|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
53-527 |
0e+00 |
|
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: 974.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 53 GVYNGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:cd07130 1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 133 SLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICG 212
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 213 NVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGR 292
Cdd:cd07130 161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 293 SLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPL 372
Cdd:cd07130 241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 373 HTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLaHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 452
Cdd:cd07130 321 HTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGL-SDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVP 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380813202 453 QGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKHYMRRSTCTINYS 527
Cdd:cd07130 400 QGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
53-527 |
0e+00 |
|
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: 909.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 53 GVYNGSWGGRG-EVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07086 1 GVIGGEWVGSGgETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 132 VSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMIC 211
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 212 GNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFG 291
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGP 371
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 372 LHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDR--PGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNN 449
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380813202 450 EVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKHYMRRSTCTINYS 527
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
36-538 |
0e+00 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 719.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 36 QPQYAWLKELGLREENEGVY-NGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIV 114
Cdd:PLN02315 5 RKEYEFLSEIGLSSRNLGCYvGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 115 RQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAF 194
Cdd:PLN02315 85 RQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 195 NFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTG 274
Cdd:PLN02315 165 NFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 275 STQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAY 354
Cdd:PLN02315 245 SSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 355 AQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTgLAHDASIAHTETFAPILY 434
Cdd:PLN02315 325 KQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 435 VFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWK 514
Cdd:PLN02315 404 VMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWK 483
|
490 500
....*....|....*....|....
gi 380813202 515 HYMRRSTCTINYSKDLPLAQGIKF 538
Cdd:PLN02315 484 QYMRRSTCTINYGNELPLAQGINF 507
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
89-524 |
4.42e-171 |
|
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: 490.57 E-value: 4.42e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 89 EETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPI 168
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 169 LPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLednkLPGAIC 248
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAG----LPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 249 SLTCGGAD-IGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAG 327
Cdd:cd07078 157 NVVTGDGDeVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 328 QRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDR-PG 406
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 407 NYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIP 486
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVA--ERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 380813202 487 TSGAEIGGAFGGEKHTGGGRESGSDAWKHYMRRSTCTI 524
Cdd:cd07078 395 SVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
61-521 |
4.17e-170 |
|
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: 488.96 E-value: 4.17e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 61 GRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 141 VEGVGEVQEYVDICDYAVGLSRMIGGPILPSeRPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGA 220
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 221 PTTSLISVAvtkiIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGG 299
Cdd:pfam00171 163 ELTPLTALL----LAELFEEAGLPaGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 300 NNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVS 379
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 380 MFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSI 459
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380813202 460 FTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKHYMRRST 521
Cdd:pfam00171 399 FTSDLERALRVA--RRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
56-526 |
1.84e-167 |
|
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: 483.09 E-value: 1.84e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:COG1012 11 GGEWvaAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 134 LEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGN 213
Cdd:COG1012 91 LETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 214 VCLWKGAPTTSLISVAvtkiIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGR 292
Cdd:COG1012 171 TVVLKPAEQTPLSALL----LAELLEEAGLPaGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 293 SLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPL 372
Cdd:COG1012 247 VTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 373 HTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDR-PGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEV 451
Cdd:COG1012 327 ISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDT 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380813202 452 KQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKHYMRRSTCTINY 526
Cdd:COG1012 407 EYGLAASVFTRDLARARRVA--RRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
56-527 |
1.51e-132 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 394.02 E-value: 1.51e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSWGGR--GEVITTYCPAN-NEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:cd07131 4 GGEWVDSasGETFDSRNPADlEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 133 SLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICG 212
Cdd:cd07131 84 TREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 213 NVCLWKGAPTTSlisvAVTKIIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFG 291
Cdd:cd07131 164 NTVVFKPAEDTP----ACALKLVELFAEAGLPpGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGP 371
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 372 LHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDR----PGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAW 447
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 448 NNEVKQGLSSSIFTKDLGRIFRWLGpkgsDC--GIVNVNIPTSGAEIGGAFGGEKHTGGG-RESGSDAWKHYMRRSTCTI 524
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARR----DLeaGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
...
gi 380813202 525 NYS 527
Cdd:cd07131 476 DYS 478
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
93-524 |
6.22e-128 |
|
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: 378.11 E-value: 6.22e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 93 KKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSE 172
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 173 RPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLednkLPGAICSLTC 252
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG----LPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 253 GGAD-IGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCT 331
Cdd:cd06534 157 GGGDeVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 332 TARRLFVHESIHDEVVNRLKkayaqirvgnpwdsnvlygplhtkqavsmflgaveeakkeggtvvyggkvmdrpgnyvep 411
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV------------------------------------------------------------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 412 TIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAE 491
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVA--ERLRAGTVYINDSSIGVG 334
|
410 420 430
....*....|....*....|....*....|...
gi 380813202 492 IGGAFGGEKHTGGGRESGSDAWKHYMRRSTCTI 524
Cdd:cd06534 335 PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
52-512 |
3.31e-118 |
|
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: 356.94 E-value: 3.31e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 52 EGVYNGSWGGRGEVITTYCPAN-NEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGS 130
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 131 LVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMI 210
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 211 CGNVCLWKGAPTTSLISVAvtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQER 289
Cdd:cd07097 162 YGNTVVFKPAELTPASAWA----LVEILEEAGLPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 290 FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLY 369
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 370 GPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRP--GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAW 447
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380813202 448 NNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSDA 512
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFK--RRVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEAA 461
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
71-517 |
1.13e-111 |
|
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: 339.41 E-value: 1.13e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVqey 150
Cdd:cd07103 4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 151 vdicDYAVGL-------SRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPvavygwnnaIAMI---------CGNV 214
Cdd:cd07103 81 ----DYAASFlewfaeeARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFP---------AAMItrkiapalaAGCT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 215 CLWKGAPTTSLISVAvtkiIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRS 293
Cdd:cd07103 148 VVLKPAEETPLSALA----LAELAEEAGLPaGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 294 LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLH 373
Cdd:cd07103 224 SLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 374 TKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQ 453
Cdd:cd07103 304 NERAVEKVEALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPY 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380813202 454 GLSSSIFTKDLGRIFRwLGpKGSDCGIVNVNIPT-SGAEIggAFGGEKHTGGGRESGSDAWKHYM 517
Cdd:cd07103 384 GLAAYVFTRDLARAWR-VA-EALEAGMVGINTGLiSDAEA--PFGGVKESGLGREGGKEGLEEYL 444
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
63-469 |
1.72e-105 |
|
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: 324.22 E-value: 1.72e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVE 142
Cdd:cd07088 12 GETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 143 GVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPT 222
Cdd:cd07088 92 ARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 223 TSLISVAVTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNN 301
Cdd:cd07088 172 TPLNALEFAELVDEA----GLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 302 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMF 381
Cdd:cd07088 248 PAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 382 LGAVEEAKKEGGTVVYGGKVMD-RPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIF 460
Cdd:cd07088 328 EEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIY 407
|
....*....
gi 380813202 461 TKDLGRIFR 469
Cdd:cd07088 408 TENLNTAMR 416
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
71-518 |
7.92e-102 |
|
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: 314.49 E-value: 7.92e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWK--IWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQ 148
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 149 EYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISV 228
Cdd:cd07114 84 YLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 229 AVTKIiakVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFED 308
Cdd:cd07114 164 ELAKL---AEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 309 ADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEA 388
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 389 KKEGGTVVYGGKVMDRP----GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 464
Cdd:cd07114 321 REEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 380813202 465 GRIFRWlgPKGSDCGIVNVNI-----PTSgaeiggAFGGEKHTGGGRESGSDAWKHYMR 518
Cdd:cd07114 401 ARAHRV--ARAIEAGTVWVNTyralsPSS------PFGGFKDSGIGRENGIEAIREYTQ 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
87-513 |
1.26e-98 |
|
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: 305.22 E-value: 1.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 87 DYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGG 166
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 167 PILPSERPGHALIEQWNPVGLVGIITAFNFPV-----AVygwnnAIAMICGNVCLWKGAPTTslisvAVTK--IIAKVLE 239
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLilamrSV-----APALALGNAVVLKPDSRT-----PVTGglLIAEIFE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 240 DNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVAlmvqERFGRSL----LELGGNNAIIAFEDADLSLV 314
Cdd:cd07104 151 EAGLPkGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIG----ELAGRHLkkvaLELGGNNPLIVLDDADLDLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 315 VPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGT 394
Cdd:cd07104 227 VSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 395 VVYGGKvmdRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRwLGpK 474
Cdd:cd07104 307 LLTGGT---YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMA-FA-E 381
|
410 420 430
....*....|....*....|....*....|....*....
gi 380813202 475 GSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAW 513
Cdd:cd07104 382 RLETGMVHINDQTVNDEPHVPFGGVKASGGGRFGGPASL 420
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
71-510 |
5.00e-94 |
|
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: 293.85 E-value: 5.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07150 6 PADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 151 VDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVav 230
Cdd:cd07150 86 PELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 231 tkIIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDA 309
Cdd:cd07150 164 --KIAEIMEEAGLPkGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 310 DLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAK 389
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 390 KEGGTVVYGGKvmdRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 469
Cdd:cd07150 322 AKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFK 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 380813202 470 WlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGS 510
Cdd:cd07150 399 L--AERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGE 437
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
71-521 |
4.97e-93 |
|
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: 291.35 E-value: 4.97e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 151 VDICDYAVGLSrmiggpiLPSER----PGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLI 226
Cdd:cd07106 84 VAWLRYTASLD-------LPDEVieddDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 227 SVAVTKIIAKVLEdnklPGAICSLTcGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAF 306
Cdd:cd07106 157 TLKLGELAQEVLP----PGVLNVVS-GGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 307 EDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVE 386
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 387 EAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGR 466
Cdd:cd07106 312 DAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 380813202 467 IFRwLGPKgSDCGIVNVNiptSGAEIGGA--FGGEKHTGGGRESGSDAWKHYMRRST 521
Cdd:cd07106 392 AEA-VARR-LEAGTVWIN---THGALDPDapFGGHKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
71-518 |
6.43e-92 |
|
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: 288.46 E-value: 6.43e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGV-GEVQE 149
Cdd:cd07092 4 PATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 150 YVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07092 84 AVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 230 VTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDA 309
Cdd:cd07092 164 LAELAAEVLP----PGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 310 DLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAK 389
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 390 KeGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 469
Cdd:cd07092 320 A-HARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 380813202 470 WLGPKGSDCGIVNVNIPTSgAEIggAFGGEKHTGGGRESGSDAWKHYMR 518
Cdd:cd07092 399 LSARLDFGTVWVNTHIPLA-AEM--PHGGFKQSGYGKDLSIYALEDYTR 444
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
57-509 |
1.92e-91 |
|
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: 287.66 E-value: 1.92e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 57 GSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSL 134
Cdd:cd07151 1 GEWrdGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 135 EMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNV 214
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 215 CLWKGAPTTslisvAVTK--IIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFG 291
Cdd:cd07151 161 VVLKPASDT-----PITGglLLAKIFEEAGLPKGVLNVVVGaGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGP 371
Cdd:cd07151 236 KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 372 LHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMdrpGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEV 451
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDT 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 380813202 452 KQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESG 509
Cdd:cd07151 393 EYGLSGAVFTSDLERGVQF--ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNG 448
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
71-516 |
8.11e-91 |
|
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: 285.87 E-value: 8.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG-EVQE 149
Cdd:cd07115 4 PATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 150 YVDICDYAVGLSRMIGGPILPSeRPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07115 84 AADTFRYYAGWADKIEGEVIPV-RGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 230 VTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFED 308
Cdd:cd07115 163 IAELMAEA----GFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 309 ADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEA 388
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 389 KKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIF 468
Cdd:cd07115 319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 380813202 469 RWlgPKGSDCGIVNVNipTSGA-EIGGAFGGEKHTGGGRESGSDAWKHY 516
Cdd:cd07115 399 RV--AAALKAGTVWIN--TYNRfDPGSPFGGYKQSGFGREMGREALDEY 443
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
54-526 |
5.87e-89 |
|
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: 282.96 E-value: 5.87e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 54 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 133 SLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSeRPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICG 212
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEM-VPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 213 NVCLWKGAPTTSLISVAVtkiiAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVG---KQVALMVQE 288
Cdd:cd07124 195 NTVVLKPAEDTPVIAAKL----VEILEEAGLPpGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGlriYERAAKVQP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 289 RFG---RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDS 365
Cdd:cd07124 271 GQKwlkRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 366 NVLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRP--GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEE 443
Cdd:cd07124 351 EVYMGPVIDKGARDRIRRYIEIGKSE-GRLLLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 444 VFAWNNEVKQGLSSSIFTKDLGRI--FRwlgpKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTG-GGRESGSDAWKHYMRR 519
Cdd:cd07124 430 ALEIANDTEYGLTGGVFSRSPEHLerAR----REFEVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDYLLQFMQP 505
|
....*..
gi 380813202 520 STCTINY 526
Cdd:cd07124 506 KTVTENF 512
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
68-517 |
7.43e-88 |
|
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: 278.29 E-value: 7.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 68 TYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGev 147
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 148 qeyVDI----------CDYAVGLsrmiGGPILPSErPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLW 217
Cdd:cd07093 79 ---RDIpraaanfrffADYILQL----DGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 218 KGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLE 296
Cdd:cd07093 151 KPSEWTPLTAW----LLAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 297 LGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQ 376
Cdd:cd07093 227 LGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 377 AVSMFLGAVEEAKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 452
Cdd:cd07093 307 HLEKVLGYVELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTP 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380813202 453 QGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN------IPTsgaeiggAFGGEKHTGGGRESGSDAWKHYM 517
Cdd:cd07093 387 YGLAAYVWTRDLGRAHRV--ARRLEAGTVWVNcwlvrdLRT-------PFGGVKASGIGREGGDYSLEFYT 448
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
66-508 |
7.99e-88 |
|
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: 278.08 E-value: 7.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 66 ITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 146 EVQEYVDICDYAVGLSRMIGGPILPSE----RPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 222 TTSLISVAVTKIIAKVlednKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGN 300
Cdd:cd07145 161 NTPLTAIELAKILEEA----GLPpGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 301 NAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSM 380
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 381 FLGAVEEAKKEGGTVVYGGKVMDrpGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIF 460
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 380813202 461 TKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 508
Cdd:cd07145 395 TNDINRALKV--ARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREG 440
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
52-517 |
1.07e-87 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 279.27 E-value: 1.07e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 52 EGVYNGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLG 129
Cdd:PLN02278 26 QGLIGGKWtdAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 130 SLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAM 209
Cdd:PLN02278 106 QLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 210 ICGNVCLWKGAPTTSLISVAVTKIiakVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQER 289
Cdd:PLN02278 186 AAGCTVVVKPSELTPLTALAAAEL---ALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 290 FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLY 369
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 370 GPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNN 449
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAN 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380813202 450 EVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN---IPTSGAeiggAFGGEKHTGGGRESGSDAWKHYM 517
Cdd:PLN02278 423 DTEAGLAAYIFTRDLQRAWRV--SEALEYGIVGVNeglISTEVA----PFGGVKQSGLGREGSKYGIDEYL 487
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
68-518 |
1.81e-87 |
|
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: 277.26 E-value: 1.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 68 TYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEV 147
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 148 QEYVDICDYAVGL-SRMIGGPI-LPSERPGHALIEqwnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSL 225
Cdd:cd07090 81 DSSADCLEYYAGLaPTLSGEHVpLPGGSFAYTRRE---PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 226 ISVavtkIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIA 305
Cdd:cd07090 158 TAL----LLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 306 FEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAV 385
Cdd:cd07090 234 FDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 386 EEAKKEGGTVVYGGKVMD-----RPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIF 460
Cdd:cd07090 314 ESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVF 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 380813202 461 TKDLGRIFRWLGP-KGSDCGIVNVNIptSGAEIggAFGGEKHTGGGRESGSDAWKHYMR 518
Cdd:cd07090 394 TRDLQRAHRVIAQlQAGTCWINTYNI--SPVEV--PFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
71-526 |
2.56e-87 |
|
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: 276.95 E-value: 2.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07107 4 PATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 151 VDICDYAVGLSRMIGGPILPSErPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAV 230
Cdd:cd07107 84 AALLDYFAGLVTELKGETIPVG-GRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 231 TKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDAD 310
Cdd:cd07107 163 AELAREVLP----PGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 311 LSLVVPSALFAA-VGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAK 389
Cdd:cd07107 239 PEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 390 KEGGTVVYGGKVMDRP----GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLG 465
Cdd:cd07107 319 REGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380813202 466 RIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAWKHYMRRSTCTINY 526
Cdd:cd07107 399 QAHR--TARRVEAGYVWIN-GSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
89-507 |
1.27e-86 |
|
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: 273.95 E-value: 1.27e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 89 EETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICD-YAVGLSRMIGGP 167
Cdd:cd07100 2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRyYAENAEAFLADE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 168 ILPSErPGHALIeQWNPVGLVGIITAFNFP---VAVYGwnnAIAMICGNVCLWKGAPTTSLISVAvtkiIAKVLEDNKLP 244
Cdd:cd07100 82 PIETD-AGKAYV-RYEPLGVVLGIMPWNFPfwqVFRFA---APNLMAGNTVLLKHASNVPGCALA----IEELFREAGFP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 245 -GAICSLTCGGADIGTAMAkDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAV 323
Cdd:cd07100 153 eGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 324 GTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMD 403
Cdd:cd07100 232 QNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 404 RPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLG---RIFRWLgpkgsDCGI 480
Cdd:cd07100 312 GPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLEraeRVARRL-----EAGM 386
|
410 420
....*....|....*....|....*...
gi 380813202 481 VNVNIPT-SGAEIggAFGGEKHTGGGRE 507
Cdd:cd07100 387 VFINGMVkSDPRL--PFGGVKRSGYGRE 412
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
66-507 |
1.78e-86 |
|
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: 274.47 E-value: 1.78e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 66 ITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 146 EVQEYVDICDYAVGLSRMIGGPILPSE-------RPGHALIEqwnPVGLVGIITAFNFPVavygwnN--------AIAmi 210
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFDaspggegRIGFTIRE---PIGVVAAITPFNFPL------NlvahkvgpAIA-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 211 CGNVCLWKGAPTTSLISVAvtkiIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQER 289
Cdd:cd07149 150 AGNAVVLKPASQTPLSALK----LAELLLEAGLPkGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 290 fgRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLY 369
Cdd:cd07149 226 --KVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 370 GPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKvmdRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNN 449
Cdd:cd07149 304 GPMISEAEAERIEEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMAN 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 380813202 450 EVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 507
Cdd:cd07149 381 DSPYGLQAGVFTNDLQKALKAA--RELEVGGVMINdSSTFRVD-HMPYGGVKESGTGRE 436
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
56-517 |
5.95e-84 |
|
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: 268.80 E-value: 5.95e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAW--KIWADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07119 3 DGEWveAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 132 VSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMIC 211
Cdd:cd07119 83 ETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVR-EPVGVCGLITPWNYPLLQAAWKLAPALAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 212 GNVCLWKGAPTTSLISVAVTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERF 290
Cdd:cd07119 162 GNTVVIKPSEVTPLTTIALFELIEEA----GLPAGVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 291 GRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYG 370
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 371 PLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFA 446
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380813202 447 WNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN---IPTSGAEiggaFGGEKHTGGGRESGSDAWKHYM 517
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVA--RRLRAGTVWINdyhPYFAEAP----WGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
56-516 |
1.08e-83 |
|
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: 268.17 E-value: 1.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07117 6 NGEWvkGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 134 LEMGKILVEGVGevqeyVDIcDYAVGLSRMIGGPILPSERPGHALIEQW------NPVGLVGIITAFNFPVAVYGWNNAI 207
Cdd:cd07117 86 LDNGKPIRETRA-----VDI-PLAADHFRYFAGVIRAEEGSANMIDEDTlsivlrEPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 208 AMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDnklpGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQ 287
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPK----GVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 288 ERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNV 367
Cdd:cd07117 236 KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 368 LYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEE 443
Cdd:cd07117 316 QMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380813202 444 VFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRESGSDAWKHY 516
Cdd:cd07117 396 VIDMANDSEYGLGGGVFTKDINRALRV--ARAVETGRVWVNtynqIPA-----GAPFGGYKKSGIGRETHKSMLDAY 465
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
71-524 |
1.19e-83 |
|
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: 267.30 E-value: 1.19e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL-VEGVGEVQE 149
Cdd:cd07108 4 PATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 150 YVDICDYAVGLSRMIGGPILPSeRPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07108 84 LADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 230 VTKIIAKVLednklPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFED 308
Cdd:cd07108 163 LAEILAQVL-----PAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 309 ADLSLVVPSALFAAVGT-AGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEE 387
Cdd:cd07108 238 ADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 388 AKKE-GGTVVYGGK----VMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTK 462
Cdd:cd07108 318 GLSTsGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380813202 463 DLGRIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAW-KHYMRRSTCTI 524
Cdd:cd07108 398 DLGRALR--AAHALEAGWVQVN-QGGGQQPGQSYGGFKQSGLGREASLEGMlEHFTQKKTVNI 457
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
69-517 |
1.42e-83 |
|
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: 267.19 E-value: 1.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 69 YCPANNEPIARVRQASVADYEETVKKAKEAWKIWA-DIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILV-EGVGE 146
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMtARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 147 VQEYVDICDYAVGLSRMIGGPI-----LPSERPGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWEFdlpvpALRGGPGRRVVRR-EPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 222 TTSLISVAVTKIIAkvlEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNN 301
Cdd:cd07089 161 DTPLSALLLGEIIA---ETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 302 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMF 381
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 382 LGAVEEAKKEGGTVVYGGKvmdRP-----GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLS 456
Cdd:cd07089 318 EGYIARGRDEGARLVTGGG---RPagldkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380813202 457 SSIFTKDLGR---IFRWLgpkgsDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAWKHYM 517
Cdd:cd07089 395 GGVWSADVDRayrVARRI-----RTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
56-524 |
2.42e-82 |
|
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: 264.46 E-value: 2.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKI--WADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07091 9 NNEFvdSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 132 VSLEMGKILVEG-VGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMI 210
Cdd:cd07091 89 ESLDNGKPLEESaKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRR-EPIGVCGQIIPWNFPLLMLAWKLAPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 211 CGNVCLWKGAPTTSLISVAVTKIIAKVLednkLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVALMV-QE 288
Cdd:cd07091 168 AGNTVVLKPAEQTPLSALYLAELIKEAG----FPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAaKS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 289 RFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVL 368
Cdd:cd07091 244 NLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 369 YGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWN 448
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 449 NEVKQGLSSSIFTKDLGRIFR----------WLgpkgsDC-GIVNVNIPtsgaeiggaFGGEKHTGGGRESGSDAWKHYM 517
Cdd:cd07091 404 NDTEYGLAAGVFTKDINKALRvsralkagtvWV-----NTyNVFDAAVP---------FGGFKQSGFGRELGEEGLEEYT 469
|
....*..
gi 380813202 518 RRSTCTI 524
Cdd:cd07091 470 QVKAVTI 476
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
69-518 |
2.45e-81 |
|
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: 261.00 E-value: 2.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 69 YCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQ 148
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 149 EYVDICDYAVGLSrmigGPILPSER-------PGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:cd07099 81 LALEAIDWAARNA----PRVLAPRKvptgllmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 222 TTSLISVAVTKIIAKVLednkLPGAICSLTCGGADIGTAMAkDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNN 301
Cdd:cd07099 157 VTPLVGELLAEAWAAAG----PPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 302 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMF 381
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 382 LGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT 461
Cdd:cd07099 312 RRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380813202 462 KDL---GRIFRWLgpkgsDCGIVNVNIPTSGAEIGGA-FGGEKHTGGGRESGSDAWKHYMR 518
Cdd:cd07099 392 RDLaraEAIARRL-----EAGAVSINDVLLTAGIPALpFGGVKDSGGGRRHGAEGLREFCR 447
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
56-518 |
4.06e-81 |
|
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: 261.27 E-value: 4.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKI--WADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07142 9 NGQFvdAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 132 VSLEMGKILVEG-VGEVQEYVDICDYAVGLSRMIGGPILPSERPGHA--LIEqwnPVGLVGIITAFNFPVAVYGWNNAIA 208
Cdd:cd07142 89 ETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVytLHE---PIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 209 MICGNVCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVA-LMV 286
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSAL----LAAKLAAEAGLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMqLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 287 QERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSN 366
Cdd:cd07142 242 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 367 VLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFA 446
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380813202 447 WNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKHYMR 518
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLS--RALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
56-469 |
3.38e-80 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 258.69 E-value: 3.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW-GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSL 134
Cdd:PRK13473 8 NGELvAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 135 EMGK-ILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGN 213
Cdd:PRK13473 88 NCGKpLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 214 VCLWKGAPTTSLISVAVTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRS 293
Cdd:PRK13473 168 TVVLKPSEITPLTALKLAELAADILP----PGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 294 LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLH 373
Cdd:PRK13473 244 HLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 374 TKQAVSMFLGAVEEAKKEG-GTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 452
Cdd:PRK13473 324 SAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSD 403
|
410
....*....|....*..
gi 380813202 453 QGLSSSIFTKDLGRIFR 469
Cdd:PRK13473 404 YGLASSVWTRDVGRAHR 420
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
71-524 |
6.28e-79 |
|
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: 254.85 E-value: 6.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKIWA-DIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQE 149
Cdd:cd07109 4 PSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 150 YVDICDYAVGLSRMIGGPILPSErPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07109 84 AARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 230 vtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFED 308
Cdd:cd07109 163 ----LAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 309 ADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDsNVLYGPLHTKQAVSMFLGAVEEA 388
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 389 KKEGGTVVYGG-KVMDRP--GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLG 465
Cdd:cd07109 318 RARGARIVAGGrIAEGAPagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 380813202 466 RIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKHYMRRSTCTI 524
Cdd:cd07109 398 RALRV--ARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
71-524 |
1.17e-78 |
|
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: 254.18 E-value: 1.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKI--WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQ 148
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 149 EYVDICDYAVGLSRMIGGPI---LPSERPGHALIEqwnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSl 225
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSynnLGDDMLGLVLRE---PIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 226 isvAVTKIIAKVLEDNKLPGAICS-LTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAII 304
Cdd:cd07118 160 ---GTTLMLAELLIEAGLPAGVVNiVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 305 AFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGA 384
Cdd:cd07118 237 VFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 385 VEEAKKEGGTVVYGGKVMD-RPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 463
Cdd:cd07118 317 VDAGRAEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380813202 464 LGRIFrwLGPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRESGSDAWKHYMRRSTCTI 524
Cdd:cd07118 397 IDTAL--TVARRIRAGTVWVNtFLDGSPEL--PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
66-507 |
1.47e-78 |
|
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: 253.71 E-value: 1.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 66 ITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 146 EVQEYVDICDYAVGLSRMIGGPILP---SER-PGH-ALIEQWnPVGLVGIITAFNFPV--AVYGWNNAIAMicGNVCLWK 218
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldiSARgEGRqGLVRRF-PIGPVSAITPFNFPLnlVAHKVAPAIAA--GCPFVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 219 GAPTTSLISVavtkIIAKVLEDNKLP-GAICSLTCGgADIGTAMAKDERVNLLSFTGSTQVGkqvaLMVQERFGRS--LL 295
Cdd:cd07147 158 PASRTPLSAL----ILGEVLAETGLPkGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVG----WDLKARAGKKkvVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 296 ELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTK 375
Cdd:cd07147 229 ELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 376 QAVSMFLGAVEEAKKEGGTVVYGGKvmdRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGL 455
Cdd:cd07147 309 SEAERVEGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGL 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 380813202 456 SSSIFTKDLGRIFR-WlgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 507
Cdd:cd07147 386 QAGVFTRDLEKALRaW---DELEVGGVVINdVPTFRVD-HMPYGGVKDSGIGRE 435
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
56-526 |
3.14e-78 |
|
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: 253.81 E-value: 3.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07559 6 NGEWvaPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 134 LEMGKILVEGVGevqeyVDIcDYAVGLSRMIGGPILPSERPGHALIEQ------WNPVGLVGIITAFNFPVAVYGWNNAI 207
Cdd:cd07559 86 LDNGKPIRETLA-----ADI-PLAIDHFRYFAGVIRAQEGSLSEIDEDtlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 208 AMICGNVCLWKGAPTTSLISVAVTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQ 287
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDLLP----KGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 288 ERFGRSLLELGGNNAIIAFEDADLSL--VVPSALFAAVGTA---GQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNP 362
Cdd:cd07559 236 ENLIPVTLELGGKSPNIFFDDAMDADddFDDKAEEGQLGFAfnqGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 363 WDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLAHDASIAHTETFAPILYVFKF 438
Cdd:cd07559 316 LDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 439 KNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRESGSDAWK 514
Cdd:cd07559 396 KDEEEAIAIANDTEYGLGGGVWTRDINRALRV--ARGIQTGRVWVNcyhqYPA-----HAPFGGYKKSGIGRETHKMMLD 468
|
490
....*....|..
gi 380813202 515 HYMRRSTCTINY 526
Cdd:cd07559 469 HYQQTKNILVSY 480
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
68-512 |
1.54e-77 |
|
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: 251.49 E-value: 1.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 68 TYCPANNEPIARVRQASVADYEETVKKAKEAWK--IWADIPApKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 146 EVQEYVDICDYAVGLSRMIGGPILPSErPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSL 225
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPE-PGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 226 ISVAVTKIIAKVLEdnkLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAII 304
Cdd:cd07120 159 INAAIIRILAEIPS---LPaGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 305 AFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGA 384
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 385 VEEAKKEGGTVVY-GGKVMDR--PGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT 461
Cdd:cd07120 316 VERAIAAGAEVVLrGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 380813202 462 KDLGRIFRWlgPKGSDCGIVNVNipTSGAEIGGA-FGGEKHTGGGRESGSDA 512
Cdd:cd07120 396 RDLARAMRV--ARAIRAGTVWIN--DWNKLFAEAeEGGYRQSGLGRLHGVAA 443
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
63-518 |
5.77e-77 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 250.95 E-value: 5.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVE 142
Cdd:PRK13252 21 GETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 143 G-VGEVQEYVDICDYAVGLSRMIGGPILPSeRPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:PRK13252 101 TsVVDIVTGADVLEYYAGLAPALEGEQIPL-RGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 222 TTSLISVAvtkiIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNN 301
Cdd:PRK13252 180 VTPLTALK----LAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 302 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMF 381
Cdd:PRK13252 256 PLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 382 LGAVEEAKKEGGTVVYGGKVMDR----PGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSS 457
Cdd:PRK13252 336 LGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAA 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380813202 458 SIFTKDLGRIFRWLGpkGSDCGIVNVNipTSG---AEIggAFGGEKHTGGGRESGSDAWKHYMR 518
Cdd:PRK13252 416 GVFTADLSRAHRVIH--QLEAGICWIN--TWGespAEM--PVGGYKQSGIGRENGIATLEHYTQ 473
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
56-525 |
9.70e-77 |
|
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: 249.80 E-value: 9.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW-GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWA-DIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07082 7 NGEWkESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWpTMPLEERIDCLHKFADLLKENKEEVANLLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 134 LEMGKILVEGVGEVQEYVDICDYAV-GLSRMIGGPILPSERPGH----ALIEQwNPVGLVGIITAFNFPVavygwNNAI- 207
Cdd:cd07082 87 WEIGKTLKDALKEVDRTIDYIRDTIeELKRLDGDSLPGDWFPGTkgkiAQVRR-EPLGVVLAIGPFNYPL-----NLTVs 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 208 ----AMICGNVCLWKGAPTTSLISVavtkIIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQv 282
Cdd:cd07082 161 klipALIMGNTVVFKPATQGVLLGI----PLAEAFHDAGFPkGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNR- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 283 aLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNP 362
Cdd:cd07082 236 -LKKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 363 WDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKvmDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEE 442
Cdd:cd07082 315 WDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 443 EVFAWNNEVKQGLSSSIFTKDLGRIF---RWLgpkgsDCGIVNVNIPTS-GAEIgGAFGGEKHTGGGRESGSDAWKHYMR 518
Cdd:cd07082 393 EAIELANKSNYGLQASIFTKDINKARklaDAL-----EVGTVNINSKCQrGPDH-FPFLGRKDSGIGTQGIGDALRSMTR 466
|
....*..
gi 380813202 519 RSTCTIN 525
Cdd:cd07082 467 RKGIVIN 473
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
66-507 |
1.71e-76 |
|
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: 248.50 E-value: 1.71e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 66 ITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 146 EVQEYVDICDYAVGLSRMIGGPILPSE----RPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 222 TTSLISVAVTKIIakvLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKqvALMVQERFGRSLLELGGNN 301
Cdd:cd07094 161 KTPLSALELAKIL---VEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGE--ALRANAGGKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 302 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMF 381
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 382 LGAVEEAKKEGGTVVYGGKvmdRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT 461
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 380813202 462 KDLGRIFRwlGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRE 507
Cdd:cd07094 393 RDLNVAFK--AAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGRE 436
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
63-526 |
1.99e-76 |
|
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: 249.33 E-value: 1.99e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKI--WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:cd07140 20 GKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 141 VEGVG-EVQEYVDICDYAVGLSRMIGGPILP--SERPGHAL-IEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCL 216
Cdd:cd07140 100 TLALKtHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 217 WKGAPTTSLISVAVTKIIAKVledNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQE-RFGRSLL 295
Cdd:cd07140 180 LKPAQVTPLTALKFAELTVKA---GFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVsNLKKVSL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 296 ELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTK 375
Cdd:cd07140 257 ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 376 QAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNE--EEVFAWNNEVKQ 453
Cdd:cd07140 337 AHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEY 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380813202 454 GLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKHYMRRSTCTINY 526
Cdd:cd07140 417 GLASGVFTKDINKALYV--SDKLEAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIEY 486
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
71-524 |
4.16e-76 |
|
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: 247.27 E-value: 4.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRqasvADYEETVKKAKE-AWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQE 149
Cdd:cd07146 6 PYTGEVVGTVP----AGTEEALREALAlAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 150 YVDICDYAVGLSRMIGGPILPSERPGHA----LIEQWNPVGLVGIITAFNFPVavygwNNAIAMIC-----GNVCLWKGA 220
Cdd:cd07146 82 AADVLRFAAAEALRDDGESFSCDLTANGkarkIFTLREPLGVVLAITPFNHPL-----NQVAHKIApaiaaNNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 221 PTTSLISVAvtkiIAKVLEDNKLPGAICSLTCGG-ADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERfgRSLLELGG 299
Cdd:cd07146 157 EKTPLSAIY----LADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--RQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 300 NNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVS 379
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 380 MFLGAVEEAKKEGGTVVYGGKvmdRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSI 459
Cdd:cd07146 311 QIENRVEEAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380813202 460 FTKDLGRIFRWLgpKGSDCGIVNVN------IPTSgaeiggAFGGEKHTG-GGRESGSDAWKHYMRRSTCTI 524
Cdd:cd07146 388 CTNDLDTIKRLV--ERLDVGTVNVNevpgfrSELS------PFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
56-507 |
9.66e-76 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 247.51 E-value: 9.66e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:PRK11241 16 NGEWldANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 134 LEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGN 213
Cdd:PRK11241 96 LEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 214 VCLWKGAPTTSLISVAvtkiIAKVLEDNKLPGAICSLTCGGA-DIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGR 292
Cdd:PRK11241 176 TMVLKPASQTPFSALA----LAELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 293 SLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPL 372
Cdd:PRK11241 252 VSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 373 HTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 452
Cdd:PRK11241 332 IDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTE 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 380813202 453 QGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIgGAFGGEKHTGGGRE 507
Cdd:PRK11241 412 FGLAAYFYARDLSRVFRV--GEALEYGIVGINTGIISNEV-APFGGIKASGLGRE 463
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
56-517 |
1.20e-75 |
|
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: 246.72 E-value: 1.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAW--KIWADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07139 4 GGRWvaPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 132 VSLEMGK-ILVEGVGEVQEYVDICDYAVGLSRmigGPILPSERP----GHALIEQwNPVGLVGIITAFNFPVAVYGWNNA 206
Cdd:cd07139 84 WTAENGMpISWSRRAQGPGPAALLRYYAALAR---DFPFEERRPgsggGHVLVRR-EPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 207 IAMICGNVCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMV 286
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAY----LLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 287 QERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSN 366
Cdd:cd07139 236 GERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 367 VLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKvmdRP-----GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNE 441
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGG---RPagldrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380813202 442 EEVFAWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVNIPTSgaEIGGAFGGEKHTGGGRESGSDAWKHYM 517
Cdd:cd07139 393 DDAVRIANDSDYGLSGSVWTADVERglaVARRI-----RTGTVGVNGFRL--DFGAPFGGFKQSGIGREGGPEGLDAYL 464
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
63-524 |
5.89e-75 |
|
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: 245.34 E-value: 5.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKI---WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGK- 138
Cdd:cd07141 21 GKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 139 ILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWK 218
Cdd:cd07141 101 FSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRH-EPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 219 GAPTTSLISVAVTKIIAkvlEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKqvalMVQERFGRS----- 293
Cdd:cd07141 180 PAEQTPLTALYLASLIK---EAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGK----LIQQAAGKSnlkrv 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 294 LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLH 373
Cdd:cd07141 253 TLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 374 TKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQ 453
Cdd:cd07141 333 DEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTY 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380813202 454 GLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAeIGGAFGGEKHTGGGRESGSDAWKHYMRRSTCTI 524
Cdd:cd07141 413 GLAAAVFTKDIDKAITF--SNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
71-509 |
1.93e-74 |
|
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: 243.41 E-value: 1.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 151 VDICDYAVGLS---RMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLIS 227
Cdd:cd07110 84 AGCFEYYADLAeqlDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 228 VAVTKIIAKVlednKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAF 306
Cdd:cd07110 164 LELAEIAAEA----GLPpGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 307 EDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVE 386
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 387 EAKKEGGTVVYGGKVMD--RPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 464
Cdd:cd07110 320 RGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 380813202 465 GRIFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRESG 509
Cdd:cd07110 400 ERCDRV--AEALEAGIVWINCSQP-CFPQAPWGGYKRSGIGRELG 441
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
77-517 |
5.38e-74 |
|
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: 241.81 E-value: 5.38e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 77 IARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDY 156
Cdd:cd07152 4 LGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 157 AVGLSRMIGGPILPSErPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTslisvAVTK--II 234
Cdd:cd07152 84 AAGLPTQPQGEILPSA-PGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRT-----PVSGgvVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 235 AKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVAlmvqERFGRSL----LELGGNNAIIAFEDAD 310
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVG----EAAGRHLkkvsLELGGKNALIVLDDAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 311 LSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKK 390
Cdd:cd07152 234 LDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 391 EGGTVVYGGKvmdRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRw 470
Cdd:cd07152 314 AGARLEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA- 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 380813202 471 LGPKgSDCGIVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSDAWKHYM 517
Cdd:cd07152 390 LADR-LRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFT 436
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
71-526 |
1.09e-73 |
|
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: 241.96 E-value: 1.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKI-WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGK-ILVEGVGEVQ 148
Cdd:cd07113 22 PATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKsIHLSRAFEVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 149 EYVDICDYAVGLSRMIGG----PILPS---ERpgHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:cd07113 102 QSANFLRYFAGWATKINGetlaPSIPSmqgER--YTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 222 TTSLISVAvtkiIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNN 301
Cdd:cd07113 180 FTPLTLLR----VAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 302 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMF 381
Cdd:cd07113 256 AAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 382 LGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT 461
Cdd:cd07113 336 CSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWT 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380813202 462 KDLGRIFRWLgPKgSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRESGSDAWKHYMRRSTCTINY 526
Cdd:cd07113 416 NNLSKALRYI-PR-IEAGTVWVNMHTF-LDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY 477
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
35-525 |
4.52e-72 |
|
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: 237.69 E-value: 4.52e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 35 NQPqyawlkeLGLREENEGVYNGSwggrGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWK-IWADIPAPKRGEI 113
Cdd:cd07144 5 DQP-------TGLFINNEFVKSSD----GETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFEsWWSKVTGEERGEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 114 VRQIGDALREKIQVLGSLVSLEMGKIL-VEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQwNPVGLVGIIT 192
Cdd:cd07144 74 LDKLADLVEKNRDLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLH-EPYGVCGQII 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 193 AFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLiSVAVtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLS 271
Cdd:cd07144 153 PWNYPLAMAAWKLAPALAAGNTVVIKPAENTPL-SLLY---FANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 272 FTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLK 351
Cdd:cd07144 229 FTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 352 KAYAQI-RVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGG---KVMDRPGNYVEPTIVTGLAHDASIAHTE 427
Cdd:cd07144 309 EHVKQNyKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 428 TFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRE 507
Cdd:cd07144 389 IFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVA--RELEAGMVWIN-SSNDSDVGVPFGGFKMSGIGRE 465
|
490
....*....|....*...
gi 380813202 508 SGSDAWKHYMRRSTCTIN 525
Cdd:cd07144 466 LGEYGLETYTQTKAVHIN 483
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
56-486 |
1.80e-70 |
|
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: 233.56 E-value: 1.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07085 6 NGEWveSKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLIT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 134 LEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGN 213
Cdd:cd07085 86 LEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 214 VCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvalmVQER---F 290
Cdd:cd07085 166 TFVLKPSERVPGAAM----RLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEY----IYERaaaN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 291 GRSLLELGG-NNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLY 369
Cdd:cd07085 238 GKRVQALGGaKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 370 GPLHTKQAVSMFLGAVEEAKKEGGTVVYGG---KVMDRP-GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVF 445
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVLDGrgvKVPGYEnGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 380813202 446 AWNNEVKQGLSSSIFTKD--LGRIFRwlgpKGSDCGIVNVNIP 486
Cdd:cd07085 398 AIINANPYGNGAAIFTRSgaAARKFQ----REVDAGMVGINVP 436
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
70-517 |
8.46e-69 |
|
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: 228.35 E-value: 8.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 70 CPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKilvegvGEVQE 149
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGK------ARRHA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 150 YVDICDYAVGlSRMIG---GPILPSERPGHAL------IEQWNPVGLVGIITAFNFPVAVyGWNNAI-AMICGNVCLWKG 219
Cdd:cd07101 76 FEEVLDVAIV-ARYYArraERLLKPRRRRGAIpvltrtTVNRRPKGVVGVISPWNYPLTL-AVSDAIpALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 220 APTTSLISVAVTKIiakvLEDNKLPGAICSLTCG-GADIGTAMAkdERVNLLSFTGSTQVGKQVAlmvqERFGRSL---- 294
Cdd:cd07101 154 DSQTALTALWAVEL----LIEAGLPRDLWQVVTGpGSEVGGAIV--DNADYVMFTGSTATGRVVA----ERAGRRLigcs 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 295 LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHT 374
Cdd:cd07101 224 LELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLIS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 375 KQAVSMFLGAVEEAKKEGGTVVYGGKVmdRP--GNYV-EPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEV 451
Cdd:cd07101 304 QAQLDRVTAHVDDAVAKGATVLAGGRA--RPdlGPYFyEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDT 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380813202 452 KQGLSSSIFTKDLGRIfRWLGPKgSDCGIVNVN--IPTSGAEIGGAFGGEKHTGGGRESGSDAWKHYM 517
Cdd:cd07101 382 DYGLNASVWTRDGARG-RRIAAR-LRAGTVNVNegYAAAWASIDAPMGGMKDSGLGRRHGAEGLLKYT 447
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
63-517 |
1.56e-68 |
|
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: 227.87 E-value: 1.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWK--IWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 141 VEGV-GEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKG 219
Cdd:cd07112 81 SDALaVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITR-EPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 220 APTTSLisvavTKI-IAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQvaLMvqERFGRS---- 293
Cdd:cd07112 160 AEQSPL-----TALrLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRR--FL--EYSGQSnlkr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 294 -LLELGGNNAIIAFEDA-DLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGP 371
Cdd:cd07112 231 vWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 372 LHTKQAVSMFLGAVEEAKKEGGTVVYGGKV--MDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNN 449
Cdd:cd07112 311 LVSEAHFDKVLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALAN 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380813202 450 EVKQGLSSSIFTKDLGRIFRwlGPKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKHYM 517
Cdd:cd07112 391 DSVYGLAASVWTSDLSRAHR--VARRLRAGTVWVNC-FDEGDITTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
49-525 |
2.52e-68 |
|
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: 227.80 E-value: 2.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 49 EENEGVY-NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKI-WA-DIPAPKRGEIVRQIGDALRE 123
Cdd:cd07143 4 EQPTGLFiNGEFvdSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGlKVSGSKRGRCLSKLADLMER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 124 KIQVLGSLVSLEMGK-ILVEGVGEVQEYVDICDYAVGLSRMIGGPILP--SERPGHALIEqwnPVGLVGIITAFNFPVAV 200
Cdd:cd07143 84 NLDYLASIEALDNGKtFGTAKRVDVQASADTFRYYGGWADKIHGQVIEtdIKKLTYTRHE---PIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 201 YGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAkvlEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGK 280
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIP---EAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 281 qvalMVQERFGRS-----LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYA 355
Cdd:cd07143 238 ----KVMEAAAKSnlkkvTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 356 QIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYV 435
Cdd:cd07143 314 KLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 436 FKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGP-KGSDCGIVNVNIPTSGAeiggAFGGEKHTGGGRESGSDAWK 514
Cdd:cd07143 394 IKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANAlKAGTVWVNCYNLLHHQV----PFGGYKQSGIGRELGEYALE 469
|
490
....*....|.
gi 380813202 515 HYMRRSTCTIN 525
Cdd:cd07143 470 NYTQIKAVHIN 480
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
56-517 |
4.28e-67 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 225.38 E-value: 4.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW-----GGRGEVITtycPANNEPIARVRQASVADYEETVKKAKEAW-----KIWADIPAPKRGEIVRQIGDALREKI 125
Cdd:PLN02467 13 GGEWrepvlGKRIPVVN---PATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 126 QVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGG----PI-LPSER-PGHALieqWNPVGLVGIITAFNFPVA 199
Cdd:PLN02467 90 SELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkqkaPVsLPMETfKGYVL---KEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 200 VYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVlednKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQV 278
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREV----GLPpGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 279 GKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIR 358
Cdd:PLN02467 243 GRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 359 VGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKvmdRP-----GNYVEPTIVTGLAHDASIAHTETFAPIL 433
Cdd:PLN02467 323 ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGK---RPehlkkGFFIEPTIITDVTTSMQIWREEVFGPVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 434 YVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN--------IPtsgaeiggaFGGEKHTGGG 505
Cdd:PLN02467 400 CVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERV--SEAFQAGIVWINcsqpcfcqAP---------WGGIKRSGFG 468
|
490
....*....|..
gi 380813202 506 RESGSDAWKHYM 517
Cdd:PLN02467 469 RELGEWGLENYL 480
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
60-511 |
5.97e-66 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 222.83 E-value: 5.97e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 60 GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKI 139
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 140 LVEGVGEVQEYVDICDYavgLSRMIGGPILPSERPGhAL------IEQWNPVGLVGIITAFNFPVAVyGWNNAI-AMICG 212
Cdd:PRK09407 108 RRHAFEEVLDVALTARY---YARRAPKLLAPRRRAG-ALpvltktTELRQPKGVVGVISPWNYPLTL-AVSDAIpALLAG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 213 NVCLWKGAPTTSLISVAVtkiiAKVLEDNKLPGAICSLTCG-GADIGTAMAkdERVNLLSFTGSTQVGKQVAlmvqERFG 291
Cdd:PRK09407 183 NAVVLKPDSQTPLTALAA----VELLYEAGLPRDLWQVVTGpGPVVGTALV--DNADYLMFTGSTATGRVLA----EQAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 292 RSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNV 367
Cdd:PRK09407 253 RRLigfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 368 LYGPLHTKQ---AVSMFlgaVEEAKKEGGTVVYGGKVmdRP--GNYV-EPTIVTGLAHDASIAHTETFAPILYVFKFKNE 441
Cdd:PRK09407 333 DMGSLISEAqleTVSAH---VDDAVAKGATVLAGGKA--RPdlGPLFyEPTVLTGVTPDMELAREETFGPVVSVYPVADV 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380813202 442 EEVFAWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVN---IPTSGAeIGGAFGGEKHTGGGRESGSD 511
Cdd:PRK09407 408 DEAVERANDTPYGLNASVWTGDTARgraIAARI-----RAGTVNVNegyAAAWGS-VDAPMGGMKDSGLGRRHGAE 477
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
56-509 |
3.70e-65 |
|
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: 218.91 E-value: 3.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW-----GGRGEVIttyCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGS 130
Cdd:cd07138 4 DGAWvapagTETIDVI---NPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 131 LVSLEMG-------KILVE-GVGEVQEYVDIC-DYAVglsrmiggpilpSERPGHALIeQWNPVGLVGIITAFNFPVavy 201
Cdd:cd07138 81 AITLEMGapitlarAAQVGlGIGHLRAAADALkDFEF------------EERRGNSLV-VREPIGVCGLITPWNWPL--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 202 gwnNAI------AMICGNVCLWKG---APTTSLIsvavtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLS 271
Cdd:cd07138 145 ---NQIvlkvapALAAGCTVVLKPsevAPLSAII-------LAEILDEAGLPAGVFNLVNGdGPVVGEALSAHPDVDMVS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 272 FTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLK 351
Cdd:cd07138 215 FTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 352 KAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGkvMDRP-----GNYVEPTIVTGLAHDASIAHT 426
Cdd:cd07138 295 AAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG--PGRPeglerGYFVKPTVFADVTPDMTIARE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 427 ETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVNipTSGAEIGGAFGGEKHTG 503
Cdd:cd07138 373 EIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERaraVARRL-----RAGQVHIN--GAAFNPGAPFGGYKQSG 445
|
....*.
gi 380813202 504 GGRESG 509
Cdd:cd07138 446 NGREWG 451
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
115-469 |
1.08e-64 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 216.14 E-value: 1.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 115 RQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAF 194
Cdd:PRK10090 2 RKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 195 NFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVNLLSFT 273
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI----GLPKGVFNLVLGrGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 274 GSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKA 353
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 354 YAQIRVGNPWD-SNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPI 432
Cdd:PRK10090 238 MQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 380813202 433 LYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 469
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMK 354
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
54-519 |
4.61e-64 |
|
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: 217.06 E-value: 4.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 54 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 133 SLEMGKILVEGVGEVQEYVDICDY-AVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMIC 211
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYyARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 212 GNVCLWKGAPTTSLISVAVTKIIAkvlEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQER-- 289
Cdd:cd07083 182 GNTVIAKPAEDAVVVGYKVFEIFH---EAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLap 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 290 ----FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDS 365
Cdd:cd07083 259 gqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 366 NVLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEE--E 443
Cdd:cd07083 339 GTDLGPVIDAEQEAKVLSYIEHGKNE-GQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaE 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380813202 444 VFAWNNEVKQGLSSSIFTKDLGRIfRWLGPKgSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdawKHYMRR 519
Cdd:cd07083 418 ALEVANSTPYGLTGGVYSRKREHL-EEARRE-FHVGNLYINRKITGALVGvQPFGGFKLSGTNAKTGG---PHYLRR 489
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
28-525 |
1.80e-63 |
|
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: 215.91 E-value: 1.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 28 FMSTLLINQPQYAWLKE-LGLREENEG----VYNGSWGGRGEVITTYCPANNE-PIARVRQASVADYEETVKKAKEAWKI 101
Cdd:cd07125 5 FVNRIFDLEVPLEALADaLKAFDEKEWeaipIINGEETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 102 WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICD-YAVGLSRMIGGPILPS---ERPGHa 177
Cdd:cd07125 85 WSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRyYAAQARELFSDPELPGptgELNGL- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 178 lieQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIiakvLEDNKLPGAICSLT-CGGAD 256
Cdd:cd07125 164 ---ELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVEL----LHEAGVPRDVLQLVpGDGEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 257 IGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLL---ELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTA 333
Cdd:cd07125 237 IGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPILPliaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 334 RRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRPGNYVEPTI 413
Cdd:cd07125 317 RLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 414 VTGlahDASIAH-TETFAPILYVFKFKNE--EEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGA 490
Cdd:cd07125 396 IEI---VGIFDLtTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWR--ERVEAGNLYINRNITGA 470
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 380813202 491 eIGGA--FGGEKHTGGGRESGSdawKHYMRR----STCTIN 525
Cdd:cd07125 471 -IVGRqpFGGWGLSGTGPKAGG---PNYLLRfgneKTVSLN 507
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
63-518 |
3.73e-63 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 214.68 E-value: 3.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWK--IWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:PLN02766 35 GKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 141 VEGvgevqEYVDI------CDYAVGLSRMIGGPILPSERP--GHALIEqwnPVGLVGIITAFNFPVAVYGWNNAIAMICG 212
Cdd:PLN02766 115 ALG-----KAVDIpaaaglLRYYAGAADKIHGETLKMSRQlqGYTLKE---PIGVVGHIIPWNFPSTMFFMKVAPALAAG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 213 NVCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKqvalMVQERFG 291
Cdd:PLN02766 187 CTMVVKPAEQTPLSAL----FYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGR----KIMQAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 292 RS-----LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSN 366
Cdd:PLN02766 259 TSnlkqvSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 367 VLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFA 446
Cdd:PLN02766 339 ARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIK 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380813202 447 WNNEVKQGLSSSIFTKDL---GRIFRWLgpkgsDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKHYMR 518
Cdd:PLN02766 419 KANNTKYGLAAGIVTKDLdvaNTVSRSI-----RAGTIWVNC-YFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
37-520 |
9.39e-63 |
|
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: 213.03 E-value: 9.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 37 PQYAWLKELGLREeneGVY-NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEI 113
Cdd:cd07111 10 CALAWLDAHDRSF---GHFiNGKWvkPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 114 VRQIGDALREKIQVLGSLVSLEMGKilveGVGEVQEyVDICDYAVGLSRMIG-GPILPSERPGhalieqWNPVGLVGIIT 192
Cdd:cd07111 87 LYRIARHIQKHQRLFAVLESLDNGK----PIRESRD-CDIPLVARHFYHHAGwAQLLDTELAG------WKPVGVVGQIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 193 AFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVlednKLPGAICSLTCGGADIGTAMAKDERVNLLSF 272
Cdd:cd07111 156 PWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEA----GLPPGVLNIVTGNGSFGSALANHPGVDKVAF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 273 TGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKK 352
Cdd:cd07111 232 TGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 353 AYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPI 432
Cdd:cd07111 312 RMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 433 LYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRwLGPkGSDCGIVNVNI-----PTSGaeiggaFGGEKHTGGGRE 507
Cdd:cd07111 392 LVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALE-VAL-SLKAGVVWINGhnlfdAAAG------FGGYRESGFGRE 463
|
490
....*....|...
gi 380813202 508 SGSDAWKHYMRRS 520
Cdd:cd07111 464 GGKEGLYEYLRPS 476
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
71-466 |
2.12e-61 |
|
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: 208.64 E-value: 2.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 151 VDICDYAVGLSRMIGGPILPSERPG-HALIEQwNPVGLVGIITAFNFP--VAVygwnNAI--AMICGNVCLWKGAPTTSL 225
Cdd:cd07102 83 LERARYMISIAEEALADIRVPEKDGfERYIRR-EPLGVVLIIAPWNYPylTAV----NAVipALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 226 ISVAvtkiIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIA 305
Cdd:cd07102 158 CGER----FAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 306 FEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAV 385
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 386 EEAKKEGGTVVYGGK---VMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTK 462
Cdd:cd07102 314 ADAIAKGARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
....
gi 380813202 463 DLGR 466
Cdd:cd07102 394 DIAR 397
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
87-512 |
5.71e-61 |
|
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: 207.04 E-value: 5.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 87 DYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMG------KILVEGVGEVqeyvdICDYAVGL 160
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGataawaGFNVDLAAGM-----LREAASLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 161 SRMIGGPIlPSERPGH-ALIEQwNPVGLVGIITAFNFPVAVYGwnNAIAM--ICGNVCLWKG---APTTSLIsvavtkiI 234
Cdd:cd07105 76 TQIIGGSI-PSDKPGTlAMVVK-EPVGVVLGIAPWNAPVILGT--RAIAYplAAGNTVVLKAselSPRTHWL-------I 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 235 AKVLEDNKLP-GAICSLTCGGAD---IGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDAD 310
Cdd:cd07105 145 GRVFHEAGLPkGVLNVVTHSPEDapeVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDAD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 311 LSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIrvgnPWDSNVLyGPLHTKQAVSMFLGAVEEAKK 390
Cdd:cd07105 225 LDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKL----FAGPVVL-GSLVSAAAADRVKELVDDALS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 391 EGGTVVYGGKVMDRP-GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 469
Cdd:cd07105 300 KGAKLVVGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALA 379
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 380813202 470 wLGpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDA 512
Cdd:cd07105 380 -VA-KRIESGAVHINGMTVHDEPTLPHGGVKSSGYGRFNGKWG 420
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
54-469 |
3.03e-60 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 207.09 E-value: 3.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 54 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:PRK03137 40 IIGGERITTEDKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 133 SLEMGKILVEGVGEVQEYVDICDY----AVGLSRmiGGPILPseRPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIA 208
Cdd:PRK03137 120 VKEAGKPWAEADADTAEAIDFLEYyarqMLKLAD--GKPVES--RPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 209 MICGNVCLWKGAPTTSLISVAVtkiiAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVG---KQVAL 284
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKF----VEVLEEAGLPaGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlriYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 285 MVQE---RFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGN 361
Cdd:PRK03137 272 KVQPgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 362 PWDSNVLyGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNE 441
Cdd:PRK03137 352 PEDNAYM-GPVINQASFDKIMSYIEIGKEE-GRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420
....*....|....*....|....*...
gi 380813202 442 EEVFAWNNEVKQGLSSSIFTKDLGRIFR 469
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEK 457
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
87-512 |
1.14e-59 |
|
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: 203.66 E-value: 1.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 87 DYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGG 166
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 167 PiLPSERPGHALIEQWNPVGLVGIITAFNFPVAVYgwNNAI--AMICGNVCLWKGAPTTSlisvAVTKIIAKVLEDNKLP 244
Cdd:cd07095 81 E-RATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLP--NGHIvpALLAGNTVVFKPSELTP----AVAELMVELWEEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 245 GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSL-LELGGNNAIIAFEDADLSLVVPSALFAAV 323
Cdd:cd07095 154 PGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 324 GTAGQRCTTARRLFVHES-IHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVM 402
Cdd:cd07095 234 LTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 403 DRPGNYVEPTI--VTGLahdASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDlGRIFRWLGPKgSDCGI 480
Cdd:cd07095 314 VAGTAFLSPGIidVTDA---ADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDD-EALFERFLAR-IRAGI 388
|
410 420 430
....*....|....*....|....*....|..
gi 380813202 481 VNVNIPTSGAEIGGAFGGEKHTGGGRESGSDA 512
Cdd:cd07095 389 VNWNRPTTGASSTAPFGGVGLSGNHRPSAYYA 420
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
63-518 |
1.89e-59 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 205.81 E-value: 1.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWK--IWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:PLN02466 72 GKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 141 VEGVG-EVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKG 219
Cdd:PLN02466 152 EQSAKaELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLH-EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 220 APTTSLISVAVtkiiAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKqvalMVQERFGRS----- 293
Cdd:PLN02466 231 AEQTPLSALYA----AKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGK----IVLELAAKSnlkpv 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 294 LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLH 373
Cdd:PLN02466 303 TLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQI 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 374 TKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQ 453
Cdd:PLN02466 383 DSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRY 462
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380813202 454 GLSSSIFTKDL---GRIFRWLgpkgsDCGIVNVN--------IPtsgaeiggaFGGEKHTGGGRESGSDAWKHYMR 518
Cdd:PLN02466 463 GLAAGVFTQNLdtaNTLSRAL-----RVGTVWVNcfdvfdaaIP---------FGGYKMSGIGREKGIYSLNNYLQ 524
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
69-509 |
8.76e-55 |
|
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: 191.36 E-value: 8.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 69 YCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGV-GEV 147
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 148 qeyVDICDYAVGLSRMIGGPILPSERPGHALIE------QWNPVGLVGIITAFNFPvavygWNNAI-----AMICGNVCL 216
Cdd:cd07098 81 ---LVTCEKIRWTLKHGEKALRPESRPGGLLMFykrarvEYEPLGVVGAIVSWNYP-----FHNLLgpiiaALFAGNAIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 217 WKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLE 296
Cdd:cd07098 153 VKVSEQVAWSSGFFLSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 297 LGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQ 376
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 377 AVSMFLGAVEEAKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 452
Cdd:cd07098 313 RFDRLEELVADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380813202 453 QGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNiptsgaEIGGA-------FGGEKHTGGGRESG 509
Cdd:cd07098 393 YGLGASVFGKDIKRARRIA--SQLETGMVAIN------DFGVNyyvqqlpFGGVKGSGFGRFAG 448
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
71-507 |
5.70e-51 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 181.21 E-value: 5.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:PRK13968 14 PATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 151 VDICD-YAVGlsrmigGPILPSERP-----GHALIEqWNPVGLVGIITAFNFPVavygWN---NAIAMI-CGNVCLWKGA 220
Cdd:PRK13968 94 ANLCDwYAEH------GPAMLKAEPtlvenQQAVIE-YRPLGTILAIMPWNFPL----WQvmrGAVPILlAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 221 PTTslisVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGN 300
Cdd:PRK13968 163 PNV----MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 301 NAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSM 380
Cdd:PRK13968 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 381 FLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIF 460
Cdd:PRK13968 319 LHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 380813202 461 TKDLGRIFRWlgPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRE 507
Cdd:PRK13968 399 TTDETQARQM--AARLECGGVFINgYCASDARV--AFGGVKKSGFGRE 442
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
60-523 |
5.98e-51 |
|
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: 181.62 E-value: 5.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 60 GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKI 139
Cdd:TIGR01722 12 GASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 140 LVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKG 219
Cdd:TIGR01722 92 HSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 220 APTTSLISVAVtkiiAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGG 299
Cdd:TIGR01722 172 SEKVPSAAVKL----AELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 300 NNAIIAFEDADLSLVVPSALFAAVGTAGQRCtTARRLFVHESIHDEVVNRLKKAYAQIRVGnPW-DSNVLYGPLHTKQAV 378
Cdd:TIGR01722 248 KNHMVVMPDADKDAAADALVGAAYGAAGQRC-MAISAAVLVGAADEWVPEIRERAEKIRIG-PGdDPGAEMGPLITPQAK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 379 SMFLGAVEEAKKEGGTVVYGG---KVMDRP-GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQG 454
Cdd:TIGR01722 326 DRVASLIAGGAAEGAEVLLDGrgyKVDGYEeGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYG 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380813202 455 LSSSIFTKDLG--RIFRWLgpkgSDCGIVNVNIPTSGAEIGGAFGGEKHT--GGGRESGSDAWKHYMRRSTCT 523
Cdd:TIGR01722 406 NGTAIFTRDGAaaRRFQHE----IEVGQVGVNVPIPVPLPYFSFTGWKDSffGDHHIYGKQGTHFYTRGKTVT 474
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
56-526 |
4.27e-47 |
|
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: 171.10 E-value: 4.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSWGG--RGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07116 6 GGEWVApvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 134 LEMGKILVEGVG-EVQEYVDICDYAVGLSRMIGGPI--LPSERPGHALIEqwnPVGLVGIITAFNFPVAVYGWNNAIAMI 210
Cdd:cd07116 86 WDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSIseIDENTVAYHFHE---PLGVVGQIIPWNFPLLMATWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 211 CGNVCLWKGAPTTSLISVAVTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERF 290
Cdd:cd07116 163 AGNCVVLKPAEQTPASILVLMELIGDLLP----PGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 291 GRSLLELGGNNAIIAFED---ADLSLVVPS----ALFAAvgTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPW 363
Cdd:cd07116 239 IPVTLELGGKSPNIFFADvmdADDAFFDKAlegfVMFAL--NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 364 DSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGN-----YVEPTIVTGlaHDASIAHTETFAPILYVFKF 438
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggyYVPTTFKGG--NKMRIFQEEIFGPVLAVTTF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 439 KNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRESGSDAWK 514
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRM--GRGIQAGRVWTNcyhlYPA-----HAAFGGYKQSGIGRENHKMMLD 467
|
490
....*....|..
gi 380813202 515 HYMRRSTCTINY 526
Cdd:cd07116 468 HYQQTKNLLVSY 479
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
56-521 |
1.61e-46 |
|
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: 169.71 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSWGGRGEVITTYCPANNEPI-ARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSL 134
Cdd:TIGR01238 43 GHSYKADGEAQPVTNPADRRDIvGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 135 EMGKILVEGVGEVQEYVDICDYAVGLSRmiggPILPSERPghalieqwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNV 214
Cdd:TIGR01238 123 EAGKTIHNAIAEVREAVDFCRYYAKQVR----DVLGEFSV--------ESRGVFVCISPWNFPLAIFTGQISAALAAGNT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 215 CLWKGAPTTSLISvavTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERF---G 291
Cdd:TIGR01238 191 VIAKPAEQTSLIA---YRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdapV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGP 371
Cdd:TIGR01238 268 PLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 372 LHTKQAVSMFLGAVEEAKKEGGTV---VYGGKVMDRPGNYVEPTIVTglAHDASIAHTETFAPILYVFKFKNEE--EVFA 446
Cdd:TIGR01238 348 VIDAEAKQNLLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAREldQIVD 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380813202 447 WNNEVKQGLSSSIFTKDLGRIfRWLgPKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdawKHYMRRST 521
Cdd:TIGR01238 426 QINQTGYGLTMGVHSRIETTY-RWI-EKHARVGNCYVNRNQVGAVVGvQPFGGQGLSGTGPKAGG---PHYLYRLT 496
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
66-507 |
4.06e-46 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 167.61 E-value: 4.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 66 ITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 146 EVQEYVDICDY-----------------AVGLSRmiggpilpserpghALIeQWNPVGLVGIITAFNFPVavygWN---- 204
Cdd:PRK09406 83 EALKCAKGFRYyaehaealladepadaaAVGASR--------------AYV-RYQPLGVVLAVMPWNFPL----WQvvrf 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 205 NAIAMICGNVCLWKGA---PTTSLIsvavtkiIAKVLEDNKLP-GAICSLTCGgADIGTAMAKDERVNLLSFTGSTQVGK 280
Cdd:PRK09406 144 AAPALMAGNVGLLKHAsnvPQTALY-------LADLFRRAGFPdGCFQTLLVG-SGAVEAILRDPRVAAATLTGSEPAGR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 281 QVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVG 360
Cdd:PRK09406 216 AVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 361 NPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKN 440
Cdd:PRK09406 296 DPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380813202 441 EEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEIGgaFGGEKHTGGGRE 507
Cdd:PRK09406 376 IDEAIEIANATTFGLGSNAWTRDEAEQERFI--DDLEAGQVFINgMTVSYPELP--FGGVKRSGYGRE 439
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
63-442 |
2.82e-45 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 171.27 E-value: 2.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 63 GEVITTYCPAN-NEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILV 141
Cdd:COG4230 569 GEARPVRNPADhSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLP 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 142 EGVGEVQEYVDICD-YAVGLSRMIGGPilpserpghaliEQWNPVGLVGIITAFNFPVA-----VygwnnAIAMICGNVC 215
Cdd:COG4230 649 DAIAEVREAVDFCRyYAAQARRLFAAP------------TVLRGRGVFVCISPWNFPLAiftgqV-----AAALAAGNTV 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 216 LWKGAPTTSLI-SVAVtkiiaKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRS 293
Cdd:COG4230 712 LAKPAEQTPLIaARAV-----RLLHEAGVPADVLQLLPGdGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPI 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 294 LL---ELGGNNAIIAfedaDLS-L---VVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSN 366
Cdd:COG4230 787 VPliaETGGQNAMIV----DSSaLpeqVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLS 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 367 VLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRP--GNYVEPTIVtglaHDASIAH--TETFAPILYVFKFKNEE 442
Cdd:COG4230 863 TDVGPVIDAEARANLEAHIERMRAE-GRLVHQLPLPEECanGTFVAPTLI----EIDSISDleREVFGPVLHVVRYKADE 937
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
38-507 |
4.08e-45 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 165.84 E-value: 4.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 38 QYAWLKELGLREENEGVYNGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWK--IWADIPAPKRGEI 113
Cdd:PRK09847 7 AYWQDKALSLAIENRLFINGEYtaAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 114 VRQIGDALREKIQVLGSLVSLEMGKIL-------VEGVGEVQEYvdicdYAVGLSRMIGgPILPSERPGHALIEQwNPVG 186
Cdd:PRK09847 87 LNKLADLMEAHAEELALLETLDTGKPIrhslrddIPGAARAIRW-----YAEAIDKVYG-EVATTSSHELAMIVR-EPVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 187 LVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAvtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDE 265
Cdd:PRK09847 160 VIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIR----LAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 266 RVNLLSFTGSTQVGKQVALMV-QERFGRSLLELGGNNAIIAFEDA-DLSLVVPSALFAAVGTAGQRCTTARRLFVHESIH 343
Cdd:PRK09847 236 DIDAIAFTGSTRTGKQLLKDAgDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 344 DEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGgTVVYGGKVMDRPGnYVEPTIVTGLAHDASI 423
Cdd:PRK09847 316 DEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 424 AHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGaEIGGAFGGEKHTG 503
Cdd:PRK09847 394 SREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRM--SRRLKAGSVFVNNYNDG-DMTVPFGGYKQSG 470
|
....
gi 380813202 504 GGRE 507
Cdd:PRK09847 471 NGRD 474
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
56-508 |
5.58e-45 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 165.13 E-value: 5.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW-GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSL 134
Cdd:PRK09457 6 NGDWiAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 135 EMGKILVEGVGEVQEYVDICDYAV-------GLSRmiggpilpSERPGHALIEQWNPVGLVGIITAFNFPVAVYgwNNAI 207
Cdd:PRK09457 86 ETGKPLWEAATEVTAMINKIAISIqayhertGEKR--------SEMADGAAVLRHRPHGVVAVFGPYNFPGHLP--NGHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 208 --AMICGNVCLWKGAPTTSlisvAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVG----KQ 281
Cdd:PRK09457 156 vpALLAGNTVVFKPSELTP----WVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGyllhRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 282 VAlmvqERFGRSL-LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIH-DEVVNRLKKAYAQIRV 359
Cdd:PRK09457 232 FA----GQPEKILaLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 360 GnPWDSNV--LYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTI--VTGLahdASIAHTETFAPILYV 435
Cdd:PRK09457 308 G-RWDAEPqpFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIidVTGV---AELPDEEYFGPLLQV 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380813202 436 FKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 508
Cdd:PRK09457 384 VRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFL--LEIRAGIVNWNKPLTGASSAAPFGGVGASGNHRPS 454
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
71-519 |
1.58e-44 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 169.28 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PAN-NEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQE 149
Cdd:PRK11905 574 PADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVRE 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 150 YVDICD-YAVGLSRMIGGPILPserpghalieqwnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLI-S 227
Cdd:PRK11905 654 AVDFLRyYAAQARRLLNGPGHK-------------PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIaA 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 228 VAVtkiiaKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLL---ELGGNNAI 303
Cdd:PRK11905 721 RAV-----RLLHEAGVPKDALQLLPGdGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAM 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 304 IAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLG 383
Cdd:PRK11905 796 IVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEA 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 384 AVEEAKKEGGTVvyggKVMDRP-----GNYVEPTI--VTGLAHdasIAHtETFAPILYVFKFKNEE--EVFAWNNEVKQG 454
Cdd:PRK11905 876 HIEAMRAAGRLV----HQLPLPaetekGTFVAPTLieIDSISD---LER-EVFGPVLHVVRFKADEldRVIDDINATGYG 947
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380813202 455 LSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdawKHYMRR 519
Cdd:PRK11905 948 LTFGLHSRIDETIAHVT--SRIRAGNIYVNRNIIGAVVGvQPFGGEGLSGTGPKAGG---PLYLGR 1008
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
71-505 |
2.99e-44 |
|
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: 162.59 E-value: 2.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKIWAD-IPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQE 149
Cdd:cd07148 6 PFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNwLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 150 YVDICDYAVGLSRMIGGPILP-------SERPGHALIEqwnPVGLVGIITAFNFPV--AVYGWNNAIAMICGnvCLWKGA 220
Cdd:cd07148 86 AIDGVELAADELGQLGGREIPmgltpasAGRIAFTTRE---PIGVVVAISAFNHPLnlIVHQVAPAIAAGCP--VIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 221 PTTSLISVAVTKIiakvLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGkqvaLMVQERFG---RSLLEL 297
Cdd:cd07148 161 LATPLSCLAFVDL----LHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVG----WMLRSKLApgtRCALEH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 298 GGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQA 377
Cdd:cd07148 233 GGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPRE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 378 VSMFLGAVEEAKKEGGTVVYGGKVMDRpgNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSS 457
Cdd:cd07148 313 VDRVEEWVNEAVAAGARLLCGGKRLSD--TTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 380813202 458 SIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGG 505
Cdd:cd07148 391 AVFTKDLDVALKAV--RRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
60-442 |
8.82e-44 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 166.91 E-value: 8.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 60 GGRGEVITTYCPANNE-PIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGK 138
Cdd:PRK11904 558 NGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGK 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 139 ILVEGVGEVQEYVDICD-YAVGLSRMIGGPI-LPSerpghalieqwnPVG------LVG-----IITAFNFPVAVYGWNN 205
Cdd:PRK11904 638 TLQDAIAEVREAVDFCRyYAAQARRLFGAPEkLPG------------PTGesnelrLHGrgvfvCISPWNFPLAIFLGQV 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 206 AIAMICGNVCLWKGAPTTSLISVAVTKIiakvLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVAL 284
Cdd:PRK11904 706 AAALAAGNTVIAKPAEQTPLIAAEAVKL----LHEAGIPKDVLQLLPGdGATVGAALTADPRIAGVAFTGSTETARIINR 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 285 MVQERFGRSL---LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGN 361
Cdd:PRK11904 782 TLAARDGPIVpliAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGD 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 362 PWDSNVLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMD--RPGNYVEPTIVtglaHDASIAH--TETFAPILYVFK 437
Cdd:PRK11904 862 PRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPAgtENGHFVAPTAF----EIDSISQleREVFGPILHVIR 936
|
....*
gi 380813202 438 FKNEE 442
Cdd:PRK11904 937 YKASD 941
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
56-466 |
1.65e-40 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 152.99 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:PLN00412 21 DGEWrtSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 134 LEMGKILVEGVGEVQEYVDICDYAV--GLSRMIGGPILPS------ERPGHALIEQWnPVGLVGIITAFNFPVAVYGWNN 205
Cdd:PLN00412 101 KEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFLVSdsfpgnERNKYCLTSKI-PLGVVLAIPPFNYPVNLAVSKI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 206 AIAMICGNVCLWKgAPTTSliSVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGS---TQVGKQv 282
Cdd:PLN00412 180 APALIAGNAVVLK-PPTQG--AVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGdtgIAISKK- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 283 ALMVQERfgrslLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNP 362
Cdd:PLN00412 256 AGMVPLQ-----MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 363 WDsNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKvmdRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEE 442
Cdd:PLN00412 331 ED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWK---REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVE 406
|
410 420
....*....|....*....|....
gi 380813202 443 EVFAWNNEVKQGLSSSIFTKDLGR 466
Cdd:PLN00412 407 EGIHHCNASNFGLQGCVFTRDINK 430
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
71-505 |
2.16e-40 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 154.52 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 71 PANNEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:PLN02419 136 PATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 151 VDICDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVav 230
Cdd:PLN02419 216 LEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASV-- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 231 tkIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDAD 310
Cdd:PLN02419 294 --ILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDAN 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 311 LSLVVPSALFAAVGTAGQRCTT-ARRLFVHE--SIHDEVVNRLKKayAQIRVGNPWDSNVlyGPLHTKQAVSMFLGAVEE 387
Cdd:PLN02419 372 IDATLNALLAAGFGAAGQRCMAlSTVVFVGDakSWEDKLVERAKA--LKVTCGSEPDADL--GPVISKQAKERICRLIQS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 388 AKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 463
Cdd:PLN02419 448 GVDDGAKLLLDGRDIVVPgyekGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSS 527
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 380813202 464 --LGRIFRwlgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGG 505
Cdd:PLN02419 528 gaAARKFQ----MDIEAGQIGINVPIPVPLPFFSFTGNKASFAG 567
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
173-505 |
2.12e-34 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 135.93 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 173 RPGHALIeQWNPVGLVGIITAFNFPV--AVYGWNNAIAmiCGNVCLWKgaptTSLISVAVTKIIAKVLeDNKLPGAICSL 250
Cdd:PTZ00381 99 GPGKSYI-IPEPLGVVLVIGAWNYPLnlTLIPLAGAIA--AGNTVVLK----PSELSPHTSKLMAKLL-TKYLDPSYVRV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 251 TCGGADIGTAMAKdERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRC 330
Cdd:PTZ00381 171 IEGGVEVTTELLK-EPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTC 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 331 TTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVlYGPL----HTKQAVSMFlgaveeaKKEGGTVVYGGKVmDRPG 406
Cdd:PTZ00381 250 VAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSED-YSRIvnefHTKRLAELI-------KDHGGKVVYGGEV-DIEN 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 407 NYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDlGRIFRWLGPKGSDCGIV----- 481
Cdd:PTZ00381 321 KYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGED-KRHKELVLENTSSGAVVindcv 399
|
330 340
....*....|....*....|....*...
gi 380813202 482 ----NVNIPtsgaeiggaFGGEKHTGGG 505
Cdd:PTZ00381 400 fhllNPNLP---------FGGVGNSGMG 418
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
77-442 |
7.16e-34 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 137.03 E-value: 7.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 77 IARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDY 156
Cdd:PRK11809 673 VGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRY 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 157 AVGLSRmiggpilpserpGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIak 236
Cdd:PRK11809 753 YAGQVR------------DDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRIL-- 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 237 vLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALMVQERF---GRS---LLELGGNNAIIAFEDAD 310
Cdd:PRK11809 819 -LEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqGRPiplIAETGGQNAMIVDSSAL 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 311 LSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKK 390
Cdd:PRK11809 898 TEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRA 977
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 380813202 391 EGGTV---VYGGKVMDRPGNYVEPTivtgLAHDASIAH--TETFAPILYVFKFKNEE 442
Cdd:PRK11809 978 KGRPVfqaARENSEDWQSGTFVPPT----LIELDSFDElkREVFGPVLHVVRYNRNQ 1030
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
63-463 |
7.45e-33 |
|
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: 131.55 E-value: 7.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 63 GEVITTYCPAN-NEPIARVRQASVADYEETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKI-QVLGSLVSLEMGKIL 140
Cdd:cd07123 45 GNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLGQGKNV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 141 VEGvgEVQEYVDICD-------YAVGLSRmiggpilpsERPGHALIEQWNPV------GLVGIITAFNFpVAVYGwNNAI 207
Cdd:cd07123 125 WQA--EIDAACELIDflrfnvkYAEELYA---------QQPLSSPAGVWNRLeyrpleGFVYAVSPFNF-TAIGG-NLAG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 208 A-MICGNVCLWKGAPTTSLISVAVTKIiakvLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVALM 285
Cdd:cd07123 192 ApALMGNVVLWKPSDTAVLSNYLVYKI----LEEAGLPpGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 286 VQER------FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRV 359
Cdd:cd07123 268 IGENldryrtYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKM 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 360 GNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGG-TVVYGGKVMDRPGNYVEPTIVTGLAHDASIAHTETFAPIL--YVF 436
Cdd:cd07123 348 GDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEaEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLtvYVY 427
|
410 420
....*....|....*....|....*...
gi 380813202 437 KFKNEEEVFAWNNEV-KQGLSSSIFTKD 463
Cdd:cd07123 428 PDSDFEETLELVDTTsPYALTGAIFAQD 455
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
173-463 |
8.84e-33 |
|
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: 129.95 E-value: 8.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 173 RPGHALIEQwNPVGLVGIITAFNFPV------AVygwnNAIAmiCGNVCLWKG---APTTSlisvavtKIIAKVLEDnKL 243
Cdd:cd07087 90 QPAKAYVIP-EPLGVVLIIGPWNYPLqlalapLI----GAIA--AGNTVVLKPselAPATS-------ALLAKLIPK-YF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 244 PGAICSLTCGGADIGTAMAKdERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAV 323
Cdd:cd07087 155 DPEAVAVVEGGVEVATALLA-EPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 324 GTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVlYGPL----HTKQAVSMFlgaveeakkEGGTVVYGG 399
Cdd:cd07087 234 LNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPD-YGRIinerHFDRLASLL---------DDGKVVIGG 303
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380813202 400 KVmDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 463
Cdd:cd07087 304 QV-DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSED 366
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
184-463 |
1.75e-29 |
|
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: 120.79 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 184 PVGLVGIITAFNFPV-----AVYGwnnAIAmiCGNVCLWKG---APTTSLIsvaVTKIIAKVLEdnklPGAICSLTCGGA 255
Cdd:cd07135 108 PLGVVLIIGPWNYPVllalsPLVG---AIA--AGCTVVLKPselTPHTAAL---LAELVPKYLD----PDAFQVVQGGVP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 256 DIGTAMakDERVNLLSFTGSTQVGKQVAlmvqERFGRSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCT 331
Cdd:cd07135 176 ETTALL--EQKFDKIFYTGSGRVGRIIA----EAAAKHLtpvtLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 332 TARRLFVHESIHDEVVNRLKKAYAQiRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKkegGTVVYGGKvMDRPGNYVEP 411
Cdd:cd07135 250 APDYVLVDPSVYDEFVEELKKVLDE-FYPGGANASPDYTRIVNPRHFNRLKSLLDTTK---GKVVIGGE-MDEATRFIPP 324
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 380813202 412 TIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 463
Cdd:cd07135 325 TIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDD 376
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
184-463 |
6.05e-29 |
|
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: 119.15 E-value: 6.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 184 PVGLVGIITAFNFP-----VAVYGwnnAIAmiCGNVCLWKgaPttSLISVAVTKIIAKVLEDNKLPGAICSLTcGGADIG 258
Cdd:cd07136 100 PYGVVLIIAPWNYPfqlalAPLIG---AIA--AGNTAVLK--P--SELTPNTSKVIAKIIEETFDEEYVAVVE-GGVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 259 TAMAkDERVNLLSFTGSTQVGKQVAlmvqERFGRSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTAR 334
Cdd:cd07136 170 QELL-DQKFDYIFFTGSVRVGKIVM----EAAAKHLtpvtLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 335 RLFVHESIHDEVVNRLKKaYAQIRVGNPWDSNVLYGPL----HTKQAVSMFlgaveeakkEGGTVVYGGKVmDRPGNYVE 410
Cdd:cd07136 245 YVLVHESVKEKFIKELKE-EIKKFYGEDPLESPDYGRIinekHFDRLAGLL---------DNGKIVFGGNT-DRETLYIE 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 380813202 411 PTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 463
Cdd:cd07136 314 PTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSED 366
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
184-509 |
2.37e-25 |
|
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: 108.47 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 184 PVGLVGIITAFNFPVA------VYgwnnAIAmiCGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLpgAICSltcGGADI 257
Cdd:cd07134 100 PKGVCLIISPWNYPFNlafgplVS----AIA--AGNTAILKPSELTPHTSAVIAKIIREAFDEDEV--AVFE---GDAEV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 258 GTAmakdervnLLS-------FTGSTQVGKqvalMVQERFGRSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTA 326
Cdd:cd07134 169 AQA--------LLElpfdhifFTGSPAVGK----IVMAAAAKHLasvtLELGGKSPTIVDETADLKKAAKKIAWGKFLNA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 327 GQRCTTARRLFVHESIHDEVVNRLKKAYAQIrvgnpwdsnvlYGPLHTKQAVSMF------------LGAVEEAKKEGGT 394
Cdd:cd07134 237 GQTCIAPDYVFVHESVKDAFVEHLKAEIEKF-----------YGKDAARKASPDLarivndrhfdrlKGLLDDAVAKGAK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 395 VVYGGKVmDRPGNYVEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPK 474
Cdd:cd07134 306 VEFGGQF-DAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLART 384
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 380813202 475 GS-DCGI-------VNVNIPtsgaeiggaFGGEKHTGGGRESG 509
Cdd:cd07134 385 SSgGVVVndvvlhfLNPNLP---------FGGVNNSGIGSYHG 418
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
95-520 |
1.03e-24 |
|
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: 106.94 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 95 AKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGK--ILVEGVGEVQEYVDICDYAVGLSRMIGGPI--LP 170
Cdd:cd07084 8 ADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKgwMFAENICGDQVQLRARAFVIYSYRIPHEPGnhLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 171 SERPGHALIEQWnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLednKLPGAICSL 250
Cdd:cd07084 88 QGLKQQSHGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAG---LLPPEDVTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 251 TCGGADIGTAMAKDERVNLLSFTGSTQVGKqvALMVQERFGRSLLELGGNNAIIAFEDAD-LSLVVPSALFAAVGTAGQR 329
Cdd:cd07084 164 INGDGKTMQALLLHPNPKMVLFTGSSRVAE--KLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 330 CTTARRLFVHESIHDE-VVNRLKKAYAQIRvgnpwDSNVLYGPLHTKQAVSMflgaVEEAKKEGGTVV-YGGKVM---DR 404
Cdd:cd07084 242 CTAQSMLFVPENWSKTpLVEKLKALLARRK-----LEDLLLGPVQTFTTLAM----IAHMENLLGSVLlFSGKELknhSI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 405 PGNY----VEPTIVTGLAHDAS-IAHT-ETFAPILYVFKFKNEEEVFAWN-NEVKQG-LSSSIFTKD---LGRifrwLGP 473
Cdd:cd07084 313 PSIYgacvASALFVPIDEILKTyELVTeEIFGPFAIVVEYKKDQLALVLElLERMHGsLTAAIYSNDpifLQE----LIG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 380813202 474 KGSDCGIVNVNIPTSgaeiGGAFGGEKHTGGGRES-------GSDAWKHYMRRS 520
Cdd:cd07084 389 NLWVAGRTYAILRGR----TGVAPNQNHGGGPAADprgagigGPEAIKLVWRCH 438
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
56-520 |
1.42e-24 |
|
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: 106.97 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSW-GGRGEVITTYCPANNEPIARVRQASVaDYEETVKKAKEawkiwadIPAPK--------RGEIVRQIGDALREK-- 124
Cdd:cd07128 6 AGQWhAGTGDGRTLHDAVTGEVVARVSSEGL-DFAAAVAYARE-------KGGPAlraltfheRAAMLKALAKYLMERke 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 125 -----------------------IQVL---GSLVSLEM--GKILVEGVGEVqeyvdicdyavgLSR---MIGGPILpSER 173
Cdd:cd07128 78 dlyalsaatgatrrdswididggIGTLfayASLGRRELpnAHFLVEGDVEP------------LSKdgtFVGQHIL-TPR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 174 PGHALIeqwnpvglvgiITAFNFPVavygW----NNAIAMICGNVCLWKGAPTTSLISVAVTKIIakvLEDNKLP-GAIc 248
Cdd:cd07128 145 RGVAVH-----------INAFNFPV----WgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDI---VESGLLPeGAL- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 249 SLTCGGAdiGTAMAKDERVNLLSFTGSTQVGKQVALM--VQERFGRSLLELGGNNAIIAFEDA-----DLSLVVPSALFA 321
Cdd:cd07128 206 QLICGSV--GDLLDHLGEQDVVAFTGSAATAAKLRAHpnIVARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVARE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 322 AVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKV 401
Cdd:cd07128 284 MTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 402 MDRP-------GNYVEPTIVTGL-AHDASIAH-TETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD---LGRIFR 469
Cdd:cd07128 363 RFEVvgadaekGAFFPPTLLLCDdPDAATAVHdVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDpafARELVL 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 470 WLGPKGsdcGIVNVNIPTSGAEIGG--------AFGGEKHTGGGRE-SGSDAWKHYMRRS 520
Cdd:cd07128 443 GAAPYH---GRLLVLNRDSAKESTGhgsplpqlVHGGPGRAGGGEElGGLRGVKHYMQRT 499
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
181-463 |
8.40e-21 |
|
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: 94.98 E-value: 8.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 181 QWNPVGLVGIITAFNFPVA-----VYGwnnAIAmiCGNVCLWKgaPttSLISVAVTKIIAKVLE---DNKLPGAICsltc 252
Cdd:cd07132 97 YKEPLGVVLIIGAWNYPLQltlvpLVG---AIA--AGNCVVIK--P--SEVSPATAKLLAELIPkylDKECYPVVL---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 253 GGADIGTAMAKdERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTT 332
Cdd:cd07132 164 GGVEETTELLK-QRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 333 ARRLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVlYGPL----HTKQAVSMFlgaveeakkEGGTVVYGGKVmDRPGNY 408
Cdd:cd07132 243 PDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPD-YGRIindrHFQRLKKLL---------SGGKVAIGGQT-DEKERY 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 380813202 409 VEPTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 463
Cdd:cd07132 312 IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
173-446 |
2.25e-20 |
|
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: 93.70 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 173 RPGHALIeQWNPVGLVGIITAFNFPVAVygwnnAIA-MIC----GNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLpgai 247
Cdd:cd07133 91 LPAKAEV-EYQPLGVVGIIVPWNYPLYL-----ALGpLIAalaaGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV---- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 248 cSLTCGGADIGTAMAK---DervNLLsFTGSTQVGKQVALMVQErfgrSL----LELGGNN-AIIAfEDADLSLVVPSAL 319
Cdd:cd07133 161 -AVVTGGADVAAAFSSlpfD---HLL-FTGSTAVGRHVMRAAAE----NLtpvtLELGGKSpAIIA-PDADLAKAAERIA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 320 FAAVGTAGQRCTTARRLFVHESIHDEVVNRLKKAYAQI---RVGNPwDsnvlYGPLHTKQAVSMFLGAVEEAKKEGGTVV 396
Cdd:cd07133 231 FGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNP-D----YTSIINERHYARLQGLLEDARAKGARVI 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 380813202 397 yggKVMDRPGNYVE-----PTIVTGLAHDASIAHTETFAPILYVFKFKNEEEVFA 446
Cdd:cd07133 306 ---ELNPAGEDFAAtrklpPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAID 357
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
191-520 |
2.39e-19 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 91.30 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 191 ITAFNFPVavYG-WNNA-IAMICGNVCLWKGAPTTSLISvavTKIIAKVLEDNKLPGAICSLTCGGAdiGTAMAKDERVN 268
Cdd:PRK11903 155 INAFNFPA--WGlWEKAaPALLAGVPVIVKPATATAWLT---QRMVKDVVAAGILPAGALSVVCGSS--AGLLDHLQPFD 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 269 LLSFTGSTQVGKQVALM--VQERFGRSLLELGGNNAIIAFEDADLSlvvpSALFAAVG---------TAGQRCTTARRLF 337
Cdd:PRK11903 228 VVSFTGSAETAAVLRSHpaVVQRSVRVNVEADSLNSALLGPDAAPG----SEAFDLFVkevvremtvKSGQKCTAIRRIF 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 338 VHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTK-QAVSMFLGAveEAKKEGGTVVYGGKV---MDRP---GNYVE 410
Cdd:PRK11903 304 VPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRaQLAAVRAGL--AALRAQAEVLFDGGGfalVDADpavAACVG 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 411 PTI-VTGLAHDASIAH-TETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD---LGRIFRWLGPKGsdcGIVNVNI 485
Cdd:PRK11903 382 PTLlGASDPDAATAVHdVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDaafLAAAALELADSH---GRVHVIS 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 380813202 486 PTSGAEIGG--------AFGGEKHTGGGRE-SGSDAWKHYMRRS 520
Cdd:PRK11903 459 PDVAALHTGhgnvmpqsLHGGPGRAGGGEElGGLRALAFYHRRS 502
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
184-515 |
7.31e-18 |
|
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: 85.93 E-value: 7.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 184 PVGLVGIITAFNFPVA-----VYGwnnAIAmiCGNVCLWKgaptTSLISVAVTKIIAKVLEDNKLPGAIcSLTCGGADIG 258
Cdd:cd07137 101 PLGVVLVISAWNFPFLlslepVIG---AIA--AGNAVVLK----PSELAPATSALLAKLIPEYLDTKAI-KVIEGGVPET 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 259 TAMAkDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGT-AGQRCTTARRLF 337
Cdd:cd07137 171 TALL-EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 338 VHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTK--QAVSMFLGAVEEAKKeggtVVYGGKVmDRPGNYVEPTIVT 415
Cdd:cd07137 250 VEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHhfQRLSRLLDDPSVADK----IVHGGER-DEKNLYIEPTILL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 416 GLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT--KDLGRIFRWLGPKGS----DCgIVNVNIPTSg 489
Cdd:cd07137 325 DPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTknKELKRRIVAETSSGGvtfnDT-VVQYAIDTL- 402
|
330 340
....*....|....*....|....*....
gi 380813202 490 aeiggAFGGEKHTGGGRESGS---DAWKH 515
Cdd:cd07137 403 -----PFGGVGESGFGAYHGKfsfDAFSH 426
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
184-515 |
1.45e-15 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 79.32 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 184 PVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKgaptTSLISVAVTKIIAKVLEDNKLPGAICSLTcgGADIGTAMAK 263
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLK----PSELAPASSALLAKLLEQYLDSSAVRVVE--GAVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 264 DERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVG-TAGQRCTTARRLFVHESI 342
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEY 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 343 HDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSmfLGAVEEAKKEGGTVVYGGKvMDRPGNYVEPTIVTGLAHDAS 422
Cdd:PLN02174 266 APKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDR--LSKLLDEKEVSDKIVYGGE-KDRENLKIAPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 423 IAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDlGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHT 502
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHN-KKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGES 421
|
330
....*....|....*.
gi 380813202 503 GGGRESGS---DAWKH 515
Cdd:PLN02174 422 GMGAYHGKfsfDAFSH 437
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
184-520 |
1.09e-13 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 73.22 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 184 PVGLVGIITAFNFPV--AVYGWNNAIAmiCGNVCLWKG---APTTSLIsvaVTKIIAKVLeDNKlpgAIcSLTCGGADIG 258
Cdd:PLN02203 108 PLGVVLIFSSWNFPIglSLEPLIGAIA--AGNAVVLKPselAPATSAF---LAANIPKYL-DSK---AV-KVIEGGPAVG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 259 TAMAkDERVNLLSFTGSTQVGKQVALMVQERFGRSLLELGGNN-AIIAFEDA--DLSLVVPSALFAAVGT-AGQRCTTAR 334
Cdd:PLN02203 178 EQLL-QHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCpCIVDSLSSsrDTKVAVNRIVGGKWGScAGQACIAID 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 335 RLFVHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTK--QAVSMFLgaveEAKKEGGTVVYGGKvMDRPGNYVEPT 412
Cdd:PLN02203 257 YVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKhfQRLSNLL----KDPRVAASIVHGGS-IDEKKLFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 413 IVTGLAHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEi 492
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACD- 410
|
330 340 350
....*....|....*....|....*....|....
gi 380813202 493 GGAFGGEKHTGGGRESGS---DAWKHY---MRRS 520
Cdd:PLN02203 411 SLPFGGVGESGFGRYHGKysfDTFSHEkavLRRS 444
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
56-443 |
2.84e-11 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 65.59 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 56 NGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAKEAWK--IWADIPAPKR----GEIVRQIGDALReKIQV-- 127
Cdd:cd07126 4 AGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKsgLHNPLKNPERyllyGDVSHRVAHELR-KPEVed 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 128 -LGSLVSLEMGKILVEGVGEV---QEYV-----DICDYavgLSR--MIGGPILPSERPGHalieQWnPVGLVGIITAFNF 196
Cdd:cd07126 83 fFARLIQRVAPKSDAQALGEVvvtRKFLenfagDQVRF---LARsfNVPGDHQGQQSSGY----RW-PYGPVAIITPFNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 197 PVAVYGWNNAIAMICGNVCLWKGaptTSLISVAVTKIIaKVLEDNKLPGAICSLT-CGGADIGTAMaKDERVNLLSFTGS 275
Cdd:cd07126 155 PLEIPALQLMGALFMGNKPLLKV---DSKVSVVMEQFL-RLLHLCGMPATDVDLIhSDGPTMNKIL-LEANPRMTLFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 276 TQVGKQVALMVQerfGRSLLELGGNNAIIAFED-ADLSLVVPSALFAAVGTAGQRCTTARRLFVHES-IHDEVVNRLKKA 353
Cdd:cd07126 230 SKVAERLALELH---GKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 354 YAQIRVgnpwdSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVM---DRPGNY--VEPTIV------TGLAHDAS 422
Cdd:cd07126 307 AEQRKL-----EDLTIGPVLTWTTERILDHVDKLLAIPGAKVLFGGKPLtnhSIPSIYgaYEPTAVfvpleeIAIEENFE 381
|
410 420
....*....|....*....|.
gi 380813202 423 IAHTETFAPILYVFKFKNEEE 443
Cdd:cd07126 382 LVTTEVFGPFQVVTEYKDEQL 402
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
184-459 |
4.61e-08 |
|
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: 55.63 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 184 PVGLVGIITAFNFPVA--VYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSL-TCGGADIGTA 260
Cdd:cd07129 105 PLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAALRATGLPAGVFSLlQGGGREVGVA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 261 MAKDERVNLLSFTGSTQVGKQVALMVQER------FGrsllELGGNNAIIafedadlslVVPSAL----------FAA-- 322
Cdd:cd07129 185 LVKHPAIKAVGFTGSRRGGRALFDAAAARpepipfYA----ELGSVNPVF---------ILPGALaergeaiaqgFVGsl 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 323 VGTAGQRCTTARRLFVHESIH-DEVVNRLKKAYAQIRVgnpwdsnvlyGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKV 401
Cdd:cd07129 252 TLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPA----------QTMLTPGIAEAYRQGVEALAAAPGVRVLAGGA 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380813202 402 MDRPGNYVEPTI--VTG---LAHDAsiAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSI 459
Cdd:cd07129 322 AAEGGNQAAPTLfkVDAaafLADPA--LQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATI 382
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
89-522 |
1.08e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 48.03 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 89 EETVKKAKEAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGvgEVQEYVDICDYAVGLSRMIGGP- 167
Cdd:cd07081 2 DDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVED--KVIKNHFAAEYIYNVYKDEKTCg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 168 ILPSERPGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAI 247
Cdd:cd07081 80 VLTGDENGGTLIIA-EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 248 CSlTCGGADIGTAMA--KDERVNLLSFTGSTQVGKQValmvqERFGRSLLELG-GNNAIIAFEDADLSLVVPSALFAAVG 324
Cdd:cd07081 159 IG-WIDNPSIELAQRlmKFPGIGLLLATGGPAVVKAA-----YSSGKPAIGVGaGNTPVVIDETADIKRAVQSIVKSKTF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 325 TAGQRCTTARRLFVHESIHDEVVNRLKKAYAQIRVGNpwdsnvlygPLHTKQAVSMFLGAVEEA--KKEGGTV--VYGGK 400
Cdd:cd07081 233 DNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAE---------ELQQVQPVILKNGDVNRDivGQDAYKIaaAAGLK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 401 VmdrPGN----YVEptiVTGLAHDASIAHtETFAPILYVFKFKNEEEVFAWNNEVKQ----GLSSSIFTKDLGRIFR--W 470
Cdd:cd07081 304 V---PQEtrilIGE---VTSLAEHEPFAH-EKLSPVLAMYRAANFADADAKALALKLeggcGHTSAMYSDNIKAIENmnQ 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380813202 471 LGPKgSDCGIVNVNIPTSGAEIGGAFG---------GEKHTGGGRESGSDAWKHYMRRSTC 522
Cdd:cd07081 377 FANA-MKTSRFVKNGPCSQGGLGDLYNfrgwpsmtlGCGTWGGNSVSENVGPKHLVNLKTV 436
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
184-437 |
6.02e-05 |
|
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: 45.55 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 184 PVGLVGIITAFNFPVavygWNNAIAMIC----GNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCG--GADI 257
Cdd:cd07127 193 PRGVALVIGCSTFPT----WNGYPGLFAslatGNPVIVKPHPAAILPLAITVQVAREVLAEAGFDPNLVTLAADtpEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 258 GTAMAKDERVNLLSFTGSTQVGKQvaLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLF 337
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSNAFGDW--LEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIY 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380813202 338 V----------HESiHDEVVNRLKKAYAQIrVGNPWDSNVLYGPLHTkQAVsmfLGAVEEAKKEGGTVVYGGKVM--DRP 405
Cdd:cd07127 347 VprdgiqtddgRKS-FDEVAADLAAAIDGL-LADPARAAALLGAIQS-PDT---LARIAEARQLGEVLLASEAVAhpEFP 420
|
250 260 270
....*....|....*....|....*....|...
gi 380813202 406 GNYVE-PTIVTGLAHDASIAHTETFAPILYVFK 437
Cdd:cd07127 421 DARVRtPLLLKLDASDEAAYAEERFGPIAFVVA 453
|
|
| |
