|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
25-499 |
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: 948.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 25 GVYNGSWGGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLV 104
Cdd:cd07130 1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 105 SLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITG 184
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 185 NVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGK 264
Cdd:cd07130 161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 265 SLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPL 344
Cdd:cd07130 241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 345 HTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLaHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVK 424
Cdd:cd07130 321 HTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGL-SDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVP 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188035915 425 QGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYS 499
Cdd:cd07130 400 QGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
25-499 |
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: 886.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 25 GVYNGSWGGRG-EVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRL 103
Cdd:cd07086 1 GVIGGEWVGSGgETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 104 VSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALIT 183
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 184 GNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFG 263
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 264 KSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGP 343
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 344 LHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDH--PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNN 421
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188035915 422 EVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYS 499
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
9-510 |
0e+00 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 717.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 9 PQYAWLQDLGLREDNEGVY-NGSWGGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVR 87
Cdd:PLN02315 6 KEYEFLSEIGLSSRNLGCYvGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 88 KIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFN 167
Cdd:PLN02315 86 QIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 168 FPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGS 247
Cdd:PLN02315 166 FPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 248 TQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYS 327
Cdd:PLN02315 246 SKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 328 QIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTgLAHDAPIVHQETFAPILYV 407
Cdd:PLN02315 326 QVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 408 FKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQ 487
Cdd:PLN02315 405 MKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQ 484
|
490 500
....*....|....*....|...
gi 188035915 488 YMRRSTCTINYSTSLPLAQGIKF 510
Cdd:PLN02315 485 YMRRSTCTINYGNELPLAQGINF 507
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
61-496 |
6.95e-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: 484.02 E-value: 6.95e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 61 EETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPT 140
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 141 LPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLednlLPGAIC 220
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAG----LPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 221 SLVCGGAD-IGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAG 299
Cdd:cd07078 157 NVVTGDGDeVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 300 QRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMD-HPG 378
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEgGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 379 NYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIP 458
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVA--ERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 188035915 459 TSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 496
Cdd:cd07078 395 SVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
33-493 |
1.43e-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: 473.94 E-value: 1.43e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 33 GRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKIL 112
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 113 VEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSeRPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGA 192
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 193 PTTSLVSVAVTKIIAQVLednlLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGG 271
Cdd:pfam00171 163 ELTPLTALLLAELFEEAG----LPAGVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 272 NNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVS 351
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 352 MFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSI 431
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 188035915 432 FTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRST 493
Cdd:pfam00171 399 FTSDLERALRVA--RRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
28-498 |
3.80e-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: 473.46 E-value: 3.80e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 105
Cdd:COG1012 11 GGEWvaAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 106 LEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGN 185
Cdd:COG1012 91 LETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 186 VCLWKGAPTTSLVSVAVTKIIAQVledNLLPGAIcSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGK 264
Cdd:COG1012 171 TVVLKPAEQTPLSALLLAELLEEA---GLPAGVL-NVVTGdGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 265 SLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPL 344
Cdd:COG1012 247 VTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 345 HTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDH-PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEV 423
Cdd:COG1012 327 ISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDT 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188035915 424 KQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 498
Cdd:COG1012 407 EYGLAASVFTRDLARARRVA--RRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
28-499 |
1.64e-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: 390.17 E-value: 1.64e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSWGGR--GEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLV 104
Cdd:cd07131 4 GGEWVDSasGETFDSRNPADlEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 105 SLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITG 184
Cdd:cd07131 84 TREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 185 NVCLWKGAPTTSlvsvAVTKIIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFG 263
Cdd:cd07131 164 NTVVFKPAEDTP----ACALKLVELFAEAGLPPGVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 264 KSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGP 343
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 344 LHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDH----PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEW 419
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 420 NNEVKQGLSSSIFTKDLGRIFRWLGpkgsDC--GIVNVNIPTSGAEIGGAFGGEKHTGGG-RESGSDAWKQYMRRSTCTI 496
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARR----DLeaGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
...
gi 188035915 497 NYS 499
Cdd:cd07131 476 DYS 478
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
67-496 |
2.99e-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: 372.72 E-value: 2.99e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 67 AKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERP 146
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 147 GHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVlednLLPGAICSLVCGG 226
Cdd:cd06534 83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEA----GLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 227 AD-IGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTV 305
Cdd:cd06534 159 GDeVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 306 RRLFLHESIHNEVVDRLRsaysqirvgnpwdpnilygplhtkqavsmfvraveeakkqggtvvyggkvmdhpgnyvepTI 385
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV------------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 386 VTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIG 465
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVA--ERLRAGTVYINDSSIGVGPE 336
|
410 420 430
....*....|....*....|....*....|.
gi 188035915 466 GAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 496
Cdd:cd06534 337 APFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
24-484 |
7.90e-115 |
|
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: 347.31 E-value: 7.90e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 24 EGVYNGSWGGRGEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGR 102
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 103 LVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALI 182
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 183 TGNVCLWKGAPTTSLVSVAVTKIIAQVLednlLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQER 261
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAG----LPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 262 FGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILY 341
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 342 GPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKV--MDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEW 419
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188035915 420 NNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSDA 484
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFK--RRVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEAA 461
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
43-489 |
4.53e-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: 334.40 E-value: 4.53e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVqey 122
Cdd:cd07103 4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 123 vdvcDYAAGL-------SRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTT 195
Cdd:cd07103 81 ----DYAASFlewfaeeARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 196 SLVSVAvtkiIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNA 274
Cdd:cd07103 157 PLSALA----LAELAEEAGLPAGVLNVVTGsPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 275 IIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFV 354
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 355 RAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTK 434
Cdd:cd07103 313 ALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 188035915 435 DLGRIFRwLGpKGSDCGIVNVNIPT-SGAEIggAFGGEKHTGGGRESGSDAWKQYM 489
Cdd:cd07103 393 DLARAWR-VA-EALEAGMVGINTGLiSDAEA--PFGGVKESGLGREGGKEGLEEYL 444
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
43-490 |
6.06e-107 |
|
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: 326.43 E-value: 6.06e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQ 120
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 121 EYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSV 200
Cdd:cd07114 84 YLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 201 AVTKIiaqVLEDNLLPGAIcSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFE 279
Cdd:cd07114 164 ELAKL---AEEAGFPPGVV-NVVTGfGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 280 DADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEE 359
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 360 AKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 435
Cdd:cd07114 320 AREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 436 LGRIFRWlgPKGSDCGIVNVNI-----PTSgaeiggAFGGEKHTGGGRESGSDAWKQYMR 490
Cdd:cd07114 400 LARAHRV--ARAIEAGTVWVNTyralsPSS------PFGGFKDSGIGRENGIEAIREYTQ 451
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
35-441 |
2.60e-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: 317.67 E-value: 2.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 35 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVE 114
Cdd:cd07088 12 GETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 115 GIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPT 194
Cdd:cd07088 92 ARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 195 TSLVSVAVTKIIAQVlednLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 273
Cdd:cd07088 172 TPLNALEFAELVDEA----GLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 274 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 353
Cdd:cd07088 248 PAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 354 VRAVEEAKKQGGTVVYGGKVMDH-PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIF 432
Cdd:cd07088 328 EEMVERAVEAGATLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIY 407
|
....*....
gi 188035915 433 TKDLGRIFR 441
Cdd:cd07088 408 TENLNTAMR 416
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
43-493 |
8.79e-99 |
|
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: 305.22 E-value: 8.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 122
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 123 VDVCDYAAGLSrmiggptLPSER----PGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLV 198
Cdd:cd07106 84 VAWLRYTASLD-------LPDEVieddDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 199 SVAVTKIIAQVLednllPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVAlmvqERFGKSL----LELGGNNA 274
Cdd:cd07106 157 TLKLGELAQEVL-----PPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVM----ASAAKTLkrvtLELGGNDA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 275 IIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFV 354
Cdd:cd07106 228 AIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 355 RAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTK 434
Cdd:cd07106 308 ELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188035915 435 DLGRIFRwLGPKgSDCGIVNVNiptSGAEIGGA--FGGEKHTGGGRESGSDAWKQYMRRST 493
Cdd:cd07106 388 DLERAEA-VARR-LEAGTVWIN---THGALDPDapFGGHKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
43-482 |
1.53e-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: 294.62 E-value: 1.53e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 122
Cdd:cd07150 6 PADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 123 VDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVaVFGWNN-AIALITGNVCLWKGAPTTSLVSVa 201
Cdd:cd07150 86 PELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPL-ILATKKvAFALAAGNTVVLKPSEETPVIGL- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 202 vtkIIAQVLEDNLLPGAICSLV-CGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFED 280
Cdd:cd07150 164 ---KIAEIMEEAGLPKGVFNVVtGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 281 ADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEA 360
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 361 KKQGGTVVYGGKvmdHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIF 440
Cdd:cd07150 321 VAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAF 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 188035915 441 RWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGS 482
Cdd:cd07150 398 KL--AERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGE 437
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
59-488 |
2.52e-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: 293.28 E-value: 2.52e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 59 DYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGG 138
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 139 PTLPSERPGHALIEMWNPLGLVGIITAFNFPV-----AVfgwnnAIALITGNVCLWKGAPTTSlVSVAVtkIIAQVLEDN 213
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLilamrSV-----APALALGNAVVLKPDSRTP-VTGGL--LIAEIFEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 214 LLP-GAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLF 292
Cdd:cd07104 153 GLPkGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 293 AAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGK 372
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 373 vmdHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRwLGpKGSDCGI 452
Cdd:cd07104 313 ---YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMA-FA-ERLETGM 387
|
410 420 430
....*....|....*....|....*....|....*.
gi 188035915 453 VNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQY 488
Cdd:cd07104 388 VHINDQTVNDEPHVPFGGVKASGGGRFGGPASLEEF 423
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
38-480 |
1.62e-90 |
|
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: 284.24 E-value: 1.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 38 ITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIG 117
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 118 EVQEYVDVCDYAAGLSRMIGGPTLPSE----RPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 193
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 194 TTSLVSVAVTKIIaqvLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 273
Cdd:cd07145 161 NTPLTAIELAKIL---EEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 274 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 353
Cdd:cd07145 238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 354 VRAVEEAKKQGGTVVYGGKVMDhpGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT 433
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFT 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 188035915 434 KDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 480
Cdd:cd07145 396 NDINRALKV--ARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREG 440
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
38-479 |
3.85e-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: 282.95 E-value: 3.85e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 38 ITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIG 117
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 118 EVQEYVDVCDYAAGLSRMIGGPTLPSE-------RPGHALIEmwnPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWK 190
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFDaspggegRIGFTIRE---PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 191 GAPTTSLVSVAvtkiIAQVLEDNLLPGAICSLVCGGAD-IGTTMARDERVNLLSFTGSTQVGKEVALMVQERfgKSLLEL 269
Cdd:cd07149 158 PASQTPLSALK----LAELLLEAGLPKGALNVVTGSGEtVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--KVTLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 270 GGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQA 349
Cdd:cd07149 232 GSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 350 VSMFVRAVEEAKKQGGTVVYGGKVMdhpGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSS 429
Cdd:cd07149 312 AERIEEWVEEAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQA 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 188035915 430 SIFTKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 479
Cdd:cd07149 389 GVFTNDLQKALKAA--RELEVGGVMINdSSTFRVD-HMPYGGVKESGTGRE 436
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
43-490 |
6.13e-90 |
|
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: 6.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGI-GEVQE 121
Cdd:cd07092 4 PATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 122 YVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVA 201
Cdd:cd07092 84 AVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 202 VTKIIAQVLednllPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFED 280
Cdd:cd07092 164 LAELAAEVL-----PPGVVNVVCGgGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 281 ADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEA 360
Cdd:cd07092 239 ADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 361 KKqGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIF 440
Cdd:cd07092 319 PA-HARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAM 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 188035915 441 RWLGPKGSDCGIVNVNIPTSgAEIggAFGGEKHTGGGRESGSDAWKQYMR 490
Cdd:cd07092 398 RLSARLDFGTVWVNTHIPLA-AEM--PHGGFKQSGYGKDLSIYALEDYTR 444
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
43-498 |
8.35e-89 |
|
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: 8.35e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 122
Cdd:cd07107 4 PATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 123 VDVCDYAAGLSRMIGGPTLPSErPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVav 202
Cdd:cd07107 84 AALLDYFAGLVTELKGETIPVG-GRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSAL-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 203 tkIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDAD 282
Cdd:cd07107 161 --RLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 283 LSLVVPSvlfAAVG----TAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVE 358
Cdd:cd07107 239 PEAAADA---AVAGmnftWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 359 EAKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTK 434
Cdd:cd07107 316 SAKREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188035915 435 DLGRIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 498
Cdd:cd07107 396 DISQAHR--TARRVEAGYVWIN-GSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
61-479 |
9.14e-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: 278.57 E-value: 9.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 61 EETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGlsrmiGGPT 140
Cdd:cd07100 2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAE-----NAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 141 LPSERP-----GHALIEmWNPLGLVGIITAFNFP---VAVFGwnnAIALITGNVCLWKGAPTTSLVSVAvtkiIAQVLED 212
Cdd:cd07100 77 FLADEPietdaGKAYVR-YEPLGVVLGIMPWNFPfwqVFRFA---APNLMAGNTVLLKHASNVPGCALA----IEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 213 NLLP-GAICSLVCGGADIGTTMArDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVL 291
Cdd:cd07100 149 AGFPeGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 292 FAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGG 371
Cdd:cd07100 228 KGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 372 KVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLG---RIFRWLgpkgs 448
Cdd:cd07100 308 KRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLEraeRVARRL----- 382
|
410 420 430
....*....|....*....|....*....|..
gi 188035915 449 DCGIVNVNIPT-SGAEIggAFGGEKHTGGGRE 479
Cdd:cd07100 383 EAGMVFINGMVkSDPRL--PFGGVKRSGYGRE 412
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
26-498 |
7.90e-88 |
|
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: 279.11 E-value: 7.90e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 26 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLV 104
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 105 SLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSeRPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITG 184
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEM-VPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 185 NVCLWKGAPTTSLVSVAVtkiiAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGStqvgKEVALMVQERFG 263
Cdd:cd07124 195 NTVVLKPAEDTPVIAAKL----VEILEEAGLPPGVVNFLPGpGEEVGDYLVEHPDVRFIAFTGS----REVGLRIYERAA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 264 KS----------LLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGN 333
Cdd:cd07124 267 KVqpgqkwlkrvIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 334 PWDPNILYGPLHTKQAVSMFVRAVEEAkKQGGTVVYGGKVMDHP--GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQ 411
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIG-KSEGRLLLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 412 DEEEVFEWNNEVKQGLSSSIFTKDLGRI--FRwlgpKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTG-GGRESGSDAWKQ 487
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLerAR----REFEVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDYLLQ 501
|
490
....*....|.
gi 188035915 488 YMRRSTCTINY 498
Cdd:cd07124 502 FMQPKTVTENF 512
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
43-488 |
1.09e-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: 1.09e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEG-IGEVQE 121
Cdd:cd07115 4 PATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDVPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 122 YVDVCDYAAGLSRMIGGPTLPSeRPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVA 201
Cdd:cd07115 84 AADTFRYYAGWADKIEGEVIPV-RGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 202 VTKIIAQVLednlLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFED 280
Cdd:cd07115 163 IAELMAEAG----FPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 281 ADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEA 360
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 361 KKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIF 440
Cdd:cd07115 319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 188035915 441 RWlgPKGSDCGIVNVNipTSGA-EIGGAFGGEKHTGGGRESGSDAWKQY 488
Cdd:cd07115 399 RV--AAALKAGTVWIN--TYNRfDPGSPFGGYKQSGFGREMGREALDEY 443
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
29-481 |
4.13e-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: 273.03 E-value: 4.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 29 GSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSL 106
Cdd:cd07151 1 GEWrdGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 107 EMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNV 186
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 187 CLWKGAPTTslvsvAVTK--IIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFG 263
Cdd:cd07151 161 VVLKPASDT-----PITGglLLAKIFEEAGLPKGVLNVVVGaGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 264 KSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGP 343
Cdd:cd07151 236 KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 344 LHTKQAVSMFVRAVEEAKKQGGTVVYGGkvmDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEV 423
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEGATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDT 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 188035915 424 KQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESG 481
Cdd:cd07151 393 EYGLSGAVFTSDLERGVQF--ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNG 448
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
43-479 |
2.55e-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: 270.77 E-value: 2.55e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKIL-VEGIGEVQE 121
Cdd:cd07108 4 PATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 122 YVDVCDYAAGLSRMIGGPTLPSeRPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVA 201
Cdd:cd07108 84 LADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 202 VTKIIAQVLednllPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFED 280
Cdd:cd07108 163 LAEILAQVL-----PAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 281 ADLSLVVPSVLFAAVGT-AGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEE 359
Cdd:cd07108 238 ADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 360 AKK-QGGTVVYGGK----VMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTK 434
Cdd:cd07108 318 GLStSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 188035915 435 DLGRIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRE 479
Cdd:cd07108 398 DLGRALR--AAHALEAGWVQVN-QGGGQQPGQSYGGFKQSGLGRE 439
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
14-489 |
3.09e-84 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 269.25 E-value: 3.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 14 LQDLGLREDnEGVYNGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGD 91
Cdd:PLN02278 17 LRNAGLLRT-QGLIGGKWtdAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 92 AFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVA 171
Cdd:PLN02278 96 LIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 172 VFGWNNAIALITGNVCLWKGAPTTSLVSVAvtkiiAQVL--EDNLLPGAIcSLVCGGA-DIGTTMARDERVNLLSFTGST 248
Cdd:PLN02278 176 MITRKVGPALAAGCTVVVKPSELTPLTALA-----AAELalQAGIPPGVL-NVVMGDApEIGDALLASPKVRKITFTGST 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 249 QVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQ 328
Cdd:PLN02278 250 AVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 329 IRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVF 408
Cdd:PLN02278 330 LVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 409 KFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN---IPTSGAeiggAFGGEKHTGGGRESGSDAW 485
Cdd:PLN02278 410 RFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRV--SEALEYGIVGVNeglISTEVA----PFGGVKQSGLGREGSKYGI 483
|
....
gi 188035915 486 KQYM 489
Cdd:PLN02278 484 DEYL 487
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
28-489 |
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: 266.87 E-value: 1.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKRGEIVRKIGDAFREKIQLLGRL 103
Cdd:cd07119 3 DGEWveAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDsgEWPHLPAQERAALLFRIADKIREDAEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 104 VSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIeMWNPLGLVGIITAFNFPVAVFGWNNAIALIT 183
Cdd:cd07119 83 ETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRT-VREPVGVCGLITPWNYPLLQAAWKLAPALAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 184 GNVCLWKGAPTTSLVSVAVTKIIAQVLednlLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERF 262
Cdd:cd07119 162 GNTVVIKPSEVTPLTTIALFELIEEAG----LPAGVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 263 GKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYG 342
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 343 PLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFE 418
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188035915 419 WNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN---IPTSGAEiggaFGGEKHTGGGRESGSDAWKQYM 489
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVA--RRLRAGTVWINdyhPYFAEAP----WGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
40-484 |
6.46e-83 |
|
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: 264.43 E-value: 6.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 40 TYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGI-GE 118
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 119 VQEYVDVCDYAAGLSRMIGGPTLPSErPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLV 198
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 199 SVavtkIIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIA 277
Cdd:cd07093 160 AW----LLAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 278 FEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAV 357
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 358 EEAKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT 433
Cdd:cd07093 316 ELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 188035915 434 KDLGRIFRWlgPKGSDCGIVNVN------IPTsgaeiggAFGGEKHTGGGRESGSDA 484
Cdd:cd07093 396 RDLGRAHRV--ARRLEAGTVWVNcwlvrdLRT-------PFGGVKASGIGREGGDYS 443
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
38-479 |
7.58e-83 |
|
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: 264.11 E-value: 7.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 38 ITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIG 117
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 118 EVQEYVDVCDYAAGLSRMIGGPTLP---SER-PGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 193
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldiSARgEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 194 TTSLVSVavtkIIAQVL-EDNLLPGAICSLVCGgADIGTTMARDERVNLLSFTGSTQVGkevaLMVQERFGKS--LLELG 270
Cdd:cd07147 161 RTPLSAL----ILGEVLaETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVG----WDLKARAGKKkvVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 271 GNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAV 350
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 351 SMFVRAVEEAKKQGGTVVYGGKVmdhPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSS 430
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 188035915 431 IFTKDLGRIFR-WlgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 479
Cdd:cd07147 389 VFTRDLEKALRaW---DELEVGGVVINdVPTFRVD-HMPYGGVKDSGIGRE 435
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
40-490 |
1.60e-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: 263.40 E-value: 1.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 40 TYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEV 119
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 120 QEYVDVCDYAAGLSRMIGGPT--LPSERPGHALIEmwnPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSL 197
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHvpLPGGSFAYTRRE---PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 198 VSVavtkIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIA 277
Cdd:cd07090 158 TAL----LLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 278 FEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAV 357
Cdd:cd07090 234 FDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 358 EEAKKQGGTVVYGGKVMDHP-----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIF 432
Cdd:cd07090 314 ESAKQEGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVF 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 188035915 433 TKDLGRIFRWLGP-KGSDCGIVNVNIptSGAEIggAFGGEKHTGGGRESGSDAWKQYMR 490
Cdd:cd07090 394 TRDLQRAHRVIAQlQAGTCWINTYNI--SPVEV--PFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
41-490 |
5.58e-82 |
|
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: 5.58e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 41 YCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQ 120
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 121 EYVDVCDYAAGLSRMIggptLPSERPGHALIEMWN-------PLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 193
Cdd:cd07099 81 LALEAIDWAARNAPRV----LAPRKVPTGLLMPNKkatveyrPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 194 TTSLVSVAVTKIIAQVLednlLPGAICSLVCGGADIGTTMArDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 273
Cdd:cd07099 157 VTPLVGELLAEAWAAAG----PPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 274 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 353
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 354 VRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT 433
Cdd:cd07099 312 RRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188035915 434 KDL---GRIFRWLgpkgsDCGIVNVNIPTSGAEIGGA-FGGEKHTGGGRESGSDAWKQYMR 490
Cdd:cd07099 392 RDLaraEAIARRL-----EAGAVSINDVLLTAGIPALpFGGVKDSGGGRRHGAEGLREFCR 447
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
41-489 |
3.65e-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: 259.87 E-value: 3.65e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 41 YCPANNEPIARVRQASLKDYEETIGKAKKAWNIWA-DIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILV-EGIGE 118
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMtARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 119 VQEYVDVCDYAAGLSRM-----IGGPTLPSERPGHALIEMwNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 193
Cdd:cd07089 82 VDGPIGHLRYFADLADSfpwefDLPVPALRGGPGRRVVRR-EPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 194 TTSLVSVAVTKIIAqvlEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 273
Cdd:cd07089 161 DTPLSALLLGEIIA---ETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 274 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 353
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 354 VRAVEEAKKQGGTVVYGGKVMDH--PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSI 431
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188035915 432 FTKDLGR---IFRWLgpkgsDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 489
Cdd:cd07089 398 WSADVDRayrVARRI-----RTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
43-496 |
6.61e-81 |
|
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: 6.61e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKkawNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 122
Cdd:cd07146 6 PYTGEVVGTVPAGTEEALREALALAA---SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 123 VDVCDYAAGLSRMIGGPTLPSERPGHA----LIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLV 198
Cdd:cd07146 83 ADVLRFAAAEALRDDGESFSCDLTANGkarkIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 199 SVAvtkiIAQVLEDNLLPGAICSLVCGG-ADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERfgKSLLELGGNNAIIA 277
Cdd:cd07146 163 AIY----LADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--RQLLELGGNDPLIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 278 FEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAV 357
Cdd:cd07146 237 MDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 358 EEAKKQGGTVVYGGKvmdHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLG 437
Cdd:cd07146 317 EEAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188035915 438 RIFRWLgpKGSDCGIVNVN------IPTSgaeiggAFGGEKHTG-GGRESGSDAWKQYMRRSTCTI 496
Cdd:cd07146 394 TIKRLV--ERLDVGTVNVNevpgfrSELS------PFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
40-489 |
1.04e-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: 1.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 40 TYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPApKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIG 117
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 118 EVQEYVDVCDYAAGLSRMIGGPTLPSErPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSL 197
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPE-PGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 198 VSVAVTKIIAQVleDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIA 277
Cdd:cd07120 159 INAAIIRILAEI--PSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 278 FEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAV 357
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 358 EEAKKQGGTVVY-GGKVMDH--PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTK 434
Cdd:cd07120 317 ERAIAAGAEVVLrGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 188035915 435 DLGRIFRWlgPKGSDCGIVNVNipTSGAEIGGA-FGGEKHTGGGRESGSDAWKQYM 489
Cdd:cd07120 397 DLARAMRV--ARAIRAGTVWIN--DWNKLFAEAeEGGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
43-496 |
2.02e-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: 257.93 E-value: 2.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWNIWA-DIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQE 121
Cdd:cd07109 4 PSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 122 YVDVCDYAAGLSRMIGGPTLPSErPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVA 201
Cdd:cd07109 84 AARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 202 vtkiIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFED 280
Cdd:cd07109 163 ----LAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 281 ADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPW-DPNilYGPLHTKQAVSMFVRAVEE 359
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLeDPD--LGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 360 AKKQGGTVVYGGKVMDHP---GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDL 436
Cdd:cd07109 317 ARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 437 GRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 496
Cdd:cd07109 397 DRALRV--ARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
43-496 |
1.22e-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: 255.73 E-value: 1.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWNI--WADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQ 120
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 121 EYVDVCDYAAGLSRMIGGPT---LPSERPGHALIEmwnPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSl 197
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSynnLGDDMLGLVLRE---PIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 198 vsvAVTKIIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAII 276
Cdd:cd07118 160 ---GTTLMLAELLIEAGLPAGVVNIVTGyGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 277 AFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRA 356
Cdd:cd07118 237 VFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 357 VEEAKKQGGTVVYGGKVMDH-PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 435
Cdd:cd07118 317 VDAGRAEGATLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 188035915 436 LGRIFrwLGPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 496
Cdd:cd07118 397 IDTAL--TVARRIRAGTVWVNtFLDGSPEL--PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
28-496 |
1.71e-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: 255.98 E-value: 1.71e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNI--WADIPAPKRGEIVRKIGDAFREKIQLLGRL 103
Cdd:cd07091 9 NNEFvdSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 104 VSLEMGKILVEGI-GEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMwNPLGLVGIITAFNFPVAVFGWNNAIALI 182
Cdd:cd07091 89 ESLDNGKPLEESAkGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRR-EPIGVCGQIIPWNFPLLMLAWKLAPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 183 TGNVCLWKGAPTTSLVSVAVtkiiAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQER 261
Cdd:cd07091 168 AGNTVVLKPAEQTPLSALYL----AELIKEAGFPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 262 FGKSL-LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNIL 340
Cdd:cd07091 244 NLKKVtLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 341 YGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWN 420
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 421 NEVKQGLSSSIFTKDLGRIFR----------WLgpkgsDC-GIVNVNIPtsgaeiggaFGGEKHTGGGRESGSDAWKQYM 489
Cdd:cd07091 404 NDTEYGLAAGVFTKDINKALRvsralkagtvWV-----NTyNVFDAAVP---------FGGFKQSGFGRELGEEGLEEYT 469
|
....*..
gi 188035915 490 RRSTCTI 496
Cdd:cd07091 470 QVKAVTI 476
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
28-441 |
7.64e-79 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 254.45 E-value: 7.64e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW-GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSL 106
Cdd:PRK13473 8 NGELvAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 107 EMGK-ILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGN 185
Cdd:PRK13473 88 NCGKpLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 186 VCLWKGAPTTSLVSVAVtkiiAQVLEDNLLPGAIcSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVAlmvqERFGK 264
Cdd:PRK13473 168 TVVLKPSEITPLTALKL----AELAADILPPGVL-NVVTGrGATVGDALVGHPKVRMVSLTGSIATGKHVL----SAAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 265 SL----LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNIL 340
Cdd:PRK13473 239 SVkrthLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 341 YGPLHTKQAVSMFVRAVEEAKKQG-GTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEW 419
Cdd:PRK13473 319 LGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRW 398
|
410 420
....*....|....*....|..
gi 188035915 420 NNEVKQGLSSSIFTKDLGRIFR 441
Cdd:PRK13473 399 ANDSDYGLASSVWTRDVGRAHR 420
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
28-481 |
6.24e-78 |
|
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: 6.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKRGEIVRKIGDAFREKIQLLGRL 103
Cdd:cd07139 4 GGRWvaPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDngPWPRLSPAERAAVLRRLADALEARADELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 104 VSLEMGK-ILVEGIGEVQEYVDVCDYAAGLSRmigGPTLPSERP----GHALI--EmwnPLGLVGIITAFNFPVAVFGWN 176
Cdd:cd07139 84 WTAENGMpISWSRRAQGPGPAALLRYYAALAR---DFPFEERRPgsggGHVLVrrE---PVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 177 NAIALITGNVCLWKGAPTTSLVSVavtkIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVAL 256
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAY----LLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 257 MVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWD 336
Cdd:cd07139 234 VCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 337 PNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHP--GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEE 414
Cdd:cd07139 314 PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLdrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 415 EVFEWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVNIPTSgaEIGGAFGGEKHTGGGRESG 481
Cdd:cd07139 394 DAVRIANDSDYGLSGSVWTADVERglaVARRI-----RTGTVGVNGFRL--DFGAPFGGFKQSGIGREGG 456
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
38-479 |
4.50e-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: 249.27 E-value: 4.50e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 38 ITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIG 117
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 118 EVQEYVDVCDYAAGLSRMIGGPTLPSE----RPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 193
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 194 TTSLVSVAVTKIIaqvLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKevALMVQERFGKSLLELGGNN 273
Cdd:cd07094 161 KTPLSALELAKIL---VEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGE--ALRANAGGKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 274 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 353
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 354 VRAVEEAKKQGGTVVYGGKvmdHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT 433
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 188035915 434 KDLGRIFRwlGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRE 479
Cdd:cd07094 393 RDLNVAFK--AAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGRE 436
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
28-490 |
8.47e-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: 249.33 E-value: 8.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNI--WADIPAPKRGEIVRKIGDAFREKIQLLGRL 103
Cdd:cd07142 9 NGQFvdAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 104 VSLEMGKILVEG-IGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIeMWNPLGLVGIITAFNFPVAVFGWNNAIALI 182
Cdd:cd07142 89 ETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYT-LHEPIGVVGQIIPWNFPLLMFAWKVGPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 183 TGNVCLWKGAPTTSLVSVAVTKIIAQVLednlLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVA-LMVQE 260
Cdd:cd07142 168 CGNTIVLKPAEQTPLSALLAAKLAAEAG----LPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMqLAAKS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 261 RFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNIL 340
Cdd:cd07142 244 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 341 YGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWN 420
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 421 NEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMR 490
Cdd:cd07142 404 NNSKYGLAAGVFSKNIDTANTLS--RALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
28-489 |
9.48e-76 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 246.74 E-value: 9.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 105
Cdd:PRK11241 16 NGEWldANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 106 LEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGN 185
Cdd:PRK11241 96 LEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 186 VCLWKGAPTTSLVSVAvtkiIAQVLEDNLLPGAICSLVCGGA-DIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGK 264
Cdd:PRK11241 176 TMVLKPASQTPFSALA----LAELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 265 SLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPL 344
Cdd:PRK11241 252 VSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 345 HTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVK 424
Cdd:PRK11241 332 IDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTE 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188035915 425 QGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIgGAFGGEKHTGGGRESGSDAWKQYM 489
Cdd:PRK11241 412 FGLAAYFYARDLSRVFRV--GEALEYGIVGINTGIISNEV-APFGGIKASGLGREGSKYGIEDYL 473
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
28-480 |
1.45e-75 |
|
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: 245.83 E-value: 1.45e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 105
Cdd:cd07117 6 NGEWvkGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 106 LEMGKILVEGIGevqeyVDVcDYAAGLSRMIGGPTLPSERPGHAL------IEMWNPLGLVGIITAFNFPVAVFGWNNAI 179
Cdd:cd07117 86 LDNGKPIRETRA-----VDI-PLAADHFRYFAGVIRAEEGSANMIdedtlsIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 180 ALITGNVCLWKGAPTTSLVSVAVTKIIAQVLednllPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMV 258
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDVL-----PKGVVNIVTGkGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 259 QERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPN 338
Cdd:cd07117 235 AKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 339 ILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEE 414
Cdd:cd07117 315 TQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTED 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 415 EVFEWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRES 480
Cdd:cd07117 395 EVIDMANDSEYGLGGGVFTKDINRALRV--ARAVETGRVWVNtynqIPA-----GAPFGGYKKSGIGRET 457
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
28-497 |
3.71e-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: 242.09 E-value: 3.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW-GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWA-DIPAPKRGEIVRKIGDAFREKIQLLGRLVS 105
Cdd:cd07082 7 NGEWkESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWpTMPLEERIDCLHKFADLLKENKEEVANLLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 106 LEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHAL----IEMWNPLGLVGIITAFNFPVavfgwNNAI-- 179
Cdd:cd07082 87 WEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaQVRREPLGVVLAIGPFNYPL-----NLTVsk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 180 ---ALITGNVCLWKGAPTTSLVSVavtkIIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVG---K 252
Cdd:cd07082 162 lipALIMGNTVVFKPATQGVLLGI----PLAEAFHDAGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGnrlK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 253 EVALMVQerfgkSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVG 332
Cdd:cd07082 238 KQHPMKR-----LVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 333 NPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDhpGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQD 412
Cdd:cd07082 313 MPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVND 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 413 EEEVFEWNNEVKQGLSSSIFTKDLGRIF---RWLgpkgsDCGIVNVNIPTS-GAEIgGAFGGEKHTGGGRESGSDAWKQY 488
Cdd:cd07082 391 IEEAIELANKSNYGLQASIFTKDINKARklaDAL-----EVGTVNINSKCQrGPDH-FPFLGRKDSGIGTQGIGDALRSM 464
|
....*....
gi 188035915 489 MRRSTCTIN 497
Cdd:cd07082 465 TRRKGIVIN 473
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
35-490 |
9.83e-74 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 241.32 E-value: 9.83e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 35 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVE 114
Cdd:PRK13252 21 GETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 115 GI-GEVQEYVDVCDYAAGLSRMIGGPTLPSeRPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 193
Cdd:PRK13252 101 TSvVDIVTGADVLEYYAGLAPALEGEQIPL-RGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 194 TTSLVSVAvtkiIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 273
Cdd:PRK13252 180 VTPLTALK----LAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 274 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 353
Cdd:PRK13252 256 PLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 354 VRAVEEAKKQGGTVVYGGKVMDH----PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSS 429
Cdd:PRK13252 336 LGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAA 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188035915 430 SIFTKDLGRIFRWLGpkGSDCGIVNVNipTSG---AEIggAFGGEKHTGGGRESGSDAWKQYMR 490
Cdd:PRK13252 416 GVFTADLSRAHRVIH--QLEAGICWIN--TWGespAEM--PVGGYKQSGIGRENGIATLEHYTQ 473
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
43-498 |
1.28e-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: 240.81 E-value: 1.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAW-NIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGK-ILVEGIGEVQ 120
Cdd:cd07113 22 PATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKsIHLSRAFEVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 121 EYVDVCDYAAGLSRMIGG----PTLPSerPGHALIEMWN---PLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 193
Cdd:cd07113 102 QSANFLRYFAGWATKINGetlaPSIPS--MQGERYTAFTrrePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 194 TTSLVSVAvtkiIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 273
Cdd:cd07113 180 FTPLTLLR----VAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 274 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 353
Cdd:cd07113 256 AAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 354 VRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT 433
Cdd:cd07113 336 CSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWT 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188035915 434 KDLGRIFRWLgPKgSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 498
Cdd:cd07113 416 NNLSKALRYI-PR-IEAGTVWVNMHTF-LDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY 477
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
28-479 |
1.39e-72 |
|
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: 238.40 E-value: 1.39e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 105
Cdd:cd07559 6 NGEWvaPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 106 LEMGKILVEGIG-EVQEYVDVCDYAAGLSR-------MIGGPTLPserpghalIEMWNPLGLVGIITAFNFPVAVFGWNN 177
Cdd:cd07559 86 LDNGKPIRETLAaDIPLAIDHFRYFAGVIRaqegslsEIDEDTLS--------YHFHEPLGVVGQIIPWNFPLLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 178 AIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLednllPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVAL 256
Cdd:cd07559 158 APALAAGNTVVLKPASQTPLSILVLMELIGDLL-----PKGVVNVVTGfGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 257 MVQERFGKSLLELGGNNAIIAFEDA-------DLSLVVPSVLFAAvgTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQI 329
Cdd:cd07559 233 YAAENLIPVTLELGGKSPNIFFDDAmdadddfDDKAEEGQLGFAF--NQGEVCTCPSRALVQESIYDEFIERAVERFEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 330 RVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPIL 405
Cdd:cd07559 311 KVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVL 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188035915 406 YVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRE 479
Cdd:cd07559 391 AVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRV--ARGIQTGRVWVNcyhqYPA-----HAPFGGYKKSGIGRE 461
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
28-458 |
2.86e-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: 237.42 E-value: 2.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 105
Cdd:cd07085 6 NGEWveSKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLIT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 106 LEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGN 185
Cdd:cd07085 86 LEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 186 VCLWKGAPTTSLVSVavtkIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEvalmVQER---F 262
Cdd:cd07085 166 TFVLKPSERVPGAAM----RLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEY----IYERaaaN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 263 GKSLLELGG-NNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILY 341
Cdd:cd07085 238 GKRVQALGGaKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 342 GPLHTKQAVSMFVRAVEEAKKQGGTVVYGG---KVMDHP-GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVF 417
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVLDGrgvKVPGYEnGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 188035915 418 EWNNEVKQGLSSSIFTKD--LGRIFRwlgpKGSDCGIVNVNIP 458
Cdd:cd07085 398 AIINANPYGNGAAIFTRSgaAARKFQ----REVDAGMVGINVP 436
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
35-498 |
5.12e-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: 237.01 E-value: 5.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 35 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAW--NIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKIL 112
Cdd:cd07140 20 GKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFenGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 113 VEGIG-EVQEYVDVCDYAAGLSRMIGGPTLP--SERPGHAL-IEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCL 188
Cdd:cd07140 100 TLALKtHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 189 WKGAPTTSLVSVAVTKIIAQVledNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQE-RFGKSLL 267
Cdd:cd07140 180 LKPAQVTPLTALKFAELTVKA---GFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVsNLKKVSL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 268 ELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTK 347
Cdd:cd07140 257 ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 348 QAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDE--EEVFEWNNEVKQ 425
Cdd:cd07140 337 AHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEY 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 188035915 426 GLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 498
Cdd:cd07140 417 GLASGVFTKDINKALYV--SDKLEAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIEY 486
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
13-497 |
1.50e-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: 235.76 E-value: 1.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 13 WLQDLGLREDNEGVYNGSwggrGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAW-NIWADIPAPKRGEIVRKIGD 91
Cdd:cd07144 4 YDQPTGLFINNEFVKSSD----GETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFeSWWSKVTGEERGELLDKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 92 AFREKIQLLGRLVSLEMGKIL-VEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIeMWNPLGLVGIITAFNFPV 170
Cdd:cd07144 80 LVEKNRDLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYT-LHEPYGVCGQIIPWNYPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 171 AVFGWNNAIALITGNVCLWKGAPTTSLvSVAVtkiIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQ 249
Cdd:cd07144 159 AMAAWKLAPALAAGNTVVIKPAENTPL-SLLY---FANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 250 VGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSlvvPSVLFAAVG---TAGQRCTTVRRLFLHESIHNEVVDRLRSAY 326
Cdd:cd07144 235 TGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLD---QAVKWAAAGimyNSGQNCTATSRIYVQESIYDKFVEKFVEHV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 327 SQI-RVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGG---KVMDHPGNYVEPTIVTGLAHDAPIVHQETFA 402
Cdd:cd07144 312 KQNyKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 403 PILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGS 482
Cdd:cd07144 392 PVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVA--RELEAGMVWIN-SSNDSDVGVPFGGFKMSGIGRELGE 468
|
490
....*....|....*
gi 188035915 483 DAWKQYMRRSTCTIN 497
Cdd:cd07144 469 YGLETYTQTKAVHIN 483
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
49-489 |
1.73e-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: 1.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 49 IARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDY 128
Cdd:cd07152 4 LGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 129 AAGLSRMIGGPTLPSErPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTslvsvAVTK--II 206
Cdd:cd07152 84 AAGLPTQPQGEILPSA-PGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRT-----PVSGgvVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 207 AQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLV 286
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 287 VPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGT 366
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 367 VVYGGKvmdHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRwLGPK 446
Cdd:cd07152 318 LEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA-LADR 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 188035915 447 gSDCGIVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSDAWKQYM 489
Cdd:cd07152 394 -LRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFT 436
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
42-489 |
6.99e-69 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 227.96 E-value: 6.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 42 CPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQE 121
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 122 YVDVCDYAAGLSRMIggptLPSERPGHAL------IEMWNPLGLVGIITAFNFPVAVfGWNNAI-ALITGNVCLWKGAPT 194
Cdd:cd07101 82 VAIVARYYARRAERL----LKPRRRRGAIpvltrtTVNRRPKGVVGVISPWNYPLTL-AVSDAIpALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 195 TSLVSVAVtkiiAQVLEDNLLPGAICSLVCG-GADIGTTMArdERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNN 273
Cdd:cd07101 157 TALTALWA----VELLIEAGLPRDLWQVVTGpGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 274 AIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMF 353
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 354 VRAVEEAKKQGGTVVYGGKVMDHPGNYV-EPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIF 432
Cdd:cd07101 311 TAHVDDAVAKGATVLAGGRARPDLGPYFyEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVW 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 188035915 433 TKDLGRIfRWLGPKgSDCGIVNVN--IPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 489
Cdd:cd07101 391 TRDGARG-RRIAAR-LRAGTVNVNegYAAAWASIDAPMGGMKDSGLGRRHGAEGLLKYT 447
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
43-481 |
7.30e-69 |
|
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: 7.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 122
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 123 VDVCDYAAGLS---RMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVS 199
Cdd:cd07110 84 AGCFEYYADLAeqlDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 200 VAVTKIIAQVledNLLPGAICsLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAF 278
Cdd:cd07110 164 LELAEIAAEA---GLPPGVLN-VVTGtGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 279 EDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVE 358
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 359 EAKKQGGTVVYGGKVMDHP--GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDL 436
Cdd:cd07110 320 RGKEEGARLLCGGRRPAHLekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 188035915 437 GRIFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRESG 481
Cdd:cd07110 400 ERCDRV--AEALEAGIVWINCSQP-CFPQAPWGGYKRSGIGRELG 441
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
21-497 |
1.58e-68 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 227.80 E-value: 1.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 21 EDNEGVY-NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNI-WA-DIPAPKRGEIVRKIGDAFRE 95
Cdd:cd07143 4 EQPTGLFiNGEFvdSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGlKVSGSKRGRCLSKLADLMER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 96 KIQLLGRLVSLEMGK-ILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLP--SERPGHALIEmwnPLGLVGIITAFNFPVAV 172
Cdd:cd07143 84 NLDYLASIEALDNGKtFGTAKRVDVQASADTFRYYGGWADKIHGQVIEtdIKKLTYTRHE---PIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 173 FGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAqvlEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGK 252
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIP---EAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 253 evalMVQERFGKS-----LLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYS 327
Cdd:cd07143 238 ----KVMEAAAKSnlkkvTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 328 QIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYV 407
Cdd:cd07143 314 KLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 408 FKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLGP-KGSDCGIVNVNIPTSGAeiggAFGGEKHTGGGRESGSDAWK 486
Cdd:cd07143 394 IKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANAlKAGTVWVNCYNLLHHQV----PFGGYKQSGIGRELGEYALE 469
|
490
....*....|.
gi 188035915 487 QYMRRSTCTIN 497
Cdd:cd07143 470 NYTQIKAVHIN 480
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
35-496 |
1.81e-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: 227.62 E-value: 1.81e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 35 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNI---WADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGK- 110
Cdd:cd07141 21 GKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 111 ILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIeMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWK 190
Cdd:cd07141 101 FSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYT-RHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 191 GAPTTSLVSVAVTKIIAqvlEDNLLPGAIcSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKevalMVQERFGKS---- 265
Cdd:cd07141 180 PAEQTPLTALYLASLIK---EAGFPPGVV-NVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGK----LIQQAAGKSnlkr 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 266 -LLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPL 344
Cdd:cd07141 252 vTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 345 HTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVK 424
Cdd:cd07141 332 IDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTT 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 188035915 425 QGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAeIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 496
Cdd:cd07141 412 YGLAAAVFTKDIDKAITF--SNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
35-489 |
2.40e-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: 2.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 35 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKIL 112
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 113 VEGI-GEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMwNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKG 191
Cdd:cd07112 81 SDALaVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITR-EPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 192 APTTSLvsvavTKI-IAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKevalMVQERFGKS---- 265
Cdd:cd07112 160 AEQSPL-----TALrLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGR----RFLEYSGQSnlkr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 266 -LLELGGNNAIIAFEDA-DLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGP 343
Cdd:cd07112 231 vWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 344 LHTKQAVSMFVRAVEEAKKQGGTVVYGGKV--MDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNN 421
Cdd:cd07112 311 LVSEAHFDKVLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALAN 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188035915 422 EVKQGLSSSIFTKDLGRIFRwlGPKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 489
Cdd:cd07112 391 DSVYGLAASVWTSDLSRAHR--VARRLRAGTVWVNC-FDEGDITTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
87-441 |
9.43e-67 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 220.76 E-value: 9.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 87 RKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAF 166
Cdd:PRK10090 2 RKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 167 NFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLednlLPGAICSLVCG-GADIGTTMARDERVNLLSFT 245
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIG----LPKGVFNLVLGrGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 246 GSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSA 325
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 326 YSQIRVGNPWD-PNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPI 404
Cdd:PRK10090 238 MQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 188035915 405 LYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFR 441
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMK 354
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
43-438 |
1.13e-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: 221.74 E-value: 1.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 122
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 123 VDVCDYAAGLSRMIGGPTLPSERPG-HALIEMwNPLGLVGIITAFNFP--VAVfgwnNAI--ALITGNVCLWKGAPTTSL 197
Cdd:cd07102 83 LERARYMISIAEEALADIRVPEKDGfERYIRR-EPLGVVLIIAPWNYPylTAV----NAVipALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 198 VSVAvtkiIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIA 277
Cdd:cd07102 158 CGER----FAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 278 FEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVsMFVRA- 356
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAA-DFVRAq 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 357 VEEAKKQGGTVVYGGK---VMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT 433
Cdd:cd07102 313 IADAIAKGARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWT 392
|
....*
gi 188035915 434 KDLGR 438
Cdd:cd07102 393 KDIAR 397
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
7-492 |
3.40e-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: 221.50 E-value: 3.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 7 HHPQYAWLQDlglREDNEGVY-NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRG 83
Cdd:cd07111 8 AACALAWLDA---HDRSFGHFiNGKWvkPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 84 EIVRKIGDAFREKIQLLGRLVSLEMGKilveGIGEVQEyVDVCDYAAGLSRMIG-GPTLPSERPGhaliemWNPLGLVGI 162
Cdd:cd07111 85 RHLYRIARHIQKHQRLFAVLESLDNGK----PIRESRD-CDIPLVARHFYHHAGwAQLLDTELAG------WKPVGVVGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 163 ITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVledNLLPGaICSLVCGGADIGTTMARDERVNLL 242
Cdd:cd07111 154 IVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEA---GLPPG-VLNIVTGNGSFGSALANHPGVDKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 243 SFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRL 322
Cdd:cd07111 230 AFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 323 RSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFA 402
Cdd:cd07111 310 KERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 403 PILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRwLGPkGSDCGIVNVNI-----PTSGaeiggaFGGEKHTGGG 477
Cdd:cd07111 390 PVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALE-VAL-SLKAGVVWINGhnlfdAAAG------FGGYRESGFG 461
|
490
....*....|....*
gi 188035915 478 RESGSDAWKQYMRRS 492
Cdd:cd07111 462 REGGKEGLYEYLRPS 476
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
28-489 |
5.73e-66 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 221.53 E-value: 5.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW-----GGRGEVITtycPANNEPIARVRQASLKDYEETIGKAKKAWNI-----WADIPAPKRGEIVRKIGDAFREKI 97
Cdd:PLN02467 13 GGEWrepvlGKRIPVVN---PATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 98 QLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRMIGGP-----TLPSER-PGHALiemWNPLGLVGIITAFNFPVA 171
Cdd:PLN02467 90 SELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKqkapvSLPMETfKGYVL---KEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 172 VFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVledNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVG 251
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREV---GLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 252 KEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRV 331
Cdd:PLN02467 244 RKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 332 GNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDH--PGNYVEPTIVTGLAHDAPIVHQETFAPILYVFK 409
Cdd:PLN02467 324 SDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 410 FQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN--------IPtsgaeiggaFGGEKHTGGGRESG 481
Cdd:PLN02467 404 FSTEDEAIELANDSHYGLAGAVISNDLERCERV--SEAFQAGIVWINcsqpcfcqAP---------WGGIKRSGFGRELG 472
|
....*...
gi 188035915 482 SDAWKQYM 489
Cdd:PLN02467 473 EWGLENYL 480
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
26-491 |
3.27e-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: 219.37 E-value: 3.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 26 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLV 104
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 105 SLEMGKILVEGIGEVQEYVDVCDYAAGLS-RMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALIT 183
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYYARAAlRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 184 GNVCLWKGAPTTSLVSVAVTKIIAQVledNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQER-- 261
Cdd:cd07083 182 GNTVIAKPAEDAVVVGYKVFEIFHEA---GFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLap 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 262 ----FGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDP 337
Cdd:cd07083 259 gqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 338 NILYGPLHTKQAVSMFVRAVEEAkKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEE--E 415
Cdd:cd07083 339 GTDLGPVIDAEQEAKVLSYIEHG-KNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaE 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188035915 416 VFEWNNEVKQGLSSSIFTKDLGRIfRWLGPKgSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdawKQYMRR 491
Cdd:cd07083 418 ALEVANSTPYGLTGGVYSRKREHL-EEARRE-FHVGNLYINRKITGALVGvQPFGGFKLSGTNAKTGG---PHYLRR 489
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
32-483 |
1.53e-62 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 212.82 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 32 GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKI 111
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 112 LVEGIGEVQEYVDVCDY----AAGLSRmiggptlPSERPGhAL------IEMWNPLGLVGIITAFNFPVAVfGWNNAI-A 180
Cdd:PRK09407 108 RRHAFEEVLDVALTARYyarrAPKLLA-------PRRRAG-ALpvltktTELRQPKGVVGVISPWNYPLTL-AVSDAIpA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 181 LITGNVCLWKGAPTTSLVSVAVtkiiAQVLEDNLLPGAICSLVCG-GADIGTTMArdERVNLLSFTGSTQVGKEVAlmvq 259
Cdd:PRK09407 179 LLAGNAVVLKPDSQTPLTALAA----VELLYEAGLPRDLWQVVTGpGPVVGTALV--DNADYLMFTGSTATGRVLA---- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 260 ERFGKSL----LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPW 335
Cdd:PRK09407 249 EQAGRRLigfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 336 DPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYV-EPTIVTGLAHDAPIVHQETFAPILYVFKFQDEE 414
Cdd:PRK09407 329 DYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGPLFyEPTVLTGVTPDMELAREETFGPVVSVYPVADVD 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188035915 415 EVFEWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVN---IPTSGAeIGGAFGGEKHTGGGRESGSD 483
Cdd:PRK09407 409 EAVERANDTPYGLNASVWTGDTARgraIAARI-----RAGTVNVNegyAAAWGS-VDAPMGGMKDSGLGRRHGAE 477
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
67-484 |
2.73e-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: 2.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 67 AKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEYVDVCDYAAGLSRmiggptlpsERP 146
Cdd:cd07095 9 ARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYH---------ERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 147 GHALIEMWN--------PLGLVGIITAFNFPVAVFgwNNAI--ALITGNVCLWKGAPTTSlvsvAVTKIIAQVLEDNLLP 216
Cdd:cd07095 80 GERATPMAQgravlrhrPHGVMAVFGPFNFPGHLP--NGHIvpALLAGNTVVFKPSELTP----AVAELMVELWEEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 217 GAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSL-LELGGNNAIIAFEDADLSLVVPSVLFAAV 295
Cdd:cd07095 154 PGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 296 GTAGQRCTTVRRLFLHES-IHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVM 374
Cdd:cd07095 234 LTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 375 DHPGNYVEPTI--VTGLahdAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDlGRIFRWLGPKgSDCGI 452
Cdd:cd07095 314 VAGTAFLSPGIidVTDA---ADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDD-EALFERFLAR-IRAGI 388
|
410 420 430
....*....|....*....|....*....|..
gi 188035915 453 VNVNIPTSGAEIGGAFGGEKHTGGGRESGSDA 484
Cdd:cd07095 389 VNWNRPTTGASSTAPFGGVGLSGNHRPSAYYA 420
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
28-481 |
2.82e-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: 210.82 E-value: 2.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW-----GGRGEVIttyCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGR 102
Cdd:cd07138 4 DGAWvapagTETIDVI---NPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 103 LVSLEMG-------KILVE-GIGEVQEYVDVC-DYAAglsrmiggptlpSERPGHALIEMwNPLGLVGIITAFNFPVavf 173
Cdd:cd07138 81 AITLEMGapitlarAAQVGlGIGHLRAAADALkDFEF------------EERRGNSLVVR-EPIGVCGLITPWNWPL--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 174 gwnNAI------ALITGNVCLWKG---APTTSLvsvavtkIIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLS 243
Cdd:cd07138 145 ---NQIvlkvapALAAGCTVVLKPsevAPLSAI-------ILAEILDEAGLPAGVFNLVNGdGPVVGEALSAHPDVDMVS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 244 FTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLR 323
Cdd:cd07138 215 FTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 324 SAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGkvMDHP-----GNYVEPTIVTGLAHDAPIVHQ 398
Cdd:cd07138 295 AAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG--PGRPeglerGYFVKPTVFADVTPDMTIARE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 399 ETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVNipTSGAEIGGAFGGEKHTG 475
Cdd:cd07138 373 EIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERaraVARRL-----RAGQVHIN--GAAFNPGAPFGGYKQSG 445
|
....*.
gi 188035915 476 GGRESG 481
Cdd:cd07138 446 NGREWG 451
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
7-481 |
8.84e-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: 208.20 E-value: 8.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 7 HHPQYAWLQDLGLREDNEG----VYNGSWGGRGEVITTYCPANNE-PIARVRQASLKDYEETIGKAKKAWNIWADIPAPK 81
Cdd:cd07125 13 EVPLEALADALKAFDEKEWeaipIINGEETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 82 RGEIVRKIGDAFRE-KIQLLGrLVSLEMGKILVEGIGEVQEYVDVCD-YAAGLSRMIGGPTLPS---ERPGHalieMWNP 156
Cdd:cd07125 93 RAEILEKAADLLEAnRGELIA-LAAAEAGKTLADADAEVREAIDFCRyYAAQARELFSDPELPGptgELNGL----ELHG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 157 LGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIiaqvLEDNLLPGAICSLV-CGGADIGTTMAR 235
Cdd:cd07125 168 RGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVEL----LHEAGVPRDVLQLVpGDGEEIGEALVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 236 DERVNLLSFTGSTQVGKEVALMVQERFGKSLL---ELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHE 312
Cdd:cd07125 244 HPRIDGVIFTGSTETAKLINRALAERDGPILPliaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 313 SIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMfVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGlahD 392
Cdd:cd07125 324 EIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKL-LRAHTELMRGEAWLIAPAPLDDGNGYFVAPGIIEI---V 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 393 APIVHQ-ETFAPILYV--FKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAeIGGA-- 467
Cdd:cd07125 400 GIFDLTtEVFGPILHVirFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWR--ERVEAGNLYINRNITGA-IVGRqp 476
|
490
....*....|....
gi 188035915 468 FGGEKHTGGGRESG 481
Cdd:cd07125 477 FGGWGLSGTGPKAG 490
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
35-490 |
1.52e-59 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 204.28 E-value: 1.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 35 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKIL 112
Cdd:PLN02766 35 GKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 113 VEGigevqEYVDV------CDYAAGLSRMIGGPTLPSERP--GHALIEmwnPLGLVGIITAFNFPVAVFGWNNAIALITG 184
Cdd:PLN02766 115 ALG-----KAVDIpaaaglLRYYAGAADKIHGETLKMSRQlqGYTLKE---PIGVVGHIIPWNFPSTMFFMKVAPALAAG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 185 NVCLWKGAPTTSLVSVavtkIIAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFG 263
Cdd:PLN02766 187 CTMVVKPAEQTPLSAL----FYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 264 KSL-LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYG 342
Cdd:PLN02766 263 KQVsLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 343 PLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNE 422
Cdd:PLN02766 343 PQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANN 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188035915 423 VKQGLSSSIFTKDL---GRIFRWLgpkgsDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMR 490
Cdd:PLN02766 423 TKYGLAAGIVTKDLdvaNTVSRSI-----RAGTIWVNC-YFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
59-496 |
5.37e-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: 5.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 59 DYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMG------KILVEGIGEVQEyvdvcDYAAGL 132
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGataawaGFNVDLAAGMLR-----EAASLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 133 SRMIGGpTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAvtkiIAQVLED 212
Cdd:cd07105 76 TQIIGG-SIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWL----IGRVFHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 213 NLLP-GAICSLVCGGAD---IGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVP 288
Cdd:cd07105 151 AGLPkGVLNVVTHSPEDapeVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 289 SVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRvgnpWDPNILyGPLHTKQAVSMFVRAVEEAKKQGGTVV 368
Cdd:cd07105 231 AALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLF----AGPVVL-GSLVSAAAADRVKELVDDALSKGAKLV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 369 YGGKVMDHP-GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRwLGpKG 447
Cdd:cd07105 306 VGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALA-VA-KR 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 188035915 448 SDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 496
Cdd:cd07105 384 IESGAVHINGMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
26-441 |
1.70e-56 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 196.69 E-value: 1.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 26 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLV 104
Cdd:PRK03137 40 IIGGERITTEDKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 105 SLEMGKILVEGIGEVQEYVDVCDYAAglSRMI----GGPTLPseRPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIA 180
Cdd:PRK03137 120 VKEAGKPWAEADADTAEAIDFLEYYA--RQMLkladGKPVES--RPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 181 LITGNVCLWKGAPTTSLVSVAVtkiiAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVG---KEVAL 256
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKF----VEVLEEAGLPAGVVNFVPGsGSEVGDYLVDHPKTRFITFTGSREVGlriYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 257 MVQE--RFGKS-LLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGN 333
Cdd:PRK03137 272 KVQPgqIWLKRvIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 334 PWDPNILyGPLHTKQAVSMFVRAVEEAKKQgGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDE 413
Cdd:PRK03137 352 PEDNAYM-GPVINQASFDKIMSYIEIGKEE-GRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420
....*....|....*....|....*...
gi 188035915 414 EEVFEWNNEVKQGLSSSIFTKDLGRIFR 441
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEK 457
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
41-481 |
2.68e-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: 2.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 41 YCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEG-IGEV 119
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 120 qeyVDVCDYAAGLSRMiGGPTL-PSERPGHALieMW--------NPLGLVGIITAFNFPVAVFgWNNAI-ALITGNVCLW 189
Cdd:cd07098 81 ---LVTCEKIRWTLKH-GEKALrPESRPGGLL--MFykrarveyEPLGVVGAIVSWNYPFHNL-LGPIIaALFAGNAIVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 190 KGAPTTSLVSVAVTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLEL 269
Cdd:cd07098 154 KVSEQVAWSSGFFLSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 270 GGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQA 349
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 350 VSMFVRAVEEAKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQ 425
Cdd:cd07098 314 FDRLEELVADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEY 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 188035915 426 GLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNiptsgaEIGGA-------FGGEKHTGGGRESG 481
Cdd:cd07098 394 GLGASVFGKDIKRARRIA--SQLETGMVAIN------DFGVNyyvqqlpFGGVKGSGFGRFAG 448
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
35-490 |
1.95e-55 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 194.26 E-value: 1.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 35 GEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKIL 112
Cdd:PLN02466 72 GKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 113 VEGIG-EVQEYVDVCDYAAGLSRMIGGPTLPSERPgHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKG 191
Cdd:PLN02466 152 EQSAKaELPMFARLFRYYAGWADKIHGLTVPADGP-HHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 192 APTTSLVSVAVTKIIaqvLEDNLLPGaICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKevalMVQERFGKS----- 265
Cdd:PLN02466 231 AEQTPLSALYAAKLL---HEAGLPPG-VLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGK----IVLELAAKSnlkpv 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 266 LLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLH 345
Cdd:PLN02466 303 TLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQI 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 346 TKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQ 425
Cdd:PLN02466 383 DSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRY 462
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188035915 426 GLSSSIFTKDL---GRIFRWLgpkgsDCGIVNVN--------IPtsgaeiggaFGGEKHTGGGRESGSDAWKQYMR 490
Cdd:PLN02466 463 GLAAGVFTQNLdtaNTLSRAL-----RVGTVWVNcfdvfdaaIP---------FGGYKMSGIGREKGIYSLNNYLQ 524
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
43-479 |
4.26e-53 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 186.22 E-value: 4.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 122
Cdd:PRK13968 14 PATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 123 VDVCDYAA--GLSRMIGGPTLPSERpgHALIEmWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTslvsV 200
Cdd:PRK13968 94 ANLCDWYAehGPAMLKAEPTLVENQ--QAVIE-YRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV----M 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 201 AVTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFED 280
Cdd:PRK13968 167 GCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 281 ADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEA 360
Cdd:PRK13968 247 ADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 361 KKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIF 440
Cdd:PRK13968 327 LAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQAR 406
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 188035915 441 RWlgPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRE 479
Cdd:PRK13968 407 QM--AARLECGGVFINgYCASDARV--AFGGVKKSGFGRE 442
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
32-495 |
6.02e-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: 6.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 32 GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKI 111
Cdd:TIGR01722 12 GASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 112 LVEGIGEVQEYVDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKG 191
Cdd:TIGR01722 92 HSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 192 APTTSLVSVAVtkiiAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVaLMVQERFGKSLLELGG 271
Cdd:TIGR01722 172 SEKVPSAAVKL----AELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYI-HTTGSAHGKRVQALGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 272 -NNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIhNEVVDRLRSAYSQIRVGnPW-DPNILYGPLHTKQA 349
Cdd:TIGR01722 247 aKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIG-PGdDPGAEMGPLITPQA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 350 VSMFVRAVEEAKKQGGTVVYGG---KVMDHP-GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQ 425
Cdd:TIGR01722 325 KDRVASLIAGGAAEGAEVLLDGrgyKVDGYEeGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPY 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188035915 426 GLSSSIFTKDLG--RIFRWLgpkgSDCGIVNVNIPTSGAEIGGAFGGEKHT--GGGRESGSDAWKQYMRRSTCT 495
Cdd:TIGR01722 405 GNGTAIFTRDGAaaRRFQHE----IEVGQVGVNVPIPVPLPYFSFTGWKDSffGDHHIYGKQGTHFYTRGKTVT 474
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
35-414 |
1.26e-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: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 35 GEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILV 113
Cdd:COG4230 569 GEARPVRNPADhSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLP 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 114 EGIGEVQEYVDVCDYAAGLSRmiggpTLPSERPGHAliemwnPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAP 193
Cdd:COG4230 649 DAIAEVREAVDFCRYYAAQAR-----RLFAAPTVLR------GRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAE 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 194 TTSLVSVAVTKII------AQVLedNLLPGAicslvcgGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLL 267
Cdd:COG4230 718 QTPLIAARAVRLLheagvpADVL--QLLPGD-------GETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVP 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 268 ---ELGGNNAIIAfedaDLS-L---VVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNIL 340
Cdd:COG4230 789 liaETGGQNAMIV----DSSaLpeqVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTD 864
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188035915 341 YGPLHTKQAVSMFVRAVEEAKKQgGTVVYGGKVMDHP--GNYVEPTI--VTGLAHdapiVHQETFAPILYVFKFQDEE 414
Cdd:COG4230 865 VGPVIDAEARANLEAHIERMRAE-GRLVHQLPLPEECanGTFVAPTLieIDSISD----LEREVFGPVLHVVRYKADE 937
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
35-479 |
4.84e-49 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 175.31 E-value: 4.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 35 GEVITTYCPANNEPIarvrqaslkdyEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVE 114
Cdd:PRK09406 11 GETVKTFTALTDDEV-----------DAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 115 GIGEVQEYVDVCDYAAGlsrmiGGPTLPSERPGHA-------LIEMWNPLGLVGIITAFNFP---VAVFGwnnAIALITG 184
Cdd:PRK09406 80 AKAEALKCAKGFRYYAE-----HAEALLADEPADAaavgasrAYVRYQPLGVVLAVMPWNFPlwqVVRFA---APALMAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 185 NVCLWKGA---PTTSLVsvavtkiIAQVLEDNLLP-GAICSLVCGGADIGTTMaRDERVNLLSFTGSTQVGKEVALMVQE 260
Cdd:PRK09406 152 NVGLLKHAsnvPQTALY-------LADLFRRAGFPdGCFQTLLVGSGAVEAIL-RDPRVAAATLTGSEPAGRAVAAIAGD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 261 RFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNIL 340
Cdd:PRK09406 224 EIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 341 YGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWN 420
Cdd:PRK09406 304 VGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIA 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 421 NEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEIGgaFGGEKHTGGGRE 479
Cdd:PRK09406 384 NATTFGLGSNAWTRDEAEQERFI--DDLEAGQVFINgMTVSYPELP--FGGVKRSGYGRE 439
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
28-492 |
7.48e-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: 175.48 E-value: 7.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSWGGRGEVITTYCPANNEPI-ARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSL 106
Cdd:TIGR01238 43 GHSYKADGEAQPVTNPADRRDIvGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 107 EMGKILVEGIGEVQEYVDVCDYAAGLSRmiggPTLPSERPghaliemwNPLGLVGIITAFNFPVAVFGWNNAIALITGNV 186
Cdd:TIGR01238 123 EAGKTIHNAIAEVREAVDFCRYYAKQVR----DVLGEFSV--------ESRGVFVCISPWNFPLAIFTGQISAALAAGNT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 187 CLWKGAPTTSLVSvavTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERF---G 263
Cdd:TIGR01238 191 VIAKPAEQTSLIA---YRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdapV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 264 KSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGP 343
Cdd:TIGR01238 268 PLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 344 LHTKQAVSMFVRAVEEAKKQGGTV---VYGGKVMDHPGNYVEPTIVTglAHDAPIVHQETFAPILYVFKFQDEE--EVFE 418
Cdd:TIGR01238 348 VIDAEAKQNLLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAREldQIVD 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188035915 419 WNNEVKQGLSSSIFTKDLGRIfRWLgPKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSDAWKQYMRRS 492
Cdd:TIGR01238 426 QINQTGYGLTMGVHSRIETTY-RWI-EKHARVGNCYVNRNQVGAVVGvQPFGGQGLSGTGPKAGGPHYLYRLTQV 498
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
28-480 |
9.27e-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: 172.25 E-value: 9.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSWGG--RGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 105
Cdd:cd07116 6 GGEWVApvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 106 LEMGKILVEGIG-EVQEYVDVCDYAAGLSRMIGG--PTLPSERPGHALIEmwnPLGLVGIITAFNFPVAVFGWNNAIALI 182
Cdd:cd07116 86 WDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGsiSEIDENTVAYHFHE---PLGVVGQIIPWNFPLLMATWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 183 TGNVCLWKGAPTTSLVSVAVTKIIAqvledNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQER 261
Cdd:cd07116 163 AGNCVVLKPAEQTPASILVLMELIG-----DLLPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 262 FGKSLLELGGNNAIIAFED---ADLSLVVPS----VLFAAvgTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNP 334
Cdd:cd07116 238 IIPVTLELGGKSPNIFFADvmdADDAFFDKAlegfVMFAL--NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 335 WDPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGN----YVEPTIVTGlAHDAPIVHQETFAPILYVFKF 410
Cdd:cd07116 316 LDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTF 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188035915 411 QDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRES 480
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRM--GRGIQAGRVWTNcyhlYPA-----HAAFGGYKQSGIGREN 461
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
32-416 |
2.45e-45 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 170.76 E-value: 2.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 32 GGRGEVITTYCPANNE-PIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGK 110
Cdd:PRK11904 558 NGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGK 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 111 ILVEGIGEVQEYVDVCDYAAGLSR-MIGGPT-LPS---ERpghaliemwNPLGLVG-----IITAFNFPVAVFGWNNAIA 180
Cdd:PRK11904 638 TLQDAIAEVREAVDFCRYYAAQARrLFGAPEkLPGptgES---------NELRLHGrgvfvCISPWNFPLAIFLGQVAAA 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 181 LITGNVCLWKGAPTTSLVSVAVTK------IIAQVLEdnLLPGAicslvcgGADIGTTMARDERVNLLSFTGSTQVGKEV 254
Cdd:PRK11904 709 LAAGNTVIAKPAEQTPLIAAEAVKllheagIPKDVLQ--LLPGD-------GATVGAALTADPRIAGVAFTGSTETARII 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 255 ALMVQERFGKSL---LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRV 331
Cdd:PRK11904 780 NRTLAARDGPIVpliAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKV 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 332 GNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQgGTVVYGGKVMD--HPGNYVEPTI--VTGLAHdapiVHQETFAPILYV 407
Cdd:PRK11904 860 GDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPAgtENGHFVAPTAfeIDSISQ----LEREVFGPILHV 934
|
410
....*....|.
gi 188035915 408 --FKFQDEEEV 416
Cdd:PRK11904 935 irYKASDLDKV 945
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
43-491 |
2.84e-45 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 170.82 E-value: 2.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQE 121
Cdd:PRK11905 574 PADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVRE 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 122 YVDVCD-YAAGLSRMIGGPTLPserpghaliemwnPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLV-S 199
Cdd:PRK11905 654 AVDFLRyYAAQARRLLNGPGHK-------------PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIaA 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 200 VAVtkiiaQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLL---ELGGNNAI 275
Cdd:PRK11905 721 RAV-----RLLHEAGVPKDALQLLPGdGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAM 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 276 IAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVR 355
Cdd:PRK11905 796 IVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEA 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 356 AVEEAKKQgGTVVYGGKVMDH--PGNYVEPTI--VTGLAHdapiVHQETFAPILYV--FKFQDEEEVFEWNNEVKQGLSS 429
Cdd:PRK11905 876 HIEAMRAA-GRLVHQLPLPAEteKGTFVAPTLieIDSISD----LEREVFGPVLHVvrFKADELDRVIDDINATGYGLTF 950
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 188035915 430 SIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdawKQYMRR 491
Cdd:PRK11905 951 GLHSRIDETIAHVT--SRIRAGNIYVNRNIIGAVVGvQPFGGEGLSGTGPKAGG---PLYLGR 1008
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
28-480 |
4.29e-45 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 165.13 E-value: 4.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW-GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSL 106
Cdd:PRK09457 6 NGDWiAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 107 EMGKILVEGIGEVQEyvdvcdyaaglsrMIGGPTLP----SERPGHALIEMWN--------PLGLVGIITAFNFPvavfG 174
Cdd:PRK09457 86 ETGKPLWEAATEVTA-------------MINKIAISiqayHERTGEKRSEMADgaavlrhrPHGVVAVFGPYNFP----G 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 175 W--NNAI--ALITGNVCLWKGAPTTSlvsvAVTKIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQV 250
Cdd:PRK09457 149 HlpNGHIvpALLAGNTVVFKPSELTP----WVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 251 GkeVALMVQ--ERFGKSL-LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIH-NEVVDRLRSAY 326
Cdd:PRK09457 225 G--YLLHRQfaGQPEKILaLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 327 SQIRVGNPW-DPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGNYVEPTI--VTGLAhDAPivHQETFAP 403
Cdd:PRK09457 303 KRLTVGRWDaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIidVTGVA-ELP--DEEYFGP 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188035915 404 ILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 480
Cdd:PRK09457 380 LLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFL--LEIRAGIVNWNKPLTGASSAAPFGGVGASGNHRPS 454
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
43-477 |
6.23e-45 |
|
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: 6.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAK---KAWNIWadIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEV 119
Cdd:cd07148 6 PFDLKPIGEVPTVDWAAIDKALDTAHalfLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 120 QEYVDVCDYAAGLSRMIGGPTLP----SERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTT 195
Cdd:cd07148 84 TRAIDGVELAADELGQLGGREIPmgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 196 SLVSVAVTKIiaqvLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGkevaLMVQERFG---KSLLELGGN 272
Cdd:cd07148 164 PLSCLAFVDL----LHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVG----WMLRSKLApgtRCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 273 NAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSM 352
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 353 FVRAVEEAKKQGGTVVYGGKVMDHpgNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIF 432
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRLSD--TTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 188035915 433 TKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGG 477
Cdd:cd07148 394 TKDLDVALKAV--RRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
7-496 |
3.83e-43 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 159.68 E-value: 3.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 7 HHPQYAWLQDLGLREDNEGVYNGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWN--IWADIPAPKR 82
Cdd:PRK09847 4 HHLAYWQDKALSLAIENRLFINGEYtaAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 83 GEIVRKIGDAFREKIQLLGRLVSLEMGKIL-------VEGIGEVQEYvdvcdYAAGLSRMIG--GPTLPSERpghALIEM 153
Cdd:PRK09847 84 KAVLNKLADLMEAHAEELALLETLDTGKPIrhslrddIPGAARAIRW-----YAEAIDKVYGevATTSSHEL---AMIVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 154 wNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAvtkiIAQVLEDNLLPGAICSLVCG-GADIGTT 232
Cdd:PRK09847 156 -EPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIR----LAGLAKEAGLPDGVLNVVTGfGHEAGQA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 233 MARDERVNLLSFTGSTQVGKEVALMVQERFGKSL-LELGGNNAIIAFEDA-DLSLVVPSVLFAAVGTAGQRCTTVRRLFL 310
Cdd:PRK09847 231 LSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMKRVwLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 311 HESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLhTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPGnYVEPTIVTGLA 390
Cdd:PRK09847 311 EESIADEFLALLKQQAQNWQPGHPLDPATTMGTL-IDCAHADSVHSFIREGESKGQLLLDGRNAGLAA-AIGPTIFVDVD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 391 HDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGaEIGGAFGG 470
Cdd:PRK09847 389 PNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRM--SRRLKAGSVFVNNYNDG-DMTVPFGG 465
|
490 500
....*....|....*....|....*.
gi 188035915 471 EKHTGGGRESGSDAWKQYMRRSTCTI 496
Cdd:PRK09847 466 YKQSGNGRDKSLHALEKFTELKTIWI 491
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
43-505 |
9.33e-41 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 154.90 E-value: 9.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 43 PANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGIGEVQEY 122
Cdd:PLN02419 136 PATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 123 VDVCDYAAGLSRMIGGPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVav 202
Cdd:PLN02419 216 LEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASV-- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 203 tkIIAQVLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDAD 282
Cdd:PLN02419 294 --ILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDAN 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 283 LSLVVPSVLFAAVGTAGQRCTTVRRLFL---HESIHNEVVDRLRSaysqIRVGNPWDPNILYGPLHTKQAVSMFVRAVEE 359
Cdd:PLN02419 372 IDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVERAKA----LKVTCGSEPDADLGPVISKQAKERICRLIQS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 360 AKKQGGTVVYGGKVMDHP----GNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 435
Cdd:PLN02419 448 GVDDGAKLLLDGRDIVVPgyekGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSS 527
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188035915 436 --LGRIFRwlgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGR-----ESGSDAWKQYMRRSTCTINYSTSLPLA 505
Cdd:PLN02419 528 gaAARKFQ----MDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDlnfygKAGVDFFTQIKLVTQKQKDIHSPFSLA 600
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
28-438 |
3.59e-39 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 148.75 E-value: 3.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW--GGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVS 105
Cdd:PLN00412 21 DGEWrtSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 106 LEMGKILVEGIGEVQEYVDVCDYAA--GLSRMIGGPTLPSER-PGHALIEMWN----PLGLVGIITAFNFPVAVFGWNNA 178
Cdd:PLN00412 101 KEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFLVSDSfPGNERNKYCLtskiPLGVVLAIPPFNYPVNLAVSKIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 179 IALITGNVCLWKgAPTTSLVSVAVTkiiAQVLEDNLLPGAICSLVCG-GADIGTTMARDERVNLLSFTGStqvgkEVALM 257
Cdd:PLN00412 181 PALIAGNAVVLK-PPTQGAVAALHM---VHCFHLAGFPKGLISCVTGkGSEIGDFLTMHPGVNCISFTGG-----DTGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 258 VQERFGKSLL--ELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPW 335
Cdd:PLN00412 252 ISKKAGMVPLqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 336 DpNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKvmdHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEE 415
Cdd:PLN00412 332 D-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWK---REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEE 407
|
410 420
....*....|....*....|...
gi 188035915 416 VFEWNNEVKQGLSSSIFTKDLGR 438
Cdd:PLN00412 408 GIHHCNASNFGLQGCVFTRDINK 430
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
49-481 |
1.00e-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: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 49 IARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQ-LLGRLVSlEMGKILVEGIGEVQEYVDVCD 127
Cdd:PRK11809 673 VGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQtLMGLLVR-EAGKTFSNAIAEVREAVDFLR 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 128 YAAGLSRmiggPTLPSERpgHaliemwNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKII- 206
Cdd:PRK11809 752 YYAGQVR----DDFDNDT--H------RPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILl 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 207 -AQVLED--NLLPGAicslvcgGADIGTTMARDERVNLLSFTGSTQVGKEVALMVQERF---GKS---LLELGGNNAIIA 277
Cdd:PRK11809 820 eAGVPAGvvQLLPGR-------GETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqGRPiplIAETGGQNAMIV 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 278 FEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAV 357
Cdd:PRK11809 893 DSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHI 972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 358 EEAKKQGGTV---VYGGKVMDHPGNYVEPTIVTGLAHDApiVHQETFAPILYVFKFQDEE--EVFEWNNEVKQGLSSSIF 432
Cdd:PRK11809 973 QAMRAKGRPVfqaARENSEDWQSGTFVPPTLIELDSFDE--LKREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVH 1050
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 188035915 433 TK------------DLGRIFrwlgpkgsdcgiVNVNIptSGAEIG-GAFGGEKHTGGGRESG 481
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) ... |
35-435 |
3.19e-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: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 35 GEVITTYCPAN-NEPIARVRQASLKDYEETIGKAKKAWNIWADIPAPKRGEIVRKIGD----AFREKI---QLLGRlvsl 106
Cdd:cd07123 45 GNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADllsgKYRYELnaaTMLGQ---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 107 emGKILVEG-IGEVQEYVDV----CDYAAGLSRmiggptlpsERPGHALIEMWN-----PL-GLVGIITAFNFpvavfgw 175
Cdd:cd07123 121 --GKNVWQAeIDAACELIDFlrfnVKYAEELYA---------QQPLSSPAGVWNrleyrPLeGFVYAVSPFNF------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 176 nNAIAL-------ITGNVCLWKGAPTTSLVSVAVTKIIaqvLEDNLLPGAICSLVCGGADIGTTMARDERVNLLSFTGST 248
Cdd:cd07123 183 -TAIGGnlagapaLMGNVVLWKPSDTAVLSNYLVYKIL---EEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGST 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 249 QVGKEVALMVQER------FGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRL 322
Cdd:cd07123 259 PTFKSLWKQIGENldryrtYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 323 RSAYSQIRVGNPWDPNILYGPLHTKQAVSMFVRAVEEAKKQGG-TVVYGGKVMDHPGNYVEPTIVTGLAHDAPIVHQETF 401
Cdd:cd07123 339 LEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEaEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIF 418
|
410 420 430
....*....|....*....|....*....|....*..
gi 188035915 402 APILYVFKFQDE--EEVFEWNNEV-KQGLSSSIFTKD 435
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 ... |
139-435 |
6.66e-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: 6.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 139 PTLPSERPGHALIEmWNPLGLVGIITAFNFPV------AVfgwnNAIAliTGNVCLWKG---APTTSlvsvavtKIIAQV 209
Cdd:cd07087 84 SVPLLLQPAKAYVI-PEPLGVVLIIGPWNYPLqlalapLI----GAIA--AGNTVVLKPselAPATS-------ALLAKL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 210 LEDNLLPGAIcSLVCGGADIgTTMARDERVNLLSFTGSTQVGKEVAlmvqERFGKSL----LELGGNNAIIAFEDADLSL 285
Cdd:cd07087 150 IPKYFDPEAV-AVVEGGVEV-ATALLAEPFDHIFFTGSPAVGKIVM----EAAAKHLtpvtLELGGKSPCIVDKDANLEV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 286 VVPSVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNPWD-PNilYGPL----HTKQAVSMFvraveea 360
Cdd:cd07087 224 AARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKEsPD--YGRIinerHFDRLASLL------- 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188035915 361 kkQGGTVVYGGKVmDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 435
Cdd:cd07087 295 --DDGKVVIGGQV-DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSED 366
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
156-435 |
7.53e-33 |
|
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: 7.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 156 PLGLVGIITAFNFPV-----AVFGwnnAIAliTGNVCLWKGapttSLVSVAVTKIIAQVLEDNLLPGAIcSLVCGGADiG 230
Cdd:cd07135 108 PLGVVLIIGPWNYPVllalsPLVG---AIA--AGCTVVLKP----SELTPHTAALLAELVPKYLDPDAF-QVVQGGVP-E 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 231 TTMARDERVNLLSFTGSTQVGKEVAlmvqERFGKSL----LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVR 306
Cdd:cd07135 177 TTALLEQKFDKIFYTGSGRVGRIIA----EAAAKHLtpvtLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 307 RLFLHESIHNEVVDRLRSAYsQIRVGNPWDPNILYGPLHTKQAvsmFVRAVEEAKKQGGTVVYGGKvMDHPGNYVEPTIV 386
Cdd:cd07135 253 YVLVDPSVYDEFVEELKKVL-DEFYPGGANASPDYTRIVNPRH---FNRLKSLLDTTKGKVVIGGE-MDEATRFIPPTIV 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 188035915 387 TGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 435
Cdd:cd07135 328 SDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDD 376
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
156-477 |
1.56e-32 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 130.15 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 156 PLGLVGIITAFNFPV--AVFGWNNAIAliTGNVCLWKgaptTSLVSVAVTKIIAQVLeDNLLPGAICSLVCGGADIgTTM 233
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLnlTLIPLAGAIA--AGNTVVLK----PSELSPHTSKLMAKLL-TKYLDPSYVRVIEGGVEV-TTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 234 ARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHES 313
Cdd:PTZ00381 181 LLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 314 IHNEVVDRLRSAYSQIRVGNPW---DPNILYGPLHTKQAVSMFvraveeaKKQGGTVVYGGKVmDHPGNYVEPTIVTGLA 390
Cdd:PTZ00381 261 IKDKFIEALKEAIKEFFGEDPKkseDYSRIVNEFHTKRLAELI-------KDHGGKVVYGGEV-DIENKYVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 391 HDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDlGRIFRWLGPKGSDCGIV---------NVNIPtsg 461
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGED-KRHKELVLENTSSGAVVindcvfhllNPNLP--- 408
|
330
....*....|....*.
gi 188035915 462 aeiggaFGGEKHTGGG 477
Cdd:PTZ00381 409 ------FGGVGNSGMG 418
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
156-481 |
3.09e-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: 116.56 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 156 PLGLVGIITAFNFPVA-VFG-WNNAIAliTGNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLpgaicSLVCGGADIGTtm 233
Cdd:cd07134 100 PKGVCLIISPWNYPFNlAFGpLVSAIA--AGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-----AVFEGDAEVAQ-- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 234 ardervNLLS-------FTGSTQVGKevalMVQERFGKSL----LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRC 302
Cdd:cd07134 171 ------ALLElpfdhifFTGSPAVGK----IVMAAAAKHLasvtLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 303 TTVRRLFLHESIHNEVVDRLRSAYSQIrvgnpwdpnilYGPLHTKQAVSMFVRAV------------EEAKKQGGTVVYG 370
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLKAEIEKF-----------YGKDAARKASPDLARIVndrhfdrlkgllDDAVAKGAKVEFG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 371 GKVmDHPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLGPKGS-D 449
Cdd:cd07134 310 GQF-DAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSgG 388
|
330 340 350
....*....|....*....|....*....|....*....
gi 188035915 450 CGI-------VNVNIPtsgaeiggaFGGEKHTGGGRESG 481
Cdd:cd07134 389 VVVndvvlhfLNPNLP---------FGGVNNSGIGSYHG 418
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
156-435 |
6.53e-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: 6.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 156 PLGLVGIITAFNFP-----VAVFGwnnAIAliTGNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLpgaicSLVCGGADIG 230
Cdd:cd07136 100 PYGVVLIIAPWNYPfqlalAPLIG---AIA--AGNTAVLKPSELTPNTSKVIAKIIEETFDEEYV-----AVVEGGVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 231 TTMArDERVNLLSFTGSTQVGKEVAlmvqERFGKSL----LELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVR 306
Cdd:cd07136 170 QELL-DQKFDYIFFTGSVRVGKIVM----EAAAKHLtpvtLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 307 RLFLHESIHNEVVDRLRSaysQIRvgnpwdpnILYG--PLHTKQavsmFVRAVEEakK---------QGGTVVYGGKVmD 375
Cdd:cd07136 245 YVLVHESVKEKFIKELKE---EIK--------KFYGedPLESPD----YGRIINE--KhfdrlagllDNGKIVFGGNT-D 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 376 HPGNYVEPTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 435
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 ... |
28-492 |
1.14e-26 |
|
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: 113.13 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSW-GGRGEVITTYCPANNEPIARVR------QASLKDYEETIGKAKKAWNIwadipaPKRGEIVRKIGDAFREKIQLL 100
Cdd:cd07128 6 AGQWhAGTGDGRTLHDAVTGEVVARVSsegldfAAAVAYAREKGGPALRALTF------HERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 101 GRLvSLEMG------KILVEG-IGEVQEYvdvcdyaAGLSR--------MIGGPTLP-SERPGHALIEMWNPLGLVGI-I 163
Cdd:cd07128 80 YAL-SAATGatrrdsWIDIDGgIGTLFAY-------ASLGRrelpnahfLVEGDVEPlSKDGTFVGQHILTPRRGVAVhI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 164 TAFNFPVavfgW----NNAIALITGNVCLWKGAPTTSLVSVAVTKIIaqvLEDNLLP-GAIcSLVCGGAdiGTTMARDER 238
Cdd:cd07128 152 NAFNFPV----WgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDI---VESGLLPeGAL-QLICGSV--GDLLDHLGE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 239 VNLLSFTGSTQVGKEV---ALMVQE--RF---GKSLlelggNNAIIAfEDA-----DLSLVVPSVLFAAVGTAGQRCTTV 305
Cdd:cd07128 222 QDVVAFTGSAATAAKLrahPNIVARsiRFnaeADSL-----NAAILG-PDAtpgtpEFDLFVKEVAREMTVKAGQKCTAI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 306 RRLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLhTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHP-------G 378
Cdd:cd07128 296 RRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPL-VSREQREDVRAAVATLLAEAEVVFGGPDRFEVvgadaekG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 379 NYVEPTIVTGL-AHDAPIVHQ-ETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD---LGRIFRWLGPKGsdcGIV 453
Cdd:cd07128 375 AFFPPTLLLCDdPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDpafARELVLGAAPYH---GRL 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 188035915 454 NVNIPTSGAEIGG--------AFGGEKHTGGGRE-SGSDAWKQYMRRS 492
Cdd:cd07128 452 LVLNRDSAKESTGhgsplpqlVHGGPGRAGGGEElGGLRGVKHYMQRT 499
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
140-492 |
1.89e-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: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 140 TLPSERPGHALIEMWnPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLednLLPGAI 219
Cdd:cd07084 85 HLGQGLKQQSHGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAG---LLPPED 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 220 CSLVCGGADIGTTMARDERVNLLSFTGSTQVGKevALMVQERFGKSLLELGGNNAIIAFEDAD-LSLVVPSVLFAAVGTA 298
Cdd:cd07084 161 VTLINGDGKTMQALLLHPNPKMVLFTGSSRVAE--KLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 299 GQRCTTVRRLFLHESIHNE-VVDRLRSAYSQIRVGnpwdpNILYGPLHTKQAVSMfvraVEEAKKQGGTVV-YGGKVM-- 374
Cdd:cd07084 239 GQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLE-----DLLLGPVQTFTTLAM----IAHMENLLGSVLlFSGKELkn 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 375 -DHPGNY----VEPTIVTGLAHDA--PIVHQETFAPILYVFKFQDEEE--VFEWNNEVKQGLSSSIFTKD---LGRifrw 442
Cdd:cd07084 310 hSIPSIYgacvASALFVPIDEILKtyELVTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDpifLQE---- 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 188035915 443 LGPKGSDCGIVNVNIPTSgaeiGGAFGGEKHTGGGRES-------GSDAWKQYMRRS 492
Cdd:cd07084 386 LIGNLWVAGRTYAILRGR----TGVAPNQNHGGGPAADprgagigGPEAIKLVWRCH 438
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
154-435 |
5.74e-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: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 154 WNPLGLVGIITAFNFPVA-----VFGwnnAIAliTGNVCLWKgaPttSLVSVAVTKIIAQVLEDNLLPgaIC-SLVCGGA 227
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQltlvpLVG---AIA--AGNCVVIK--P--SEVSPATAKLLAELIPKYLDK--ECyPVVLGGV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 228 DIgTTMARDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRR 307
Cdd:cd07132 167 EE-TTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 308 LFLHESIHNEVVDRLRSAYSQIRVGNPWD-PNilYGPLhtkqaVSM--FVRAVEEAKkqGGTVVYGGKVmDHPGNYVEPT 384
Cdd:cd07132 246 VLCTPEVQEKFVEALKKTLKEFYGEDPKEsPD--YGRI-----INDrhFQRLKKLLS--GGKVAIGGQT-DEKERYIAPT 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 188035915 385 IVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD 435
Cdd:cd07132 316 VLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
145-416 |
6.37e-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: 6.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 145 RPGHALIEmWNPLGLVGIITAFNFPVAVfgwnnAIA-LIT----GNVCLWKG---APTTSLVsvavtkiIAQVLEDNLLP 216
Cdd:cd07133 91 LPAKAEVE-YQPLGVVGIIVPWNYPLYL-----ALGpLIAalaaGNRVMIKPsefTPRTSAL-------LAELLAEYFDE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 217 GAICsLVCGGADIG---TTMARDervNLLsFTGSTQVGKEVALMVqerfGKSL----LELGGNN-AIIAfEDADLSLVVP 288
Cdd:cd07133 158 DEVA-VVTGGADVAaafSSLPFD---HLL-FTGSTAVGRHVMRAA----AENLtpvtLELGGKSpAIIA-PDADLAKAAE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 289 SVLFAAVGTAGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRvgnpwdPNILYGPLHTkqavSM-----FVR---AVEEA 360
Cdd:cd07133 228 RIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMY------PTLADNPDYT----SIinerhYARlqgLLEDA 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188035915 361 KKQGGTVVyggKVMDHPGNYVE-----PTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEV 416
Cdd:cd07133 298 RAKGARVI---ELNPAGEDFAAtrklpPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEA 355
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
163-492 |
6.51e-21 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 95.93 E-value: 6.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 163 ITAFNFPvavfGW----NNAIALITGNVCLWKGAPTTSLVSvavTKIIAQVLEDNLLPGAICSLVCGGAdiGTTMARDER 238
Cdd:PRK11903 155 INAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLT---QRMVKDVVAAGILPAGALSVVCGSS--AGLLDHLQP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 239 VNLLSFTGSTQVGKEVALM--VQERFGKSLLELGGNNAIIAFEDAD-----LSLVVPSVLFAAVGTAGQRCTTVRRLFLH 311
Cdd:PRK11903 226 FDVVSFTGSAETAAVLRSHpaVVQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVP 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 312 ESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTK-QAVSmfVRAVEEAKKQGGTVVYGGKV---MDHP---GNYVEPT 384
Cdd:PRK11903 306 EALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRaQLAA--VRAGLAALRAQAEVLFDGGGfalVDADpavAACVGPT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 385 I-VTGLAHDAPIVHQ-ETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKD---LGRIFRWLGPKGsdcGIVNVNIPT 459
Cdd:PRK11903 384 LlGASDPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDaafLAAAALELADSH---GRVHVISPD 460
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 188035915 460 SGAEIGG--------AFGGEKHTGGGRE-SGSDAWKQYMRRS 492
Cdd:PRK11903 461 VAALHTGhgnvmpqsLHGGPGRAGGGEElGGLRALAFYHRRS 502
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
156-481 |
3.92e-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: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 156 PLGLVGIITAFNFPVA-----VFGwnnAIAliTGNVCLWKgaptTSLVSVAVTKIIAQVLEDNLLPGAIcSLVCGGADIG 230
Cdd:cd07137 101 PLGVVLVISAWNFPFLlslepVIG---AIA--AGNAVVLK----PSELAPATSALLAKLIPEYLDTKAI-KVIEGGVPET 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 231 TTMArDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGT-AGQRCTTVRRLF 309
Cdd:cd07137 171 TALL-EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 310 LHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTK--QAVSMFVRAVEEAKKqggtVVYGGKVmDHPGNYVEPTIVT 387
Cdd:cd07137 250 VEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHhfQRLSRLLDDPSVADK----IVHGGER-DEKNLYIEPTILL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 388 GLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFT--KDLGRIFRWLGPKGS----DCgIVNVNIPTSg 461
Cdd:cd07137 325 DPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTknKELKRRIVAETSSGGvtfnDT-VVQYAIDTL- 402
|
330 340
....*....|....*....|
gi 188035915 462 aeiggAFGGEKHTGGGRESG 481
Cdd:cd07137 403 -----PFGGVGESGFGAYHG 417
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
156-481 |
7.23e-16 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 80.09 E-value: 7.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 156 PLGLVGIITAFNFPVaVFGWNNAIALIT-GNVCLWKgaptTSLVSVAVTKIIAQVLEDNLLPGAIcsLVCGGADIGTTMA 234
Cdd:PLN02174 112 PLGVVLVISAWNYPF-LLSIDPVIGAISaGNAVVLK----PSELAPASSALLAKLLEQYLDSSAV--RVVEGAVTETTAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 235 RDERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVG-TAGQRCTTVRRLFLHES 313
Cdd:PLN02174 185 LEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 314 IHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQaVSMFVRAVEEaKKQGGTVVYGGKvMDHPGNYVEPTIVTGLAHDA 393
Cdd:PLN02174 265 YAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTH-FDRLSKLLDE-KEVSDKIVYGGE-KDRENLKIAPTILLDVPLDS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 394 PIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDlGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKH 473
Cdd:PLN02174 342 LIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHN-KKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGE 420
|
....*...
gi 188035915 474 TGGGRESG 481
Cdd:PLN02174 421 SGMGAYHG 428
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
156-492 |
5.50e-15 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 77.07 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 156 PLGLVGIITAFNFPVA-----VFGwnnaiALITGNVCLWKgaptTSLVSVAVTKIIAQVLEDNLLPGAIcSLVCGGADIG 230
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGlslepLIG-----AIAAGNAVVLK----PSELAPATSAFLAANIPKYLDSKAV-KVIEGGPAVG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 231 TTMARdERVNLLSFTGSTQVGKEVALMVQERFGKSLLELGGN-NAIIAFEDA--DLSLVVPSVLFAAVGT-AGQRCTTVR 306
Cdd:PLN02203 178 EQLLQ-HKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKcPCIVDSLSSsrDTKVAVNRIVGGKWGScAGQACIAID 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 307 RLFLHESIHNEVVDRLRSAYSQIRVGNPWDPNILYGPLHTKQavsmFVRAVE--EAKKQGGTVVYGGKvMDHPGNYVEPT 384
Cdd:PLN02203 257 YVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKH----FQRLSNllKDPRVAASIVHGGS-IDEKKLFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 385 IVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEi 464
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACD- 410
|
330 340 350
....*....|....*....|....*....|....
gi 188035915 465 GGAFGGEKHTGGGRESGSDAW------KQYMRRS 492
Cdd:PLN02203 411 SLPFGGVGESGFGRYHGKYSFdtfsheKAVLRRS 444
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
28-435 |
4.25e-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: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 28 NGSWGGRGEVITTYCPANNEPIARVRQASLKDYEETIGKAKKA--WNIWADIPAPKR----GEIVRKIGDAFR--EKIQL 99
Cdd:cd07126 4 AGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCpkSGLHNPLKNPERyllyGDVSHRVAHELRkpEVEDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 100 LGRLVSLEMGKILVEGIGEV---QEYVDvcDYAAGLSRMIG-GPTLPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGW 175
Cdd:cd07126 84 FARLIQRVAPKSDAQALGEVvvtRKFLE--NFAGDQVRFLArSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 176 NNAIALITGNVCLWKGaptTSLVSVAVTKIIaQVLEDNLLPGAICSLV-CGGADIGTTMARDErVNLLSFTGSTQVGKEV 254
Cdd:cd07126 162 QLMGALFMGNKPLLKV---DSKVSVVMEQFL-RLLHLCGMPATDVDLIhSDGPTMNKILLEAN-PRMTLFTGSSKVAERL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 255 ALMVQerfGKSLLELGGNNAIIAFED-ADLSLVVPSVLFAAVGTAGQRCTTVRRLFLHES-IHNEVVDRLRSAYSQIRVg 332
Cdd:cd07126 237 ALELH---GKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALAEQRKL- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 333 npwdPNILYGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVM---DHPGNY--VEPTIV------TGLAHDAPIVHQETF 401
Cdd:cd07126 313 ----EDLTIGPVLTWTTERILDHVDKLLAIPGAKVLFGGKPLtnhSIPSIYgaYEPTAVfvpleeIAIEENFELVTTEVF 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 188035915 402 APILYVFKFQDEEE--VFEWNNEVKQGLSSSIFTKD 435
Cdd:cd07126 389 GPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSND 424
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
156-442 |
9.90e-10 |
|
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: 60.96 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 156 PLGLVGIITAFNFPVavfgWNNA----IALITGNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLPGAICSLVCG--GADI 229
Cdd:cd07127 193 PRGVALVIGCSTFPT----WNGYpglfASLATGNPVIVKPHPAAILPLAITVQVAREVLAEAGFDPNLVTLAADtpEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 230 GTTMARDERVNLLSFTGSTQVGKEvaLMVQERFGKSLLELGGNNAIIAFEDADLSLVVPSVLFAAVGTAGQRCTTVRRLF 309
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSNAFGDW--LEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIY 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 310 L-HESIHN--------EVVDRLRSAYSQIrVGNPWDPNILYGPLhtkqaVSMFVRAVEEAKKQGGTVVYGGKVMDHP--- 377
Cdd:cd07127 347 VpRDGIQTddgrksfdEVAADLAAAIDGL-LADPARAAALLGAI-----QSPDTLARIAEARQLGEVLLASEAVAHPefp 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188035915 378 GNYVE-PTIVTGLAHDAPIVHQETFAPILYVFKFQDEEEVFEWNNEV---KQGLSSSIFTKDLGRIFRW 442
Cdd:cd07127 421 DARVRtPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESvreHGAMTVGVYSTDPEVVERV 489
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
156-431 |
9.25e-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: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 156 PLGLVGIITAFNFPVA--VFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLPGAICSLV-CGGADIGTT 232
Cdd:cd07129 105 PLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAALRATGLPAGVFSLLqGGGREVGVA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 233 MARDERVNLLSFTGSTQVGKEVALMVQER------FGksllELGGNNAIIAFEDA------DLSLV-VPSVLFAavgtAG 299
Cdd:cd07129 185 LVKHPAIKAVGFTGSRRGGRALFDAAAARpepipfYA----ELGSVNPVFILPGAlaergeAIAQGfVGSLTLG----AG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 300 QRCTTVRRLFLhesIHNEVVDRLRSAYSQ-IRVGNPwdpnilyGPLHTKQAVSMFVRAVEEAKKQGGTVVYGGKVMDHPG 378
Cdd:cd07129 257 QFCTNPGLVLV---PAGPAGDAFIAALAEaLAAAPA-------QTMLTPGIAEAYRQGVEALAAAPGVRVLAGGAAAEGG 326
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 188035915 379 NYVEPTI--VTG---LAHDApiVHQETFAPILYVFKFQDEEEVFEWNNEVKQGLSSSI 431
Cdd:cd07129 327 NQAAPTLfkVDAaafLADPA--LQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATI 382
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
61-465 |
1.26e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 47.65 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 61 EETIGKAKKAWNIWADIPAPKRGEIVRKIGDAFREKIQLLGRLVSLEMGKILVEGigEVQEYVDVCDYAAGLSRMIGGPT 140
Cdd:cd07081 2 DDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVED--KVIKNHFAAEYIYNVYKDEKTCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 141 LPSERPGHALIEMWNPLGLVGIITAFNFPVAVFGWNNAIALITGNVCLWKGAPTTSLVSVAVTKIIAQVLEDNLLPGAIC 220
Cdd:cd07081 80 VLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 221 SLVcGGADIGTTMA--RDERVNLLSFTGSTQVGKEValmvqERFGKSLLELG-GNNAIIAFEDADLSLVVPSVLFAAVGT 297
Cdd:cd07081 160 GWI-DNPSIELAQRlmKFPGIGLLLATGGPAVVKAA-----YSSGKPAIGVGaGNTPVVIDETADIKRAVQSIVKSKTFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 298 AGQRCTTVRRLFLHESIHNEVVDRLRSAYSQIRVGNpwdpnilygplHTKQAVSMFVRAVEEAKKQGGTVVYggKVMDHP 377
Cdd:cd07081 234 NGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAE-----------ELQQVQPVILKNGDVNRDIVGQDAY--KIAAAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035915 378 GNYVEPTI------VTGLAHDAPIVHqETFAPILYVFKFQDEEEVFEWNNEVKQ----GLSSSIFTKDLGRIFR--WLGP 445
Cdd:cd07081 301 GLKVPQETriligeVTSLAEHEPFAH-EKLSPVLAMYRAANFADADAKALALKLeggcGHTSAMYSDNIKAIENmnQFAN 379
|
410 420
....*....|....*....|
gi 188035915 446 KgSDCGIVNVNIPTSGAEIG 465
Cdd:cd07081 380 A-MKTSRFVKNGPCSQGGLG 398
|
|
| |
