|
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: 950.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 53 GVYNGSWGGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLV 132
Cdd:cd07130 1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 133 SLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITG 212
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 213 NVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGK 292
Cdd:cd07130 161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 293 SLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPL 372
Cdd:cd07130 241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 373 HTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLaHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVK 452
Cdd:cd07130 321 HTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGL-SDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVP 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219757 453 QGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYS 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: 889.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 53 GVYNGSWGGRG-EVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRL 131
Cdd:cd07086 1 GVIGGEWVGSGgETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 132 VSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALIT 211
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 212 GNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFG 291
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 292 KSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGP 371
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 372 LHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDH--PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNN 449
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219757 450 EVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYS 527
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
37-538 |
0e+00 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 717.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 37 PQYAWLQDLGLREDNEGVY-NGSWGGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVR 115
Cdd:PLN02315 6 KEYEFLSEIGLSSRNLGCYvGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 116 KIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFN 195
Cdd:PLN02315 86 QIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 196 FPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGS 275
Cdd:PLN02315 166 FPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 276 TQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYS 355
Cdd:PLN02315 246 SKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 356 QIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTgLAHDAPIVHQETFAPILYV 435
Cdd:PLN02315 326 QVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 436 FKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQ 515
Cdd:PLN02315 405 MKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQ 484
|
490 500
....*....|....*....|...
gi 188219757 516 YMRRSTCTINYSTSLPLAQGIKF 538
Cdd:PLN02315 485 YMRRSTCTINYGNELPLAQGINF 507
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
89-524 |
5.64e-169 |
|
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: 485.17 E-value: 5.64e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 89 EETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPT 168
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 169 LPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLednlLPGAIC 248
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAG----LPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 249 SLVCGGAD-IGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAG 327
Cdd:cd07078 157 NVVTGDGDeVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 328 QRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMD-HPG 406
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEgGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 407 NYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIP 486
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVA--ERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 188219757 487 TSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 524
Cdd:cd07078 395 SVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
61-521 |
1.21e-164 |
|
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: 475.10 E-value: 1.21e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 61 GRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKIL 140
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 141 VEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSeRPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGA 220
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 221 PTTSLVSVAVTKIIAQVLednlLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGG 299
Cdd:pfam00171 163 ELTPLTALLLAELFEEAG----LPAGVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 300 NNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVS 379
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 380 MFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSI 459
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 188219757 460 FTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRST 521
Cdd:pfam00171 399 FTSDLERALRVA--RRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
56-526 |
3.46e-164 |
|
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: 474.61 E-value: 3.46e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 133
Cdd:COG1012 11 GGEWvaAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 134 LEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGN 213
Cdd:COG1012 91 LETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 214 VCLWKGAPTTSLVSVAVTKIIAQVledNLLPGAIcSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGK 292
Cdd:COG1012 171 TVVLKPAEQTPLSALLLAELLEEA---GLPAGVL-NVVTGdGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 293 SLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPL 372
Cdd:COG1012 247 VTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 373 HTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDH-PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEV 451
Cdd:COG1012 327 ISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDT 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219757 452 KQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 526
Cdd:COG1012 407 EYGLAASVFTRDLARARRVA--RRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
56-527 |
1.82e-131 |
|
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: 391.33 E-value: 1.82e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSWGGR--GEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLV 132
Cdd:cd07131 4 GGEWVDSasGETFDSRNPADlEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 133 SLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITG 212
Cdd:cd07131 84 TREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 213 NVCLWKGAPTTSlvsvAVTKIIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFG 291
Cdd:cd07131 164 NTVVFKPAEDTP----ACALKLVELFAEAGLPPGVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 292 KSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGP 371
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 372 LHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDH----PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEW 447
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 448 NNEVKQGLSSSIFTKDLGRIFRWLGpkgsDC--GIVNVNIPTSGAEIGGAFGGEKHTGGG-RESGSDAWKQYMRRSTCTI 524
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARR----DLeaGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
...
gi 188219757 525 NYS 527
Cdd:cd07131 476 DYS 478
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
95-524 |
2.60e-126 |
|
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: 373.87 E-value: 2.60e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 95 AKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERP 174
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 175 GHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVlednLLPGAICSLVCGG 254
Cdd:cd06534 83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEA----GLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 255 AD-IGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTV 333
Cdd:cd06534 159 GDeVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 334 RRLFLHESIHNEVVDRLRsaysqirvgnpwdpnilygplhtkqavsmfvraveeakkqggtvvyggkvmdhpgnyvepTI 413
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV------------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 414 VTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIG 493
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVA--ERLRAGTVYINDSSIGVGPE 336
|
410 420 430
....*....|....*....|....*....|.
gi 188219757 494 GAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 524
Cdd:cd06534 337 APFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
52-512 |
1.00e-114 |
|
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: 348.08 E-value: 1.00e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 52 EGVYNGSWGGRGEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGR 130
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 131 LVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALI 210
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 211 TGNVCLWKGAPTTSLVSVAVTKIIAQVLednlLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQER 289
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAG----LPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 290 FGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILY 369
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 370 GPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKV--MDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEW 447
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188219757 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 |
4.52e-110 |
|
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: 335.17 E-value: 4.52e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVqey 150
Cdd:cd07103 4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 151 vdvcDYAAGL-------SRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTT 223
Cdd:cd07103 81 ----DYAASFlewfaeeARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 224 SLVSVAvtkiIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNA 302
Cdd:cd07103 157 PLSALA----LAELAEEAGLPAGVLNVVTGsPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 303 IIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFV 382
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 383 RAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTK 462
Cdd:cd07103 313 ALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 188219757 463 DLGRIFRwLGpKGSDCGIVNVNIPT-SGAEIggAFGGEKHTGGGRESGSDAWKQYM 517
Cdd:cd07103 393 DLARAWR-VA-EALEAGMVGINTGLiSDAEA--PFGGVKESGLGREGGKEGLEEYL 444
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
71-518 |
1.20e-106 |
|
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: 326.82 E-value: 1.20e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQ 148
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 149 EYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSV 228
Cdd:cd07114 84 YLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 229 AVTKIiaqVLEDNLLPGAIcSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFE 307
Cdd:cd07114 164 ELAKL---AEEAGFPPGVV-NVVTGfGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 308 DADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEE 387
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 388 AKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 463
Cdd:cd07114 320 AREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 464 LGRIFRWlgPKGSDCGIVNVNI-----PTSgaeiggAFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:cd07114 400 LARAHRV--ARAIEAGTVWVNTyralsPSS------PFGGFKDSGIGRENGIEAIREYTQ 451
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
63-469 |
1.57e-103 |
|
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: 319.21 E-value: 1.57e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 63 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVE 142
Cdd:cd07088 12 GETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 143 GIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPT 222
Cdd:cd07088 92 ARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 223 TSLVSVAVTKIIAQVlednLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 301
Cdd:cd07088 172 TPLNALEFAELVDEA----GLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 302 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 381
Cdd:cd07088 248 PAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 382 VRAVEEAKKQGGTVVYGGKVMDH-PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIF 460
Cdd:cd07088 328 EEMVERAVEAGATLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIY 407
|
....*....
gi 188219757 461 TKDLGRIFR 469
Cdd:cd07088 408 TENLNTAMR 416
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
71-521 |
1.28e-98 |
|
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: 305.61 E-value: 1.28e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 150
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 151 VDVCDYAAGLSrmiggptLPSER----PGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLV 226
Cdd:cd07106 84 VAWLRYTASLD-------LPDEVieddDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 227 SVAVTKIIAQVLednllPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVAlmvqERFGKSL----LELGGNNA 302
Cdd:cd07106 157 TLKLGELAQEVL-----PPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVM----ASAAKTLkrvtLELGGNDA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 303 IIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFV 382
Cdd:cd07106 228 AIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 383 RAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTK 462
Cdd:cd07106 308 ELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188219757 463 DLGRIFRwLGPKgSDCGIVNVNiptSGAEIGGA--FGGEKHTGGGRESGSDAWKQYMRRST 521
Cdd:cd07106 388 DLERAEA-VARR-LEAGTVWIN---THGALDPDapFGGHKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
71-510 |
2.12e-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: 295.01 E-value: 2.12e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 150
Cdd:cd07150 6 PADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 151 VDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVaVFGWNN-AIALITGNVCLWKGAPTTSLVSVa 229
Cdd:cd07150 86 PELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPL-ILATKKvAFALAAGNTVVLKPSEETPVIGL- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 230 vtkIIAQVLEDNLLPGAICSLV-CGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFED 308
Cdd:cd07150 164 ---KIAEIMEEAGLPKGVFNVVtGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 309 ADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEA 388
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 389 KKQGGTVVYGGKvmdHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIF 468
Cdd:cd07150 321 VAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAF 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 188219757 469 RWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGS 510
Cdd:cd07150 398 KL--AERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGE 437
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
87-516 |
4.29e-94 |
|
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: 293.67 E-value: 4.29e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 87 DYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGG 166
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 167 PTLPSERPGHALIEMWNPLGLVGIITAFNFPV-----AVfgwnnAIALITGNVCLWKGAPTTSlVSVAVtkIIAQVLEDN 241
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLilamrSV-----APALALGNAVVLKPDSRTP-VTGGL--LIAEIFEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 242 LLP-GAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLF 320
Cdd:cd07104 153 GLPkGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 321 AAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGK 400
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 401 vmdHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRwLGpKGSDCGI 480
Cdd:cd07104 313 ---YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMA-FA-ERLETGM 387
|
410 420 430
....*....|....*....|....*....|....*.
gi 188219757 481 VNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQY 516
Cdd:cd07104 388 VHINDQTVNDEPHVPFGGVKASGGGRFGGPASLEEF 423
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
66-508 |
9.42e-91 |
|
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: 285.78 E-value: 9.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 66 ITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIG 145
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 146 EVQEYVDVCDYAAGLSRMIGGPTLPSE----RPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 221
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 222 TTSLVSVAVTKIIaqvLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 301
Cdd:cd07145 161 NTPLTAIELAKIL---EEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 302 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 381
Cdd:cd07145 238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 382 VRAVEEAKKQGGTVVYGGKVMDhpGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT 461
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFT 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 188219757 462 KDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 508
Cdd:cd07145 396 NDINRALKV--ARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREG 440
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
66-507 |
3.58e-90 |
|
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: 284.10 E-value: 3.58e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 66 ITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIG 145
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 146 EVQEYVDVCDYAAGLSRMIGGPTLPSE-------RPGHALIEmwnPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWK 218
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFDaspggegRIGFTIRE---PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 219 GAPTTSLVSVAvtkiIAQVLEDNLLPGAICSLVCGGAD-IGTTMARDERVNLLSFTGSTQVGKEVALMVQERfgKSLLEL 297
Cdd:cd07149 158 PASQTPLSALK----LAELLLEAGLPKGALNVVTGSGEtVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--KVTLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 298 GGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQA 377
Cdd:cd07149 232 GSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 378 VSMFVRAVEEAKKQGGTVVYGGKVMdhpGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSS 457
Cdd:cd07149 312 AERIEEWVEEAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQA 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 188219757 458 SIFTKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 507
Cdd:cd07149 389 GVFTNDLQKALKAA--RELEVGGVMINdSSTFRVD-HMPYGGVKESGTGRE 436
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
71-518 |
1.34e-89 |
|
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: 282.68 E-value: 1.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGI-GEVQE 149
Cdd:cd07092 4 PATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 150 YVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVA 229
Cdd:cd07092 84 AVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 230 VTKIIAQVLednllPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFED 308
Cdd:cd07092 164 LAELAAEVL-----PPGVVNVVCGgGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 309 ADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEA 388
Cdd:cd07092 239 ADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 389 KKqGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIF 468
Cdd:cd07092 319 PA-HARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAM 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 188219757 469 RWLGPKGSDCGIVNVNIPTSgAEIggAFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:cd07092 398 RLSARLDFGTVWVNTHIPLA-AEM--PHGGFKQSGYGKDLSIYALEDYTR 444
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
89-507 |
8.44e-89 |
|
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: 279.73 E-value: 8.44e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 89 EETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGlsrmiGGPT 168
Cdd:cd07100 2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAE-----NAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 169 LPSERP-----GHALIEmWNPLGLVGIITAFNFP---VAVFGwnnAIALITGNVCLWKGAPTTSLVSVAvtkiIAQVLED 240
Cdd:cd07100 77 FLADEPietdaGKAYVR-YEPLGVVLGIMPWNFPfwqVFRFA---APNLMAGNTVLLKHASNVPGCALA----IEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 241 NLLP-GAICSLVCGGADIGTTMArDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVL 319
Cdd:cd07100 149 AGFPeGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 320 FAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGG 399
Cdd:cd07100 228 KGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 400 KVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLG---RIFRWLgpkgs 476
Cdd:cd07100 308 KRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLEraeRVARRL----- 382
|
410 420 430
....*....|....*....|....*....|..
gi 188219757 477 DCGIVNVNIPT-SGAEIggAFGGEKHTGGGRE 507
Cdd:cd07100 383 EAGMVFINGMVkSDPRL--PFGGVKRSGYGRE 412
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
71-526 |
1.96e-88 |
|
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: 279.65 E-value: 1.96e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 150
Cdd:cd07107 4 PATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 151 VDVCDYAAGLSRMIGGPTLPSErPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVav 230
Cdd:cd07107 84 AALLDYFAGLVTELKGETIPVG-GRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSAL-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 231 tkIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDAD 310
Cdd:cd07107 161 --RLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 311 LSLVVPSvlfAAVG----TAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVE 386
Cdd:cd07107 239 PEAAADA---AVAGmnftWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 387 EAKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTK 462
Cdd:cd07107 316 SAKREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188219757 463 DLGRIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 526
Cdd:cd07107 396 DISQAHR--TARRVEAGYVWIN-GSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
54-526 |
1.05e-87 |
|
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: 279.49 E-value: 1.05e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 54 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLV 132
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 133 SLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSeRPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITG 212
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEM-VPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 213 NVCLWKGAPTTSLVSVAVtkiiAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGStqvgKEVALMVQERFG 291
Cdd:cd07124 195 NTVVLKPAEDTPVIAAKL----VEILEEAGLPPGVVNFLPGpGEEVGDYLVEHPDVRFIAFTGS----REVGLRIYERAA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 292 KS----------LLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGN 361
Cdd:cd07124 267 KVqpgqkwlkrvIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 362 PWDPNILYGPLHTKQAVSMFVRAVEEAkKQGGTVVYGGKVMDHP--GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQ 439
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIG-KSEGRLLLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 440 DEEEVFEWNNEVKQGLSSSIFTKDLGRI--FRwlgpKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTG-GGRESGSDAWKQ 515
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLerAR----REFEVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDYLLQ 501
|
490
....*....|.
gi 188219757 516 YMRRSTCTINY 526
Cdd:cd07124 502 FMQPKTVTENF 512
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
71-516 |
2.56e-87 |
|
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: 276.63 E-value: 2.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEG-IGEVQE 149
Cdd:cd07115 4 PATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDVPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 150 YVDVCDYAAGLSRMIGGPTLPSeRPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVA 229
Cdd:cd07115 84 AADTFRYYAGWADKIEGEVIPV-RGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 230 VTKIIAQVLednlLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFED 308
Cdd:cd07115 163 IAELMAEAG----FPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 309 ADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEA 388
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 389 KKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIF 468
Cdd:cd07115 319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 188219757 469 RWlgPKGSDCGIVNVNipTSGA-EIGGAFGGEKHTGGGRESGSDAWKQY 516
Cdd:cd07115 399 RV--AAALKAGTVWIN--TYNRfDPGSPFGGYKQSGFGREMGREALDEY 443
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
57-509 |
3.63e-86 |
|
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: 274.18 E-value: 3.63e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 57 GSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSL 134
Cdd:cd07151 1 GEWrdGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 135 EMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNV 214
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 215 CLWKGAPTTslvsvAVTK--IIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFG 291
Cdd:cd07151 161 VVLKPASDT-----PITGglLLAKIFEEAGLPKGVLNVVVGaGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 292 KSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGP 371
Cdd:cd07151 236 KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 372 LHTKQAVSMFVRAVEEAKKQGGTVVYGGkvmDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEV 451
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEGATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDT 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 188219757 452 KQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESG 509
Cdd:cd07151 393 EYGLSGAVFTSDLERGVQF--ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNG 448
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
71-507 |
3.61e-85 |
|
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: 271.16 E-value: 3.61e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKIL-VEGIGEVQE 149
Cdd:cd07108 4 PATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 150 YVDVCDYAAGLSRMIGGPTLPSeRPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVA 229
Cdd:cd07108 84 LADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 230 VTKIIAQVLednllPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFED 308
Cdd:cd07108 163 LAEILAQVL-----PAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 309 ADLSLVVPSVLFAAVGT-AGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEE 387
Cdd:cd07108 238 ADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 388 AKK-QGGTVVYGGK----VMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTK 462
Cdd:cd07108 318 GLStSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 188219757 463 DLGRIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRE 507
Cdd:cd07108 398 DLGRALR--AAHALEAGWVQVN-QGGGQQPGQSYGGFKQSGLGRE 439
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
42-517 |
3.57e-84 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 270.02 E-value: 3.57e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 42 LQDLGLREDnEGVYNGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGD 119
Cdd:PLN02278 17 LRNAGLLRT-QGLIGGKWtdAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 120 AFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVA 199
Cdd:PLN02278 96 LIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 200 VFGWNNAIALITGNVCLWKGAPTTSLVSVAvtkiiAQVL--EDNLLPGAIcSLVCGGA-DIGTTMARDERVNLLSFTGST 276
Cdd:PLN02278 176 MITRKVGPALAAGCTVVVKPSELTPLTALA-----AAELalQAGIPPGVL-NVVMGDApEIGDALLASPKVRKITFTGST 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 277 QVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQ 356
Cdd:PLN02278 250 AVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 357 IRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVF 436
Cdd:PLN02278 330 LVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 437 KFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN---IPTSGAeiggAFGGEKHTGGGRESGSDAW 513
Cdd:PLN02278 410 RFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRV--SEALEYGIVGVNeglISTEVA----PFGGVKQSGLGREGSKYGI 483
|
....
gi 188219757 514 KQYM 517
Cdd:PLN02278 484 DEYL 487
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
56-517 |
1.57e-83 |
|
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: 267.64 E-value: 1.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKRGEIVRKIGDAFREKIQLLGRL 131
Cdd:cd07119 3 DGEWveAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDsgEWPHLPAQERAALLFRIADKIREDAEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 132 VSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIeMWNPLGLVGIITAFNFPVAVFGWNNAIALIT 211
Cdd:cd07119 83 ETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRT-VREPVGVCGLITPWNYPLLQAAWKLAPALAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 212 GNVCLWKGAPTTSLVSVAVTKIIAQVLednlLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERF 290
Cdd:cd07119 162 GNTVVIKPSEVTPLTTIALFELIEEAG----LPAGVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 291 GKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYG 370
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 371 PLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFE 446
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188219757 447 WNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN---IPTSGAEiggaFGGEKHTGGGRESGSDAWKQYM 517
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVA--RRLRAGTVWINdyhPYFAEAP----WGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
68-512 |
1.06e-82 |
|
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: 264.81 E-value: 1.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 68 TYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGI-GE 146
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 147 VQEYVDVCDYAAGLSRMIGGPTLPSErPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLV 226
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 227 SVavtkIIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIA 305
Cdd:cd07093 160 AW----LLAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 306 FEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAV 385
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 386 EEAKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT 461
Cdd:cd07093 316 ELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 188219757 462 KDLGRIFRWlgPKGSDCGIVNVN------IPTsgaeiggAFGGEKHTGGGRESGSDA 512
Cdd:cd07093 396 RDLGRAHRV--ARRLEAGTVWVNcwlvrdLRT-------PFGGVKASGIGREGGDYS 443
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
66-507 |
1.13e-82 |
|
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: 264.49 E-value: 1.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 66 ITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIG 145
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 146 EVQEYVDVCDYAAGLSRMIGGPTLP---SER-PGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 221
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldiSARgEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 222 TTSLVSVavtkIIAQVL-EDNLLPGAICSLVCGgADIGTTMARDERVNLLSFTGSTQVGkevaLMVQERFGKS--LLELG 298
Cdd:cd07147 161 RTPLSAL----ILGEVLaETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVG----WDLKARAGKKkvVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 299 GNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAV 378
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 379 SMFVRAVEEAKKQGGTVVYGGKVmdhPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSS 458
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 188219757 459 IFTKDLGRIFR-WlgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 507
Cdd:cd07147 389 VFTRDLEKALRaW---DELEVGGVVINdVPTFRVD-HMPYGGVKDSGIGRE 435
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
68-518 |
1.63e-82 |
|
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: 264.17 E-value: 1.63e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 68 TYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEV 147
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 148 QEYVDVCDYAAGLSRMIGGPT--LPSERPGHALIEmwnPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSL 225
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHvpLPGGSFAYTRRE---PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 226 VSVavtkIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIA 305
Cdd:cd07090 158 TAL----LLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 306 FEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAV 385
Cdd:cd07090 234 FDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 386 EEAKKQGGTVVYGGKVMDHP-----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIF 460
Cdd:cd07090 314 ESAKQEGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVF 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 188219757 461 TKDLGRIFRWLGP-KGSDCGIVNVNIptSGAEIggAFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:cd07090 394 TRDLQRAHRVIAQlQAGTCWINTYNI--SPVEV--PFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
69-518 |
1.23e-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: 261.77 E-value: 1.23e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 69 YCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQ 148
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 149 EYVDVCDYAAGLSRMIggptLPSERPGHALIEMWN-------PLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 221
Cdd:cd07099 81 LALEAIDWAARNAPRV----LAPRKVPTGLLMPNKkatveyrPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 222 TTSLVSVAVTKIIAQVLednlLPGAICSLVCGGADIGTTMArDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 301
Cdd:cd07099 157 VTPLVGELLAEAWAAAG----PPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 302 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 381
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 382 VRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT 461
Cdd:cd07099 312 RRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188219757 462 KDL---GRIFRWLgpkgsDCGIVNVNIPTSGAEIGGA-FGGEKHTGGGRESGSDAWKQYMR 518
Cdd:cd07099 392 RDLaraEAIARRL-----EAGAVSINDVLLTAGIPALpFGGVKDSGGGRRHGAEGLREFCR 447
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
69-517 |
5.94e-81 |
|
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: 260.25 E-value: 5.94e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 69 YCPANNEPIARVRQASLKDYEETIGKAKKAWNIWA-DIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILV-EGIGE 146
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMtARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 147 VQEYVDVCDYAAGLSRM-----IGGPTLPSERPGHALIEMwNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 221
Cdd:cd07089 82 VDGPIGHLRYFADLADSfpwefDLPVPALRGGPGRRVVRR-EPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 222 TTSLVSVAVTKIIAqvlEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 301
Cdd:cd07089 161 DTPLSALLLGEIIA---ETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 302 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 381
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 382 VRAVEEAKKQGGTVVYGGKVMDH--PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSI 459
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188219757 460 FTKDLGR---IFRWLgpkgsDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 517
Cdd:cd07089 398 WSADVDRayrVARRI-----RTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
71-524 |
1.42e-80 |
|
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: 259.21 E-value: 1.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKkawNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 150
Cdd:cd07146 6 PYTGEVVGTVPAGTEEALREALALAA---SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 151 VDVCDYAAGLSRMIGGPTLPSERPGHA----LIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLV 226
Cdd:cd07146 83 ADVLRFAAAEALRDDGESFSCDLTANGkarkIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 227 SVAvtkiIAQVLEDNLLPGAICSLVCGG-ADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERfgKSLLELGGNNAIIA 305
Cdd:cd07146 163 AIY----LADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--RQLLELGGNDPLIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 306 FEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAV 385
Cdd:cd07146 237 MDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 386 EEAKKQGGTVVYGGKvmdHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLG 465
Cdd:cd07146 317 EEAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188219757 466 RIFRWLgpKGSDCGIVNVN------IPTSgaeiggAFGGEKHTG-GGRESGSDAWKQYMRRSTCTI 524
Cdd:cd07146 394 TIKRLV--ERLDVGTVNVNevpgfrSELS------PFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
71-524 |
2.01e-80 |
|
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: 258.70 E-value: 2.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWNIWA-DIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQE 149
Cdd:cd07109 4 PSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 150 YVDVCDYAAGLSRMIGGPTLPSErPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVA 229
Cdd:cd07109 84 AARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 230 vtkiIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFED 308
Cdd:cd07109 163 ----LAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 309 ADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPW-DPNilYGPLHTKQAVSMFVRAVEE 387
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLeDPD--LGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 388 AKKQGGTVVYGGKVMDHP---GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDL 464
Cdd:cd07109 317 ARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 465 GRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 524
Cdd:cd07109 397 DRALRV--ARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
68-517 |
2.06e-80 |
|
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: 258.81 E-value: 2.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 68 TYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPApKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIG 145
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 146 EVQEYVDVCDYAAGLSRMIGGPTLPSErPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSL 225
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPE-PGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 226 VSVAVTKIIAQVleDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIA 305
Cdd:cd07120 159 INAAIIRILAEI--PSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 306 FEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAV 385
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 386 EEAKKQGGTVVY-GGKVMDH--PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTK 462
Cdd:cd07120 317 ERAIAAGAEVVLrGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 188219757 463 DLGRIFRWlgPKGSDCGIVNVNipTSGAEIGGA-FGGEKHTGGGRESGSDAWKQYM 517
Cdd:cd07120 397 DLARAMRV--ARAIRAGTVWIN--DWNKLFAEAeEGGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
56-524 |
1.45e-79 |
|
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: 257.14 E-value: 1.45e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNI--WADIPAPKRGEIVRKIGDAFREKIQLLGRL 131
Cdd:cd07091 9 NNEFvdSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 132 VSLEMGKILVEGI-GEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMwNPLGLVGIITAFNFPVAVFGWNNAIALI 210
Cdd:cd07091 89 ESLDNGKPLEESAkGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRR-EPIGVCGQIIPWNFPLLMLAWKLAPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 211 TGNVCLWKGAPTTSLVSVAVtkiiAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQER 289
Cdd:cd07091 168 AGNTVVLKPAEQTPLSALYL----AELIKEAGFPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 290 FGKSL-LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNIL 368
Cdd:cd07091 244 NLKKVtLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 369 YGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWN 448
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 449 NEVKQGLSSSIFTKDLGRIFR----------WLgpkgsDC-GIVNVNIPtsgaeiggaFGGEKHTGGGRESGSDAWKQYM 517
Cdd:cd07091 404 NDTEYGLAAGVFTKDINKALRvsralkagtvWV-----NTyNVFDAAVP---------FGGFKQSGFGRELGEEGLEEYT 469
|
....*..
gi 188219757 518 RRSTCTI 524
Cdd:cd07091 470 QVKAVTI 476
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
71-524 |
1.80e-79 |
|
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: 256.50 E-value: 1.80e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWNI--WADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQ 148
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 149 EYVDVCDYAAGLSRMIGGPT---LPSERPGHALIEmwnPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSl 225
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSynnLGDDMLGLVLRE---PIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 226 vsvAVTKIIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAII 304
Cdd:cd07118 160 ---GTTLMLAELLIEAGLPAGVVNIVTGyGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 305 AFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRA 384
Cdd:cd07118 237 VFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 385 VEEAKKQGGTVVYGGKVMDH-PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 463
Cdd:cd07118 317 VDAGRAEGATLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 188219757 464 LGRIFrwLGPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 524
Cdd:cd07118 397 IDTAL--TVARRIRAGTVWVNtFLDGSPEL--PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
56-469 |
1.59e-78 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 254.45 E-value: 1.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW-GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSL 134
Cdd:PRK13473 8 NGELvAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 135 EMGK-ILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGN 213
Cdd:PRK13473 88 NCGKpLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 214 VCLWKGAPTTSLVSVAVtkiiAQVLEDNLLPGAIcSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVAlmvqERFGK 292
Cdd:PRK13473 168 TVVLKPSEITPLTALKL----AELAADILPPGVL-NVVTGrGATVGDALVGHPKVRMVSLTGSIATGKHVL----SAAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 293 SL----LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNIL 368
Cdd:PRK13473 239 SVkrthLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 369 YGPLHTKQAVSMFVRAVEEAKKQG-GTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEW 447
Cdd:PRK13473 319 LGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRW 398
|
410 420
....*....|....*....|..
gi 188219757 448 NNEVKQGLSSSIFTKDLGRIFR 469
Cdd:PRK13473 399 ANDSDYGLASSVWTRDVGRAHR 420
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
56-509 |
1.31e-77 |
|
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: 252.11 E-value: 1.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKRGEIVRKIGDAFREKIQLLGRL 131
Cdd:cd07139 4 GGRWvaPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDngPWPRLSPAERAAVLRRLADALEARADELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 132 VSLEMGK-ILVEGIGEVQEYVDVCDYAAGLSRmigGPTLPSERP----GHALI--EmwnPLGLVGIITAFNFPVAVFGWN 204
Cdd:cd07139 84 WTAENGMpISWSRRAQGPGPAALLRYYAALAR---DFPFEERRPgsggGHVLVrrE---PVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 205 NAIALITGNVCLWKGAPTTSLVSVavtkIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVAL 284
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAY----LLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 285 MVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWD 364
Cdd:cd07139 234 VCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 365 PNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHP--GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEE 442
Cdd:cd07139 314 PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLdrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 443 EVFEWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVNIPTSgaEIGGAFGGEKHTGGGRESG 509
Cdd:cd07139 394 DAVRIANDSDYGLSGSVWTADVERglaVARRI-----RTGTVGVNGFRL--DFGAPFGGFKQSGIGREGG 456
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
56-518 |
7.24e-77 |
|
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: 250.10 E-value: 7.24e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNI--WADIPAPKRGEIVRKIGDAFREKIQLLGRL 131
Cdd:cd07142 9 NGQFvdAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 132 VSLEMGKILVEG-IGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIeMWNPLGLVGIITAFNFPVAVFGWNNAIALI 210
Cdd:cd07142 89 ETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYT-LHEPIGVVGQIIPWNFPLLMFAWKVGPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 211 TGNVCLWKGAPTTSLVSVAVTKIIAQVLednlLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVA-LMVQE 288
Cdd:cd07142 168 CGNTIVLKPAEQTPLSALLAAKLAAEAG----LPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMqLAAKS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 289 RFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNIL 368
Cdd:cd07142 244 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 369 YGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWN 448
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 449 NEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:cd07142 404 NNSKYGLAAGVFSKNIDTANTLS--RALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
66-507 |
7.25e-77 |
|
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: 249.66 E-value: 7.25e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 66 ITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIG 145
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 146 EVQEYVDVCDYAAGLSRMIGGPTLPSE----RPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 221
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 222 TTSLVSVAVTKIIaqvLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKevALMVQERFGKSLLELGGNN 301
Cdd:cd07094 161 KTPLSALELAKIL---VEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGE--ALRANAGGKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 302 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 381
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 382 VRAVEEAKKQGGTVVYGGKvmdHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT 461
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 188219757 462 KDLGRIFRwlGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRE 507
Cdd:cd07094 393 RDLNVAFK--AAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGRE 436
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
56-508 |
8.62e-76 |
|
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: 247.37 E-value: 8.62e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 133
Cdd:cd07117 6 NGEWvkGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 134 LEMGKILVEGIGevqeyVDVcDYAAGLSRMIGGPTLPSERPGHAL------IEMWNPLGLVGIITAFNFPVAVFGWNNAI 207
Cdd:cd07117 86 LDNGKPIRETRA-----VDI-PLAADHFRYFAGVIRAEEGSANMIdedtlsIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 208 ALITGNVCLWKGAPTTSLVSVAVTKIIAQVLednllPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMV 286
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDVL-----PKGVVNIVTGkGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 287 QERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPN 366
Cdd:cd07117 235 AKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 367 ILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEE 442
Cdd:cd07117 315 TQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTED 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 443 EVFEWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRES 508
Cdd:cd07117 395 EVIDMANDSEYGLGGGVFTKDINRALRV--ARAVETGRVWVNtynqIPA-----GAPFGGYKKSGIGRET 457
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
56-517 |
1.02e-75 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 247.51 E-value: 1.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 133
Cdd:PRK11241 16 NGEWldANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 134 LEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGN 213
Cdd:PRK11241 96 LEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 214 VCLWKGAPTTSLVSVAvtkiIAQVLEDNLLPGAICSLVCGGA-DIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGK 292
Cdd:PRK11241 176 TMVLKPASQTPFSALA----LAELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 293 SLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPL 372
Cdd:PRK11241 252 VSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 373 HTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVK 452
Cdd:PRK11241 332 IDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTE 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219757 453 QGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIgGAFGGEKHTGGGRESGSDAWKQYM 517
Cdd:PRK11241 412 FGLAAYFYARDLSRVFRV--GEALEYGIVGINTGIISNEV-APFGGIKASGLGREGSKYGIEDYL 473
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
56-525 |
2.82e-74 |
|
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: 243.25 E-value: 2.82e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW-GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWA-DIPAPKRGEIVRKIGDAFREKIQLLGRLVS 133
Cdd:cd07082 7 NGEWkESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWpTMPLEERIDCLHKFADLLKENKEEVANLLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 134 LEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHAL----IEMWNPLGLVGIITAFNFPVavfgwNNAI-- 207
Cdd:cd07082 87 WEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaQVRREPLGVVLAIGPFNYPL-----NLTVsk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 208 ---ALITGNVCLWKGAPTTSLVSVavtkIIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVG---K 280
Cdd:cd07082 162 lipALIMGNTVVFKPATQGVLLGI----PLAEAFHDAGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGnrlK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 281 EVALMVQerfgkSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVG 360
Cdd:cd07082 238 KQHPMKR-----LVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 361 NPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDhpGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQD 440
Cdd:cd07082 313 MPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVND 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 441 EEEVFEWNNEVKQGLSSSIFTKDLGRIF---RWLgpkgsDCGIVNVNIPTS-GAEIgGAFGGEKHTGGGRESGSDAWKQY 516
Cdd:cd07082 391 IEEAIELANKSNYGLQASIFTKDINKARklaDAL-----EVGTVNINSKCQrGPDH-FPFLGRKDSGIGTQGIGDALRSM 464
|
....*....
gi 188219757 517 MRRSTCTIN 525
Cdd:cd07082 465 TRRKGIVIN 473
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
63-518 |
1.25e-73 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 242.09 E-value: 1.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 63 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVE 142
Cdd:PRK13252 21 GETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 143 GI-GEVQEYVDVCDYAAGLSRMIGGPTLPSeRPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 221
Cdd:PRK13252 101 TSvVDIVTGADVLEYYAGLAPALEGEQIPL-RGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 222 TTSLVSVAvtkiIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 301
Cdd:PRK13252 180 VTPLTALK----LAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 302 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 381
Cdd:PRK13252 256 PLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 382 VRAVEEAKKQGGTVVYGGKVMDH----PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSS 457
Cdd:PRK13252 336 LGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAA 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188219757 458 SIFTKDLGRIFRWLGpkGSDCGIVNVNipTSG---AEIggAFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:PRK13252 416 GVFTADLSRAHRVIH--QLEAGICWIN--TWGespAEM--PVGGYKQSGIGRENGIATLEHYTQ 473
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
71-526 |
2.28e-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: 241.19 E-value: 2.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAW-NIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGK-ILVEGIGEVQ 148
Cdd:cd07113 22 PATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKsIHLSRAFEVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 149 EYVDVCDYAAGLSRMIGG----PTLPSerPGHALIEMWN---PLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 221
Cdd:cd07113 102 QSANFLRYFAGWATKINGetlaPSIPS--MQGERYTAFTrrePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 222 TTSLVSVAvtkiIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 301
Cdd:cd07113 180 FTPLTLLR----VAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 302 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 381
Cdd:cd07113 256 AAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 382 VRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT 461
Cdd:cd07113 336 CSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWT 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219757 462 KDLGRIFRWLgPKgSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 526
Cdd:cd07113 416 NNLSKALRYI-PR-IEAGTVWVNMHTF-LDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY 477
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
56-507 |
7.73e-73 |
|
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: 239.55 E-value: 7.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 133
Cdd:cd07559 6 NGEWvaPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 134 LEMGKILVEGIG-EVQEYVDVCDYAAGLSR-------MIGGPTLPserpghalIEMWNPLGLVGIITAFNFPVAVFGWNN 205
Cdd:cd07559 86 LDNGKPIRETLAaDIPLAIDHFRYFAGVIRaqegslsEIDEDTLS--------YHFHEPLGVVGQIIPWNFPLLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 206 AIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLednllPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVAL 284
Cdd:cd07559 158 APALAAGNTVVLKPASQTPLSILVLMELIGDLL-----PKGVVNVVTGfGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 285 MVQERFGKSLLELGGNNAIIAFEDA-------DLSLVVPSVLFAAvgTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQI 357
Cdd:cd07559 233 YAAENLIPVTLELGGKSPNIFFDDAmdadddfDDKAEEGQLGFAF--NQGEVCTCPSRALVQESIYDEFIERAVERFEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 358 RVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPIL 433
Cdd:cd07559 311 KVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVL 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219757 434 YVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRE 507
Cdd:cd07559 391 AVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRV--ARGIQTGRVWVNcyhqYPA-----HAPFGGYKKSGIGRE 461
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
56-486 |
3.65e-72 |
|
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: 237.80 E-value: 3.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 133
Cdd:cd07085 6 NGEWveSKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLIT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 134 LEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGN 213
Cdd:cd07085 86 LEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 214 VCLWKGAPTTSLVSVavtkIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEvalmVQER---F 290
Cdd:cd07085 166 TFVLKPSERVPGAAM----RLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEY----IYERaaaN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 291 GKSLLELGG-NNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILY 369
Cdd:cd07085 238 GKRVQALGGaKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 370 GPLHTKQAVSMFVRAVEEAKKQGGTVVYGG---KVMDHP-GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVF 445
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVLDGrgvKVPGYEnGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 188219757 446 EWNNEVKQGLSSSIFTKD--LGRIFRwlgpKGSDCGIVNVNIP 486
Cdd:cd07085 398 AIINANPYGNGAAIFTRSgaAARKFQ----REVDAGMVGINVP 436
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
63-526 |
8.23e-72 |
|
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: 237.39 E-value: 8.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 63 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAW--NIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKIL 140
Cdd:cd07140 20 GKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFenGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 141 VEGIG-EVQEYVDVCDYAAGLSRMIGGPTLP--SERPGHAL-IEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCL 216
Cdd:cd07140 100 TLALKtHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 217 WKGAPTTSLVSVAVTKIIAQ------VLedNLLPGAicslvcgGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQE-R 289
Cdd:cd07140 180 LKPAQVTPLTALKFAELTVKagfpkgVI--NILPGS-------GSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVsN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 290 FGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILY 369
Cdd:cd07140 251 LKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 370 GPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDE--EEVFEW 447
Cdd:cd07140 331 GPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQR 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188219757 448 NNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 526
Cdd:cd07140 411 ANDTEYGLASGVFTKDINKALYV--SDKLEAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIEY 486
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
41-525 |
1.44e-71 |
|
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: 236.54 E-value: 1.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 41 WLQDLGLREDNEGVYNGSwggrGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAW-NIWADIPAPKRGEIVRKIGD 119
Cdd:cd07144 4 YDQPTGLFINNEFVKSSD----GETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFeSWWSKVTGEERGELLDKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 120 AFREKIQLLGRLVSLEMGKIL-VEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIeMWNPLGLVGIITAFNFPV 198
Cdd:cd07144 80 LVEKNRDLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYT-LHEPYGVCGQIIPWNYPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 199 AVFGWNNAIALITGNVCLWKGAPTTSLvSVAVtkiIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQ 277
Cdd:cd07144 159 AMAAWKLAPALAAGNTVVIKPAENTPL-SLLY---FANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 278 VGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSlvvPSVLFAAVG---TAGQRCTTVRRLFLHESIHNEVVDRLRSAY 354
Cdd:cd07144 235 TGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLD---QAVKWAAAGimyNSGQNCTATSRIYVQESIYDKFVEKFVEHV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 355 SQI-RVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGG---KVMDHPGNYVEPTIVTGLAHDAPIVHQETFA 430
Cdd:cd07144 312 KQNyKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 431 PILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGS 510
Cdd:cd07144 392 PVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVA--RELEAGMVWIN-SSNDSDVGVPFGGFKMSGIGRELGE 468
|
490
....*....|....*
gi 188219757 511 DAWKQYMRRSTCTIN 525
Cdd:cd07144 469 YGLETYTQTKAVHIN 483
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
77-517 |
3.12e-70 |
|
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: 231.80 E-value: 3.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 77 IARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDY 156
Cdd:cd07152 4 LGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 157 AAGLSRMIGGPTLPSErPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTslvsvAVTK--II 234
Cdd:cd07152 84 AAGLPTQPQGEILPSA-PGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRT-----PVSGgvVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 235 AQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLV 314
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 315 VPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGT 394
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 395 VVYGGKvmdHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRwLGPK 474
Cdd:cd07152 318 LEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA-LADR 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 188219757 475 gSDCGIVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSDAWKQYM 517
Cdd:cd07152 394 -LRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFT 436
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
49-525 |
9.09e-69 |
|
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: 228.95 E-value: 9.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 49 EDNEGVY-NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNI-WA-DIPAPKRGEIVRKIGDAFRE 123
Cdd:cd07143 4 EQPTGLFiNGEFvdSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGlKVSGSKRGRCLSKLADLMER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 124 KIQLLGRLVSLEMGK-ILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLP--SERPGHALIEmwnPLGLVGIITAFNFPVAV 200
Cdd:cd07143 84 NLDYLASIEALDNGKtFGTAKRVDVQASADTFRYYGGWADKIHGQVIEtdIKKLTYTRHE---PIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 201 FGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAqvlEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGK 280
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIP---EAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 281 evalMVQERFGKS-----LLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYS 355
Cdd:cd07143 238 ----KVMEAAAKSnlkkvTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 356 QIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYV 435
Cdd:cd07143 314 KLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 436 FKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLGP-KGSDCGIVNVNIPTSGAeiggAFGGEKHTGGGRESGSDAWK 514
Cdd:cd07143 394 IKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANAlKAGTVWVNCYNLLHHQV----PFGGYKQSGIGRELGEYALE 469
|
490
....*....|.
gi 188219757 515 QYMRRSTCTIN 525
Cdd:cd07143 470 NYTQIKAVHIN 480
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
70-517 |
1.40e-68 |
|
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: 227.96 E-value: 1.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 70 CPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQE 149
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 150 YVDVCDYAAGLSRMIggptLPSERPGHAL------IEMWNPLGLVGIITAFNFPVAVfGWNNAI-ALITGNVCLWKGAPT 222
Cdd:cd07101 82 VAIVARYYARRAERL----LKPRRRRGAIpvltrtTVNRRPKGVVGVISPWNYPLTL-AVSDAIpALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 223 TSLVSVAVtkiiAQVLEDNLLPGAICSLVCG-GADIGTTMArdERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 301
Cdd:cd07101 157 TALTALWA----VELLIEAGLPRDLWQVVTGpGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 302 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 381
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 382 VRAVEEAKKQGGTVVYGGKVMDHPGNYV-EPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIF 460
Cdd:cd07101 311 TAHVDDAVAKGATVLAGGRARPDLGPYFyEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVW 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 188219757 461 TKDLGRIfRWLGPKgSDCGIVNVN--IPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 517
Cdd:cd07101 391 TRDGARG-RRIAAR-LRAGTVNVNegYAAAWASIDAPMGGMKDSGLGRRHGAEGLLKYT 447
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
63-524 |
1.76e-68 |
|
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: 228.39 E-value: 1.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 63 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNI---WADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGK- 138
Cdd:cd07141 21 GKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 139 ILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIeMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWK 218
Cdd:cd07141 101 FSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYT-RHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 219 GAPTTSLVSVAVTKIIAqvlEDNLLPGAIcSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKevalMVQERFGKS---- 293
Cdd:cd07141 180 PAEQTPLTALYLASLIK---EAGFPPGVV-NVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGK----LIQQAAGKSnlkr 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 294 -LLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPL 372
Cdd:cd07141 252 vTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 373 HTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVK 452
Cdd:cd07141 332 IDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTT 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 188219757 453 QGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAeIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 524
Cdd:cd07141 412 YGLAAAVFTKDIDKAITF--SNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
71-509 |
1.92e-68 |
|
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: 227.62 E-value: 1.92e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 150
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 151 VDVCDYAAGLS---RMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVS 227
Cdd:cd07110 84 AGCFEYYADLAeqlDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 228 VAVTKIIAQVledNLLPGAICsLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAF 306
Cdd:cd07110 164 LELAEIAAEA---GLPPGVLN-VVTGtGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 307 EDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVE 386
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 387 EAKKQGGTVVYGGKVMDHP--GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDL 464
Cdd:cd07110 320 RGKEEGARLLCGGRRPAHLekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 188219757 465 GRIFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRESG 509
Cdd:cd07110 400 ERCDRV--AEALEAGIVWINCSQP-CFPQAPWGGYKRSGIGRELG 441
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
63-517 |
4.61e-67 |
|
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: 224.02 E-value: 4.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 63 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKIL 140
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 141 VEGI-GEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMwNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKG 219
Cdd:cd07112 81 SDALaVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITR-EPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 220 APTTSLvsvavTKI-IAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKevalMVQERFGKS---- 293
Cdd:cd07112 160 AEQSPL-----TALrLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGR----RFLEYSGQSnlkr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 294 -LLELGGNNAIIAFEDA-DLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGP 371
Cdd:cd07112 231 vWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 372 LHTKQAVSMFVRAVEEAKKQGGTVVYGGKV--MDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNN 449
Cdd:cd07112 311 LVSEAHFDKVLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALAN 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219757 450 EVKQGLSSSIFTKDLGRIFRwlGPKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 517
Cdd:cd07112 391 DSVYGLAASVWTSDLSRAHR--VARRLRAGTVWVNC-FDEGDITTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
115-469 |
5.47e-67 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 222.30 E-value: 5.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 115 RKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAF 194
Cdd:PRK10090 2 RKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 195 NFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLednlLPGAICSLVCG-GADIGTTMARDERVNLLSFT 273
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIG----LPKGVFNLVLGrGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 274 GSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSA 353
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 354 YSQIRVGNPWD-PNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPI 432
Cdd:PRK10090 238 MQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 188219757 433 LYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFR 469
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMK 354
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
71-466 |
1.61e-66 |
|
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: 222.12 E-value: 1.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 150
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 151 VDVCDYAAGLSRMIGGPTLPSERPG-HALIEMwNPLGLVGIITAFNFP--VAVfgwnNAI--ALITGNVCLWKGAPTTSL 225
Cdd:cd07102 83 LERARYMISIAEEALADIRVPEKDGfERYIRR-EPLGVVLIIAPWNYPylTAV----NAVipALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 226 VSVAvtkiIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIA 305
Cdd:cd07102 158 CGER----FAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 306 FEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVsMFVRA- 384
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAA-DFVRAq 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 385 VEEAKKQGGTVVYGGK---VMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT 461
Cdd:cd07102 313 IADAIAKGARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWT 392
|
....*
gi 188219757 462 KDLGR 466
Cdd:cd07102 393 KDIAR 397
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
35-520 |
9.78e-66 |
|
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: 221.12 E-value: 9.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 35 HHPQYAWLQDlglREDNEGVY-NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRG 111
Cdd:cd07111 8 AACALAWLDA---HDRSFGHFiNGKWvkPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 112 EIVRKIGDAFREKIQLLGRLVSLEMGKilveGIGEVQEyVDVCDYAAGLSRMIG-GPTLPSERPGhaliemWNPLGLVGI 190
Cdd:cd07111 85 RHLYRIARHIQKHQRLFAVLESLDNGK----PIRESRD-CDIPLVARHFYHHAGwAQLLDTELAG------WKPVGVVGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 191 ITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVledNLLPGaICSLVCGGADIGTTMARDERVNLL 270
Cdd:cd07111 154 IVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEA---GLPPG-VLNIVTGNGSFGSALANHPGVDKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 271 SFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRL 350
Cdd:cd07111 230 AFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 351 RSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFA 430
Cdd:cd07111 310 KERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 431 PILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRwLGPkGSDCGIVNVNI-----PTSGaeiggaFGGEKHTGGG 505
Cdd:cd07111 390 PVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALE-VAL-SLKAGVVWINGhnlfdAAAG------FGGYRESGFG 461
|
490
....*....|....*
gi 188219757 506 RESGSDAWKQYMRRS 520
Cdd:cd07111 462 REGGKEGLYEYLRPS 476
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
56-517 |
2.25e-65 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 220.76 E-value: 2.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW-----GGRGEVITtycPANNEPIARVRQASLKDYEETIGKAKKAWNI-----WADIPAPKRGEIVRKIGDAFREKI 125
Cdd:PLN02467 13 GGEWrepvlGKRIPVVN---PATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 126 QLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGP-----TLPSER-PGHALiemWNPLGLVGIITAFNFPVA 199
Cdd:PLN02467 90 SELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKqkapvSLPMETfKGYVL---KEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 200 VFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVledNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVG 279
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREV---GLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 280 KEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRV 359
Cdd:PLN02467 244 RKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 360 GNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDH--PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFK 437
Cdd:PLN02467 324 SDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 438 FQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN--------IPtsgaeiggaFGGEKHTGGGRESG 509
Cdd:PLN02467 404 FSTEDEAIELANDSHYGLAGAVISNDLERCERV--SEAFQAGIVWINcsqpcfcqAP---------WGGIKRSGFGRELG 472
|
....*...
gi 188219757 510 SDAWKQYM 517
Cdd:PLN02467 473 EWGLENYL 480
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
54-519 |
4.64e-65 |
|
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: 219.76 E-value: 4.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 54 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLV 132
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 133 SLEMGKILVEGIGEVQEYVDVCDYAAGLS-RMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALIT 211
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYYARAAlRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 212 GNVCLWKGAPTTSLVSVAVTKIIAQVledNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQER-- 289
Cdd:cd07083 182 GNTVIAKPAEDAVVVGYKVFEIFHEA---GFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLap 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 290 ----FGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDP 365
Cdd:cd07083 259 gqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 366 NILYGPLHTKQAVSMFVRAVEEAkKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEE--E 443
Cdd:cd07083 339 GTDLGPVIDAEQEAKVLSYIEHG-KNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaE 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188219757 444 VFEWNNEVKQGLSSSIFTKDLGRIfRWLGPKgSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdawKQYMRR 519
Cdd:cd07083 418 ALEVANSTPYGLTGGVYSRKREHL-EEARRE-FHVGNLYINRKITGALVGvQPFGGFKLSGTNAKTGG---PHYLRR 489
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
60-511 |
3.27e-62 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 212.82 E-value: 3.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 60 GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKI 139
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 140 LVEGIGEVQEYVDVCDY----AAGLSRmiggptlPSERPGhAL------IEMWNPLGLVGIITAFNFPVAVfGWNNAI-A 208
Cdd:PRK09407 108 RRHAFEEVLDVALTARYyarrAPKLLA-------PRRRAG-ALpvltktTELRQPKGVVGVISPWNYPLTL-AVSDAIpA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 209 LITGNVCLWKGAPTTSLVSVAVtkiiAQVLEDNLLPGAICSLVCG-GADIGTTMArdERVNLLSFTGSTQVGKEVAlmvq 287
Cdd:PRK09407 179 LLAGNAVVLKPDSQTPLTALAA----VELLYEAGLPRDLWQVVTGpGPVVGTALV--DNADYLMFTGSTATGRVLA---- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 288 ERFGKSL----LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPW 363
Cdd:PRK09407 249 EQAGRRLigfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 364 DPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYV-EPTIVTGLAHDAPIVHQETFAPILYVFKFQDEE 442
Cdd:PRK09407 329 DYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGPLFyEPTVLTGVTPDMELAREETFGPVVSVYPVADVD 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219757 443 EVFEWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVN---IPTSGAeIGGAFGGEKHTGGGRESGSD 511
Cdd:PRK09407 409 EAVERANDTPYGLNASVWTGDTARgraIAARI-----RAGTVNVNegyAAAWGS-VDAPMGGMKDSGLGRRHGAE 477
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
56-509 |
3.28e-62 |
|
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: 211.21 E-value: 3.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW-----GGRGEVIttyCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGR 130
Cdd:cd07138 4 DGAWvapagTETIDVI---NPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 131 LVSLEMG-------KILVE-GIGEVQEYVDVC-DYAAglsrmiggptlpSERPGHALIEMwNPLGLVGIITAFNFPVavf 201
Cdd:cd07138 81 AITLEMGapitlarAAQVGlGIGHLRAAADALkDFEF------------EERRGNSLVVR-EPIGVCGLITPWNWPL--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 202 gwnNAI------ALITGNVCLWKG---APTTSLvsvavtkIIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLS 271
Cdd:cd07138 145 ---NQIvlkvapALAAGCTVVLKPsevAPLSAI-------ILAEILDEAGLPAGVFNLVNGdGPVVGEALSAHPDVDMVS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 272 FTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLR 351
Cdd:cd07138 215 FTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 352 SAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGkvMDHP-----GNYVEPTIVTGLAHDAPIVHQ 426
Cdd:cd07138 295 AAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG--PGRPeglerGYFVKPTVFADVTPDMTIARE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 427 ETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVNipTSGAEIGGAFGGEKHTG 503
Cdd:cd07138 373 EIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERaraVARRL-----RAGQVHIN--GAAFNPGAPFGGYKQSG 445
|
....*.
gi 188219757 504 GGRESG 509
Cdd:cd07138 446 NGREWG 451
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
95-512 |
4.91e-62 |
|
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: 209.82 E-value: 4.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 95 AKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRmiggptlpsERP 174
Cdd:cd07095 9 ARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYH---------ERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 175 GHALIEMWN--------PLGLVGIITAFNFPVAVFgwNNAI--ALITGNVCLWKGAPTTSlvsvAVTKIIAQVLEDNLLP 244
Cdd:cd07095 80 GERATPMAQgravlrhrPHGVMAVFGPFNFPGHLP--NGHIvpALLAGNTVVFKPSELTP----AVAELMVELWEEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 245 GAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSL-LELGGNNAIIAFEDADLSLVVPSVLFAAV 323
Cdd:cd07095 154 PGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 324 GTAGQRCTTVRRLFLHES-IHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVM 402
Cdd:cd07095 234 LTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 403 DHPGNYVEPTI--VTGLahdAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDlGRIFRWLGPKgSDCGI 480
Cdd:cd07095 314 VAGTAFLSPGIidVTDA---ADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDD-EALFERFLAR-IRAGI 388
|
410 420 430
....*....|....*....|....*....|..
gi 188219757 481 VNVNIPTSGAEIGGAFGGEKHTGGGRESGSDA 512
Cdd:cd07095 389 VNWNRPTTGASSTAPFGGVGLSGNHRPSAYYA 420
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
35-509 |
8.59e-61 |
|
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: 208.97 E-value: 8.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 35 HHPQYAWLQDLGLREDNEG----VYNGSWGGRGEVITTYCPANNE-PIARVRQASLKDYEETIGKAKKAWNIWADIPAPK 109
Cdd:cd07125 13 EVPLEALADALKAFDEKEWeaipIINGEETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 110 RGEIVRKIGDAFRE-KIQLLGrLVSLEMGKILVEGIGEVQEYVDVCD-YAAGLSRMIGGPTLPS---ERPGHalieMWNP 184
Cdd:cd07125 93 RAEILEKAADLLEAnRGELIA-LAAAEAGKTLADADAEVREAIDFCRyYAAQARELFSDPELPGptgELNGL----ELHG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 185 LGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIiaqvLEDNLLPGAICSLV-CGGADIGTTMAR 263
Cdd:cd07125 168 RGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVEL----LHEAGVPRDVLQLVpGDGEEIGEALVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 264 DERVNLLSFTGSTQVGKEVALMVQERFGKSLL---ELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHE 340
Cdd:cd07125 244 HPRIDGVIFTGSTETAKLINRALAERDGPILPliaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 341 SIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMfVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGlahD 420
Cdd:cd07125 324 EIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKL-LRAHTELMRGEAWLIAPAPLDDGNGYFVAPGIIEI---V 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 421 APIVHQ-ETFAPILYV--FKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAeIGGA-- 495
Cdd:cd07125 400 GIFDLTtEVFGPILHVirFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWR--ERVEAGNLYINRNITGA-IVGRqp 476
|
490
....*....|....
gi 188219757 496 FGGEKHTGGGRESG 509
Cdd:cd07125 477 FGGWGLSGTGPKAG 490
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
63-518 |
1.46e-59 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 205.05 E-value: 1.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 63 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKIL 140
Cdd:PLN02766 35 GKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 141 VEGigevqEYVDV------CDYAAGLSRMIGGPTLPSERP--GHALIEmwnPLGLVGIITAFNFPVAVFGWNNAIALITG 212
Cdd:PLN02766 115 ALG-----KAVDIpaaaglLRYYAGAADKIHGETLKMSRQlqGYTLKE---PIGVVGHIIPWNFPSTMFFMKVAPALAAG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 213 NVCLWKGAPTTSLVSVavtkIIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFG 291
Cdd:PLN02766 187 CTMVVKPAEQTPLSAL----FYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 292 KSL-LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYG 370
Cdd:PLN02766 263 KQVsLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 371 PLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNE 450
Cdd:PLN02766 343 PQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANN 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188219757 451 VKQGLSSSIFTKDL---GRIFRWLgpkgsDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:PLN02766 423 TKYGLAAGIVTKDLdvaNTVSRSI-----RAGTIWVNC-YFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
87-524 |
7.76e-57 |
|
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: 195.87 E-value: 7.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 87 DYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMG------KILVEGIGEVQEyvdvcDYAAGL 160
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGataawaGFNVDLAAGMLR-----EAASLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 161 SRMIGGpTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAvtkiIAQVLED 240
Cdd:cd07105 76 TQIIGG-SIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWL----IGRVFHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 241 NLLP-GAICSLVCGGAD---IGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVP 316
Cdd:cd07105 151 AGLPkGVLNVVTHSPEDapeVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 317 SVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRvgnpWDPNILyGPLHTKQAVSMFVRAVEEAKKQGGTVV 396
Cdd:cd07105 231 AALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLF----AGPVVL-GSLVSAAAADRVKELVDDALSKGAKLV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 397 YGGKVMDHP-GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRwLGpKG 475
Cdd:cd07105 306 VGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALA-VA-KR 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 188219757 476 SDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 524
Cdd:cd07105 384 IESGAVHINGMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
54-469 |
1.57e-56 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 197.46 E-value: 1.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 54 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLV 132
Cdd:PRK03137 40 IIGGERITTEDKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 133 SLEMGKILVEGIGEVQEYVDVCDYAAglSRMI----GGPTLPseRPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIA 208
Cdd:PRK03137 120 VKEAGKPWAEADADTAEAIDFLEYYA--RQMLkladGKPVES--RPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 209 LITGNVCLWKGAPTTSLVSVAVtkiiAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVG---KEVAL 284
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKF----VEVLEEAGLPAGVVNFVPGsGSEVGDYLVDHPKTRFITFTGSREVGlriYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 285 MVQE--RFGKS-LLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGN 361
Cdd:PRK03137 272 KVQPgqIWLKRvIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 362 PWDPNILyGPLHTKQAVSMFVRAVEEAKKQgGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDE 441
Cdd:PRK03137 352 PEDNAYM-GPVINQASFDKIMSYIEIGKEE-GRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420
....*....|....*....|....*...
gi 188219757 442 EEVFEWNNEVKQGLSSSIFTKDLGRIFR 469
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEK 457
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
69-509 |
4.11e-56 |
|
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: 194.83 E-value: 4.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 69 YCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEG-IGEV 147
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 148 qeyVDVCDYAAGLSRMiGGPTL-PSERPGHALieMW--------NPLGLVGIITAFNFPVAVFgWNNAI-ALITGNVCLW 217
Cdd:cd07098 81 ---LVTCEKIRWTLKH-GEKALrPESRPGGLL--MFykrarveyEPLGVVGAIVSWNYPFHNL-LGPIIaALFAGNAIVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 218 KGAPTTSLVSVAVTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLEL 297
Cdd:cd07098 154 KVSEQVAWSSGFFLSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 298 GGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQA 377
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 378 VSMFVRAVEEAKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQ 453
Cdd:cd07098 314 FDRLEELVADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEY 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 188219757 454 GLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNiptsgaEIGGA-------FGGEKHTGGGRESG 509
Cdd:cd07098 394 GLGASVFGKDIKRARRIA--SQLETGMVAIN------DFGVNyyvqqlpFGGVKGSGFGRFAG 448
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
63-518 |
3.02e-55 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 194.64 E-value: 3.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 63 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKIL 140
Cdd:PLN02466 72 GKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 141 VEGIG-EVQEYVDVCDYAAGLSRMIGGPTLPSERPgHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKG 219
Cdd:PLN02466 152 EQSAKaELPMFARLFRYYAGWADKIHGLTVPADGP-HHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 220 APTTSLVSVAVTKIIaqvLEDNLLPGaICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKevalMVQERFGKS----- 293
Cdd:PLN02466 231 AEQTPLSALYAAKLL---HEAGLPPG-VLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGK----IVLELAAKSnlkpv 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 294 LLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLH 373
Cdd:PLN02466 303 TLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQI 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 374 TKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQ 453
Cdd:PLN02466 383 DSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRY 462
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188219757 454 GLSSSIFTKDL---GRIFRWLgpkgsDCGIVNVN--------IPtsgaeiggaFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:PLN02466 463 GLAAGVFTQNLdtaNTLSRAL-----RVGTVWVNcfdvfdaaIP---------FGGYKMSGIGREKGIYSLNNYLQ 524
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
71-507 |
7.41e-53 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 186.22 E-value: 7.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 150
Cdd:PRK13968 14 PATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 151 VDVCDYAA--GLSRMIGGPTLPSERpgHALIEmWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTslvsV 228
Cdd:PRK13968 94 ANLCDWYAehGPAMLKAEPTLVENQ--QAVIE-YRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV----M 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 229 AVTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFED 308
Cdd:PRK13968 167 GCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 309 ADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEA 388
Cdd:PRK13968 247 ADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 389 KKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIF 468
Cdd:PRK13968 327 LAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQAR 406
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 188219757 469 RWlgPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRE 507
Cdd:PRK13968 407 QM--AARLECGGVFINgYCASDARV--AFGGVKKSGFGRE 442
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
60-523 |
9.28e-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: 180.85 E-value: 9.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 60 GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKI 139
Cdd:TIGR01722 12 GASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 140 LVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKG 219
Cdd:TIGR01722 92 HSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 220 APTTSLVSVAVtkiiAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVaLMVQERFGKSLLELGG 299
Cdd:TIGR01722 172 SEKVPSAAVKL----AELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYI-HTTGSAHGKRVQALGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 300 -NNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIhNEVVDRLRSAYSQIRVGnPW-DPNILYGPLHTKQA 377
Cdd:TIGR01722 247 aKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIG-PGdDPGAEMGPLITPQA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 378 VSMFVRAVEEAKKQGGTVVYGG---KVMDHP-GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQ 453
Cdd:TIGR01722 325 KDRVASLIAGGAAEGAEVLLDGrgyKVDGYEeGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPY 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188219757 454 GLSSSIFTKDLG--RIFRWLgpkgSDCGIVNVNIPTSGAEIGGAFGGEKHT--GGGRESGSDAWKQYMRRSTCT 523
Cdd:TIGR01722 405 GNGTAIFTRDGAaaRRFQHE----IEVGQVGVNVPIPVPLPYFSFTGWKDSffGDHHIYGKQGTHFYTRGKTVT 474
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
63-442 |
1.93e-49 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 183.60 E-value: 1.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 63 GEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILV 141
Cdd:COG4230 569 GEARPVRNPADhSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLP 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 142 EGIGEVQEYVDVCDYAAGLSRmiggpTLPSERPGHAliemwnPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 221
Cdd:COG4230 649 DAIAEVREAVDFCRYYAAQAR-----RLFAAPTVLR------GRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAE 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 222 TTSLVSVAVTKII------AQVLedNLLPGAicslvcgGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLL 295
Cdd:COG4230 718 QTPLIAARAVRLLheagvpADVL--QLLPGD-------GETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVP 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 296 ---ELGGNNAIIAfedaDLS-L---VVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNIL 368
Cdd:COG4230 789 liaETGGQNAMIV----DSSaLpeqVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTD 864
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219757 369 YGPLHTKQAVSMFVRAVEEAKKQgGTVVYGGKVMDHP--GNYVEPTI--VTGLAHdapiVHQETFAPILYVFKFQDEE 442
Cdd:COG4230 865 VGPVIDAEARANLEAHIERMRAE-GRLVHQLPLPEECanGTFVAPTLieIDSISD----LEREVFGPVLHVVRYKADE 937
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
63-507 |
8.17e-49 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 175.31 E-value: 8.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 63 GEVITTYCPANNEPIarvrqaslkdyEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVE 142
Cdd:PRK09406 11 GETVKTFTALTDDEV-----------DAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 143 GIGEVQEYVDVCDYAAGlsrmiGGPTLPSERPGHA-------LIEMWNPLGLVGIITAFNFP---VAVFGwnnAIALITG 212
Cdd:PRK09406 80 AKAEALKCAKGFRYYAE-----HAEALLADEPADAaavgasrAYVRYQPLGVVLAVMPWNFPlwqVVRFA---APALMAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 213 NVCLWKGA---PTTSLVsvavtkiIAQVLEDNLLP-GAICSLVCGGADIGTTMaRDERVNLLSFTGSTQVGKEVALMVQE 288
Cdd:PRK09406 152 NVGLLKHAsnvPQTALY-------LADLFRRAGFPdGCFQTLLVGSGAVEAIL-RDPRVAAATLTGSEPAGRAVAAIAGD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 289 RFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNIL 368
Cdd:PRK09406 224 EIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 369 YGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWN 448
Cdd:PRK09406 304 VGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIA 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 449 NEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEIGgaFGGEKHTGGGRE 507
Cdd:PRK09406 384 NATTFGLGSNAWTRDEAEQERFI--DDLEAGQVFINgMTVSYPELP--FGGVKRSGYGRE 439
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
56-520 |
9.92e-49 |
|
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: 175.87 E-value: 9.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSWGGRGEVITTYCPANNEPI-ARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSL 134
Cdd:TIGR01238 43 GHSYKADGEAQPVTNPADRRDIvGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 135 EMGKILVEGIGEVQEYVDVCDYAAGLSRmiggPTLPSERPghaliemwNPLGLVGIITAFNFPVAVFGWNNAIALITGNV 214
Cdd:TIGR01238 123 EAGKTIHNAIAEVREAVDFCRYYAKQVR----DVLGEFSV--------ESRGVFVCISPWNFPLAIFTGQISAALAAGNT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 215 CLWKGAPTTSLVSvavTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERF---G 291
Cdd:TIGR01238 191 VIAKPAEQTSLIA---YRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdapV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 292 KSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGP 371
Cdd:TIGR01238 268 PLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 372 LHTKQAVSMFVRAVEEAKKQGGTV---VYGGKVMDHPGNYVEPTIVTglAHDAPIVHQETFAPILYVFKFQDEE--EVFE 446
Cdd:TIGR01238 348 VIDAEAKQNLLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAREldQIVD 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219757 447 WNNEVKQGLSSSIFTKDLGRIfRWLgPKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSDAWKQYMRRS 520
Cdd:TIGR01238 426 QINQTGYGLTMGVHSRIETTY-RWI-EKHARVGNCYVNRNQVGAVVGvQPFGGQGLSGTGPKAGGPHYLYRLTQV 498
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
56-508 |
8.42e-48 |
|
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: 173.02 E-value: 8.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSWGG--RGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 133
Cdd:cd07116 6 GGEWVApvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 134 LEMGKILVEGIG-EVQEYVDVCDYAAGLSRMIGG--PTLPSERPGHALIEmwnPLGLVGIITAFNFPVAVFGWNNAIALI 210
Cdd:cd07116 86 WDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGsiSEIDENTVAYHFHE---PLGVVGQIIPWNFPLLMATWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 211 TGNVCLWKGAPTTSLVSVAVTKIIAqvledNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQER 289
Cdd:cd07116 163 AGNCVVLKPAEQTPASILVLMELIG-----DLLPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 290 FGKSLLELGGNNAIIAFED---ADLSLVVPS----VLFAAvgTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNP 362
Cdd:cd07116 238 IIPVTLELGGKSPNIFFADvmdADDAFFDKAlegfVMFAL--NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 363 WDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGN-----YVEPTIVTGlaHDAPIVHQETFAPILYVFK 437
Cdd:cd07116 316 LDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggyYVPTTFKGG--NKMRIFQEEIFGPVLAVTT 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219757 438 FQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRES 508
Cdd:cd07116 394 FKDEEEALEIANDTLYGLGAGVWTRDGNTAYRM--GRGIQAGRVWTNcyhlYPA-----HAAFGGYKQSGIGREN 461
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
60-444 |
3.23e-45 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 171.15 E-value: 3.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 60 GGRGEVITTYCPANNE-PIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGK 138
Cdd:PRK11904 558 NGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGK 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 139 ILVEGIGEVQEYVDVCDYAAGLSR-MIGGPT-LPS---ERpghaliemwNPLGLVG-----IITAFNFPVAVFGWNNAIA 208
Cdd:PRK11904 638 TLQDAIAEVREAVDFCRYYAAQARrLFGAPEkLPGptgES---------NELRLHGrgvfvCISPWNFPLAIFLGQVAAA 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 209 LITGNVCLWKGAPTTSLVSVAVTK------IIAQVLEdnLLPGAicslvcgGADIGTTMARDERVNLLSFTGSTQVGKEV 282
Cdd:PRK11904 709 LAAGNTVIAKPAEQTPLIAAEAVKllheagIPKDVLQ--LLPGD-------GATVGAALTADPRIAGVAFTGSTETARII 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 283 ALMVQERFGKSL---LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRV 359
Cdd:PRK11904 780 NRTLAARDGPIVpliAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKV 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 360 GNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQgGTVVYGGKVMD--HPGNYVEPTI--VTGLAHdapiVHQETFAPILYV 435
Cdd:PRK11904 860 GDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPAgtENGHFVAPTAfeIDSISQ----LEREVFGPILHV 934
|
410
....*....|.
gi 188219757 436 --FKFQDEEEV 444
Cdd:PRK11904 935 irYKASDLDKV 945
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
71-519 |
4.30e-45 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 170.82 E-value: 4.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQE 149
Cdd:PRK11905 574 PADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVRE 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 150 YVDVCD-YAAGLSRMIGGPTLPserpghaliemwnPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLV-S 227
Cdd:PRK11905 654 AVDFLRyYAAQARRLLNGPGHK-------------PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIaA 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 228 VAVtkiiaQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLL---ELGGNNAI 303
Cdd:PRK11905 721 RAV-----RLLHEAGVPKDALQLLPGdGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAM 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 304 IAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVR 383
Cdd:PRK11905 796 IVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEA 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 384 AVEEAKKQgGTVVYGGKVMDH--PGNYVEPTI--VTGLAHdapiVHQETFAPILYV--FKFQDEEEVFEWNNEVKQGLSS 457
Cdd:PRK11905 876 HIEAMRAA-GRLVHQLPLPAEteKGTFVAPTLieIDSISD----LEREVFGPVLHVvrFKADELDRVIDDINATGYGLTF 950
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 188219757 458 SIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdawKQYMRR 519
Cdd:PRK11905 951 GLHSRIDETIAHVT--SRIRAGNIYVNRNIIGAVVGvQPFGGEGLSGTGPKAGG---PLYLGR 1008
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
56-508 |
6.75e-45 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 165.13 E-value: 6.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW-GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSL 134
Cdd:PRK09457 6 NGDWiAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 135 EMGKILVEGIGEVQEyvdvcdyaaglsrMIGGPTLP----SERPGHALIEMWN--------PLGLVGIITAFNFPvavfG 202
Cdd:PRK09457 86 ETGKPLWEAATEVTA-------------MINKIAISiqayHERTGEKRSEMADgaavlrhrPHGVVAVFGPYNFP----G 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 203 W--NNAI--ALITGNVCLWKGAPTTSlvsvAVTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQV 278
Cdd:PRK09457 149 HlpNGHIvpALLAGNTVVFKPSELTP----WVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 279 GkeVALMVQ--ERFGKSL-LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIH-NEVVDRLRSAY 354
Cdd:PRK09457 225 G--YLLHRQfaGQPEKILaLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 355 SQIRVGNPW-DPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTI--VTGLAhDAPivHQETFAP 431
Cdd:PRK09457 303 KRLTVGRWDaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIidVTGVA-ELP--DEEYFGP 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188219757 432 ILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 508
Cdd:PRK09457 380 LLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFL--LEIRAGIVNWNKPLTGASSAAPFGGVGASGNHRPS 454
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
71-505 |
1.10e-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: 163.74 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAK---KAWNIWadIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEV 147
Cdd:cd07148 6 PFDLKPIGEVPTVDWAAIDKALDTAHalfLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 148 QEYVDVCDYAAGLSRMIGGPTLP----SERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTT 223
Cdd:cd07148 84 TRAIDGVELAADELGQLGGREIPmgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 224 SLVSVAVTKIiaqvLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGkevaLMVQERFG---KSLLELGGN 300
Cdd:cd07148 164 PLSCLAFVDL----LHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVG----WMLRSKLApgtRCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 301 NAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSM 380
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 381 FVRAVEEAKKQGGTVVYGGKVMDHpgNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIF 460
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRLSD--TTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 188219757 461 TKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGG 505
Cdd:cd07148 394 TKDLDVALKAV--RRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
35-524 |
6.79e-43 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 159.68 E-value: 6.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 35 HHPQYAWLQDLGLREDNEGVYNGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKR 110
Cdd:PRK09847 4 HHLAYWQDKALSLAIENRLFINGEYtaAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 111 GEIVRKIGDAFREKIQLLGRLVSLEMGKIL-------VEGIGEVQEYvdvcdYAAGLSRMIG--GPTLPSERpghALIEM 181
Cdd:PRK09847 84 KAVLNKLADLMEAHAEELALLETLDTGKPIrhslrddIPGAARAIRW-----YAEAIDKVYGevATTSSHEL---AMIVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 182 wNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAvtkiIAQVLEDNLLPGAICSLVCG-GADIGTT 260
Cdd:PRK09847 156 -EPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIR----LAGLAKEAGLPDGVLNVVTGfGHEAGQA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 261 MARDERVNLLSFTGSTQVGKEVALMVQERFGKSL-LELGGNNAIIAFEDA-DLSLVVPSVLFAAVGTAGQRCTTVRRLFL 338
Cdd:PRK09847 231 LSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMKRVwLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 339 HESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLhTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGnYVEPTIVTGLA 418
Cdd:PRK09847 311 EESIADEFLALLKQQAQNWQPGHPLDPATTMGTL-IDCAHADSVHSFIREGESKGQLLLDGRNAGLAA-AIGPTIFVDVD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 419 HDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGaEIGGAFGG 498
Cdd:PRK09847 389 PNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRM--SRRLKAGSVFVNNYNDG-DMTVPFGG 465
|
490 500
....*....|....*....|....*.
gi 188219757 499 EKHTGGGRESGSDAWKQYMRRSTCTI 524
Cdd:PRK09847 466 YKQSGNGRDKSLHALEKFTELKTIWI 491
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
71-533 |
1.47e-40 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 154.90 E-value: 1.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 71 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 150
Cdd:PLN02419 136 PATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 151 VDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVav 230
Cdd:PLN02419 216 LEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASV-- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 231 tkIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDAD 310
Cdd:PLN02419 294 --ILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDAN 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 311 LSLVVPSVLFAAVGTAGQRCTTVRRLFL---HESIHNEVVDRLRSaysqIRVGNPWDPNILYGPLHTKQAVSMFVRAVEE 387
Cdd:PLN02419 372 IDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVERAKA----LKVTCGSEPDADLGPVISKQAKERICRLIQS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 388 AKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 463
Cdd:PLN02419 448 GVDDGAKLLLDGRDIVVPgyekGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSS 527
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188219757 464 --LGRIFRwlgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGR-----ESGSDAWKQYMRRSTCTINYSTSLPLA 533
Cdd:PLN02419 528 gaAARKFQ----MDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDlnfygKAGVDFFTQIKLVTQKQKDIHSPFSLA 600
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
56-466 |
5.48e-39 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 148.75 E-value: 5.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 133
Cdd:PLN00412 21 DGEWrtSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 134 LEMGKILVEGIGEVQEYVDVCDYAA--GLSRMIGGPTLPSER-PGHALIEMWN----PLGLVGIITAFNFPVAVFGWNNA 206
Cdd:PLN00412 101 KEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFLVSDSfPGNERNKYCLtskiPLGVVLAIPPFNYPVNLAVSKIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 207 IALITGNVCLWKgAPTTSLVSVAVTkiiAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGStqvgkEVALM 285
Cdd:PLN00412 181 PALIAGNAVVLK-PPTQGAVAALHM---VHCFHLAGFPKGLISCVTGkGSEIGDFLTMHPGVNCISFTGG-----DTGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 286 VQERFGKSLL--ELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPW 363
Cdd:PLN00412 252 ISKKAGMVPLqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 364 DpNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKvmdHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEE 443
Cdd:PLN00412 332 D-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWK---REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEE 407
|
410 420
....*....|....*....|...
gi 188219757 444 VFEWNNEVKQGLSSSIFTKDLGR 466
Cdd:PLN00412 408 GIHHCNASNFGLQGCVFTRDINK 430
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
77-509 |
1.57e-36 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 145.12 E-value: 1.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 77 IARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQ-LLGRLVSlEMGKILVEGIGEVQEYVDVCD 155
Cdd:PRK11809 673 VGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQtLMGLLVR-EAGKTFSNAIAEVREAVDFLR 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 156 YAAGLSRmiggPTLPSERpgHaliemwNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKII- 234
Cdd:PRK11809 752 YYAGQVR----DDFDNDT--H------RPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILl 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 235 -AQVLED--NLLPGAicslvcgGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERF---GKS---LLELGGNNAIIA 305
Cdd:PRK11809 820 eAGVPAGvvQLLPGR-------GETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqGRPiplIAETGGQNAMIV 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 306 FEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAV 385
Cdd:PRK11809 893 DSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHI 972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 386 EEAKKQGGTV---VYGGKVMDHPGNYVEPTIVTGLAHDApiVHQETFAPILYVFKFQDEE--EVFEWNNEVKQGLSSSIF 460
Cdd:PRK11809 973 QAMRAKGRPVfqaARENSEDWQSGTFVPPTLIELDSFDE--LKREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVH 1050
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 188219757 461 TK------------DLGRIFrwlgpkgsdcgiVNVNIptSGAEIG-GAFGGEKHTGGGRESG 509
Cdd:PRK11809 1051 TRidetiaqvtgsaHVGNLY------------VNRNM--VGAVVGvQPFGGEGLSGTGPKAG 1098
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
63-463 |
4.08e-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: 132.33 E-value: 4.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 63 GEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGD----AFREKI---QLLGRlvsl 134
Cdd:cd07123 45 GNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADllsgKYRYELnaaTMLGQ---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 135 emGKILVEG-IGEVQEYVDV----CDYAAGLSRmiggptlpsERPGHALIEMWN-----PL-GLVGIITAFNFpvavfgw 203
Cdd:cd07123 121 --GKNVWQAeIDAACELIDFlrfnVKYAEELYA---------QQPLSSPAGVWNrleyrPLeGFVYAVSPFNF------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 204 nNAIAL-------ITGNVCLWKGAPTTSLVSVAVTKIIaqvLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGST 276
Cdd:cd07123 183 -TAIGGnlagapaLMGNVVLWKPSDTAVLSNYLVYKIL---EEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGST 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 277 QVGKEVALMVQER------FGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRL 350
Cdd:cd07123 259 PTFKSLWKQIGENldryrtYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 351 RSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGG-TVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETF 429
Cdd:cd07123 339 LEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEaEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIF 418
|
410 420 430
....*....|....*....|....*....|....*..
gi 188219757 430 APILYVFKFQDE--EEVFEWNNEV-KQGLSSSIFTKD 463
Cdd:cd07123 419 GPVLTVYVYPDSdfEETLELVDTTsPYALTGAIFAQD 455
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
167-463 |
9.19e-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: 9.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 167 PTLPSERPGHALIEmWNPLGLVGIITAFNFPV------AVfgwnNAIAliTGNVCLWKG---APTTSlvsvavtKIIAQV 237
Cdd:cd07087 84 SVPLLLQPAKAYVI-PEPLGVVLIIGPWNYPLqlalapLI----GAIA--AGNTVVLKPselAPATS-------ALLAKL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 238 LEDNLLPGAIcSLVCGGADIgTTMARDERVNLLSFTGSTQVGKEVAlmvqERFGKSL----LELGGNNAIIAFEDADLSL 313
Cdd:cd07087 150 IPKYFDPEAV-AVVEGGVEV-ATALLAEPFDHIFFTGSPAVGKIVM----EAAAKHLtpvtLELGGKSPCIVDKDANLEV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 314 VVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWD-PNilYGPL----HTKQAVSMFvraveea 388
Cdd:cd07087 224 AARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKEsPD--YGRIinerHFDRLASLL------- 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219757 389 kkQGGTVVYGGKVmDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 463
Cdd:cd07087 295 --DDGKVVIGGQV-DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSED 366
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
184-463 |
1.04e-32 |
|
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: 130.03 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 184 PLGLVGIITAFNFPV-----AVFGwnnAIAliTGNVCLWKGapttSLVSVAVTKIIAQVLEDNLLPGAIcSLVCGGADiG 258
Cdd:cd07135 108 PLGVVLIIGPWNYPVllalsPLVG---AIA--AGCTVVLKP----SELTPHTAALLAELVPKYLDPDAF-QVVQGGVP-E 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 259 TTMARDERVNLLSFTGSTQVGKEVAlmvqERFGKSL----LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVR 334
Cdd:cd07135 177 TTALLEQKFDKIFYTGSGRVGRIIA----EAAAKHLtpvtLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 335 RLFLHESIHNEVVDRLRSAYsQIRVGNPWDPNILYGPLHTKQAvsmFVRAVEEAKKQGGTVVYGGKvMDHPGNYVEPTIV 414
Cdd:cd07135 253 YVLVDPSVYDEFVEELKKVL-DEFYPGGANASPDYTRIVNPRH---FNRLKSLLDTTKGKVVIGGE-MDEATRFIPPTIV 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 188219757 415 TGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 463
Cdd:cd07135 328 SDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDD 376
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
184-505 |
2.16e-32 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 130.15 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 184 PLGLVGIITAFNFPV--AVFGWNNAIAliTGNVCLWKgaptTSLVSVAVTKIIAQVLeDNLLPGAICSLVCGGADIgTTM 261
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLnlTLIPLAGAIA--AGNTVVLK----PSELSPHTSKLMAKLL-TKYLDPSYVRVIEGGVEV-TTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 262 ARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHES 341
Cdd:PTZ00381 181 LLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 342 IHNEVVDRLRSAYSQIRVGNPW---DPNILYGPLHTKQAVSMFvraveeaKKQGGTVVYGGKVmDHPGNYVEPTIVTGLA 418
Cdd:PTZ00381 261 IKDKFIEALKEAIKEFFGEDPKkseDYSRIVNEFHTKRLAELI-------KDHGGKVVYGGEV-DIENKYVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 419 HDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDlGRIFRWLGPKGSDCGIV---------NVNIPtsg 489
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGED-KRHKELVLENTSSGAVVindcvfhllNPNLP--- 408
|
330
....*....|....*.
gi 188219757 490 aeiggaFGGEKHTGGG 505
Cdd:PTZ00381 409 ------FGGVGNSGMG 418
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
184-509 |
3.41e-28 |
|
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: 116.94 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 184 PLGLVGIITAFNFPVA-VFG-WNNAIAliTGNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLpgaicSLVCGGADIGTtm 261
Cdd:cd07134 100 PKGVCLIISPWNYPFNlAFGpLVSAIA--AGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-----AVFEGDAEVAQ-- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 262 ardervNLLS-------FTGSTQVGKevalMVQERFGKSL----LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRC 330
Cdd:cd07134 171 ------ALLElpfdhifFTGSPAVGK----IVMAAAAKHLasvtLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 331 TTVRRLFLHESIHNEVVDRLRSAYSQIrvgnpwdpnilYGPLHTKQAVSMFVRAV------------EEAKKQGGTVVYG 398
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLKAEIEKF-----------YGKDAARKASPDLARIVndrhfdrlkgllDDAVAKGAKVEFG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 399 GKVmDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLGPKGS-D 477
Cdd:cd07134 310 GQF-DAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSgG 388
|
330 340 350
....*....|....*....|....*....|....*....
gi 188219757 478 CGI-------VNVNIPtsgaeiggaFGGEKHTGGGRESG 509
Cdd:cd07134 389 VVVndvvlhfLNPNLP---------FGGVNNSGIGSYHG 418
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
184-463 |
8.38e-28 |
|
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: 116.06 E-value: 8.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 184 PLGLVGIITAFNFP-----VAVFGwnnAIAliTGNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLpgaicSLVCGGADIG 258
Cdd:cd07136 100 PYGVVLIIAPWNYPfqlalAPLIG---AIA--AGNTAVLKPSELTPNTSKVIAKIIEETFDEEYV-----AVVEGGVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 259 TTMArDERVNLLSFTGSTQVGKEVAlmvqERFGKSL----LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVR 334
Cdd:cd07136 170 QELL-DQKFDYIFFTGSVRVGKIVM----EAAAKHLtpvtLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 335 RLFLHESIHNEVVDRLRSaysQIRvgnpwdpnILYG--PLHTKQavsmFVRAVEEakK---------QGGTVVYGGKVmD 403
Cdd:cd07136 245 YVLVHESVKEKFIKELKE---EIK--------KFYGedPLESPD----YGRIINE--KhfdrlagllDNGKIVFGGNT-D 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 404 HPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 463
Cdd:cd07136 307 RETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSED 366
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
56-520 |
9.85e-27 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 113.52 E-value: 9.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSW-GGRGEVITTYCPANNEPIARVR------QASLKDYEETIGKAKKAWNIwadipaPKRGEIVRKIGDAFREKIQLL 128
Cdd:cd07128 6 AGQWhAGTGDGRTLHDAVTGEVVARVSsegldfAAAVAYAREKGGPALRALTF------HERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 129 GRLvSLEMG------KILVEG-IGEVQEYvdvcdyaAGLSR--------MIGGPTLP-SERPGHALIEMWNPLGLVGI-I 191
Cdd:cd07128 80 YAL-SAATGatrrdsWIDIDGgIGTLFAY-------ASLGRrelpnahfLVEGDVEPlSKDGTFVGQHILTPRRGVAVhI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 192 TAFNFPVavfgW----NNAIALITGNVCLWKGAPTTSLVSVAVTKIIaqvLEDNLLP-GAIcSLVCGGAdiGTTMARDER 266
Cdd:cd07128 152 NAFNFPV----WgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDI---VESGLLPeGAL-QLICGSV--GDLLDHLGE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 267 VNLLSFTGSTQVGKEV---ALMVQE--RF---GKSLlelggNNAIIAfEDA-----DLSLVVPSVLFAAVGTAGQRCTTV 333
Cdd:cd07128 222 QDVVAFTGSAATAAKLrahPNIVARsiRFnaeADSL-----NAAILG-PDAtpgtpEFDLFVKEVAREMTVKAGQKCTAI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 334 RRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLhTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHP-------G 406
Cdd:cd07128 296 RRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPL-VSREQREDVRAAVATLLAEAEVVFGGPDRFEVvgadaekG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 407 NYVEPTIVTGL-AHDAPIVHQ-ETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD---LGRIFRWLGPKGsdcGIV 481
Cdd:cd07128 375 AFFPPTLLLCDdPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDpafARELVLGAAPYH---GRL 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 188219757 482 NVNIPTSGAEIGG--------AFGGEKHTGGGRE-SGSDAWKQYMRRS 520
Cdd:cd07128 452 LVLNRDSAKESTGhgsplpqlVHGGPGRAGGGEElGGLRGVKHYMQRT 499
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
168-520 |
2.33e-25 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 108.86 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 168 TLPSERPGHALIEMWnPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLednLLPGAI 247
Cdd:cd07084 85 HLGQGLKQQSHGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAG---LLPPED 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 248 CSLVCGGADIGTTMARDERVNLLSFTGSTQVGKevALMVQERFGKSLLELGGNNAIIAFEDAD-LSLVVPSVLFAAVGTA 326
Cdd:cd07084 161 VTLINGDGKTMQALLLHPNPKMVLFTGSSRVAE--KLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 327 GQRCTTVRRLFLHESIHNE-VVDRLRSAYSQIRVGnpwdpNILYGPLHTKQAVSMfvraVEEAKKQGGTVV-YGGKVM-- 402
Cdd:cd07084 239 GQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLE-----DLLLGPVQTFTTLAM----IAHMENLLGSVLlFSGKELkn 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 403 -DHPGNY----VEPTIVTGLAHDA--PIVHQETFAPILYVFKFQDEEE--VFEWNNEVKQGLSSSIFTKD---LGRifrw 470
Cdd:cd07084 310 hSIPSIYgacvASALFVPIDEILKtyELVTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDpifLQE---- 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 188219757 471 LGPKGSDCGIVNVNIPTSgaeiGGAFGGEKHTGGGRES-------GSDAWKQYMRRS 520
Cdd:cd07084 386 LIGNLWVAGRTYAILRGR----TGVAPNQNHGGGPAADprgagigGPEAIKLVWRCH 438
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
182-463 |
6.85e-23 |
|
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: 101.53 E-value: 6.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 182 WNPLGLVGIITAFNFPVA-----VFGwnnAIAliTGNVCLWKgaPttSLVSVAVTKIIAQVLEDNLLPgaIC-SLVCGGA 255
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQltlvpLVG---AIA--AGNCVVIK--P--SEVSPATAKLLAELIPKYLDK--ECyPVVLGGV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 256 DIgTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRR 335
Cdd:cd07132 167 EE-TTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 336 LFLHESIHNEVVDRLRSAYSQIRVGNPWD-PNilYGPLhtkqaVSM--FVRAVEEAKkqGGTVVYGGKVmDHPGNYVEPT 412
Cdd:cd07132 246 VLCTPEVQEKFVEALKKTLKEFYGEDPKEsPD--YGRI-----INDrhFQRLKKLLS--GGKVAIGGQT-DEKERYIAPT 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 188219757 413 IVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 463
Cdd:cd07132 316 VLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
173-444 |
7.50e-22 |
|
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: 97.94 E-value: 7.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 173 RPGHALIEmWNPLGLVGIITAFNFPVAVfgwnnAIA-LIT----GNVCLWKG---APTTSLVsvavtkiIAQVLEDNLLP 244
Cdd:cd07133 91 LPAKAEVE-YQPLGVVGIIVPWNYPLYL-----ALGpLIAalaaGNRVMIKPsefTPRTSAL-------LAELLAEYFDE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 245 GAICsLVCGGADIG---TTMARDervNLLsFTGSTQVGKEVALMVqerfGKSL----LELGGNN-AIIAfEDADLSLVVP 316
Cdd:cd07133 158 DEVA-VVTGGADVAaafSSLPFD---HLL-FTGSTAVGRHVMRAA----AENLtpvtLELGGKSpAIIA-PDADLAKAAE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 317 SVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRvgnpwdPNILYGPLHTkqavSM-----FVR---AVEEA 388
Cdd:cd07133 228 RIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMY------PTLADNPDYT----SIinerhYARlqgLLEDA 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188219757 389 KKQGGTVVyggKVMDHPGNYVE-----PTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEV 444
Cdd:cd07133 298 RAKGARVI---ELNPAGEDFAAtrklpPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEA 355
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
191-520 |
7.71e-21 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 95.93 E-value: 7.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 191 ITAFNFPvavfGW----NNAIALITGNVCLWKGAPTTSLVSvavTKIIAQVLEDNLLPGAICSLVCGGAdiGTTMARDER 266
Cdd:PRK11903 155 INAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLT---QRMVKDVVAAGILPAGALSVVCGSS--AGLLDHLQP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 267 VNLLSFTGSTQVGKEVALM--VQERFGKSLLELGGNNAIIAFEDAD-----LSLVVPSVLFAAVGTAGQRCTTVRRLFLH 339
Cdd:PRK11903 226 FDVVSFTGSAETAAVLRSHpaVVQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVP 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 340 ESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTK-QAVSmfVRAVEEAKKQGGTVVYGGKV---MDHP---GNYVEPT 412
Cdd:PRK11903 306 EALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRaQLAA--VRAGLAALRAQAEVLFDGGGfalVDADpavAACVGPT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 413 I-VTGLAHDAPIVHQ-ETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD---LGRIFRWLGPKGsdcGIVNVNIPT 487
Cdd:PRK11903 384 LlGASDPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDaafLAAAALELADSH---GRVHVISPD 460
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 188219757 488 SGAEIGG--------AFGGEKHTGGGRE-SGSDAWKQYMRRS 520
Cdd:PRK11903 461 VAALHTGhgnvmpqsLHGGPGRAGGGEElGGLRALAFYHRRS 502
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
184-509 |
4.74e-19 |
|
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: 89.78 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 184 PLGLVGIITAFNFPVA-----VFGwnnAIAliTGNVCLWKgaptTSLVSVAVTKIIAQVLEDNLLPGAIcSLVCGGADIG 258
Cdd:cd07137 101 PLGVVLVISAWNFPFLlslepVIG---AIA--AGNAVVLK----PSELAPATSALLAKLIPEYLDTKAI-KVIEGGVPET 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 259 TTMArDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGT-AGQRCTTVRRLF 337
Cdd:cd07137 171 TALL-EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 338 LHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTK--QAVSMFVRAVEEAKKqggtVVYGGKVmDHPGNYVEPTIVT 415
Cdd:cd07137 250 VEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHhfQRLSRLLDDPSVADK----IVHGGER-DEKNLYIEPTILL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 416 GLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT--KDLGRIFRWLGPKGS----DCgIVNVNIPTSg 489
Cdd:cd07137 325 DPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTknKELKRRIVAETSSGGvtfnDT-VVQYAIDTL- 402
|
330 340
....*....|....*....|
gi 188219757 490 aeiggAFGGEKHTGGGRESG 509
Cdd:cd07137 403 -----PFGGVGESGFGAYHG 417
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
184-509 |
9.02e-16 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 79.70 E-value: 9.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 184 PLGLVGIITAFNFPVaVFGWNNAIALIT-GNVCLWKgaptTSLVSVAVTKIIAQVLEDNLLPGAIcsLVCGGADIGTTMA 262
Cdd:PLN02174 112 PLGVVLVISAWNYPF-LLSIDPVIGAISaGNAVVLK----PSELAPASSALLAKLLEQYLDSSAV--RVVEGAVTETTAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 263 RDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVG-TAGQRCTTVRRLFLHES 341
Cdd:PLN02174 185 LEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 342 IHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQaVSMFVRAVEEaKKQGGTVVYGGKvMDHPGNYVEPTIVTGLAHDA 421
Cdd:PLN02174 265 YAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTH-FDRLSKLLDE-KEVSDKIVYGGE-KDRENLKIAPTILLDVPLDS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 422 PIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDlGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKH 501
Cdd:PLN02174 342 LIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHN-KKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGE 420
|
....*...
gi 188219757 502 TGGGRESG 509
Cdd:PLN02174 421 SGMGAYHG 428
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
184-520 |
6.53e-15 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 77.07 E-value: 6.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 184 PLGLVGIITAFNFPVA-----VFGwnnaiALITGNVCLWKgaptTSLVSVAVTKIIAQVLEDNLLPGAIcSLVCGGADIG 258
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGlslepLIG-----AIAAGNAVVLK----PSELAPATSAFLAANIPKYLDSKAV-KVIEGGPAVG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 259 TTMARdERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGN-NAIIAFEDA--DLSLVVPSVLFAAVGT-AGQRCTTVR 334
Cdd:PLN02203 178 EQLLQ-HKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKcPCIVDSLSSsrDTKVAVNRIVGGKWGScAGQACIAID 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 335 RLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQavsmFVRAVE--EAKKQGGTVVYGGKvMDHPGNYVEPT 412
Cdd:PLN02203 257 YVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKH----FQRLSNllKDPRVAASIVHGGS-IDEKKLFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 413 IVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEi 492
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACD- 410
|
330 340 350
....*....|....*....|....*....|....
gi 188219757 493 GGAFGGEKHTGGGRESGSDAW------KQYMRRS 520
Cdd:PLN02203 411 SLPFGGVGESGFGRYHGKYSFdtfsheKAVLRRS 444
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
56-463 |
4.72e-12 |
|
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: 68.29 E-value: 4.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 56 NGSWGGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKA--WNIWADIPAPKR----GEIVRKIGDAFR--EKIQL 127
Cdd:cd07126 4 AGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCpkSGLHNPLKNPERyllyGDVSHRVAHELRkpEVEDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 128 LGRLVSLEMGKILVEGIGEV---QEYVDvcDYAAGLSRMIG-GPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGW 203
Cdd:cd07126 84 FARLIQRVAPKSDAQALGEVvvtRKFLE--NFAGDQVRFLArSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 204 NNAIALITGNVCLWKGaptTSLVSVAVTKIIaQVLEDNLLPGAICSLV-CGGADIGTTMARDErVNLLSFTGSTQVGKEV 282
Cdd:cd07126 162 QLMGALFMGNKPLLKV---DSKVSVVMEQFL-RLLHLCGMPATDVDLIhSDGPTMNKILLEAN-PRMTLFTGSSKVAERL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 283 ALMVQerfGKSLLELGGNNAIIAFED-ADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHES-IHNEVVDRLRSAYSQIRVg 360
Cdd:cd07126 237 ALELH---GKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALAEQRKL- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 361 npwdPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVM---DHPGNY--VEPTIV------TGLAHDAPIVHQETF 429
Cdd:cd07126 313 ----EDLTIGPVLTWTTERILDHVDKLLAIPGAKVLFGGKPLtnhSIPSIYgaYEPTAVfvpleeIAIEENFELVTTEVF 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 188219757 430 APILYVFKFQDEEE--VFEWNNEVKQGLSSSIFTKD 463
Cdd:cd07126 389 GPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSND 424
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
184-470 |
1.29e-09 |
|
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: 60.57 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 184 PLGLVGIITAFNFPVavfgWNNA----IALITGNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLPGAICSLVCG--GADI 257
Cdd:cd07127 193 PRGVALVIGCSTFPT----WNGYpglfASLATGNPVIVKPHPAAILPLAITVQVAREVLAEAGFDPNLVTLAADtpEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 258 GTTMARDERVNLLSFTGSTQVGKEvaLMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLF 337
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSNAFGDW--LEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIY 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 338 L-HESIHN--------EVVDRLRSAYSQIrVGNPWDPNILYGPLhtkqaVSMFVRAVEEAKKQGGTVVYGGKVMDHP--- 405
Cdd:cd07127 347 VpRDGIQTddgrksfdEVAADLAAAIDGL-LADPARAAALLGAI-----QSPDTLARIAEARQLGEVLLASEAVAHPefp 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188219757 406 GNYVE-PTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEV---KQGLSSSIFTKDLGRIFRW 470
Cdd:cd07127 421 DARVRtPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESvreHGAMTVGVYSTDPEVVERV 489
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
184-459 |
9.28e-09 |
|
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: 57.55 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 184 PLGLVGIITAFNFPVA--VFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLPGAICSLV-CGGADIGTT 260
Cdd:cd07129 105 PLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAALRATGLPAGVFSLLqGGGREVGVA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 261 MARDERVNLLSFTGSTQVGKEVALMVQER------FGksllELGGNNAIIAFEDA------DLSLV-VPSVLFAavgtAG 327
Cdd:cd07129 185 LVKHPAIKAVGFTGSRRGGRALFDAAAARpepipfYA----ELGSVNPVFILPGAlaergeAIAQGfVGSLTLG----AG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 328 QRCTTVRRLFLhesIHNEVVDRLRSAYSQ-IRVGNPwdpnilyGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPG 406
Cdd:cd07129 257 QFCTNPGLVLV---PAGPAGDAFIAALAEaLAAAPA-------QTMLTPGIAEAYRQGVEALAAAPGVRVLAGGAAAEGG 326
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 188219757 407 NYVEPTI--VTG---LAHDApiVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSI 459
Cdd:cd07129 327 NQAAPTLfkVDAaafLADPA--LQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATI 382
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
89-493 |
9.15e-06 |
|
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: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 89 EETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGigEVQEYVDVCDYAAGLSRMIGGPT 168
Cdd:cd07081 2 DDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVED--KVIKNHFAAEYIYNVYKDEKTCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 169 LPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLPGAIC 248
Cdd:cd07081 80 VLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 249 SLVcGGADIGTTMA--RDERVNLLSFTGSTQVGKEValmvqERFGKSLLELG-GNNAIIAFEDADLSLVVPSVLFAAVGT 325
Cdd:cd07081 160 GWI-DNPSIELAQRlmKFPGIGLLLATGGPAVVKAA-----YSSGKPAIGVGaGNTPVVIDETADIKRAVQSIVKSKTFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 326 AGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNpwdpnilygplHTKQAVSMFVRAVEEAKKQGGTVVYggKVMDHP 405
Cdd:cd07081 234 NGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAE-----------ELQQVQPVILKNGDVNRDIVGQDAY--KIAAAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219757 406 GNYVEPTI------VTGLAHDAPIVHqETFAPILYVFKFQDEEEVFEWNNEVKQ----GLSSSIFTKDLGRIFR--WLGP 473
Cdd:cd07081 301 GLKVPQETriligeVTSLAEHEPFAH-EKLSPVLAMYRAANFADADAKALALKLeggcGHTSAMYSDNIKAIENmnQFAN 379
|
410 420
....*....|....*....|
gi 188219757 474 KgSDCGIVNVNIPTSGAEIG 493
Cdd:cd07081 380 A-MKTSRFVKNGPCSQGGLG 398
|
|
| |
