFAEEAKR--------TYGDSIP----STVAGKHLVTIKQpiGVACAITPWNFPIAMITRKAAPAL 164
Cdd:cd07128 92 DSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPlskdGTFVGQHILTPRR--GVAVHINAFNFPVWGMLEKFAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 165 AAGCSFIVKPSDETPLSAFAVVELAYQAGI-PKNLLQVVLGDSpeqiGELFTSHPLIKKISFTGSTRVGSILMAQ---AA 240
Cdd:cd07128 170 LAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSV----GDLLDHLGEQDVVAFTGSAATAAKLRAHpniVA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 241 KGIkRTSME--------LGgnaPFIVFDDADIDAAVQGA---MASKfrnAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQ 309
Cdd:cd07128 246 RSI-RFNAEadslnaaiLG---PDATPGTPEFDLFVKEVareMTVK---AGQKCTAIRRAFVPEARVDAVIEALKARLAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 310 LKIGNGLDEGINIGPVISERAKQNIQGLIDRaIEQGAQPVTPTQE---------LAGLFIQPVILK-DVKHDMDIVQQ-E 378
Cdd:cd07128 319 VVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDrfevvgadaEKGAFFPPTLLLcDDPDAATAVHDvE 397
|
410 420
....*....|....*....|..
gi 515625329 379 IFGPVAPVMKFDSDEELIEMAN 400
Cdd:cd07128 398 AFGPVATLMPYDSLAEAIELAA 419
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
43-400 |
1.79e-25 |
|
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: 108.40 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 43 LDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKRtyGD 122
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVRE--GS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 123 SIPSTV---------AGK-HLVTIKQPIGVACAITPWNFPIAMITrkA----APALAAGCSFIVKPSDETP----LSAFA 184
Cdd:cd07129 79 WLDARIdpadpdrqpLPRpDLRRMLVPLGPVAVFGASNFPLAFSV--AggdtASALAAGCPVVVKAHPAHPgtseLVARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 185 VVELAYQAGIPKNLLQVVLGDSPEqIGELFTSHPLIKKISFTGSTRVGSILMAQAAkgiKRTS-----MELGGNAPFIVF 259
Cdd:cd07129 157 IRAALRATGLPAGVFSLLQGGGRE-VGVALVKHPAIKAVGFTGSRRGGRALFDAAA---ARPEpipfyAELGSVNPVFIL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 260 DDA---DIDAAVQGAMASKFRNAGQTCVCANR-FYIHSKVHDEFVAKFDQAVQQLKIGNGLDEGinigpvISERAKQNIQ 335
Cdd:cd07129 233 PGAlaeRGEAIAQGFVGSLTLGAGQFCTNPGLvLVPAGPAGDAFIAALAEALAAAPAQTMLTPG------IAEAYRQGVE 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515625329 336 GLIDRAieqGAQPVTPTQELAGLF-IQPVILK---DVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMAN 400
Cdd:cd07129 307 ALAAAP---GVRVLAGGAAAEGGNqAAPTLFKvdaAAFLADPALQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
20-399 |
1.39e-17 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 85.14 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 20 AVAVTNPATGELIGHApisSETELDRAIERSHIAQKEWAKIPAKS---RAAILKAWHQLILENKDDLAHLMTIEQGKPLE 96
Cdd:PRK11903 20 GTPLFDPVTGEELVRV---SATGLDLAAAFAFAREQGGAALRALTyaqRAALLAAIVKVLQANRDAYYDIATANSGTTRN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 97 EATGEVvYGASFIEWFAEEAKRTYGD----------SIPSTVA--GKHLVTIKQpiGVACAITPWNFPIAMITRKAAPAL 164
Cdd:PRK11903 97 DSAVDI-DGGIFTLGYYAKLGAALGDarllrdgeavQLGKDPAfqGQHVLVPTR--GVALFINAFNFPAWGLWEKAAPAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 165 AAGCSFIVKPSDETPLSAFAVVELAYQAGI-PKNLLQVVLGDSpeqiGELFTSHPLIKKISFTGSTRVGSILMAQAA--- 240
Cdd:PRK11903 174 LAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSS----AGLLDHLQPFDVVSFTGSAETAAVLRSHPAvvq 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 241 ----KGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKFDQAVQQLKIGNGL 316
Cdd:PRK11903 250 rsvrVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 317 DEGINIGPVISeRAKQN-IQGLIDRAIEQ-------GAQPVTPTQELAGLFIQPVIL-------KDVKHDMdivqqEIFG 381
Cdd:PRK11903 330 NDGVRMGPLVS-RAQLAaVRAGLAALRAQaevlfdgGGFALVDADPAVAACVGPTLLgasdpdaATAVHDV-----EVFG 403
|
410
....*....|....*...
gi 515625329 382 PVAPVMKFDSDEELIEMA 399
Cdd:PRK11903 404 PVATLLPYRDAAHALALA 421
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
43-303 |
5.36e-14 |
|
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: 73.84 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 43 LDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEE-------ATGEVVYGASFIEWFAE- 114
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEdkviknhFAAEYIYNVYKDEKTCGv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 115 -EAKRTYGdsipstvagkhLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKP----SDETPLSAFAVVELA 189
Cdd:cd07081 81 lTGDENGG-----------TLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 190 YQAGIPKNLLQVVLGDSPEQIGELFtSHPLIKKISFTGstrvGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQ 269
Cdd:cd07081 150 VAAGAPENLIGWIDNPSIELAQRLM-KFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQ 224
|
250 260 270
....*....|....*....|....*....|....
gi 515625329 270 GAMASKFRNAGQTCVCANRFYIHSKVHDEFVAKF 303
Cdd:cd07081 225 SIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLF 258
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
41-403 |
2.91e-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: 71.74 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 41 TELDRAIERSHIAQKEWAKIPAKSRAA----ILKAWHQLILEnkddLAH----------LMTIEQGKP--LEEATGEVVY 104
Cdd:cd07127 84 CDPDALLAAARAAMPGWRDAGARARAGvcleILQRLNARSFE----MAHavmhttgqafMMAFQAGGPhaQDRGLEAVAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 105 GAsfiewfaEEAKRTYGDSIPSTVAGKH--LVTIKQ----PIGVACAITPWNFPiamiTRKAAPA----LAAGCSFIVKP 174
Cdd:cd07127 160 AW-------REMSRIPPTAEWEKPQGKHdpLAMEKTftvvPRGVALVIGCSTFP----TWNGYPGlfasLATGNPVIVKP 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 175 SDETPLSAFAVVELAY----QAGIPKNLLQVVLGDSPEQIGELFTSHPLIKKISFTGSTRVGSILMAQAAKGIKRTsmEL 250
Cdd:cd07127 229 HPAAILPLAITVQVARevlaEAGFDPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQVYT--EK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 251 GGNAPFIVFDDADIDAAVQGAMASKFRNAGQTCVCANRFYIHS---------KVHDEFVAKFDQAVQQL----KIGNGLD 317
Cdd:cd07127 307 AGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRdgiqtddgrKSFDEVAADLAAAIDGLladpARAAALL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 318 EGINIGPVISERAKQNIQGLIDRAIEQGAQPVTPTQELAglfiQPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIE 397
Cdd:cd07127 387 GAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPDARVR----TPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIE 462
|
....*.
gi 515625329 398 MANDTI 403
Cdd:cd07127 463 LARESV 468
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
41-426 |
2.98e-13 |
|
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: 71.50 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 41 TELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAhLMTIEqgkplEEATGEVvygASFIEWFAEEAKRTY 120
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELA-EMAVE-----ETGMGRV---EDKIAKNHLAAEKTP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 121 G--DSIPSTVAGKHLVTIKQ--PIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSdetP----LSAFAVVEL---A 189
Cdd:cd07121 75 GteDLTTTAWSGDNGLTLVEyaPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPH---PgakkVSAYAVELInkaI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 190 YQAGIPKNLLQVVLGDSPEQIGELFTsHPLIKKISFTGSTRVGSILMAQAAKGIKRTSmelgGNAPFIVFDDADIDAA-- 267
Cdd:cd07121 152 AEAGGPDNLVVTVEEPTIETTNELMA-HPDINLLVVTGGPAVVKAALSSGKKAIGAGA----GNPPVVVDETADIEKAar 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 268 --VQGAmasKFRNaGQTCVCANRFYIHSKVHDEFVAKF----------DQAVQQLKIGNGLDEGINIGPVISERAKQNIQ 335
Cdd:cd07121 227 diVQGA---SFDN-NLPCIAEKEVIAVDSVADYLIAAMqrngayvlndEQAEQLLEVVLLTNKGATPNKKWVGKDASKIL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 336 GLIDRAIEQGAqpvtptqelaglfiqPVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGL--ASYFYSQ 413
Cdd:cd07121 303 KAAGIEVPADI---------------RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSK 367
|
410
....*....|...
gi 515625329 414 NIHRVWKVAEALE 426
Cdd:cd07121 368 NVENLTKMARAMQ 380
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
133-312 |
3.86e-13 |
|
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: 70.71 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 133 LVTIKQPIGVACAITPWNFPIAMITrKAAPALAAGCSFIVKPSDETPLSAFA---VVELAYQAGIPKNLLQVVLGDSPEQ 209
Cdd:cd07077 94 TYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRAlalLFQAADAAHGPKILVLYVPHPSDEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 210 IGELFtSHPLIKKISFTGSTrvGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAAVQGAMASKFRNaGQTCVCANRF 289
Cdd:cd07077 173 AEELL-SHPKIDLIVATGGR--DAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNL 248
|
170 180
....*....|....*....|....*...
gi 515625329 290 YIHSKVHDEfvaKFDQ-----AVQQLKI 312
Cdd:cd07077 249 YVVDDVLDP---LYEEfklklVVEGLKV 273
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
81-394 |
9.08e-13 |
|
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: 70.22 E-value: 9.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 81 DDLAHLMTIEQGKPLEEATGEVVYGASFIEWFAEEAKR--TYGDSIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITR 158
Cdd:cd07126 82 DFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRflARSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPAL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 159 KAAPALAAGCSFIVKPSDETPLSAFAVVELAYQAGIPKNLLQVVLGDSPEQIGELFTSHPliKKISFTGSTRVGsilmaq 238
Cdd:cd07126 162 QLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANP--RMTLFTGSSKVA------ 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 239 aakgiKRTSMELGGNapfIVFDDADIDAAVQGAMASKF--------RNA----GQTCVCANRFYIHSK-VHDEFVAKFDQ 305
Cdd:cd07126 234 -----ERLALELHGK---VKLEDAGFDWKILGPDVSDVdyvawqcdQDAyacsGQKCSAQSILFAHENwVQAGILDKLKA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 306 AVQQLKIgngldEGINIGPVIS---ERAKQNIQGLID---RAIEQGAQPVT----PTQ----ELAGLFIqPVILKDVKHD 371
Cdd:cd07126 306 LAEQRKL-----EDLTIGPVLTwttERILDHVDKLLAipgAKVLFGGKPLTnhsiPSIygayEPTAVFV-PLEEIAIEEN 379
|
330 340
....*....|....*....|...
gi 515625329 372 MDIVQQEIFGPVAPVMKFDSDEE 394
Cdd:cd07126 380 FELVTTEVFGPFQVVTEYKDEQL 402
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
41-426 |
2.03e-11 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 65.69 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 41 TELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHlMTIEQgkpleeaTGEVVYGASFIEWFAeEAKRTY 120
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAE-LAVEE-------TGMGRVEDKIAKNVA-AAEKTP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 121 G--DSIPSTVAGKHLVTIKQ--PIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSdetP----LSAFAVV---ELA 189
Cdd:PRK15398 107 GveDLTTEALTGDNGLTLIEyaPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPH---PgakkVSLRAIEllnEAI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 190 YQAGIPKNLLQVVLGDSPEQIGELFtSHPLIKKISFTGstrvGSILMAQAAKGIKRTSMELGGNAPFIVFDDADIDAA-- 267
Cdd:PRK15398 184 VAAGGPENLVVTVAEPTIETAQRLM-KHPGIALLVVTG----GPAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEKAar 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 268 --VQGAmasKFRNaGQTCVCANRFYIHSKVHDEFVAKFDQA-VQQLKigngldeginigpviseraKQNIQGLIDRAIEQ 344
Cdd:PRK15398 259 diVKGA---SFDN-NLPCIAEKEVIVVDSVADELMRLMEKNgAVLLT-------------------AEQAEKLQKVVLKN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 345 GAQPVT------PTQELAGLFIQ-----PVILKDVKHDMDIVQQEIFGPVAPVMKFDSDEELIEMANDTIYGL--ASYFY 411
Cdd:PRK15398 316 GGTVNKkwvgkdAAKILEAAGINvpkdtRLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMH 395
|
410
....*....|....*
gi 515625329 412 SQNIHRVWKVAEALE 426
Cdd:PRK15398 396 SRNVDNLNKMARAIQ 410
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
43-303 |
1.14e-08 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 57.12 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 43 LDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHlMTIEQ---GKPLEEATgEVVYGASFIeWFAEEAKRT 119
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAK-MAVEEtgmGVVEDKVI-KNHFASEYV-YNDIKDMKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 120 YGdsIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPSDETPLSAFAVVEL----AYQAGIP 195
Cdd:cd07122 78 VG--VIEEDEEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKImreaAVAAGAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 196 KNLLQVVLGDSPEQIGELFtSHPLIKKISFTGSTRvgsilMAQAAKGIKRTSMELG-GNAPFIVFDDADIDAAVQGAMAS 274
Cdd:cd07122 156 EGLIQWIEEPSIELTQELM-KHPDVDLILATGGPG-----MVKAAYSSGKPAIGVGpGNVPAYIDETADIKRAVKDIILS 229
|
250 260 270
....*....|....*....|....*....|..
gi 515625329 275 K-FRNAgqtCVCA--NRFYIHSKVHDEFVAKF 303
Cdd:cd07122 230 KtFDNG---TICAseQSVIVDDEIYDEVRAEL 258
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
35-303 |
1.33e-05 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 47.87 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 35 APISSETELDRAIERSHIAQKEWAKIPAKSRAAILKAWHQLILENKDDLAHLMTIEQGKPLEE--------ATgEVVYGA 106
Cdd:PRK13805 6 MAVTNVAELDALVEKAKKAQEEFATFTQEQVDKIVRAAALAALDARIPLAKMAVEETGRGVVEdkviknhfAS-EYIYNS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 107 sfiewFAEEakRTYGdsIPSTVAGKHLVTIKQPIGVACAITPWNFPIAMITRKAAPALAAGCSFIVKPS----DETPLSA 182
Cdd:PRK13805 85 -----YKDE--KTVG--VIEEDDEFGIIEIAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHpraqKSSIAAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515625329 183 FAVVELAYQAGIPKNLLQVVLGDSPEQIGELFTsHPLIKKISFTGSTRvgsilMAQAAKGIKRTSMELG-GNAPFIVFDD 261
Cdd:PRK13805 156 KIVLDAAVAAGAPKDIIQWIEEPSVELTNALMN-HPGIALILATGGPG-----MVKAAYSSGKPALGVGaGNVPAYIDKT 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 515625329 262 ADIDAAVQGAMASK-FRNaGQTCVCANRFYIHSKVHDEFVAKF 303
Cdd:PRK13805 230 ADIKRAVNDILLSKtFDN-GMICASEQAVIVDDEIYDEVKEEF 271
|
|
| |
