|
Name |
Accession |
Description |
Interval |
E-value |
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
6-460 |
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: 585.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 6 PAHGPAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGH 85
Cdd:COG1012 16 AAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 86 PIGNARWEASNVRDVLDYAAGGVERLNGRQIPVA--GGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILK 163
Cdd:COG1012 96 PLAEARGEVDRAADFLRYYAGEARRLYGETIPSDapGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 164 PAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKS 243
Cdd:COG1012 176 PAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 244 PNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRV 323
Cdd:COG1012 256 PAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 324 RGYVPEG-APGLR----GTAPEG-PGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLW 397
Cdd:COG1012 336 LAYIEDAvAEGAElltgGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVF 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495685909 398 TRDVGRALRVSRAVRAGNLSVNSHSAVRYA-TPFGGYGRSGLGRELGPDALTAFTETKNVFLST 460
Cdd:COG1012 416 TRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
12-456 |
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: 564.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 12 ELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNAR 91
Cdd:pfam00171 8 TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 92 WEASNVRDVLDYAAGGVERLNGRQIPVAGGVD-VTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPL 170
Cdd:pfam00171 88 GEVDRAIDVLRYYAGLARRLDGETLPSDPGRLaYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 171 TALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFAD 250
Cdd:pfam00171 168 TALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLED 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 251 ADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPEG 330
Cdd:pfam00171 248 ADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 331 -APGLR----GTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRAL 405
Cdd:pfam00171 328 kEEGAKlltgGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERAL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 495685909 406 RVSRAVRAGNLSVNSHSAVR-YATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:pfam00171 408 RVARRLEAGMVWINDYTTGDaDGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
15-458 |
7.07e-179 |
|
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: 508.24 E-value: 7.07e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAAQRG--WAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARW 92
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 93 EASNVRDVLDYAAGGVERLNGRQIPVAGGVDVTFL--EPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPL 170
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTrrEPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 171 TALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFAD 250
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 251 ADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYV--- 327
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVara 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 328 -PEGAPGLRG-TAPEGP----GFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDV 401
Cdd:cd07114 321 rEEGARVLTGgERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 495685909 402 GRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFL 458
Cdd:cd07114 401 ARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
36-458 |
3.46e-174 |
|
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: 495.58 E-value: 3.46e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 36 DAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEASNVRDVLDYAAGGVERLNGRQ 115
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 116 IP--VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIALDAGLPEHLFQVLP 193
Cdd:cd07078 81 IPspDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 194 GTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCC 273
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 274 ARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPEG-APGLR----GTAPEG-PGFWFP 347
Cdd:cd07078 241 AASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAkAEGAKllcgGKRLEGgKGYFVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 348 PTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNSHSAVRYA 427
Cdd:cd07078 321 PTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEP 400
|
410 420 430
....*....|....*....|....*....|..
gi 495685909 428 T-PFGGYGRSGLGRELGPDALTAFTETKNVFL 458
Cdd:cd07078 401 SaPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
12-456 |
2.43e-173 |
|
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: 495.19 E-value: 2.43e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 12 ELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRG--WAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIG- 88
Cdd:cd07091 20 TFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEe 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 89 NARWEASNVRDVLDYAAGGVERLNGRQIPVAGGVDV-TFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAET 167
Cdd:cd07091 100 SAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAyTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 168 TPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCA-GQVKRLTLELGGKSPNI 246
Cdd:cd07091 180 TPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAkSNLKKVTLELGGKSPNI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 247 VFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGY 326
Cdd:cd07091 260 VFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 327 VP----EGAPGLRGTAPEG-PGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDV 401
Cdd:cd07091 340 IEsgkkEGATLLTGGERHGsKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDI 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 495685909 402 GRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07091 420 NKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
15-456 |
2.26e-171 |
|
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: 489.38 E-value: 2.26e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWE- 93
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 94 ----ASNVRDVLDYAAGgverLNGRQIPVAGG-VDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETT 168
Cdd:cd07093 81 ipraAANFRFFADYILQ----LDGESYPQDGGaLNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 169 PLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVF 248
Cdd:cd07093 157 PLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 249 ADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYV- 327
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVe 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 328 ---PEGAPGLRG-----TAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTR 399
Cdd:cd07093 317 larAEGATILTGggrpeLPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 495685909 400 DVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
15-459 |
2.40e-166 |
|
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: 476.55 E-value: 2.40e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNAR-WE 93
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 94 ASNVRDVLDYAAGGVERLNGRQIPVAGG-VDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTA 172
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPfLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 173 LRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADAD 252
Cdd:cd07115 161 LRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 253 LEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPEG-A 331
Cdd:cd07115 241 LDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGrE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 332 PGLR----GTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRV 407
Cdd:cd07115 321 EGARlltgGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 495685909 408 SRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFLS 459
Cdd:cd07115 401 AAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVN 452
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
11-456 |
1.67e-164 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 472.47 E-value: 1.67e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 11 AELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNA 90
Cdd:PRK13473 17 EKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 91 R-WEASNVRDVLDYAAGGVERLNGrqiPVAG--GVDVTFL---EPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKP 164
Cdd:PRK13473 97 LnDEIPAIVDVFRFFAGAARCLEG---KAAGeyLEGHTSMirrDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 165 AETTPLTALRLAEIALDAgLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSP 244
Cdd:PRK13473 174 SEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 245 NIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVR 324
Cdd:PRK13473 253 VIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 325 GYVpEGAPGLR-------GTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLW 397
Cdd:PRK13473 333 GFV-ERAKALGhirvvtgGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVW 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 495685909 398 TRDVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:PRK13473 412 TRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
15-456 |
6.21e-164 |
|
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: 469.99 E-value: 6.21e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEA 94
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 95 SNVRDVLDYAAGGVERLNGRQIP--VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTA 172
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPspAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 173 LRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADAD 252
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 253 LEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYV----P 328
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVedavA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 329 EGA-PGLRGTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRV 407
Cdd:cd07103 321 KGAkVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 495685909 408 SRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07103 401 AEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
15-457 |
6.72e-163 |
|
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: 467.94 E-value: 6.72e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEA 94
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 95 SNVRDVLDYAAGGVERLNGRQIPVAGGVDV-TFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTAL 173
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPGGSFAyTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 174 RLAEIALDAGLPEHLFQVLPGTGPVaGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADL 253
Cdd:cd07090 161 LLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 254 EQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYV----PE 329
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIesakQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 330 GAPGLRG---TAPEGP---GFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGR 403
Cdd:cd07090 320 GAKVLCGgerVVPEDGlenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 495685909 404 ALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVF 457
Cdd:cd07090 400 AHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
13-458 |
1.03e-161 |
|
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: 464.77 E-value: 1.03e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRATAA-QRG-WAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNA 90
Cdd:cd07112 4 FATINPATGRVLAEVAACDAADVDRAVAAARRAfESGvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 91 RweASNVRDV---LDYAAGGVERLNGRQIPVagGVDVTFL---EPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKP 164
Cdd:cd07112 84 L--AVDVPSAantFRWYAEAIDKVYGEVAPT--GPDALALitrEPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 165 AETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMaRCAGQ--VKRLTLELGGK 242
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFL-EYSGQsnLKRVWLECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 243 SPNIVFADA-DLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLD 321
Cdd:cd07112 239 SPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 322 RVRGY----VPEGAPGLRG---TAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAA 394
Cdd:cd07112 319 KVLGYiesgKAEGARLVAGgkrVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495685909 395 SLWTRDVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFL 458
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
15-456 |
3.31e-159 |
|
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: 458.24 E-value: 3.31e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAAQRGWA-ALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWE 93
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 94 ASNVRDVLDYAAGGVERLNGRQIPVAGGVDV-TFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTA 172
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGPGYFVyTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 173 LRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADAD 252
Cdd:cd07109 161 LRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 253 LEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGdPADEATDMGPLISRVQLDRVRGYVPEG-A 331
Cdd:cd07109 241 LEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVARArA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 332 PGLR----GTAPEGP---GFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRA 404
Cdd:cd07109 320 RGARivagGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 495685909 405 LRVSRAVRAGNLSVNSHSAVR-YATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07109 400 LRVARRLRAGQVFVNNYGAGGgIELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
15-456 |
5.70e-157 |
|
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: 452.55 E-value: 5.70e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNAR-WE 93
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 94 ASNVRDVLDYAAGGVERLNGRQIP--VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLT 171
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGeyLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 172 ALRLAEIALDaGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADA 251
Cdd:cd07092 161 TLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 252 DLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPEGA 331
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 332 PGLR----GTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRV 407
Cdd:cd07092 320 AHARvltgGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 495685909 408 SRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07092 400 SARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
6-458 |
2.15e-156 |
|
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: 451.57 E-value: 2.15e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 6 PAHGPAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGH 85
Cdd:cd07138 9 APAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 86 PIGNAR-WEASNVRDVLDYAAGGVERLNGRQipVAGGVDVTfLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKP 164
Cdd:cd07138 89 PITLARaAQVGLGIGHLRAAADALKDFEFEE--RRGNSLVV-REPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 165 AETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSP 244
Cdd:cd07138 166 SEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 245 NIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVR 324
Cdd:cd07138 246 NIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 325 GY----VPEGA------PGlrgtAPEGP--GFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGL 392
Cdd:cd07138 326 GYiqkgIEEGArlvaggPG----RPEGLerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGL 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495685909 393 AASLWTRDVGRALRVSRAVRAGNLSVNsHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFL 458
Cdd:cd07138 402 AGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQG 466
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
6-456 |
1.31e-155 |
|
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: 450.32 E-value: 1.31e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 6 PAHGPAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRG-WAALAPADRARLLRRFAAAVDGHAEELALLEVREAG 84
Cdd:cd07144 18 KSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 85 HPI-GNARWEASNVRDVLDYAAGGVERLNGRQIPVAGG-VDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVIL 162
Cdd:cd07144 98 KPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNkLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 163 KPAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGK 242
Cdd:cd07144 178 KPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 243 SPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLL-APALSAVTVGDPADEATDMGPLISRVQLD 321
Cdd:cd07144 258 SPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFvEHVKQNYKVGSPFDDDTVVGPQVSKTQYD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 322 RVRGYV----PEGAPGLRGTAPEGP----GFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLA 393
Cdd:cd07144 338 RVLSYIekgkKEGAKLVYGGEKAPEglgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLA 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495685909 394 ASLWTRDVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07144 418 AAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
14-461 |
1.39e-155 |
|
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: 450.22 E-value: 1.39e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 14 PVLNPATGELLTTVPAATPADVDAAVRRATAA--QRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNAR 91
Cdd:cd07119 16 DIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 92 WEASNVRDVLDYAAGGVERLNGRQIPVAGGV-DVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPL 170
Cdd:cd07119 96 IDIDDVANCFRYYAGLATKETGEVYDVPPHViSRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 171 TALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFAD 250
Cdd:cd07119 176 TTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFAD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 251 ADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPEG 330
Cdd:cd07119 256 ADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 331 -APGLR----GTAPEGP----GFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDV 401
Cdd:cd07119 336 kEEGARlvcgGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDI 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 402 GRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFLSTE 461
Cdd:cd07119 416 ARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLS 475
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
15-456 |
4.46e-155 |
|
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: 447.85 E-value: 4.46e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAAQRGWA-ALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNAR-- 91
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 92 ---WEASNVRDVLDYAAG--GVERLNGRQIPVAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAE 166
Cdd:cd07089 81 qvdGPIGHLRYFADLADSfpWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 167 TTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNI 246
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 247 VFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGY 326
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 327 VPEG-APGLR----GTAPEG--PGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTR 399
Cdd:cd07089 321 IARGrDEGARlvtgGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 495685909 400 DVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07089 401 DVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
5-458 |
1.21e-154 |
|
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: 447.41 E-value: 1.21e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 5 APAHGPAELPVLNPATGELLTTVPAATPADVDAAVRRATAA--QRGWAALAPADRARLLRRFAAAVDGHAEELALLEVRE 82
Cdd:cd07139 8 VAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELARLWTAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 83 AGHPIGNARW-EASNVRDVLDYAAGGVERLN--GRQIPVAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNA 159
Cdd:cd07139 88 NGMPISWSRRaQGPGPAALLRYYAALARDFPfeERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 160 VILKPAETTPLTALRLAEIALDAGLPEHLFQVLPGtGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLEL 239
Cdd:cd07139 168 VVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLEL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 240 GGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQ 319
Cdd:cd07139 247 GGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 320 LDRVRGYVPEG-APGLR----GTAPEGP--GFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGL 392
Cdd:cd07139 327 RERVEGYIAKGrAEGARlvtgGGRPAGLdrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGL 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495685909 393 AASLWTRDVGRALRVSRAVRAGNLSVNsHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFL 458
Cdd:cd07139 407 SGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
11-457 |
1.84e-151 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 439.70 E-value: 1.84e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 11 AELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGna 90
Cdd:PRK13252 22 ETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQ-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 91 rwEASNV-----RDVLDYAAGGVERLNGRQIPVAGGVDV-TFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKP 164
Cdd:PRK13252 100 --ETSVVdivtgADVLEYYAGLAPALEGEQIPLRGGSFVyTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 165 AETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVaGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSP 244
Cdd:PRK13252 178 SEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 245 NIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVR 324
Cdd:PRK13252 257 LIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 325 GYV----PEGA----PGLRGTAPEGP-GFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAAS 395
Cdd:PRK13252 337 GYIekgkAEGArllcGGERLTEGGFAnGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAG 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495685909 396 LWTRDVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVF 457
Cdd:PRK13252 417 VFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQ 478
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
15-456 |
4.31e-149 |
|
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: 432.55 E-value: 4.31e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEA 94
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 95 SNVRDVLDYAAGGVERLNGRQ-----IPVAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTP 169
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAeravpLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 170 LTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFA 249
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 250 DADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPE 329
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 330 G-APGLR----GTAPEGP--GFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVG 402
Cdd:cd07110 321 GkEEGARllcgGRRPAHLekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 495685909 403 RALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
13-458 |
1.55e-148 |
|
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: 431.69 E-value: 1.55e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARW 92
Cdd:cd07088 15 IDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 93 EASNVRDVLDYAAGGVERLNGRQIPVAGGVDVTFL--EPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPL 170
Cdd:cd07088 95 EVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIfkVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 171 TALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFAD 250
Cdd:cd07088 175 NALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 251 ADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYV--- 327
Cdd:cd07088 255 ADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVera 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 328 -PEGAPGLRG--TAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRA 404
Cdd:cd07088 335 vEAGATLLTGgkRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTA 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 495685909 405 LRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFL 458
Cdd:cd07088 415 MRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
15-456 |
1.73e-148 |
|
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: 431.01 E-value: 1.73e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPI-GNARWE 93
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 94 ASNVRDVLDYAAGGVERLNGRQIPVAGGV-DVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTA 172
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFGPDVlTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 173 LRLAEIALDAgLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADAD 252
Cdd:cd07108 161 LLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 253 LEQAAAGAPMSF-LDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPEG- 330
Cdd:cd07108 240 LDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGl 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 331 -APG--------LRGTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDV 401
Cdd:cd07108 320 sTSGatvlrggpLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 495685909 402 GRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDA-LTAFTETKNV 456
Cdd:cd07108 400 GRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
15-458 |
1.13e-146 |
|
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: 426.17 E-value: 1.13e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEA 94
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 95 SNVRDVLDYAAGgverlngRQIPV------AGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETT 168
Cdd:cd07106 81 GGAVAWLRYTAS-------LDLPDevieddDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 169 PLTALRLAEIALDAgLPEHLFQVLPGTGPVaGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVF 248
Cdd:cd07106 154 PLCTLKLGELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 249 ADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVP 328
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 329 E-GAPGLR----GTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGR 403
Cdd:cd07106 312 DaKAKGAKvlagGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 495685909 404 ALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFL 458
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
15-456 |
2.54e-144 |
|
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: 420.63 E-value: 2.54e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEA 94
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 95 SNVRDVLDYAAGGVERLNGRQIPVAGG-VDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTAL 173
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRnLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 174 RLAEIALDAgLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADL 253
Cdd:cd07107 161 RLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 254 EQAAAGAP--MSFlDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPEG- 330
Cdd:cd07107 240 EAAADAAVagMNF-TWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAk 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 331 APGLR----GTAPEGP----GFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVG 402
Cdd:cd07107 319 REGARlvtgGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 495685909 403 RALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07107 399 QAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
5-460 |
1.56e-143 |
|
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: 419.44 E-value: 1.56e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 5 APAHGpAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAG 84
Cdd:cd07559 11 APSKG-EYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 85 HPIGNA------------RWEASNVRDvldyAAGGVERLNGRQIPVAggvdvtFLEPLGVVGVIAPWNFPMPVAAWGTAP 152
Cdd:cd07559 90 KPIRETlaadiplaidhfRYFAGVIRA----QEGSLSEIDEDTLSYH------FHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 153 ALAAGNAVILKPAETTPLTALRLAEIALDAgLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQV 232
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 233 KRLTLELGGKSPNIVFADA-----DLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADE 307
Cdd:cd07559 239 IPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 308 ATDMGPLISRVQLDRVRGYV----PEGAP----GLRGTAPEGP-GFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDE 378
Cdd:cd07559 319 ETMMGAQVSKDQLEKILSYVdigkEEGAEvltgGERLTLGGLDkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 379 EDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFL 458
Cdd:cd07559 399 EEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILV 478
|
..
gi 495685909 459 ST 460
Cdd:cd07559 479 SY 480
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
34-454 |
2.50e-142 |
|
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: 414.24 E-value: 2.50e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 34 DVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEASNVRDVLDYAAGGVERLNG 113
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 114 RQIP--VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLT-ALRLAEIALDAGLPEHLFQ 190
Cdd:cd07104 81 EILPsdVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 191 VLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAAAGAPMS-FLdNSG 269
Cdd:cd07104 161 VVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGaFL-HQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 270 QDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYV----PEGAPGLRGTAPEGPgfW 345
Cdd:cd07104 240 QICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVedavAAGARLLTGGTYEGL--F 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 346 FPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNSHSAVR 425
Cdd:cd07104 318 YQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVND 397
|
410 420 430
....*....|....*....|....*....|
gi 495685909 426 YAT-PFGGYGRSGLGRELGPDALTAFTETK 454
Cdd:cd07104 398 EPHvPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
13-454 |
4.04e-141 |
|
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: 412.13 E-value: 4.04e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARW 92
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 93 EASNVRDVLDYAAGGVERLNGRQIPV------AGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAE 166
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVdayeynERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 167 TTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNI 246
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 247 VFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGY 326
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 327 V----PEGAPGLRGTAPEgPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVG 402
Cdd:cd07145 321 VndavEKGGKILYGGKRD-EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDIN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 495685909 403 RALRVSRAVRAGNLSVNSHSAVRY-ATPFGGYGRSGLGRELGPDALTAFTETK 454
Cdd:cd07145 400 RALKVARELEAGGVVINDSTRFRWdNLPFGGFKKSGIGREGVRYTMLEMTEEK 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
14-456 |
2.39e-140 |
|
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: 411.36 E-value: 2.39e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 14 PVLNPATGELLTTVPAATPADVDAAVRRATAA-QRG--WAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNA 90
Cdd:cd07141 25 PTINPATGEKICEVQEGDKADVDKAVKAARAAfKLGspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 91 RW-EASNVRDVLDYAAGGVERLNGRQIPVAGGVDV-TFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETT 168
Cdd:cd07141 105 YLvDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTyTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 169 PLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKrLMARCAGQV--KRLTLELGGKSPNI 246
Cdd:cd07141 185 PLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGK-LIQQAAGKSnlKRVTLELGGKSPNI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 247 VFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGY 326
Cdd:cd07141 264 VFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 327 V----PEGAPGLRGTAPEG-PGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDV 401
Cdd:cd07141 344 IesgkKEGAKLECGGKRHGdKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDI 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 495685909 402 GRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07141 424 DKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
40-458 |
3.61e-137 |
|
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: 398.91 E-value: 3.61e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 40 RRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEASNVRDVLDYAAGGVERLNGRQIP-- 117
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPsp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 118 VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIALDAGLPEHLFQVLPGTGP 197
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 198 VAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTR 277
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 278 ILVQDSALDRFLDLLApalsavtvgdpadeatdmgplisrvqldrvrgyvpegapglrgtapegpgfwfppTVLTQAGER 357
Cdd:cd06534 241 LLVHESIYDEFVEKLV-------------------------------------------------------TVLVDVDPD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 358 DPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNSHSAVRYAT-PFGGYGRS 436
Cdd:cd06534 266 MPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEaPFGGVKNS 345
|
410 420
....*....|....*....|..
gi 495685909 437 GLGRELGPDALTAFTETKNVFL 458
Cdd:cd06534 346 GIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
16-458 |
2.83e-136 |
|
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: 399.79 E-value: 2.83e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 16 LNPATGELLTTVPAATPADVDAAVRRATAA-QRG-WAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWE 93
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAfDKGpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 94 ASNVRDVLDYAAGGVERLNGRQIPVAGG--VDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLT 171
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDdmLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 172 ALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADA 251
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 252 DLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVP--- 328
Cdd:cd07118 242 DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDagr 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 329 -EGAPGLRG--TAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRAL 405
Cdd:cd07118 322 aEGATLLLGgeRLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 495685909 406 RVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFL 458
Cdd:cd07118 402 TVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-458 |
1.84e-134 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 396.75 E-value: 1.84e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 7 AHGPAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHP 86
Cdd:PLN02278 36 AYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 87 IGNARWEASNVRDVLDYAAGGVERLNGRQIP--VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKP 164
Cdd:PLN02278 116 LKEAIGEVAYGASFLEYFAEEAKRVYGDIIPspFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 165 AETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSP 244
Cdd:PLN02278 196 SELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 245 NIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVR 324
Cdd:PLN02278 276 FIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 325 GYV----PEGAPGLRGTAP--EGPGFwFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWT 398
Cdd:PLN02278 356 SHVqdavSKGAKVLLGGKRhsLGGTF-YEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFT 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 399 RDVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFL 458
Cdd:PLN02278 435 RDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
5-461 |
6.88e-133 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 392.94 E-value: 6.88e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 5 APAHGpAELPVLNPATGELLTTVPAATPADVDAAVRRATAA-----QRGWAALAPADRARLLRRFAAAVDGHAEELALLE 79
Cdd:PLN02467 18 EPVLG-KRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 80 VREAGHPIGNARWEASNVRDVLDYAAGGVERLNGRQ-IPVAGGVDvTF-----LEPLGVVGVIAPWNFPMPVAAWGTAPA 153
Cdd:PLN02467 97 TLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQkAPVSLPME-TFkgyvlKEPLGVVGLITPWNYPLLMATWKVAPA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 154 LAAGNAVILKPAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVK 233
Cdd:PLN02467 176 LAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 234 RLTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGP 313
Cdd:PLN02467 256 PVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 314 LISRVQLDRVRGYVP----EGAPGLR-GTAPEG--PGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLAN 386
Cdd:PLN02467 336 VVSEGQYEKVLKFIStaksEGATILCgGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELAN 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495685909 387 DTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV--FLSTE 461
Cdd:PLN02467 416 DSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQVtkYISDE 492
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
9-458 |
8.71e-133 |
|
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: 391.61 E-value: 8.71e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 9 GPAELPVLNPA-TGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPI 87
Cdd:cd07097 12 GGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 88 GNARWEASNVRDVLDYAAGGVERLNGRQIP-VAGGVDV-TFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPA 165
Cdd:cd07097 92 PEARGEVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVeTTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 166 ETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPN 245
Cdd:cd07097 172 ELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 246 IVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRG 325
Cdd:cd07097 252 VVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 326 YV----PEGAPGLRGTAP---EGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWT 398
Cdd:cd07097 332 YIeiarSEGAKLVYGGERlkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVT 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495685909 399 RDVGRALRVSRAVRAGNLSVNSHSA-VRYATPFGGYGRSGLG-RELGPDALTAFTETKNVFL 458
Cdd:cd07097 412 TSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTVYV 473
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
15-456 |
2.81e-132 |
|
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: 390.74 E-value: 2.81e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAA-QRGWA-ALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGN-AR 91
Cdd:cd07143 26 VYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTaKR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 92 WEASNVRDVLDYAAGGVERLNGRQIPV-AGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPL 170
Cdd:cd07143 106 VDVQASADTFRYYGGWADKIHGQVIETdIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 171 TALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLM-ARCAGQVKRLTLELGGKSPNIVFA 249
Cdd:cd07143 186 SALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMeAAAKSNLKKVTLELGGKSPNIVFD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 250 DADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYV-- 327
Cdd:cd07143 266 DADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIes 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 328 --PEGAPGLRGTAPEG-PGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRA 404
Cdd:cd07143 346 gkAEGATVETGGKRHGnEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNA 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 495685909 405 LRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07143 426 IRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
13-460 |
3.30e-132 |
|
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: 390.28 E-value: 3.30e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNAR- 91
Cdd:cd07117 18 IDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 92 ----WEASNVRdvldYAAGGVERLNGRqipvAGGVDVTFL-----EPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVIL 162
Cdd:cd07117 98 vdipLAADHFR----YFAGVIRAEEGS----ANMIDEDTLsivlrEPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 163 KPAETTPLTALRLAEIALDAgLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGK 242
Cdd:cd07117 170 KPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 243 SPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDR 322
Cdd:cd07117 249 SANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 323 VRGYV----PEGAPGLRG-----TAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLA 393
Cdd:cd07117 329 ILSYVdiakEEGAKILTGghrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLG 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495685909 394 ASLWTRDVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFLST 460
Cdd:cd07117 409 GGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
13-454 |
1.00e-131 |
|
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: 388.23 E-value: 1.00e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARW 92
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 93 EASNVRDVLDYAAGGVERLNGRQIP--VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPL 170
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRGETLPsdSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 171 TALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFAD 250
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 251 ADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGY---- 326
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQveda 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 327 VPEGAPGLRGTAPEGPGFWfpPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALR 406
Cdd:cd07150 321 VAKGAKLLTGGKYDGNFYQ--PTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFK 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 495685909 407 VSRAVRAGNLSVNSHSAVRYAT-PFGGYGRSGLGRELGPDALTAFTETK 454
Cdd:cd07150 399 LAERLESGMVHINDPTILDEAHvPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
16-458 |
1.53e-130 |
|
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: 385.16 E-value: 1.53e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 16 LNPATGELLTTVPAATPADVDAAVRRATAAQRG--WAAlAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWE 93
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 94 ASNVRDVLDYAAGGVERLNGRQIPVAGGVDVTFL-EPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTA 172
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLrEPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 173 LRLAEIALDA-GLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADA 251
Cdd:cd07120 161 AAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 252 DLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPEGA 331
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 332 P-----GLRGTAPEG---PGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGR 403
Cdd:cd07120 321 AagaevVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLAR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 495685909 404 ALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFL 458
Cdd:cd07120 401 AMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
6-454 |
1.10e-129 |
|
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: 383.58 E-value: 1.10e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 6 PAHGPAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGH 85
Cdd:cd07151 5 DGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 86 PIGNARWEASNVRDVLDYAAGGVERLNGRQIP--VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILK 163
Cdd:cd07151 85 TRIKANIEWGAAMAITREAATFPLRMEGRILPsdVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 164 PAETTPLTA-LRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGK 242
Cdd:cd07151 165 PASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 243 SPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDR 322
Cdd:cd07151 245 NPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 323 VRGYV----PEGAPGLRGTAPEgpGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWT 398
Cdd:cd07151 325 LLDKIeqavEEGATLLVGGEAE--GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFT 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 495685909 399 RDVGRALRVSRAVRAGNLSVNSHSAVRYA-TPFGGYGRSGLGRELGPDALTAFTETK 454
Cdd:cd07151 403 SDLERGVQFARRIDAGMTHINDQPVNDEPhVPFGGEKNSGLGRFNGEWALEEFTTDK 459
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
4-456 |
2.31e-129 |
|
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: 382.95 E-value: 2.31e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 4 PAPAHGPAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRG-WAALAPADRARLLRRFAAAVDGHAEELALLEVRE 82
Cdd:cd07113 8 PVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQLETLC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 83 AGHPIGNAR-WEASNVRDVLDYAAGGVERLNGR----QIPVAGG---VDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPAL 154
Cdd:cd07113 88 SGKSIHLSRaFEVGQSANFLRYFAGWATKINGEtlapSIPSMQGeryTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 155 AAGNAVILKPAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVaGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKR 234
Cdd:cd07113 168 ATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 235 LTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPL 314
Cdd:cd07113 247 VTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 315 ISRVQLDRVRGYV----PEGAPGLRGT-APEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTE 389
Cdd:cd07113 327 ANQPHFDKVCSYLddarAEGDEIVRGGeALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTP 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495685909 390 YGLAASLWTRDVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07113 407 FGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
3-458 |
7.35e-128 |
|
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: 379.38 E-value: 7.35e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 3 DPAPAHGPAELPVLNPATG-ELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVR 81
Cdd:cd07131 6 EWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 82 EAGHPIGNARWEASNVRDVLDYAAGGVERLNGRQIP--VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNA 159
Cdd:cd07131 86 EMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPseLPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 160 VILKPAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLEL 239
Cdd:cd07131 166 VVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEM 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 240 GGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQ 319
Cdd:cd07131 246 GGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 320 LDRVRGYVP----EGAPGLRGT--APEG---PGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEY 390
Cdd:cd07131 326 LEKVLNYNEigkeEGATLLLGGerLTGGgyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEY 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 391 GLAASLWTRDVGRALRVSRAVRAGNLSVN-SHSAVRYATPFGGYGRSGLG-RELGPDALTAFTETKNVFL 458
Cdd:cd07131 406 GLSSAIYTEDVNKAFRARRDLEAGITYVNaPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
16-454 |
8.96e-128 |
|
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: 378.10 E-value: 8.96e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 16 LNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEAS 95
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 96 NVRDVLDYAAGGVERLNGRQ-----IPVAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPL 170
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRkvptgLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 171 TALRLAEIALDAGLPEHLFQVLPGTGPVaGEALVDHpGVAKIVFTGSTRTGKRLMARCAgqvKRLT---LELGGKSPNIV 247
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDA-GVDKVAFTGSVATGRKVMAAAA---ERLIpvvLELGGKDPMIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 248 FADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYV 327
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 328 PE----GAPGLRGTAPE-GPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVG 402
Cdd:cd07099 316 DDavakGAKALTGGARSnGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 495685909 403 RALRVSRAVRAGNLSVNSH--SAVRYATPFGGYGRSGLGRELGPDALTAFTETK 454
Cdd:cd07099 396 RAEAIARRLEAGAVSINDVllTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPK 449
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
6-456 |
3.29e-127 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 379.22 E-value: 3.29e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 6 PAHGPAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGh 85
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 86 pigNARWEAsnVRDVLD-------YAAGGVERLNGRQ----IPVAGGVDVTFLePLGVVGVIAPWNFPMPVAAWGTAPAL 154
Cdd:PRK09407 106 ---KARRHA--FEEVLDvaltaryYARRAPKLLAPRRragaLPVLTKTTELRQ-PKGVVGVISPWNYPLTLAVSDAIPAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 155 AAGNAVILKPAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHpgVAKIVFTGSTRTGKRLMARCAGQVKR 234
Cdd:PRK09407 180 LAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 235 LTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPL 314
Cdd:PRK09407 258 FSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 315 ISRVQLDRVRGYVPE----GAPGLRGTAPE---GPGFwFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLAND 387
Cdd:PRK09407 338 ISEAQLETVSAHVDDavakGATVLAGGKARpdlGPLF-YEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAND 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495685909 388 TEYGLAASLWTRDVGRALRVSRAVRAGNLSVNSHSAVRYA---TPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:PRK09407 417 TPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGsvdAPMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
13-456 |
7.90e-127 |
|
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: 375.78 E-value: 7.90e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARW 92
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 93 EASNVRDVLDYAAGGVERLNGRQIPV---AGGVD---VTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAE 166
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFdasPGGEGrigFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 167 TTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGkRLMARCAGqVKRLTLELGGKSPNI 246
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVG-EAIARKAG-LKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 247 VFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGY 326
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 327 VPE----GAPGLRGTAPEGPGFWfpPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVG 402
Cdd:cd07149 319 VEEavegGARLLTGGKRDGAILE--PTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQ 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 495685909 403 RALRVSRAVRAGNLSVNSHSAVRY-ATPFGGYGRSGLGRElGPD-ALTAFTETKNV 456
Cdd:cd07149 397 KALKAARELEVGGVMINDSSTFRVdHMPYGGVKESGTGRE-GPRyAIEEMTEIKLV 451
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
5-447 |
1.06e-125 |
|
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: 373.65 E-value: 1.06e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 5 APAHGpAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAG 84
Cdd:cd07111 32 KPENR-KSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 85 HPIGNAR-WEASNVRDVLDYAAGGVERLNgrqipvaggVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILK 163
Cdd:cd07111 111 KPIRESRdCDIPLVARHFYHHAGWAQLLD---------TELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 164 PAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVaGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKS 243
Cdd:cd07111 182 PAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 244 PNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRV 323
Cdd:cd07111 261 PFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 324 RGYVPEG-APGLR----GTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWT 398
Cdd:cd07111 341 RELVEEGrAEGADvfqpGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWS 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 495685909 399 RDVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDAL 447
Cdd:cd07111 421 ENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGL 469
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
7-456 |
1.10e-125 |
|
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: 374.14 E-value: 1.10e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 7 AHGPAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRG--WAALAPADRARLLRRFAAAVDGHAEELALLEVREAG 84
Cdd:cd07140 17 AEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 85 HPIGNA-RWEASNVRDVLDYAAGGVERLNGRQIPVAGG-----VDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGN 158
Cdd:cd07140 97 AVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPINQArpnrnLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 159 AVILKPAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCA-GQVKRLTL 237
Cdd:cd07140 177 TVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAvSNLKKVSL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 238 ELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISR 317
Cdd:cd07140 257 ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 318 VQLDRVRGY----VPEGAPGLRGTAP-EGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDE--EDAVRLANDTEY 390
Cdd:cd07140 337 AHLDKLVEYcergVKEGATLVYGGKQvDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEY 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495685909 391 GLAASLWTRDVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07140 417 GLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
18-456 |
3.10e-124 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 368.95 E-value: 3.10e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 18 PATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEASNV 97
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 98 RDVLDYAAGGVERLNGRQ-----IPVAGGVDVTFlEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTA 172
Cdd:cd07101 83 AIVARYYARRAERLLKPRrrrgaIPVLTRTTVNR-RPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 173 LRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHpgVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADAD 252
Cdd:cd07101 162 LWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 253 LEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPE--- 329
Cdd:cd07101 240 LDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDava 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 330 -GAPGLRGTAPE---GPGFwFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRAL 405
Cdd:cd07101 320 kGATVLAGGRARpdlGPYF-YEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 495685909 406 RVSRAVRAGNLSVNSHSAVRYA---TPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07101 399 RIAARLRAGTVNVNEGYAAAWAsidAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
35-457 |
1.09e-123 |
|
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: 366.79 E-value: 1.09e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 35 VDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEASNVRDVLD-YAAGGVERLNG 113
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRyYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 114 RQIPVAGG-VDVTFlEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIALDAGLPEHLFQVL 192
Cdd:cd07100 81 EPIETDAGkAYVRY-EPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 193 PGTGPVAgEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDC 272
Cdd:cd07100 160 LIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 273 CARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPE----GAPGLRG-TAPEGPGFWFP 347
Cdd:cd07100 239 IAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEavaaGATLLLGgKRPDGPGAFYP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 348 PTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNSHSAVRYA 427
Cdd:cd07100 319 PTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPR 398
|
410 420 430
....*....|....*....|....*....|
gi 495685909 428 TPFGGYGRSGLGRELGPDALTAFTETKNVF 457
Cdd:cd07100 399 LPFGGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
15-461 |
1.45e-120 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 361.14 E-value: 1.45e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRATAA-QRG-WAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNA-R 91
Cdd:PRK09847 39 TVDPVTQAPLAKIARGKSVDIDRAVSAARGVfERGdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 92 WEASNVRDVLDYAAGGVERLNGRQIPVAGG-VDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPL 170
Cdd:PRK09847 119 DDIPGAARAIRWYAEAIDKVYGEVATTSSHeLAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 171 TALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMaRCAGQ--VKRLTLELGGKSPNIVF 248
Cdd:PRK09847 199 SAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLL-KDAGDsnMKRVWLEAGGKSANIVF 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 249 ADA-DLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYV 327
Cdd:PRK09847 278 ADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 328 PEG-APG---LRGTAPEGPGFwFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGR 403
Cdd:PRK09847 358 REGeSKGqllLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSR 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 495685909 404 ALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFLSTE 461
Cdd:PRK09847 437 AHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISLE 494
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
8-456 |
6.87e-120 |
|
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: 360.00 E-value: 6.87e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 8 HGPAELPVLNPA-TGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHP 86
Cdd:cd07124 43 RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 87 IGNARWEASNVRDVLDYAAGGVERLNGRQIPVAGGVD-VTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPA 165
Cdd:cd07124 123 WAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDnRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 166 ETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCA----GQ--VKRLTLEL 239
Cdd:cd07124 203 EDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkvqpGQkwLKRVIAEM 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 240 GGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQ 319
Cdd:cd07124 283 GGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 320 LDRVRGYVPEG------APGLRGTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLA 393
Cdd:cd07124 363 RDRIRRYIEIGksegrlLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLT 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495685909 394 ASLWTRDVGRALRVSRAVRAGNLSVN--SHSAVRYATPFGGYGRSGLG-RELGPDALTAFTETKNV 456
Cdd:cd07124 443 GGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGTGsKAGGPDYLLQFMQPKTV 508
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
21-452 |
1.37e-119 |
|
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: 356.99 E-value: 1.37e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 21 GELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEASNVRDV 100
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 101 LDYAAGGVERLNGRQIP-VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTA-LRLAEI 178
Cdd:cd07152 81 LHEAAGLPTQPQGEILPsAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 179 ALDAGLPEHLFQVLPGtGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAAA 258
Cdd:cd07152 161 FEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 259 GAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPE----GAPGL 334
Cdd:cd07152 240 NGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDsvaaGARLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 335 RGTAPEGPgfWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAG 414
Cdd:cd07152 320 AGGTYDGL--FYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTG 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 495685909 415 NLSVNSHSAVRYA-TPFGGYGRSGLG-RELGPDALTAFTE 452
Cdd:cd07152 398 MLHINDQTVNDEPhNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
9-452 |
2.09e-119 |
|
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: 357.64 E-value: 2.09e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 9 GPAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIG 88
Cdd:cd07086 11 GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 89 NARWEASNVRDVLDYAAGGVERLNGRQIP--VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAE 166
Cdd:cd07086 91 EGLGEVQEMIDICDYAVGLSRMLYGLTIPseRPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 167 TTPLTALRLAEIALDA----GLPEHLFQVLPGTGPVaGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGK 242
Cdd:cd07086 171 TTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 243 SPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDR 322
Cdd:cd07086 250 NAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 323 VRGYV----PEGAPGLRGTAP---EGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAAS 395
Cdd:cd07086 330 YLNAIeiakSQGGTVLTGGKRidgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSS 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 396 LWTRDVGRALRVSRAVR--AGNLSVN-SHSAVRYATPFGGYGRSGLGRELGPDALTAFTE 452
Cdd:cd07086 410 IFTEDLREAFRWLGPKGsdCGIVNVNiPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMR 469
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
13-456 |
1.15e-118 |
|
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: 355.65 E-value: 1.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRA-TAAQRG-WAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNA 90
Cdd:cd07142 21 FPTIDPRNGEVIAHVAEGDAEDVDRAVKAArKAFDEGpWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 91 RW-EASNVRDVLDYAAGGVERLNGRQIPVAGGVDV-TFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETT 168
Cdd:cd07142 101 RYaEVPLAARLFRYYAGWADKIHGMTLPADGPHHVyTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 169 PLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCA-GQVKRLTLELGGKSPNIV 247
Cdd:cd07142 181 PLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAkSNLKPVTLELGGKSPFIV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 248 FADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYV 327
Cdd:cd07142 261 CEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 328 ----PEGAPGLRGTAPEG-PGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVG 402
Cdd:cd07142 341 ehgkEEGATLITGGDRIGsKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNID 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 495685909 403 RALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07142 421 TANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
17-456 |
4.53e-117 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 352.59 E-value: 4.53e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 17 NPATGELLTTVPAATPADVDAAVRRATAA-QRG-WAALAPADRARLLRRFAAAVDGHAEELALLEVREAG-HPIGNARWE 93
Cdd:PLN02766 42 DPRTGEVIARIAEGDKEDVDLAVKAAREAfDHGpWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGkLFALGKAVD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 94 ASNVRDVLDYAAGGVERLNGRQIPVAGGVD-VTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTA 172
Cdd:PLN02766 122 IPAAAGLLRYYAGAADKIHGETLKMSRQLQgYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 173 LRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLM-ARCAGQVKRLTLELGGKSPNIVFADA 251
Cdd:PLN02766 202 LFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMqAAATSNLKQVSLELGGKSPLLIFDDA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 252 DLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVP--- 328
Cdd:PLN02766 282 DVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEhgk 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 329 -EGAPGLRGTAPEG-PGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALR 406
Cdd:PLN02766 362 rEGATLLTGGKPCGdKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANT 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 495685909 407 VSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:PLN02766 442 VSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
13-456 |
1.47e-116 |
|
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: 349.42 E-value: 1.47e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARW 92
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 93 EASNVRDVLDYAAGGVERLNGRQIPV------AGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAE 166
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLdatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 167 TTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGqvKRLTLELGGKSPNI 246
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 247 VFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGY 326
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 327 VPE----GAPGLRGTAPEGPgfWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVG 402
Cdd:cd07094 319 VEEaveaGARLLCGGERDGA--LFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLN 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 495685909 403 RALRVSRAVRAGNLSVNSHSAVRY-ATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07094 397 VAFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
13-456 |
1.21e-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: 1.21e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARW 92
Cdd:cd07085 18 LDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 93 EASNVRDVLDYAAGGVERLNGRQIP-VAGGVDV-TFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPL 170
Cdd:cd07085 98 DVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTySYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 171 TALRLAEIALDAGLPEHLFQVLPGTGPVAgEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFAD 250
Cdd:cd07085 178 AAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 251 ADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGY---- 326
Cdd:cd07085 257 ADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLiesg 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 327 VPEGAPGL---RGTAPEG--PGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDV 401
Cdd:cd07085 337 VEEGAKLVldgRGVKVPGyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSG 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 495685909 402 GRALRVSRAVRAGNLSVNSHSAVRYAT-PFGGYGRSGLG--RELGPDALTAFTETKNV 456
Cdd:cd07085 417 AAARKFQREVDAGMVGINVPIPVPLAFfSFGGWKGSFFGdlHFYGKDGVRFYTQTKTV 474
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
5-459 |
1.66e-108 |
|
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: 329.80 E-value: 1.66e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 5 APAHGpAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAG 84
Cdd:cd07116 11 APVKG-EYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 85 HPIGNA------------RWEASNVRDvldyAAGGVERLNGRQIPVAggvdvtFLEPLGVVGVIAPWNFPMPVAAWGTAP 152
Cdd:cd07116 90 KPVRETlaadiplaidhfRYFAGCIRA----QEGSISEIDENTVAYH------FHEPLGVVGQIIPWNFPLLMATWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 153 ALAAGNAVILKPAETTPLTALRLAEIALDAgLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQV 232
Cdd:cd07116 160 ALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 233 KRLTLELGGKSPNIVFA------DADLEQAAAGAPMsFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPAD 306
Cdd:cd07116 239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEGFVM-FALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 307 EATDMGPLISRVQLDRVRGYV----PEGAP----GLRGTAPEGP--GFWFPPTVLTqaGERDPVAVEEVFGPVAVVLPFR 376
Cdd:cd07116 318 TETMIGAQASLEQLEKILSYIdigkEEGAEvltgGERNELGGLLggGYYVPTTFKG--GNKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 377 DEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 475
|
...
gi 495685909 457 FLS 459
Cdd:cd07116 476 LVS 478
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
15-458 |
2.32e-108 |
|
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: 328.55 E-value: 2.32e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 15 VLNPATGELLTTVPAATPADVDAAVRRAtAAQRgwAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEA 94
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALA-ASYR--STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 95 SNVRDVLDYAAGGVERLNGRQIP---VAGG---VDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETT 168
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGESFScdlTANGkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 169 PLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGqvKRLTLELGGKSPNIVF 248
Cdd:cd07146 160 PLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGY--KRQLLELGGNDPLIVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 249 ADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVP 328
Cdd:cd07146 238 DDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 329 E----GAPGLRGTAPEGPGFWfpPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRA 404
Cdd:cd07146 318 EaiaqGARVLLGNQRQGALYA--PTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 495685909 405 LRVSRAVRAGNLSVNSHSAVRYA-TPFGGYGRSGLG-RELGPDALTAFTETKNVFL 458
Cdd:cd07146 396 KRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
14-464 |
3.42e-108 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 331.00 E-value: 3.42e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 14 PVLNPATGELLTTVPAATPADVDAAVRRATAA--QRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNAR 91
Cdd:PLN02466 76 PTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 92 W-EASNVRDVLDYAAGGVERLNGRQIPVAGGVDVTFL-EPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTP 169
Cdd:PLN02466 156 KaELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLhEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 170 LTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCA-GQVKRLTLELGGKSPNIVF 248
Cdd:PLN02466 236 LSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAkSNLKPVTLELGGKSPFIVC 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 249 ADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLD-LLAPALSAVtVGDPADEATDMGPLISRVQLDRVRGY- 326
Cdd:PLN02466 316 EDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEkAKARALKRV-VGDPFKKGVEQGPQIDSEQFEKILRYi 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 327 ---VPEGAPGLRGTAPEGP-GFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVG 402
Cdd:PLN02466 395 ksgVESGATLECGGDRFGSkGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLD 474
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495685909 403 RALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFLSTEGPA 464
Cdd:PLN02466 475 TANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTPLKNPA 536
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
16-458 |
6.26e-108 |
|
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: 327.28 E-value: 6.26e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 16 LNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEAS 95
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 96 NVRDVLDYAAGGVER--LNGRQIPVAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTAL 173
Cdd:cd07102 81 GMLERARYMISIAEEalADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 174 RLAEIALDAGLPEHLFQVLPGTGPVaGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADL 253
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 254 EQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPE---- 329
Cdd:cd07102 240 DAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADaiak 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 330 GA----PGLRGTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRAL 405
Cdd:cd07102 320 GAraliDGALFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 495685909 406 RVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVFL 458
Cdd:cd07102 400 ALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYHL 452
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
8-456 |
2.64e-103 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 317.65 E-value: 2.64e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 8 HGPAELPVLNPA-TGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHP 86
Cdd:PRK03137 47 TTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 87 IGNARWEASNVRDVLDYAAGGVERLNGRQ--IPVAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKP 164
Cdd:PRK03137 127 WAEADADTAEAIDFLEYYARQMLKLADGKpvESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 165 AETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCA----GQV--KRLTLE 238
Cdd:PRK03137 207 ASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAkvqpGQIwlKRVIAE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 239 LGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPaDEATDMGPLISRV 318
Cdd:PRK03137 287 MGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNAYMGPVINQA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 319 QLDRVRGYVP----EGAPGLRGTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAA 394
Cdd:PRK03137 366 SFDKIMSYIEigkeEGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTG 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495685909 395 SLWTRDVGRALRVSRAVRAGNLSVN--SHSAVRYATPFGGYGRSGLGRELG-PDALTAFTETKNV 456
Cdd:PRK03137 446 AVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSGTDSKAGgPDYLLLFLQAKTV 510
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
13-456 |
5.91e-103 |
|
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: 314.57 E-value: 5.91e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARW 92
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 93 EASNVRDVLDYAAGGVERLNGRQIPV------AGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAE 166
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPLdisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 167 TTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAgEALVDHPGVAKIVFTGSTRTGKRLMARcAGQvKRLTLELGGKSPNI 246
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDA-DLLVTDERIKLLSFTGSPAVGWDLKAR-AGK-KKVVLELGGNAAVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 247 VFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGY 326
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 327 VPE----GAPGLRGTAPEGPgfWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVG 402
Cdd:cd07147 318 VNEavdaGAKLLTGGKRDGA--LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLE 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 495685909 403 RALRVSRAVRAGNLSVNSHSAVRY-ATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07147 396 KALRAWDELEVGGVVINDVPTFRVdHMPYGGVKDSGIGREGVRYAIEEMTEPRLL 450
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
7-441 |
1.83e-100 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 309.14 E-value: 1.83e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 7 AHGPAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHP 86
Cdd:PRK11241 22 ANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 87 IGNARWEASNVRDVLDYAAGGVERLNGRQIP--VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKP 164
Cdd:PRK11241 102 LAEAKGEISYAASFIEWFAEEGKRIYGDTIPghQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 165 AETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSP 244
Cdd:PRK11241 182 ASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 245 NIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVR 324
Cdd:PRK11241 262 FIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 325 GY----VPEGAPGLRGTAPEG-PGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTR 399
Cdd:PRK11241 342 EHiadaLEKGARVVCGGKAHElGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYAR 421
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 495685909 400 DVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRE 441
Cdd:PRK11241 422 DLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGRE 463
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
17-456 |
5.42e-99 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 304.61 E-value: 5.42e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 17 NPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNA------ 90
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAslgeil 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 91 ------RWEASNVRDVLDyaaggVERLNGRQIPVAGGVDVTFlEPLGVVGVIAPWNFPM-----PVAAwgtapALAAGNA 159
Cdd:cd07098 82 vtcekiRWTLKHGEKALR-----PESRPGGLLMFYKRARVEY-EPLGVVGAIVSWNYPFhnllgPIIA-----ALFAGNA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 160 VILKPAETTPLTA---LRLAEIALDA-GLPEHLFQVLPGTGPvAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRL 235
Cdd:cd07098 151 IVVKVSEQVAWSSgffLSIIRECLAAcGHDPDLVQLVTCLPE-TAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 236 TLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLI 315
Cdd:cd07098 230 VLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 316 SRVQLDRVRGY----VPEGAP----GLRGTAPEGP-GFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLAN 386
Cdd:cd07098 310 SPARFDRLEELvadaVEKGARllagGKRYPHPEYPqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIAN 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495685909 387 DTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNSHSAVRY--ATPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYvqQLPFGGVKGSGFGRFAGEEGLRGLCNPKSV 461
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
34-456 |
9.54e-99 |
|
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: 302.96 E-value: 9.54e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 34 DVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGhpiGNARWEASNV---RDVLDYAAGGVER 110
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG---ATAAWAGFNVdlaAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 111 LNGRQIPV--AGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIALDAGLPEHL 188
Cdd:cd07105 78 IIGGSIPSdkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 189 FQVL---PGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAAAGAPMSFL 265
Cdd:cd07105 158 LNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 266 DNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDpadeaTDMGPLISRVQLDRVRGYV----PEGAPGLRG--TAP 339
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVddalSKGAKLVVGglADE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 340 EGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVN 419
Cdd:cd07105 313 SPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
410 420 430
....*....|....*....|....*....|....*...
gi 495685909 420 SHSAVRYAT-PFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07105 393 GMTVHDEPTlPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
12-456 |
4.43e-98 |
|
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: 302.57 E-value: 4.43e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 12 ELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAP-ADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNA 90
Cdd:cd07082 17 TIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 91 RWEASNVRDVLDYAAGGVERLNGRQIP------VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKP 164
Cdd:cd07082 97 LKEVDRTIDYIRDTIEELKRLDGDSLPgdwfpgTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 165 AETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMArcAGQVKRLTLELGGKSP 244
Cdd:cd07082 177 ATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK--QHPMKRLVLELGGKDP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 245 NIVFADADLEQAA----AGApMSFldnSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQL 320
Cdd:cd07082 255 AIVLPDADLELAAkeivKGA-LSY---SGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 321 DRVRGYVPE----GAPGLRGTAPEGPGFwFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASL 396
Cdd:cd07082 331 DFVEGLIDDavakGATVLNGGGREGGNL-IYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASI 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495685909 397 WTRDVGRALRVSRAVRAGNLSVNSHSAvR----YatPFGGYGRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07082 410 FTKDINKARKLADALEVGTVNINSKCQ-RgpdhF--PFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
13-460 |
2.40e-94 |
|
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: 294.49 E-value: 2.40e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGE-LLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNAR 91
Cdd:cd07125 48 APVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 92 WEASNVRDVLDYAAGGVERLNGRQIPVA--GGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTP 169
Cdd:cd07125 128 AEVREAIDFCRYYAAQARELFSDPELPGptGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 170 LTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGK---RLMARCAGQVKRLTLELGGKSPNI 246
Cdd:cd07125 208 LIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKlinRALAERDGPILPLIAETGGKNAMI 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 247 VFADADLEQAAAGAPMSFLDNSGQDCCArTRIL-VQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRG 325
Cdd:cd07125 288 VDSTALPEQAVKDVVQSAFGSAGQRCSA-LRLLyLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 326 YV--PEGAPGL--RGTAPEGPGFWFPPTVLtqAGERDPVAVEEVFGPVAVVLPFRDE--EDAVRLANDTEYGLAASLWTR 399
Cdd:cd07125 367 HTelMRGEAWLiaPAPLDDGNGYFVAPGII--EIVGIFDLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSR 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495685909 400 DVGRALRVSRAVRAGNLSVNSH--SAVRYATPFGGYGRSGLGRELG-PDALTAFTETKNVFLST 460
Cdd:cd07125 445 DEREIEYWRERVEAGNLYINRNitGAIVGRQPFGGWGLSGTGPKAGgPNYLLRFGNEKTVSLNT 508
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
16-457 |
1.16e-92 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 288.17 E-value: 1.16e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 16 LNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEAS 95
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 96 NVRDVLDYAAGGVERLNGRQIPVAGGVDVT----FLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLT 171
Cdd:PRK09406 86 KCAKGFRYYAEHAEALLADEPADAAAVGASrayvRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 172 ALRLAEIALDAGLPEHLFQ-VLPGTGPVagEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFAD 250
Cdd:PRK09406 166 ALYLADLFRRAGFPDGCFQtLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 251 ADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLIS---RVQLDR-VRGY 326
Cdd:PRK09406 244 ADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATeqgRDEVEKqVDDA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 327 VPEGAPGL-RGTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRAL 405
Cdd:PRK09406 324 VAAGATILcGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQE 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 495685909 406 RVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVF 457
Cdd:PRK09406 404 RFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVW 455
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
61-460 |
3.30e-92 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 285.48 E-value: 3.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 61 LRRFAAAVDGHAEELALLEVREAGHPIGNARWEASNVRDVLDYAAGGVERLNGRQIPV--AGGVDVTFLEPLGVVGVIAP 138
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSdrPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 139 WNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGST 218
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 219 RTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSA 298
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 299 VTVGDPADEAT-DMGPLISRVQLDRVRGYVP----EGAP-GLRGTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVV 372
Cdd:PRK10090 241 VQFGNPAERNDiAMGPLINAAALERVEQKVAraveEGARvALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 373 LPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTE 452
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQ 400
|
....*...
gi 495685909 453 TKNVFLST 460
Cdd:PRK10090 401 TQVVYLQS 408
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
16-456 |
1.39e-90 |
|
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: 284.45 E-value: 1.39e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 16 LNPA-TGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEA 94
Cdd:TIGR01237 51 INPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 95 SNVRDVLDYAAGGVERLNGRQI--PVAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTA 172
Cdd:TIGR01237 131 AEAIDFMEYYARQMIELAKGKPvnSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 173 LRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCA----GQ--VKRLTLELGGKSPNI 246
Cdd:TIGR01237 211 AKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvqpGQkhLKRVIAEMGGKDTVI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 247 VFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGY 326
Cdd:TIGR01237 291 VDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEY 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 327 V----PEGAPGLRGTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVG 402
Cdd:TIGR01237 371 IeigkAEGRLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRD 450
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 495685909 403 RALRVSRAVRAGNLSVNSH--SAVRYATPFGGYGRSGLGREL-GPDALTAFTETKNV 456
Cdd:TIGR01237 451 HINRAKAEFEVGNLYFNRNitGAIVGYQPFGGFKMSGTDSKAgGPDYLALFMQAKTV 507
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
16-457 |
9.30e-84 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 265.57 E-value: 9.30e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 16 LNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEAS 95
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 96 NVRDVLD-YAAGGVERLNGRQIPVAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALR 174
Cdd:PRK13968 92 KSANLCDwYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 175 LAEIALDAGLPEHLFQVLPGTGPVAGEALVDhPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLE 254
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 255 QAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLiSRVQL-----DRVRGYVPE 329
Cdd:PRK13968 251 LAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPM-ARFDLrdelhHQVEATLAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 330 GAPGLRGTAP-EGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVS 408
Cdd:PRK13968 330 GARLLLGGEKiAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMA 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 495685909 409 RAVRAGNLSVNSHSAVRYATPFGGYGRSGLGRELGPDALTAFTETKNVF 457
Cdd:PRK13968 410 ARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
16-456 |
8.54e-82 |
|
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: 261.36 E-value: 8.54e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 16 LNP-ATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEA 94
Cdd:cd07083 37 VSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 95 SNVRDVLDYAAGGVERLNGRQ---IPVAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLT 171
Cdd:cd07083 117 AEAIDFIRYYARAALRLRYPAvevVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 172 ALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCA------GQVKRLTLELGGKSPN 245
Cdd:cd07083 197 GYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAArlapgqTWFKRLYVETGGKNAI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 246 IVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRG 325
Cdd:cd07083 277 IVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 326 YVP----EGAPGLRGTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEE--DAVRLANDTEYGLAASLWTR 399
Cdd:cd07083 357 YIEhgknEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSR 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 400 DVGRALRVSRAVRAGNLSVNSHS--AVRYATPFGGYGRSGLGRELG-PDALTAFTETKNV 456
Cdd:cd07083 437 KREHLEEARREFHVGNLYINRKItgALVGVQPFGGFKLSGTNAKTGgPHYLRRFLEMKAV 496
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
8-446 |
1.97e-81 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 259.83 E-value: 1.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 8 HGPAELPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPI 87
Cdd:cd07130 9 GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 88 GNARWEASNVRDVLDYAAGGVERLNGRQIPV--AGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPA 165
Cdd:cd07130 89 PEGLGEVQEMIDICDFAVGLSRQLYGLTIPSerPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 166 ETTPLTALR----LAEIALDAGLPEHLFQVLPGTGPVaGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGG 241
Cdd:cd07130 169 PTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGADV-GEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 242 KSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLD 321
Cdd:cd07130 248 NNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 322 RVRGYVPE-----GAPGLRGTAPEGPGFWFPPTVLTQAGErDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASL 396
Cdd:cd07130 328 NYLAAIEEaksqgGTVLFGGKVIDGPGNYVEPTIVEGLSD-APIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSI 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 495685909 397 WTRDVGRALRVSRAVRA--GNLSVN-SHSAVRYATPFGGYGRSGLGRELGPDA 446
Cdd:cd07130 407 FTTDLRNAFRWLGPKGSdcGIVNVNiGTSGAEIGGAFGGEKETGGGRESGSDA 459
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
9-439 |
9.01e-77 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 260.57 E-value: 9.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 9 GPAELPVLNPA-TGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPI 87
Cdd:PRK11905 565 DGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTL 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 88 GNARWEasnVRDVLD----YAAGGVERLNGRQIpvaggvdvtflEPLGVVGVIAPWNFPMP-----VAAwgtapALAAGN 158
Cdd:PRK11905 645 ANAIAE---VREAVDflryYAAQARRLLNGPGH-----------KPLGPVVCISPWNFPLAiftgqIAA-----ALVAGN 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 159 AVILKPAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKR----LMARCAGQVKr 234
Cdd:PRK11905 706 TVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLiqrtLAKRSGPPVP- 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 235 LTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCArTRIL-VQDSALDRFLDLLAPALSAVTVGDPADEATDMGP 313
Cdd:PRK11905 785 LIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSA-LRVLcLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGP 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 314 LISRVQLDRVRGYVP----EGAPGLRGTAPEG--PGFWFPPTVLTQAGERDPvaVEEVFGPVAVVLPFR-DEEDAVRLA- 385
Cdd:PRK11905 864 VIDAEAQANIEAHIEamraAGRLVHQLPLPAEteKGTFVAPTLIEIDSISDL--EREVFGPVLHVVRFKaDELDRVIDDi 941
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 495685909 386 NDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNSH--SAVRYATPFGGYGRSGLG 439
Cdd:PRK11905 942 NATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNiiGAVVGVQPFGGEGLSGTG 997
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
34-440 |
9.02e-77 |
|
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: 9.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 34 DVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEASNVRDVLDYAAGGV-ERLN 112
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYhERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 113 GRQIPVAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIALDAGLPEHLFQVL 192
Cdd:cd07095 81 ERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 193 PGTGPVaGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQV-KRLTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQD 271
Cdd:cd07095 161 QGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPgKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 272 C-CARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRV-----RGYVPEGAPGLRGTAPEGPGFW 345
Cdd:cd07095 240 CtCARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYllaqqDLLALGGEPLLAMERLVAGTAF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 346 FPPTVLtQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVN-----S 420
Cdd:cd07095 320 LSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNrpttgA 398
|
410 420
....*....|....*....|
gi 495685909 421 HSAVryatPFGGYGRSGLGR 440
Cdd:cd07095 399 SSTA----PFGGVGLSGNHR 414
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
16-437 |
1.53e-75 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 244.87 E-value: 1.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 16 LNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEAS 95
Cdd:PRK09457 20 RNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 96 NVRDVLD-----YAaggvERLNGRQIPVAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPL 170
Cdd:PRK09457 100 AMINKIAisiqaYH----ERTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPW 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 171 TALRLAEIALDAGLPEHLFQVLPGtGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQV-KRLTLELGGKSPNIVFA 249
Cdd:PRK09457 176 VAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPeKILALEMGGNNPLVIDE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 250 DADLEQAAAGAPMSFLDNSGQDC-CARtRILVQDSAL-DRFLDLLAPALSAVTVGDP-ADEATDMGPLISRVQLDRV--- 323
Cdd:PRK09457 255 VADIDAAVHLIIQSAFISAGQRCtCAR-RLLVPQGAQgDAFLARLVAVAKRLTVGRWdAEPQPFMGAVISEQAAQGLvaa 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 324 -RGYVPEGA-PGLRGTAPE-GPGFWFPPTV-LTQAGER-DpvavEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWT 398
Cdd:PRK09457 334 qAQLLALGGkSLLEMTQLQaGTGLLTPGIIdVTGVAELpD----EEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLS 409
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 495685909 399 RDVGRALRVSRAVRAG----NLSVNSHSAvryATPFGGYGRSG 437
Cdd:PRK09457 410 DDREDYDQFLLEIRAGivnwNKPLTGASS---AAPFGGVGASG 449
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
4-439 |
9.23e-74 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 251.78 E-value: 9.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 4 PAPAHGPAELPVLNPA-TGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVRE 82
Cdd:COG4230 563 AGEAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVRE 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 83 AGHPIGNARWEasnVR---DVLDYAAGGVERLNGrqipvaggvDVTFLEPLGVVGVIAPWNFPM-----PVAAwgtapAL 154
Cdd:COG4230 643 AGKTLPDAIAE---VReavDFCRYYAAQARRLFA---------APTVLRGRGVFVCISPWNFPLaiftgQVAA-----AL 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 155 AAGNAVILKPAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGK---RLMARCAGQ 231
Cdd:COG4230 706 AAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARlinRTLAARDGP 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 232 VKRLTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCArTRIL-VQDSALDRFLDLLAPALSAVTVGDPADEATD 310
Cdd:COG4230 786 IVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSA-LRVLcVQEDIADRVLEMLKGAMAELRVGDPADLSTD 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 311 MGPLISRVQLDRVRGYV----PEGAPGLRGTAPEGP--GFWFPPTVLtqagERDPVAV--EEVFGPVAVVLPFRDEE--- 379
Cdd:COG4230 865 VGPVIDAEARANLEAHIermrAEGRLVHQLPLPEECanGTFVAPTLI----EIDSISDleREVFGPVLHVVRYKADEldk 940
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495685909 380 --DAVrlaNDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNS--HSAVRYATPFGGYGRSGLG 439
Cdd:COG4230 941 viDAI---NATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRniIGAVVGVQPFGGEGLSGTG 1001
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
13-439 |
1.16e-73 |
|
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: 238.86 E-value: 1.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRATAAQR---GWaaLAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGN 89
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLdrnNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 90 ARWEASNVRDVLDYAAGGVERLNGRQIPV------AGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILK 163
Cdd:cd07148 79 AKVEVTRAIDGVELAADELGQLGGREIPMgltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 164 PAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAgEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVkRLTLELGGKS 243
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVA-EKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT-RCALEHGGAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 244 PNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRV 323
Cdd:cd07148 237 PVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 324 RGYVPE----GAPGLRGTAPEGPGFwFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTR 399
Cdd:cd07148 317 EEWVNEavaaGARLLCGGKRLSDTT-YAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTK 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 495685909 400 DVGRALRVSRAVRAGNLSVNSHSAVRYA-TPFGGYGRSGLG 439
Cdd:cd07148 396 DLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
14-456 |
1.21e-71 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 244.72 E-value: 1.21e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 14 PVLNPA-TGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNArw 92
Cdd:PRK11904 565 PVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDA-- 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 93 eASNVR---DVLDYAAGGVERLNGRQIPVAGGVDVT---FLEPLGVVGVIAPWNFPM-----PVAAwgtapALAAGNAVI 161
Cdd:PRK11904 643 -IAEVReavDFCRYYAAQARRLFGAPEKLPGPTGESnelRLHGRGVFVCISPWNFPLaiflgQVAA-----ALAAGNTVI 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 162 LKPAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKR----LMARcAGQVKRLTL 237
Cdd:PRK11904 717 AKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIinrtLAAR-DGPIVPLIA 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 238 ELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCArTRIL-VQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLI- 315
Cdd:PRK11904 796 ETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSA-LRVLfVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVId 874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 316 --SRVQLDR-VRGYVPEGAPGLRGTAPEGP--GFWFPPTvltqAGERDPVAV--EEVFGPVAVVLPFRDEE-DAVRLA-N 386
Cdd:PRK11904 875 aeAKANLDAhIERMKREARLLAQLPLPAGTenGHFVAPT----AFEIDSISQleREVFGPILHVIRYKASDlDKVIDAiN 950
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495685909 387 DTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNSH--SAVRYATPFGGYGRSGLG-RELGPDALTAFTETKNV 456
Cdd:PRK11904 951 ATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNqiGAVVGVQPFGGQGLSGTGpKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
128-440 |
4.12e-66 |
|
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: 218.16 E-value: 4.12e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 128 EPLGVVGVIAPWNFPM-----PVAAwgtapALAAGNAVILKPAETTPLTALRLAEIaLDAGLPEHLFQVLPGTGPVAGEA 202
Cdd:cd07087 99 EPLGVVLIIGPWNYPLqlalaPLIG-----AIAAGNTVVLKPSELAPATSALLAKL-IPKYFDPEAVAVVEGGVEVATAL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 203 L---VDHpgvakIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAAAG-APMSFLdNSGQDCCARTRI 278
Cdd:cd07087 173 LaepFDH-----IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRiAWGKFL-NAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 279 LVQDSALDRFLDLLAPALSAVtVGDPADEATDMGPLISRVQLDRVRGYVPEGAPGLRGTAPEGpGFWFPPTVLTQAGERD 358
Cdd:cd07087 247 LVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKE-ERYIAPTILDDVSPDS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 359 PVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNS---HSAVRYAtPFGGYGR 435
Cdd:cd07087 325 PLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDvllHAAIPNL-PFGGVGN 403
|
....*
gi 495685909 436 SGLGR 440
Cdd:cd07087 404 SGMGA 408
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
13-456 |
5.23e-66 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 219.75 E-value: 5.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARW 92
Cdd:TIGR01722 18 IPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 93 EASNVRDVLDYAAGGVERLNGRQIP-VAGGVDV-TFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPL 170
Cdd:TIGR01722 98 DVARGLEVVEHACGVNSLLKGETSTqVATRVDVySIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 171 TALRLAEIALDAGLPEHLFQVLPGtGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFAD 250
Cdd:TIGR01722 178 AAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 251 ADLEQAAAGAPMSFLDNSGQDCCA-RTRILVqdSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYV-- 327
Cdd:TIGR01722 257 ADKDAAADALVGAAYGAAGQRCMAiSAAVLV--GAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIag 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 328 --PEGAPGL---RGTAPEG--PGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRD 400
Cdd:TIGR01722 335 gaAEGAEVLldgRGYKVDGyeEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRD 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 495685909 401 VGRALRVSRAVRAGNLSVNSHSAVRYAT-PFGGYGRSGLG--RELGPDALTAFTETKNV 456
Cdd:TIGR01722 415 GAAARRFQHEIEVGQVGVNVPIPVPLPYfSFTGWKDSFFGdhHIYGKQGTHFYTRGKTV 473
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
13-464 |
2.72e-63 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 213.08 E-value: 2.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARW 92
Cdd:PLN00412 33 VAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 93 EASNVRDVLDYAAG-GVERLNGRQIPVAG---GVDVTFL-----EPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILK 163
Cdd:PLN00412 113 EVVRSGDLISYTAEeGVRILGEGKFLVSDsfpGNERNKYcltskIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 164 PAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTrTGKRLmARCAGQVKrLTLELGGKS 243
Cdd:PLN00412 193 PPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TGIAI-SKKAGMVP-LQMELGGKD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 244 PNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEAtDMGPLISRVQLDRV 323
Cdd:PLN00412 270 ACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDC-DITPVVSESSANFI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 324 RGYV----PEGAPGLRGTAPEGPGFWfpPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTR 399
Cdd:PLN00412 349 EGLVmdakEKGATFCQEWKREGNLIW--PLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTR 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495685909 400 DVGRALRVSRAVRAGNLSVNSHSAvRYAT--PFGGYGRSGLGRELGPDALTAFTETKNVFLSTEGPA 464
Cdd:PLN00412 427 DINKAILISDAMETGTVQINSAPA-RGPDhfPFQGLKDSGIGSQGITNSINMMTKVKSTVINLPKPS 492
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
5-439 |
2.93e-62 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 219.07 E-value: 2.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 5 APAHGPAELPVLNPA-TGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREA 83
Cdd:PRK11809 653 DPVAAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREA 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 84 GHPIGNARWEASNVRDVLDYAAGGVERlngrqipvagGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILK 163
Cdd:PRK11809 733 GKTFSNAIAEVREAVDFLRYYAGQVRD----------DFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 164 PAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGkRLMARC-------AGQVKRLT 236
Cdd:PRK11809 803 PAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVA-RLLQRNlagrldpQGRPIPLI 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 237 LELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCArTRIL-VQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLI 315
Cdd:PRK11809 882 AETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSA-LRVLcLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVI 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 316 ---SRVQLD------RVRGY------VPEGAPGLRGTapegpgfWFPPTVLtqagERDPVA--VEEVFGPVAVVLPF-RD 377
Cdd:PRK11809 961 daeAKANIErhiqamRAKGRpvfqaaRENSEDWQSGT-------FVPPTLI----ELDSFDelKREVFGPVLHVVRYnRN 1029
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495685909 378 EEDAVRLA-NDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNSH--SAVRYATPFGGYGRSGLG 439
Cdd:PRK11809 1030 QLDELIEQiNASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNmvGAVVGVQPFGGEGLSGTG 1094
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
7-454 |
6.56e-62 |
|
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: 209.38 E-value: 6.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 7 AHGPAElPVLNPAT-GELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGH 85
Cdd:TIGR01238 48 ADGEAQ-PVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 86 PIGNARWEASNVRDVLDYAAGGVERLNGRQIpvaggvdvtfLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPA 165
Cdd:TIGR01238 127 TIHNAIAEVREAVDFCRYYAKQVRDVLGEFS----------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 166 ETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKR----LMARCAGQVKrLTLELGG 241
Cdd:TIGR01238 197 EQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLinqtLAQREDAPVP-LIAETGG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 242 KSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISR---- 317
Cdd:TIGR01238 276 QNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAeakq 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 318 ---VQLDRVRGYVPEGAPGLRGTAPEGP-GFWFPPTVLtqagERDPVAV--EEVFGPVAVVLPFRDEEDA--VRLANDTE 389
Cdd:TIGR01238 356 nllAHIEHMSQTQKKIAQLTLDDSRACQhGTFVAPTLF----ELDDIAElsEEVFGPVLHVVRYKARELDqiVDQINQTG 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495685909 390 YGLAASLWTRDVGRALRVSRAVRAGNLSVNSH--SAVRYATPFGGYGRSGLG-RELGPDALTAFTETK 454
Cdd:TIGR01238 432 YGLTMGVHSRIETTYRWIEKHARVGNCYVNRNqvGAVVGVQPFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
128-457 |
5.38e-58 |
|
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: 197.44 E-value: 5.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 128 EPLGVVGVIAPWNFPM-----PVAAwgtapALAAGNAVILKPAETTPLTALRLAEIaLDAGLPEHLFQVLPGTGPVAGeA 202
Cdd:cd07135 107 EPLGVVLIIGPWNYPVllalsPLVG-----AIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVVQGGVPETT-A 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 203 LVDHpGVAKIVFTGSTRTGkRLMARCAgqVKRLT---LELGGKSPNIVFADADLEQAA----AGAPMsfldNSGQDCCAR 275
Cdd:cd07135 180 LLEQ-KFDKIFYTGSGRVG-RIIAEAA--AKHLTpvtLELGGKSPVIVTKNADLELAAkrilWGKFG----NAGQICVAP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 276 TRILVQDSALDRFLDLLAPALSAVTVGDpADEATDMGPLISRVQLDRVRGYVpEGAPG---LRGTAPEGPGFwFPPTVLT 352
Cdd:cd07135 252 DYVLVDPSVYDEFVEELKKVLDEFYPGG-ANASPDYTRIVNPRHFNRLKSLL-DTTKGkvvIGGEMDEATRF-IPPTIVS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 353 QAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNS---HSAVRYAtP 429
Cdd:cd07135 329 DVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDtliHVGVDNA-P 407
|
330 340
....*....|....*....|....*...
gi 495685909 430 FGGYGRSGLGRELGPDALTAFTETKNVF 457
Cdd:cd07135 408 FGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
37-457 |
8.52e-58 |
|
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: 196.68 E-value: 8.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 37 AAVRRATAAQRgwaalapadRARLlRRFAAAVDGHAEEL--ALLE-VREAGHPIGNArwEASNVRDVLDYAAGGVER-LN 112
Cdd:cd07134 12 LALRASTAAER---------IAKL-KRLKKAILARREEIiaALAAdFRKPAAEVDLT--EILPVLSEINHAIKHLKKwMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 113 GRQIP----VAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIALDAGLPEHL 188
Cdd:cd07134 80 PKRVRtpllLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 189 FqVLPGTGPVAGEAL---VDHpgvakIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAAAGAPMSFL 265
Cdd:cd07134 160 A-VFEGDAEVAQALLelpFDH-----IFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 266 DNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEAT-DMGPLISRVQLDRVRGYVPE----GAPGLRGTAPE 340
Cdd:cd07134 234 LNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDavakGAKVEFGGQFD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 341 GPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNs 420
Cdd:cd07134 314 AAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN- 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 495685909 421 HSAVRYAT---PFGGYGRSGLGRELGPDALTAFTETKNVF 457
Cdd:cd07134 393 DVVLHFLNpnlPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
128-457 |
1.28e-57 |
|
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: 196.17 E-value: 1.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 128 EPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIaLDAGLPEHLFQVLPGTGPVAGE--AL-V 204
Cdd:cd07133 100 QPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAEL-LAEYFDEDEVAVVTGGADVAAAfsSLpF 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 205 DHpgvakIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSA 284
Cdd:cd07133 179 DH-----LLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 285 LDRFLDLLAPALSAVTVGDPADEatDMGPLISRVQLDRVRGYVPEG-APGLRGT--APEGPGFW----FPPTVLTQAGER 357
Cdd:cd07133 254 LEEFVAAAKAAVAKMYPTLADNP--DYTSIINERHYARLQGLLEDArAKGARVIelNPAGEDFAatrkLPPTLVLNVTDD 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 358 DPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVN---SHSAVRYAtPFGGYG 434
Cdd:cd07133 332 MRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdtlLHVAQDDL-PFGGVG 410
|
330 340
....*....|....*....|...
gi 495685909 435 RSGLGRELGPDALTAFTETKNVF 457
Cdd:cd07133 411 ASGMGAYHGKEGFLTFSHAKPVF 433
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
128-456 |
4.73e-51 |
|
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: 179.24 E-value: 4.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 128 EPLGVVGVIAPWNFP-----MPVAAwgtapALAAGNAVILKPAETTPLTALRLAEIaLDAGLPEHLFQVLPGTGPVAgEA 202
Cdd:cd07136 99 EPYGVVLIIAPWNYPfqlalAPLIG-----AIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEGGVEEN-QE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 203 LVDHPgVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAA----AGapmSFLdNSGQDCCARTRI 278
Cdd:cd07136 172 LLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAkrivWG---KFL-NAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 279 LVQDSALDRFLDLLAPALSAVTVGDPADEAtDMGPLISRVQLDRVRGYVPEGAPGLRGTAPEGpGFWFPPTVLTQAGERD 358
Cdd:cd07136 247 LVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDNGKIVFGGNTDRE-TLYIEPTILDNVTWDD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 359 PVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVN---SHSAVRYaTPFGGYGR 435
Cdd:cd07136 325 PVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtiMHLANPY-LPFGGVGN 403
|
330 340
....*....|....*....|.
gi 495685909 436 SGLGRELGPDALTAFTETKNV 456
Cdd:cd07136 404 SGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
24-437 |
2.22e-49 |
|
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: 176.24 E-value: 2.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 24 LTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRfaaavdghAEELALLEVRE---AGHPIGNAR--WEA---- 94
Cdd:cd07123 60 LATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLK--------AADLLSGKYRYelnAATMLGQGKnvWQAeida 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 95 -SNVRDVLDYAAGGVERLNGRQIPVAGGVDVTFLE--PL-GVVGVIAPWNFPMPVAAWGTAPALAaGNAVILKPAETTPL 170
Cdd:cd07123 132 aCELIDFLRFNVKYAEELYAQQPLSSPAGVWNRLEyrPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 171 TALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVK------RLTLELGGKSP 244
Cdd:cd07123 211 SNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKNF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 245 NIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVR 324
Cdd:cd07123 291 HLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIK 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 325 GYVPE--GAPGLR----GTAPEGPGFWFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDE--EDAVRLANDT-EYGLAAS 395
Cdd:cd07123 371 GYIDHakSDPEAEiiagGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSdfEETLELVDTTsPYALTGA 450
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 495685909 396 LWTRD---VGRALRVSRAVrAGNLSVNSHS--AVRYATPFGGYGRSG 437
Cdd:cd07123 451 IFAQDrkaIREATDALRNA-AGNFYINDKPtgAVVGQQPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
128-458 |
5.96e-49 |
|
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: 173.56 E-value: 5.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 128 EPLGVVGVIAPWNFP-----MPVAAwgtapALAAGNAVILKPAETTPLTALRLAEIaldagLPEHL----FQVLPGTGPV 198
Cdd:cd07132 99 EPLGVVLIIGAWNYPlqltlVPLVG-----AIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLdkecYPVVLGGVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 199 AGEAL---VDHpgvakIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCAR 275
Cdd:cd07132 169 TTELLkqrFDY-----IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 276 TRILVQDSALDRFLDLLAPALSAVtVGDPADEATDMGPLISRVQLDRVRGYVPEGAPGLRGTAPEGPGFwFPPTVLTQAG 355
Cdd:cd07132 244 DYVLCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERY-IAPTVLTDVK 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 356 ERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVN---SHSAVrYATPFGG 432
Cdd:cd07132 322 PSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdtiMHYTL-DSLPFGG 400
|
330 340
....*....|....*....|....*.
gi 495685909 433 YGRSGLGRELGPDALTAFTETKNVFL 458
Cdd:cd07132 401 VGNSGMGAYHGKYSFDTFSHKRSCLV 426
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
115-457 |
6.48e-48 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 171.75 E-value: 6.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 115 QIPVAGGVDVTFL--EPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIaLDAGLPEHLFQVL 192
Cdd:PTZ00381 93 DTVGVFGPGKSYIipEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL-LTKYLDPSYVRVI 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 193 PGTGPVAGEAL---VDHpgvakIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSG 269
Cdd:PTZ00381 172 EGGVEVTTELLkepFDH-----IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 270 QDCCARTRILVQDSALDRFLDLLAPALSAVtVGDPADEATDMGPLISRVQLDRVRGYVPEGapglRGTAPEGPGF----- 344
Cdd:PTZ00381 247 QTCVAPDYVLVHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKDH----GGKVVYGGEVdienk 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 345 WFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNsHSAV 424
Cdd:PTZ00381 322 YVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN-DCVF 400
|
330 340 350
....*....|....*....|....*....|....*.
gi 495685909 425 RYAT---PFGGYGRSGLGRELGPDALTAFTETKNVF 457
Cdd:PTZ00381 401 HLLNpnlPFGGVGNSGMGAYHGKYGFDTFSHPKPVL 436
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
13-419 |
3.87e-46 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 169.16 E-value: 3.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 13 LPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARW 92
Cdd:PLN02419 131 IDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 93 EASNVRDVLDYAAGGVERLNGRQIP-VAGGVDV-TFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPL 170
Cdd:PLN02419 211 DIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTySIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 171 TALRLAEIALDAGLPEHLFQVLPGTGPVAgEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFAD 250
Cdd:PLN02419 291 ASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 251 ADLEQAAAGAPMSFLDNSGQDCCA-RTRILVQDSalDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVPE 329
Cdd:PLN02419 370 ANIDATLNALLAAGFGAAGQRCMAlSTVVFVGDA--KSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 330 GAPG-----LRGTAPEGPGF----WFPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRD 400
Cdd:PLN02419 448 GVDDgakllLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSS 527
|
410
....*....|....*....
gi 495685909 401 VGRALRVSRAVRAGNLSVN 419
Cdd:PLN02419 528 GAAARKFQMDIEAGQIGIN 546
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
7-446 |
3.15e-45 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 164.62 E-value: 3.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 7 AHGPAeLPVLNPATGELLTTVPAATPADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHP 86
Cdd:PLN02315 31 ANGPL-VSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 87 IGNARWEASNVRDVLDYAAGGVERLNGRQIPvAGGVDVTFLE---PLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILK 163
Cdd:PLN02315 110 LAEGIGEVQEIIDMCDFAVGLSRQLNGSIIP-SERPNHMMMEvwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 164 PAETTPLTALRL----AEIALDAGLPEHLFQVLPGtGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAGQVKRLTLEL 239
Cdd:PLN02315 189 GAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLEL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 240 GGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMGPLISR-- 317
Cdd:PLN02315 268 SGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPes 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 318 -------VQLDRVRGyvpeGAPGLRGTAPEGPGFWFPPTVLtQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEY 390
Cdd:PLN02315 348 kknfekgIEIIKSQG----GKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQ 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 495685909 391 GLAASLWTRDVGRALRV--SRAVRAGNLSVN-SHSAVRYATPFGGYGRSGLGRELGPDA 446
Cdd:PLN02315 423 GLSSSIFTRNPETIFKWigPLGSDCGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDS 481
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
128-456 |
1.24e-42 |
|
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: 156.03 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 128 EPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIaldagLPEHL----FQVLPGtGPVAGEAL 203
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-----IPEYLdtkaIKVIEG-GVPETTAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 204 VDHPGvAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQA----AAGapmSFLDNSGQDCCARTRIL 279
Cdd:cd07137 174 LEQKW-DKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAvrriAGG---KWGCNNGQACIAPDYVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 280 VQDSALDRFLDLLAPALSAVTVGDPAdEATDMGPLISRVQLDRVRGYVPE---GAPGLRGTAPEGPGFWFPPTVLTQAGE 356
Cdd:cd07137 250 VEESFAPTLIDALKNTLEKFFGENPK-ESKDLSRIVNSHHFQRLSRLLDDpsvADKIVHGGERDEKNLYIEPTILLDPPL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 357 RDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNShSAVRYAT---PFGGY 433
Cdd:cd07137 329 DSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFND-TVVQYAIdtlPFGGV 407
|
330 340
....*....|....*....|...
gi 495685909 434 GRSGLGRELGPDALTAFTETKNV 456
Cdd:cd07137 408 GESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
35-419 |
1.87e-38 |
|
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: 144.99 E-value: 1.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 35 VDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWE-----------ASNVRD---- 99
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGElgrttgqlrlfADLVREgswl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 100 --VLDYAAggVERlngrqiPVAGGVDVT-FLEPLGVVGVIAPWNFPMP--VAAWGTAPALAAGNAVILKPAETTPLTALR 174
Cdd:cd07129 81 daRIDPAD--PDR------QPLPRPDLRrMLVPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPGTSEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 175 LAEIALDA----GLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRLMARCAgqvKRLT-----LELGGKSPN 245
Cdd:cd07129 153 VARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAA---ARPEpipfyAELGSVNPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 246 IVFADADLEQAAAGAPM---SFLDNSGQDCcarTR----ILVQDSALDRFLDLLAPALSAvtvgdpADEATDMGPLISRV 318
Cdd:cd07129 230 FILPGALAERGEAIAQGfvgSLTLGAGQFC---TNpglvLVPAGPAGDAFIAALAEALAA------APAQTMLTPGIAEA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 319 QLDRVRGYvpEGAPGLR---GTAPEGPGFWFPPTVLTQAGE---RDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGL 392
Cdd:cd07129 301 YRQGVEAL--AAAPGVRvlaGGAAAEGGNQAAPTLFKVDAAaflADPALQEEVFGPASLVVRYDDAAELLAVAEALEGQL 378
|
410 420 430
....*....|....*....|....*....|.
gi 495685909 393 AASLW--TRDVGRALRVSRAV--RAGNLSVN 419
Cdd:cd07129 379 TATIHgeEDDLALARELLPVLerKAGRLLFN 409
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
14-443 |
4.27e-38 |
|
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: 145.11 E-value: 4.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 14 PVLNPATGELLTTVPAATpADVDAAVRRA-TAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVR----------- 81
Cdd:cd07128 18 TLHDAVTGEVVARVSSEG-LDFAAAVAYArEKGGPALRALTFHERAAMLKALAKYLMERKEDLYALSAAtgatrrdswid 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 82 -EAGhpIGNARWEASNVRDVLD----YAAGGVERLngrqipvagGVDVTF-----LEPLGVVGV-IAPWNFPmpvaAWGT 150
Cdd:cd07128 97 iDGG--IGTLFAYASLGRRELPnahfLVEGDVEPL---------SKDGTFvgqhiLTPRRGVAVhINAFNFP----VWGM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 151 ----APALAAGNAVILKPAETTPLTALRLAEIALDAG-LPEHLFQVLpgTGPVAGeaLVDHPGVAKIV-FTGSTRTGKRL 224
Cdd:cd07128 162 lekfAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLI--CGSVGD--LLDHLGEQDVVaFTGSAATAAKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 225 MArcagqvkrltlelggkSPNIV------FADADLEQAAAGAPMSFLDN-----------------SGQDCCARTRILVQ 281
Cdd:cd07128 238 RA----------------HPNIVarsirfNAEADSLNAAILGPDATPGTpefdlfvkevaremtvkAGQKCTAIRRAFVP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 282 DSALDRFLDLLAPALSAVTVGDPADEATDMGPLISRVQLDRVRGYVP---EGAPGLRGT--------APEGPGFWFPPTV 350
Cdd:cd07128 302 EARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAtllAEAEVVFGGpdrfevvgADAEKGAFFPPTL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 351 LTQAGERDPVAVE--EVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRA--GNLSVNSHSAVRY 426
Cdd:cd07128 382 LLCDDPDAATAVHdvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVLNRDSAKE 461
|
490 500
....*....|....*....|....*.
gi 495685909 427 AT----PF-----GGYGRSGLGRELG 443
Cdd:cd07128 462 STghgsPLpqlvhGGPGRAGGGEELG 487
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
14-443 |
4.70e-35 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 136.76 E-value: 4.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 14 PVLNPATGELLTTVpAATPADVDAAVrrATAAQRGWAALAP---ADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNA 90
Cdd:PRK11903 22 PLFDPVTGEELVRV-SATGLDLAAAF--AFAREQGGAALRAltyAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 91 RWEASNVRDVLDYAAGGVERLNGRQI-----PVAGGVDVTF-----LEPL-GVVGVIAPWNFPmpvaAWG----TAPALA 155
Cdd:PRK11903 99 AVDIDGGIFTLGYYAKLGAALGDARLlrdgeAVQLGKDPAFqgqhvLVPTrGVALFINAFNFP----AWGlwekAAPALL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 156 AGNAVILKPAETTPLTALRLAEIALDAG-LPEHLFQVLpgTGPVAGeaLVDHPGVAKIV-FTGSTRTGKRLMA--RCAGQ 231
Cdd:PRK11903 175 AGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVV--CGSSAG--LLDHLQPFDVVsFTGSAETAAVLRShpAVVQR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 232 VKRLTLELGGKSPNIVFADADLEQAAAGAPMS-----FLDNSGQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPAD 306
Cdd:PRK11903 251 SVRVNVEADSLNSALLGPDAAPGSEAFDLFVKevvreMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 307 EATDMGPLISRVQLDRVRgyvpEGAPGLRG--------------TAPEGPGFWFPPTVLTQAGERDPVAVE--EVFGPVA 370
Cdd:PRK11903 331 DGVRMGPLVSRAQLAAVR----AGLAALRAqaevlfdgggfalvDADPAVAACVGPTLLGASDPDAATAVHdvEVFGPVA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 371 VVLPFRDEEDAVRLANDTEYGLAASLWTRDV--------------GRALRVSRAVRAgnlSVNSHSAVRYATPFGGYGRS 436
Cdd:PRK11903 407 TLLPYRDAAHALALARRGQGSLVASVYSDDAaflaaaaleladshGRVHVISPDVAA---LHTGHGNVMPQSLHGGPGRA 483
|
....*..
gi 495685909 437 GLGRELG 443
Cdd:PRK11903 484 GGGEELG 490
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
128-457 |
8.41e-35 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 135.62 E-value: 8.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 128 EPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAeialdAGLPEHL----FQVLPGtGPVAGEAL 203
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA-----ANIPKYLdskaVKVIEG-GPAVGEQL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 204 VDHPGvAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIV---FADADLEQAA---AGAPMSflDNSGQDCCARTR 277
Cdd:PLN02203 181 LQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVnriVGGKWG--SCAGQACIAIDY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 278 ILVQDSALDRFLDLLAPALSAVtVGDPADEATDMGPLISRVQLDRVRGYVPEgaPGLRGTAPEGPGF-----WFPPTVLT 352
Cdd:PLN02203 258 VLVEERFAPILIELLKSTIKKF-FGENPRESKSMARILNKKHFQRLSNLLKD--PRVAASIVHGGSIdekklFIEPTILL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 353 QAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNShSAVRYAT---P 429
Cdd:PLN02203 335 NPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFND-AIIQYACdslP 413
|
330 340
....*....|....*....|....*...
gi 495685909 430 FGGYGRSGLGRELGPDALTAFTETKNVF 457
Cdd:PLN02203 414 FGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
128-457 |
1.61e-30 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 123.23 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 128 EPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIaLDAGLPEHLFQVLPGtGPVAGEALVDHP 207
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEG-AVTETTALLEQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 208 GvAKIVFTGSTRTGKRLMARCAGQVKRLTLELGGKSPNIVFADADLE----QAAAGapmSFLDNSGQDCCARTRILVQDS 283
Cdd:PLN02174 189 W-DKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKvtvrRIIAG---KWGCNNGQACISPDYILTTKE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 284 ALDRFLDLLAPALSAVTVGDPAdEATDMGPLISRVQLDRVRGYVPEGAPG---LRGTAPEGPGFWFPPTVLTQAGERDPV 360
Cdd:PLN02174 265 YAPKVIDAMKKELETFYGKNPM-ESKDMSRIVNSTHFDRLSKLLDEKEVSdkiVYGGEKDRENLKIAPTILLDVPLDSLI 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 361 AVEEVFGPVAVVLPFRDEEDAVRLANDTEYGLAASLWTRDVGRALRVSRAVRAGNLSVNS---HSAVrYATPFGGYGRSG 437
Cdd:PLN02174 344 MSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDiavHLAL-HTLPFGGVGESG 422
|
330 340
....*....|....*....|
gi 495685909 438 LGRELGPDALTAFTETKNVF 457
Cdd:PLN02174 423 MGAYHGKFSFDAFSHKKAVL 442
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
35-400 |
2.32e-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: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 35 VDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPI--------GNARWEA-SNVRDVLDYAA 105
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWmfaenicgDQVQLRArAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 106 GGVERLNGRQIPVAGGVDVtflePLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIALDAG-L 184
Cdd:cd07084 81 EPGNHLGQGLKQQSHGYRW----PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 185 PEHLFQVLPGTGPvAGEALVDHPGVAKIVFTGSTRTGKRLMARCAgqVKRLTLELGGKSPNIVFADAD-----LEQAAAG 259
Cdd:cd07084 157 PPEDVTLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDAK--QARIYLELAGFNWKVLGPDAQavdyvAWQCVQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 260 APMSfldnSGQDCCARTRILV-QDSALDRFLDLLAPALSAVTVGDpadeaTDMGPLISRVQLDRVRGYVPEGAPGLR--- 335
Cdd:cd07084 234 MTAC----SGQKCTAQSMLFVpENWSKTPLVEKLKALLARRKLED-----LLLGPVQTFTTLAMIAHMENLLGSVLLfsg 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495685909 336 -----GTAPEGPGFWFPPTVLTQAGERD---PVAVEEVFGPVAVVLPFRD--EEDAVRLANDTEYGLAASLWTRD 400
Cdd:cd07084 305 kelknHSIPSIYGACVASALFVPIDEILktyELVTEEIFGPFAIVVEYKKdqLALVLELLERMHGSLTAAIYSND 379
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
41-293 |
6.62e-16 |
|
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: 79.19 E-value: 6.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 41 RATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGN--ARWEA----------SNVrDVLDYAAGGV 108
Cdd:cd07077 2 SAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSliANWIAmmgcsesklyKNI-DTERGITASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 109 ERLNGRQIPVAGGVdVTFLEPLGVVGVIAPWNFPMpVAAWGTAPALAAGNAVILKPAETTPLT--ALRLAEIALDA-GLP 185
Cdd:cd07077 81 GHIQDVLLPDNGET-YVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTnrALALLFQAADAaHGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 186 EHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKrlMARCAGQVKRLTLELGGKSPNIVFADADLEQAAAGAPMS-F 264
Cdd:cd07077 159 KILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVD--AAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSkF 236
|
250 260
....*....|....*....|....*....
gi 495685909 265 LDNSGqdCCARTRILVQDSALDRFLDLLA 293
Cdd:cd07077 237 FDQNA--CASEQNLYVVDDVLDPLYEEFK 263
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
33-411 |
4.21e-15 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 77.25 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 33 ADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGhpIGNARWEASNVRDVLDYAAgGVERLn 112
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETG--MGRVEDKIAKNVAAAEKTP-GVEDL- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 113 grqIPVA----GGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKP---AETTPLTALR-LAEIALDAGL 184
Cdd:PRK15398 112 ---TTEAltgdNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgAKKVSLRAIElLNEAIVAAGG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 185 PEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGST-------RTGKRLMArcAGqvkrltlelGGKSPNIVFADADLEQAA 257
Cdd:PRK15398 189 PENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPavvkaamKSGKKAIG--AG---------AGNPPVVVDETADIEKAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 258 ----AGApmSFlDNSgQDCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDM----GPLISRVQLDRVRGYVPE 329
Cdd:PRK15398 258 rdivKGA--SF-DNN-LPCIAEKEVIVVDSVADELMRLMEKNGAVLLTAEQAEKLQKVvlknGGTVNKKWVGKDAAKILE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 330 GApGLRGTAPegpgfwfPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGL--AASLWTRDVGRALRV 407
Cdd:PRK15398 334 AA-GINVPKD-------TRLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNKM 405
|
....
gi 495685909 408 SRAV 411
Cdd:PRK15398 406 ARAI 409
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
33-392 |
4.61e-15 |
|
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: 76.89 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 33 ADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGhpIGNARWEASNVRDVLDYaAGGVERLn 112
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETG--MGRVEDKIAKNHLAAEK-TPGTEDL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 113 grqIPVA----GGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKP----AETTPLTALRLAEIALDAGL 184
Cdd:cd07121 80 ---TTTAwsgdNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgaKKVSAYAVELINKAIAEAGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 185 PEHLFQVLPGTGPVAGEALVDHPGVAKIVFTG-------STRTGKRLMarCAGqvkrltlelGGKSPNIVFADADLEQAA 257
Cdd:cd07121 157 PDNLVVTVEEPTIETTNELMAHPDINLLVVTGgpavvkaALSSGKKAI--GAG---------AGNPPVVVDETADIEKAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 258 ----AGApmSFlDNSgQDCCARTRILVQDSALDRFLDLLAPAlSAVTVGDPADEAtdmgpLISRVQLDR-----VRGYVP 328
Cdd:cd07121 226 rdivQGA--SF-DNN-LPCIAEKEVIAVDSVADYLIAAMQRN-GAYVLNDEQAEQ-----LLEVVLLTNkgatpNKKWVG 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495685909 329 EGAPGLRGTA--PEGPGfwfPPTVLTQAGERDPVAVEEVFGPVAVVLPFRDEEDAVRLANDTEYGL 392
Cdd:cd07121 296 KDASKILKAAgiEVPAD---IRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGN 358
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
35-409 |
1.28e-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: 75.77 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 35 VDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGHPIGNARWEASNVRDVLDYAAGGVERLNGR 114
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 115 QIPVAGGVDVTFLEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKP----AETTPLTALRLAEIALDAGLPEHLFQ 190
Cdd:cd07081 81 LTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 191 VLPGTGPVAGEALVDHPGVAKIVFTGstrtGKRLMARCAGQVKRLTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQ 270
Cdd:cd07081 161 WIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 271 DCCARTRILVQDSALDRFLDLLAPALSAVTVGDPADEATDMgpLISRVQLDrvRGYVPEGApglrGTAPEGPGFWFPPTV 350
Cdd:cd07081 237 ICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPV--ILKNGDVN--RDIVGQDA----YKIAAAAGLKVPQET 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495685909 351 ------LTQAGERDPvAVEEVFGPVAVVLPFRDEEDAVRLA----NDTEYGLAASLWTRDVGRALRVSR 409
Cdd:cd07081 309 riligeVTSLAEHEP-FAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIENMNQ 376
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
18-419 |
6.56e-13 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 70.59 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 18 PATGELLTTVPAAtpaDVDAAVRRATAAQRGWAALAPADRA--------RLLRR---FAAAVDgHAEELALLEVREAGHP 86
Cdd:cd07127 72 PYGVELGVTYPQC---DPDALLAAARAAMPGWRDAGARARAgvcleilqRLNARsfeMAHAVM-HTTGQAFMMAFQAGGP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 87 ---------IGNARWEASNVRDVLDYaaggvERLNGRQIPVAggVDVTF-LEPLGVVGVIAPWNFPmpvaAWGTAPA--- 153
Cdd:cd07127 148 haqdrgleaVAYAWREMSRIPPTAEW-----EKPQGKHDPLA--MEKTFtVVPRGVALVIGCSTFP----TWNGYPGlfa 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 154 -LAAGNAVILKPAettPLTALRLA-------EIALDAGLPEHL--FQVLPGTGPVAGEaLVDHPGVAKIVFTGSTRTGKR 223
Cdd:cd07127 217 sLATGNPVIVKPH---PAAILPLAitvqvarEVLAEAGFDPNLvtLAADTPEEPIAQT-LATRPEVRIIDFTGSNAFGDW 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 224 LMARCAGqvKRLTLELGGKSPNIVFADADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSAL---------DRFLDLLAP 294
Cdd:cd07127 293 LEANARQ--AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDGIqtddgrksfDEVAADLAA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 295 ALSAVtVGDPADEATDMGPLISRVQLDRVRGYVPEGAPGLRGTAPEGPGF----WFPPTVLTQAGERDPVAVEEVFGPVA 370
Cdd:cd07127 371 AIDGL-LADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFpdarVRTPLLLKLDASDEAAYAEERFGPIA 449
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 495685909 371 VVLPFRDEEDAVRLANDT--EYG-LAASLWTRDVGRALRVSRAVR--AGNLSVN 419
Cdd:cd07127 450 FVVATDSTDHSIELARESvrEHGaMTVGVYSTDPEVVERVQEAALdaGVALSIN 503
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
35-434 |
3.58e-12 |
|
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: 67.90 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 35 VDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELALLEVREAGhpIGNarWE--------ASnvRDVLDYAAG 106
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETG--MGV--VEdkviknhfAS--EYVYNDIKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 107 ----GVERLNgrqiPVAGGVDVTflEPLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKP----AETTPLTALRLAEI 178
Cdd:cd07122 75 mktvGVIEED----EEKGIVEIA--EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhpraKKCSIEAAKIMREA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 179 ALDAGLPEHLFQVLPGTGPVAGEALVDHPGVAKIVFTGSTRTGKRlmARCAGqvkrlTLELG---GKSPNIVFADADLEQ 255
Cdd:cd07122 149 AVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGGPGMVKA--AYSSG-----KPAIGvgpGNVPAYIDETADIKR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 256 AAAGAPMS--FlDNsGQDCCARTRILVQDSALDRFLDLLApALSAVTVgdPADEATDMGPLISRVQLDRVRGYVPEGAPG 333
Cdd:cd07122 222 AVKDIILSktF-DN-GTICASEQSVIVDDEIYDEVRAELK-RRGAYFL--NEEEKEKLEKALFDDGGTLNPDIVGKSAQK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 334 LRGTApegpGFWFPPTV------LTQAGERDPVAVEEVFgPVAVVLPFRDEEDAVRLAND-TEYGLA---ASLWTRDVGR 403
Cdd:cd07122 297 IAELA----GIEVPEDTkvlvaeETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKARElLEYGGAghtAVIHSNDEEV 371
|
410 420 430
....*....|....*....|....*....|.
gi 495685909 404 ALRVSRAVRAGNLSVNSHSAvryatpFGGYG 434
Cdd:cd07122 372 IEEFALRMPVSRILVNTPSS------LGGIG 396
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
129-379 |
1.61e-08 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 56.74 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 129 PLGVVGVIAPWNFPMPVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIALDAGLPEHLFQVLPGTGPVAGEALVD-HP 207
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEaNP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 208 GVakIVFTGSTRTGKRLMARCAGQVKrltLELGGKSPNIVFAD-ADLEQAAAGAPMSFLDNSGQDCCARTRILVQDSALD 286
Cdd:cd07126 222 RM--TLFTGSSKVAERLALELHGKVK---LEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 287 R-FLDLLAPA-----LSAVTVGdPADEATDMGPLISRVQLDRVRGYVPE--GAPGLRGTAPEGPGFWFP-----PTVLTQ 353
Cdd:cd07126 297 AgILDKLKALaeqrkLEDLTIG-PVLTWTTERILDHVDKLLAIPGAKVLfgGKPLTNHSIPSIYGAYEPtavfvPLEEIA 375
|
250 260
....*....|....*....|....*.
gi 495685909 354 AGERDPVAVEEVFGPVAVVLPFRDEE 379
Cdd:cd07126 376 IEENFELVTTEVFGPFQVVTEYKDEQ 401
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
37-204 |
4.00e-07 |
|
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).
Pssm-ID: 143398 Cd Length: 406 Bit Score: 52.05 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 37 AAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELA------LLEVREAGHP--------IGNARWE--ASNVRDV 100
Cdd:cd07079 2 ELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILeanakdLAAAREAGLSealldrllLTPERIEamAEGLRQV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 101 ldyAA---------GGVERLNGRQIpvaGGVDVtflePLGVVGVI--APWNfpmpVAAWGTAPALAAGNAVILKPAETTP 169
Cdd:cd07079 82 ---AAlpdpvgevlRGWTLPNGLQI---EKVRV----PLGVIGIIyeSRPN----VTVDAAALCLKSGNAVILRGGSEAL 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 495685909 170 LTALRLAEI---AL-DAGLPEHLFQVLPGTGPVAGEALV 204
Cdd:cd07079 148 HSNRALVEIiqeALeEAGLPEDAVQLIPDTDREAVQELL 186
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
33-305 |
2.43e-05 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 46.60 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 33 ADVDAAVRRATAAQRGWAALAPADRARLLRRFAAAVDGHAEELAllevreaghpignarweASNVRDVLDYAAGGV---- 108
Cdd:PRK00197 4 EYLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEIL-----------------AANAKDLAAARANGLsaam 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 109 --------ERLNG-----RQI-----PVAGGVDVTFLE----------PLGVVGVI--APWNFPMPVAAWgtapALAAGN 158
Cdd:PRK00197 67 ldrlllteARIEGiaeglRQVaalpdPVGEVLDGWTLPnglrigrvrvPLGVIGVIyeSRPNVTVDAAAL----CLKSGN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 159 AVILKPAETTPLTALRLAEI---AL-DAGLPEHLFQVLPGTgpvagealvDHPGVAK----------IVftgsTRTGKRL 224
Cdd:PRK00197 143 AVILRGGSEAIHSNRALVAViqeALeEAGLPADAVQLVETT---------DRAAVGEllkldgyvdvII----PRGGAGL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 225 MARCAGQVKRLTLElGGKSPNIVF--ADADLEQAAAgapmsFLDNsgqdccARTR----------ILVQDSALDRFLDLL 292
Cdd:PRK00197 210 IRRVVENATVPVIE-HGDGICHIYvdESADLDKALK-----IVLN------AKTQrpsvcnaletLLVHEAIAEEFLPKL 277
|
330
....*....|....*.
gi 495685909 293 APALSA--VTV-GDPA 305
Cdd:PRK00197 278 AEALAEagVELrGDEA 293
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
129-386 |
1.83e-03 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 40.34 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 129 PLGVVGVIAPWNFPMpVAAWGTAPALAAGNAVILKPAETTPLTALRLAEIALDAgLPEHLFQ------VLPGTGPVAGEA 202
Cdd:cd07080 112 PRGLVVHIIAGNVPL-LPVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLADV-DPNHPLTdsisvvYWPGGDAELEER 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 203 LVDHpgVAKIVFTGSTRTGKRLMARCAGQVKrlTLELGGK-SPNIV----FADADLEQAAAGAPMS--FLDnsgQDCCAR 275
Cdd:cd07080 190 ILAS--ADAVVAWGGEEAVKAIRSLLPPGCR--LIDFGPKySFAVIdreaLESEKLAEVADALAEDicRYD---QQACSS 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495685909 276 TR-ILVQDS---ALDRFLDLLAPALSAvtvgDPADEATDMGPLISRVQLDRVRGYVPEGapGLRGTAPEGPGfWfppTVL 351
Cdd:cd07080 263 PQvVFVEKDddeELREFAEALAAALER----LPRRYPALSLSAAESAKIARARLEAEFY--ELKGGVSRDLG-W---TVI 332
|
250 260 270
....*....|....*....|....*....|....*
gi 495685909 352 TQageRDPVAVEEVFGPVAVVLPFRDEEDAVRLAN 386
Cdd:cd07080 333 IS---DEIGLEASPLNRTVNVKPVASLDDVLRPVT 364
|
|
| |
