|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
21-497 |
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: 783.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 21 TGKEWFAsdGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLV 100
Cdd:cd07130 3 YDGEWGG--GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 101 SLEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCG 180
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 181 DTVIWKPSSKTPLCAVAIQKIACEVLAENGMPEGVFNLVIGsGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFG 260
Cdd:cd07130 161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 261 RTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGP 340
Cdd:cd07130 240 RSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 341 VADANVVKDFLAAVEEAKAQGGELLCGGTALpELGACYVSPAIFKMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNG 420
Cdd:cd07130 320 LHTKAAVDNYLAAIEEAKSQGGTVLFGGKVI-DGPGNYVEPTIVEGLSDAPIVKEETFAPILYVLKFD-TLEEAIAWNNE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199635239 421 VPHGLSSSIYTTDFREAEQFLSCSGSDCGIANVNLGTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQSGAINFS 497
Cdd:cd07130 398 VPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
22-497 |
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: 760.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 22 GKEWFASDGaKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVS 101
Cdd:cd07086 4 GGEWVGSGG-ETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 102 LEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGD 181
Cdd:cd07086 83 LEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 182 TVIWKPSSKTPLCAVAIQKIACEVLAENGMPEGVFNLVIGsGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGR 261
Cdd:cd07086 163 TVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 262 TILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPV 341
Cdd:cd07086 242 VLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 342 ADANVVKDFLAAVEEAKAQGGELLCGGTALP-ELGACYVSPAIFKMSA-DAPLVREEKFCPILYLIPYSgGLGEAIRIHN 419
Cdd:cd07086 322 INQAAVEKYLNAIEIAKSQGGTVLTGGKRIDgGEPGNYVEPTIVTGVTdDARIVQEETFAPILYVIKFD-SLEEAIAINN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199635239 420 GVPHGLSSSIYTTDFREAEQFLSCSGSDCGIANVNLGTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQSGAINFS 497
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
6-508 |
0e+00 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 538.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 6 WLESLGVAGTCPGVSTGKEWFASdgAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQI 85
Cdd:PLN02315 10 FLSEIGLSSRNLGCYVGGEWRAN--GPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 86 GVRLREKKEALGRLVSLEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFP 165
Cdd:PLN02315 88 GDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 166 ASVWSWNAMLAAVCGDTVIWKPSSKTPLCAVAIQKIACEVLAENGMPEGVFNLVIGsGRDVGEVMLEDARVRLVSFTGST 245
Cdd:PLN02315 168 CAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 246 ETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGR 325
Cdd:PLN02315 247 KVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 326 LKIGNPLEEGVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALpELGACYVSPAIFKMSADAPLVREEKFCPILYLI 405
Cdd:PLN02315 327 VKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAI-ESEGNFVQPTIVEISPDADVVKEELFGPVLYVM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 406 PYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFLSCSGSDCGIANVNLGTNGAEIGGAFGGEKETGGGRECGSDAWKG 485
Cdd:PLN02315 406 KFK-TLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQ 484
|
490 500
....*....|....*....|...
gi 1199635239 486 YMRRQSGAINFSHEMPLAQGIKF 508
Cdd:PLN02315 485 YMRRSTCTINYGNELPLAQGINF 507
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
24-496 |
4.78e-175 |
|
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: 501.19 E-value: 4.78e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLE 103
Cdd:COG1012 13 EWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 104 MGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTV 183
Cdd:COG1012 93 TGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 184 IWKPSSKTPLCAVAIqkiaCEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTI 263
Cdd:COG1012 173 VLKPAEQTPLSALLL----AELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 264 LELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVAD 343
Cdd:COG1012 249 LELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLIS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 344 ANVVKDFLAAVEEAKAQGGELLCGGTALPELGACYVSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVP 422
Cdd:COG1012 329 EAQLERVLAYIEDAVAEGAELLTGGRRPDGEGGYFVEPTVLAdVTPDMRIAREEIFGPVLSVIPFD-DEEEAIALANDTE 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199635239 423 HGLSSSIYTTDFREAEQFlsCSGSDCGIANVNLGTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQSGAINF 496
Cdd:COG1012 408 YGLAASVFTRDLARARRV--ARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
26-491 |
3.11e-161 |
|
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: 465.47 E-value: 3.11e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 26 FASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMG 105
Cdd:pfam00171 1 WVDSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 106 KILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSeRPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIW 185
Cdd:pfam00171 81 KPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 186 KPSSKTPLCAVAIQKIacevLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILE 265
Cdd:pfam00171 160 KPSELTPLTALLLAEL----FEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 266 LGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADAN 345
Cdd:pfam00171 236 LGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 346 VVKDFLAAVEEAKAQGGELLCGGTALPELGAcYVSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHG 424
Cdd:pfam00171 316 QLERVLKYVEDAKEEGAKLLTGGEAGLDNGY-FVEPTVLAnVTPDMRIAQEEIFGPVLSVIRFK-DEEEAIEIANDTEYG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199635239 425 LSSSIYTTDFREAEQFLscSGSDCGIANVNLGTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQS 491
Cdd:pfam00171 394 LAAGVFTSDLERALRVA--RRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
67-491 |
1.40e-145 |
|
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: 424.31 E-value: 1.40e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 67 FLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRL 146
Cdd:cd07078 11 FKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGELA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 147 MEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCAVAIQKIACEVlaenGMPEGVFNLVIGSGRDV 226
Cdd:cd07078 91 IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEA----GLPPGVLNVVTGDGDEV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 227 GEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVI 306
Cdd:cd07078 167 GAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 307 VHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGACYVSPAIFKM 386
Cdd:cd07078 247 VHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGYFVPPTVLTD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 387 -SADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFLscSGSDCGIANVNLGTNGAEIGGA 465
Cdd:cd07078 327 vDPDMPIAQEEIFGPVLPVIPFK-DEEEAIELANDTEYGLAAGVFTRDLERALRVA--ERLEAGTVWINDYSVGAEPSAP 403
|
410 420
....*....|....*....|....*.
gi 1199635239 466 FGGEKETGGGRECGSDAWKGYMRRQS 491
Cdd:cd07078 404 FGGVKQSGIGREGGPYGLEEYTEPKT 429
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
22-497 |
5.66e-145 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 424.84 E-value: 5.66e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 22 GKEWFASDGAKELVSYSPADGSEL-GRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLV 100
Cdd:cd07131 4 GGEWVDSASGETFDSRNPADLEEVvGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 101 SLEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCG 180
Cdd:cd07131 84 TREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 181 DTVIWKPSSKTPLCAvaiQKIAcEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFG 260
Cdd:cd07131 164 NTVVFKPAEDTPACA---LKLV-ELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 261 RTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGP 340
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 341 VADANVVKDFLAAVEEAKAQGGELLCGGTALPELG---ACYVSPAIFKMSA-DAPLVREEKFCPILYLIPYSgGLGEAIR 416
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGyekGYFVEPTVFTDVTpDMRIAQEEIFGPVVALIEVS-SLEEAIE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 417 IHNGVPHGLSSSIYTTDFREAEQFLscsgSDC--GIANVNLGTNGAEIGGAFGGEKETGGG-RECGSDAWKGYMRRQSGA 493
Cdd:cd07131 399 IANDTEYGLSSAIYTEDVNKAFRAR----RDLeaGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVY 474
|
....
gi 1199635239 494 INFS 497
Cdd:cd07131 475 VDYS 478
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
24-482 |
8.51e-132 |
|
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: 390.84 E-value: 8.51e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKElvSYSPADGSE-LGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSL 102
Cdd:cd07097 8 EWVAGGDGEE--NRNPSDTSDvVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 103 EMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDT 182
Cdd:cd07097 86 EEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 183 VIWKPSSKTPLCAVAIqkiaCEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRT 262
Cdd:cd07097 166 VVFKPAELTPASAWAL----VEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 263 ILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVA 342
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 343 DANVVKDFLAAVEEAKAQGGELLCGGTALP-ELGACYVSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNG 420
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAKLVYGGERLKrPDEGYYLAPALFaGVTNDMRIAREEIFGPVAAVIRVR-DYDEALAIAND 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199635239 421 VPHGLSSSIYTTDFREAEQFLscSGSDCGIANVNLGTNGAEIGGAFGGEKETG-GGRECGSDA 482
Cdd:cd07097 401 TEFGLSAGIVTTSLKHATHFK--RRVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEAA 461
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
37-487 |
1.17e-114 |
|
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: 345.96 E-value: 1.17e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 37 YSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQ 116
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 117 EMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPAsvwswnAM--------LAAVCgdTVIWKPS 188
Cdd:cd07103 82 YAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPA------AMitrkiapaLAAGC--TVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 189 SKTPLCAVAIQKIAcevlAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGG 268
Cdd:cd07103 154 EETPLSALALAELA----EEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 269 NNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVK 348
Cdd:cd07103 230 NAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 349 DFLAAVEEAKAQGGELLCGGTAlPELGACYVSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSS 427
Cdd:cd07103 310 KVEALVEDAVAKGAKVLTGGKR-LGLGGYFYEPTVLTdVTDDMLIMNEETFGPVAPIIPFD-TEDEVIARANDTPYGLAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199635239 428 SIYTTD----FREAEQFlscsgsDCGIanvnLGTNGAEIGGA---FGGEKETGGGRECGSDAWKGYM 487
Cdd:cd07103 388 YVFTRDlaraWRVAEAL------EAGM----VGINTGLISDAeapFGGVKESGLGREGGKEGLEEYL 444
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
67-491 |
2.22e-106 |
|
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: 321.87 E-value: 2.22e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 67 FLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRL 146
Cdd:cd06534 7 FKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 147 MEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCAVAIQKIacevLAENGMPEGVFNLVIGSGRDV 226
Cdd:cd06534 87 YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAEL----LQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 227 GEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVI 306
Cdd:cd06534 163 GAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 307 VHESRYEELAQKLTSAYgrlkignpleegVHVGPvadanvvkdflaaveeakaqggellcggtalpelgacyvspaifkm 386
Cdd:cd06534 243 VHESIYDEFVEKLVTVL------------VDVDP---------------------------------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 387 saDAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFLscSGSDCGIANVNLGTNGAEIGGAF 466
Cdd:cd06534 265 --DMPIAQEEIFGPVLPVIRFK-DEEEAIALANDTEYGLTAGVFTRDLNRALRVA--ERLRAGTVYINDSSIGVGPEAPF 339
|
410 420
....*....|....*....|....*
gi 1199635239 467 GGEKETGGGRECGSDAWKGYMRRQS 491
Cdd:cd06534 340 GGVKNSGIGREGGPYGLEEYTRTKT 364
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
36-491 |
1.11e-96 |
|
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: 300.24 E-value: 1.11e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 36 SYSPADGSELGRVRCARREDYERAAAAAEAAFLK--WREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLG 113
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 114 EVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFP--ASVWSWNAMLAAvcGDTVIWKPSSKT 191
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPllLLAKKLAPALAA--GNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 192 PLCAVAIQKIAcevlAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNA 271
Cdd:cd07114 159 PASTLELAKLA----EEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 272 SIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFL 351
Cdd:cd07114 235 NIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 352 AAVEEAKAQGGELLCGGTAL--PELGA-CYVSPAIF-KMSADAPLVREEKFCPILYLIPYSGGlGEAIRIHNGVPHGLSS 427
Cdd:cd07114 315 RYVARAREEGARVLTGGERPsgADLGAgYFFEPTILaDVTNDMRIAQEEVFGPVLSVIPFDDE-EEAIALANDSEYGLAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199635239 428 SIYTTDFREAEQFlsCSGSDCGIANVNlGTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQS 491
Cdd:cd07114 394 GIWTRDLARAHRV--ARAIEAGTVWVN-TYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKS 454
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
67-483 |
2.23e-95 |
|
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: 295.98 E-value: 2.23e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 67 FLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRL 146
Cdd:cd07104 13 QKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDVPGKES 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 147 MEQWHPLGPIAVITAYNFPASVwSWNAMLAAV-CGDTVIWKPSSKTPLCAVAIqkIAcEVLAENGMPEGVFNLVIGSGRD 225
Cdd:cd07104 93 MVRRVPLGVVGVISPFNFPLIL-AMRSVAPALaLGNAVVLKPDSRTPVTGGLL--IA-EIFEEAGLPKGVLNVVPGGGSE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 226 VGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRV 305
Cdd:cd07104 169 IGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 306 IVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTAlpeLGACYvSPAIFK 385
Cdd:cd07104 249 LVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY---EGLFY-QPTVLS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 386 -MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFlsCSGSDCGIANVNLGTNGAEIGG 464
Cdd:cd07104 325 dVTPDMPIFREEIFGPVAPVIPFD-DDEEAVELANDTEYGLSAAVFTRDLERAMAF--AERLETGMVHINDQTVNDEPHV 401
|
410
....*....|....*....
gi 1199635239 465 AFGGEKETGGGRECGSDAW 483
Cdd:cd07104 402 PFGGVKASGGGRFGGPASL 420
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
37-491 |
2.59e-95 |
|
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: 296.36 E-value: 2.59e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 37 YSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVq 116
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 117 emidvcDFAVGLSRQLYGLTFPSER----PRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTP 192
Cdd:cd07106 81 ------GGAVAWLRYTASLDLPDEVieddDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 193 LCAVAIQKIACEVLaengmPEGVFNLVIGSGrDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNAS 272
Cdd:cd07106 155 LCTLKLGELAQEVL-----PPGVLNVVSGGD-ELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 273 IVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADA---NVVKD 349
Cdd:cd07106 229 IVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKmqyDKVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 350 FlaaVEEAKAQGGELLCGGTALPELGAcYVSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSS 428
Cdd:cd07106 309 L---VEDAKAKGAKVLAGGEPLDGPGY-FIPPTIVDdPPEGSRIVDEEQFGPVLPVLKYS-DEDEVIARANDSEYGLGAS 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199635239 429 IYTTDFREAE----QFlscsgsDCGIANVNlgtNGAEIGGA--FGGEKETGGGRECGSDAWKGYMRRQS 491
Cdd:cd07106 384 VWSSDLERAEavarRL------EAGTVWIN---THGALDPDapFGGHKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
22-487 |
9.65e-95 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 296.60 E-value: 9.65e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 22 GKEWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVS 101
Cdd:PLN02278 30 GGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 102 LEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGD 181
Cdd:PLN02278 110 LEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGC 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 182 TVIWKPSSKTPLCAVAIQKIAcevlAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGR 261
Cdd:PLN02278 190 TVVVKPSELTPLTALAAAELA----LQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 262 TILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPV 341
Cdd:PLN02278 266 VSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 342 ADANVVKDFLAAVEEAKAQGGELLCGGTALPELGACYVSPAIFKMSADAPLVREEKFCPILYLIPYSGGlGEAIRIHNGV 421
Cdd:PLN02278 346 INEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE-EEAIAIANDT 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 422 PHGLSSSIYTTD----FREAEQFlscsgsDCGIANVNLGTNGAEIgGAFGGEKETGGGRECGSDAWKGYM 487
Cdd:PLN02278 425 EAGLAAYIFTRDlqraWRVSEAL------EYGIVGVNEGLISTEV-APFGGVKQSGLGREGSKYGIDEYL 487
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
22-496 |
1.23e-93 |
|
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: 294.13 E-value: 1.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 22 GKEWFASDgakELVSYSPADGSE-LGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLV 100
Cdd:cd07124 39 GKEVRTEE---KIESRNPADPSEvLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 101 SLEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGL---TFPSERPRHRlmeqWHPLGPIAVITAYNFPASVWSWNAMLAA 177
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFpveMVPGEDNRYV----YRPLGVGAVISPWNFPLAILAGMTTAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 178 VCGDTVIWKPSSKTPLCAVAIqkiaCEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGStetgRHVGVAVAR 257
Cdd:cd07124 192 VTGNTVVLKPAEDTPVIAAKL----VEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGS----REVGLRIYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 258 RFGRT----------ILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLK 327
Cdd:cd07124 264 RAAKVqpgqkwlkrvIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 328 IGNPLEEGVHVGPVADANVVKDFLAAVEEAKaQGGELLCGGTALPE-LGACYVSPAIFK-MSADAPLVREEKFCPILYLI 405
Cdd:cd07124 344 VGDPEDPEVYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEVLELaAEGYFVQPTIFAdVPPDHRLAQEEIFGPVLAVI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 406 PYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFLscSGSDCGIANVNLGTNGAEIG-GAFGGEKETG-GGRECGSDAW 483
Cdd:cd07124 423 KAK-DFDEALEIANDTEYGLTGGVFSRSPEHLERAR--REFEVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDYL 499
|
490
....*....|...
gi 1199635239 484 KGYMRRQSGAINF 496
Cdd:cd07124 500 LQFMQPKTVTENF 512
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
36-480 |
7.08e-92 |
|
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: 287.69 E-value: 7.08e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 36 SYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEV 115
Cdd:cd07150 3 DLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 116 QEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVwSWNAMLAAVC-GDTVIWKPSSKTPLC 194
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLIL-ATKKVAFALAaGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 195 AVaiqKIAcEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIV 274
Cdd:cd07150 162 GL---KIA-EIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 275 TEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAAV 354
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 355 EEAKAQGGELLCGGTalpELGACYvSPAIFK-MSADAPLVREEKFCPILYLIPYSGGLgEAIRIHNGVPHGLSSSIYTTD 433
Cdd:cd07150 318 EDAVAKGAKLLTGGK---YDGNFY-QPTVLTdVTPDMRIFREETFGPVTSVIPAKDAE-EALELANDTEYGLSAAILTND 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1199635239 434 FREAEQFLSCSGSdcGIANVNLGTNGAEIGGAFGGEKETGGGRECGS 480
Cdd:cd07150 393 LQRAFKLAERLES--GMVHINDPTILDEAHVPFGGVKASGFGREGGE 437
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
24-490 |
1.07e-90 |
|
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: 284.93 E-value: 1.07e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLE 103
Cdd:cd07088 5 EFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 104 MGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTV 183
Cdd:cd07088 85 QGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 184 IWKPSSKTPLCAVAIQKIACEVlaenGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTI 263
Cdd:cd07088 165 VIKPSEETPLNALEFAELVDEA----GLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 264 LELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVAD 343
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 344 ANVVKDFLAAVEEAKAQGGELLCGGTALPELGACYVSPAIFKMSA-DAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVP 422
Cdd:cd07088 321 EAALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTNVRqDMEIVQEEIFGPVLPVVKFS-SLDEAIELANDSE 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199635239 423 HGLSSSIYTTDFREAeqFLSCSGSDCGIANVNLgTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQ 490
Cdd:cd07088 400 YGLTSYIYTENLNTA--MRATNELEFGETYINR-ENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTK 464
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
37-477 |
1.88e-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: 283.72 E-value: 1.88e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 37 YSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQ 116
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 117 EMIDVCDFAVGLSRQLYGLTFP---SERPRHRL-MEQWHPLGPIAVITAYNFPasvwswnamLAAVC---------GDTV 183
Cdd:cd07149 84 RAIETLRLSAEEAKRLAGETIPfdaSPGGEGRIgFTIREPIGVVAAITPFNFP---------LNLVAhkvgpaiaaGNAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 184 IWKPSSKTPLCAVAIqkiaCEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRhvgvAVARRFG--R 261
Cdd:cd07149 155 VLKPASQTPLSALKL----AELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGE----AIARKAGlkK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 262 TILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPV 341
Cdd:cd07149 227 VTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 342 ADANVVKDFLAAVEEAKAQGGELLCGGTAlpeLGACYVSPAIFKMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGV 421
Cdd:cd07149 307 ISEAEAERIEEWVEEAVEGGARLLTGGKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFD-TLDEAIAMANDS 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199635239 422 PHGLSSSIYTTDFREAeqFLSCSGSDCGIANVNLGTNGAEIGGAFGGEKETGGGRE 477
Cdd:cd07149 383 PYGLQAGVFTNDLQKA--LKAARELEVGGVMINDSSTFRVDHMPYGGVKESGTGRE 436
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
36-482 |
6.94e-87 |
|
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: 274.83 E-value: 6.94e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 36 SYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGK-ILQEGLGE 114
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKpITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 115 VQEMIDVCDFAVGLSRQLYGLTFPSErPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLC 194
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 195 AVaiqkIACEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIV 274
Cdd:cd07093 160 AW----LLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 275 TEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAAV 354
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 355 EEAKAQGGELLCGGTALPEL---GACYVSPAIFK-MSADAPLVREEKFCPILYLIPYSGGlGEAIRIHNGVPHGLSSSIY 430
Cdd:cd07093 316 ELARAEGATILTGGGRPELPdleGGYFVEPTVITgLDNDSRVAQEEIFGPVVTVIPFDDE-EEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199635239 431 TTDFREAEQFlsCSGSDCGIANVN------LGTngaeiggAFGGEKETGGGRECGSDA 482
Cdd:cd07093 395 TRDLGRAHRV--ARRLEAGTVWVNcwlvrdLRT-------PFGGVKASGIGREGGDYS 443
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
37-477 |
1.79e-86 |
|
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: 273.84 E-value: 1.79e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 37 YSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQ 116
Cdd:cd07145 4 RNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 117 EMIDVCDFAVGLSRQLYGLTFPSE----RPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTP 192
Cdd:cd07145 84 RTIRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 193 LCAVAIQKIacevLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNAS 272
Cdd:cd07145 164 LTAIELAKI----LEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 273 IVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLA 352
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 353 AVEEAKAQGGELLCGGTALPelgACYVSPAIFKM-SADAPLVREEKFCPILYLIPYSGGlGEAIRIHNGVPHGLSSSIYT 431
Cdd:cd07145 320 LVNDAVEKGGKILYGGKRDE---GSFFPPTVLENdTPDMIVMKEEVFGPVLPIAKVKDD-EEAVEIANSTEYGLQASVFT 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1199635239 432 TDFREAeqfLSCSGS-DCGIANVNLGTNGAEIGGAFGGEKETGGGRE 477
Cdd:cd07145 396 NDINRA---LKVARElEAGGVVINDSTRFRWDNLPFGGFKKSGIGRE 439
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
67-479 |
4.37e-85 |
|
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: 269.33 E-value: 4.37e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 67 FLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQEMIDVCDF-AVGLSRQLYGLTFPSERPRHR 145
Cdd:cd07100 12 FLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyAENAEAFLADEPIETDAGKAY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 146 LmeQWHPLGPIAVITAYNFPAsvwsWNAM------LAAvcGDTVIWKPSSKTPLCAVAIQKIacevLAENGMPEGVF-NL 218
Cdd:cd07100 92 V--RYEPLGVVLGIMPWNFPF----WQVFrfaapnLMA--GNTVLLKHASNVPGCALAIEEL----FREAGFPEGVFqNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 219 VIGSgrDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQR 298
Cdd:cd07100 160 LIDS--DQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 299 CTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGAcY 378
Cdd:cd07100 238 CIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGA-F 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 379 VSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFlsCSGSDCGIANVN-LG 456
Cdd:cd07100 317 YPPTVLtDVTPGMPAYDEELFGPVAAVIKVK-DEEEAIALANDSPFGLGGSVFTTDLERAERV--ARRLEAGMVFINgMV 393
|
410 420
....*....|....*....|...
gi 1199635239 457 TNGAEIggAFGGEKETGGGRECG 479
Cdd:cd07100 394 KSDPRL--PFGGVKRSGYGRELG 414
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
38-486 |
6.82e-84 |
|
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: 267.00 E-value: 6.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 38 SPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLG-EVQ 116
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 117 EMIDVCDFAVGLSRQLYGLTFPSeRPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCAV 196
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPV-RGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 197 AIqkiaCEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTE 276
Cdd:cd07115 162 RI----AELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 277 HADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAAVEE 356
Cdd:cd07115 238 DADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 357 AKAQGGELLCGGTALPELGaCYVSPAIFK-MSADAPLVREEKFCPILYLIPYsGGLGEAIRIHNGVPHGLSSSIYTTDFR 435
Cdd:cd07115 318 GREEGARLLTGGKRPGARG-FFVEPTIFAaVPPEMRIAQEEIFGPVVSVMRF-RDEEEALRIANGTEYGLAAGVWTRDLG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1199635239 436 EAEQFlsCSGSDCGIANVNLgTNGAEIGGAFGGEKETGGGRECGSDAWKGY 486
Cdd:cd07115 396 RAHRV--AAALKAGTVWINT-YNRFDPGSPFGGYKQSGFGREMGREALDEY 443
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
34-477 |
2.12e-83 |
|
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: 265.45 E-value: 2.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 34 LVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLG 113
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 114 EVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQ-W---HPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSS 189
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNRLaWtirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 190 KTPLCAVAIQKIacevLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVArrFGRTILELGGN 269
Cdd:cd07094 161 KTPLSALELAKI----LVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 270 NASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKD 349
Cdd:cd07094 235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 350 FLAAVEEAKAQGGELLCGGtalpELGACYVSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSS 428
Cdd:cd07094 315 VERWVEEAVEAGARLLCGG----ERDGALFKPTVLEdVPRDTKLSTEETFGPVVPIIRYD-DFEEAIRIANSTDYGLQAG 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1199635239 429 IYTTDFREAeqFLSCSGSDCGIANVNLGTNGAEIGGAFGGEKETGGGRE 477
Cdd:cd07094 390 IFTRDLNVA--FKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGRE 436
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
38-477 |
4.33e-82 |
|
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: 262.31 E-value: 4.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 38 SPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQE 117
Cdd:cd07107 3 NPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 118 MIDVCDFAVGLSRQLYGLTFPSErPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCAVA 197
Cdd:cd07107 83 AAALLDYFAGLVTELKGETIPVG-GRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 198 IQKIACEVLaengmPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEH 277
Cdd:cd07107 162 LAELAREVL-----PPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 278 ADMKQAVPGIVFGAAGT-AGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAAVEE 356
Cdd:cd07107 237 ADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 357 AKAQGGELLCGGTAL--PEL-GACYVSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTT 432
Cdd:cd07107 317 AKREGARLVTGGGRPegPALeGGFYVEPTVFaDVTPGMRIAREEIFGPVLSVLRWR-DEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1199635239 433 DFREAeqFLSCSGSDCGIANVNlGTNGAEIGGAFGGEKETGGGRE 477
Cdd:cd07107 396 DISQA--HRTARRVEAGYVWIN-GSSRHFLGAPFGGVKNSGIGRE 437
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
38-477 |
8.07e-81 |
|
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: 259.22 E-value: 8.07e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 38 SPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQ-EGLGEVQ 116
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPEAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 117 EMIDVCDFAVGLSRQLYGLTFPSeRPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCAV 196
Cdd:cd07108 83 VLADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 197 AIQKIACEVLaengmPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTE 276
Cdd:cd07108 162 LLAEILAQVL-----PAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 277 HADMKQAVPGIVFGAAGT-AGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAAVE 355
Cdd:cd07108 237 DADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 356 EAKA-QGGELLCGGTaLPELGAC----YVSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSI 429
Cdd:cd07108 317 LGLStSGATVLRGGP-LPGEGPLadgfFVQPTIFsGVDNEWRLAREEIFGPVLCAIPWK-DEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1199635239 430 YTTDFREAEQFlsCSGSDCGIANVNLGtNGAEIGGAFGGEKETGGGRE 477
Cdd:cd07108 395 WTRDLGRALRA--AHALEAGWVQVNQG-GGQQPGQSYGGFKQSGLGRE 439
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
38-486 |
1.64e-80 |
|
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: 258.04 E-value: 1.64e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 38 SPADGSELGRVRCARREDYERAAAAAEAAFLK--WREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEV 115
Cdd:cd07118 3 SPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 116 QEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCA 195
Cdd:cd07118 83 EGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 196 VAIQKIacevLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVT 275
Cdd:cd07118 163 LMLAEL----LIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 276 EHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAAVE 355
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 356 EAKAQGGELLCGGTALPELGACYVSPAIFK-MSADAPLVREEKFCPILYLIPYsGGLGEAIRIHNGVPHGLSSSIYTTDF 434
Cdd:cd07118 319 AGRAEGATLLLGGERLASAAGLFYQPTIFTdVTPDMAIAREEIFGPVLSVLTF-DTVDEAIALANDTVYGLSAGVWSKDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1199635239 435 REAeqfLSCS-GSDCGIANVNLGTNG-AEIggAFGGEKETGGGRECGSDAWKGY 486
Cdd:cd07118 398 DTA---LTVArRIRAGTVWVNTFLDGsPEL--PFGGFKQSGIGRELGRYGVEEY 446
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
37-491 |
2.43e-80 |
|
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: 257.62 E-value: 2.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 37 YSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQ 116
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 117 EMIDVCDFAVGLSRQLYGLTFP--------SERprhrlmeqwHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPS 188
Cdd:cd07090 82 SSADCLEYYAGLAPTLSGEHVPlpggsfayTRR---------EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 189 SKTPLCAVAIqkiaCEVLAENGMPEGVFNLVIGSGrDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGG 268
Cdd:cd07090 153 PFTPLTALLL----AEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 269 NNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPV---ADAN 345
Cdd:cd07090 228 KSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALiseEHLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 346 VVKDFlaaVEEAKAQGGELLCGGTALPELGAC----YVSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNG 420
Cdd:cd07090 308 KVLGY---IESAKQEGAKVLCGGERVVPEDGLengfYVSPCVLTdCTDDMTIVREEIFGPVMSILPFD-TEEEVIRRAND 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199635239 421 VPHGLSSSIYTTDFREAEQFlscsgsdcgIANVNLGT------NGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQS 491
Cdd:cd07090 384 TTYGLAAGVFTRDLQRAHRV---------IAQLQAGTcwintyNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKT 451
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
22-491 |
2.74e-80 |
|
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: 257.89 E-value: 2.74e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 22 GKEWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLK--WREVPAPVRGEIVRQIGVRLREKKEALGRL 99
Cdd:cd07139 4 GGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 100 VSLEMGK-ILQEGLGEVQEMIDVCDFAVGLSRqlyGLTFPSERPR----HRLMEQwHPLGPIAVITAYNFPASVWSWNAM 174
Cdd:cd07139 84 WTAENGMpISWSRRAQGPGPAALLRYYAALAR---DFPFEERRPGsgggHVLVRR-EPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 175 LAAVCGDTVIWKPSSKTPLCAVAIqkiaCEVLAENGMPEGVFNLVIGsGRDVGEVMLEDARVRLVSFTGSTETGRHVGVA 254
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAYLL----AEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 255 VARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEE 334
Cdd:cd07139 235 CGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 335 GVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGA-CYVSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLG 412
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDRgWFVEPTLFaDVDNDMRIAQEEIFGPVLSVIPYD-DED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 413 EAIRIHNGVPHGLSSSIYTTDfreAEQFLSC-----SGSdcgianvnLGTNGA--EIGGAFGGEKETGGGRECGSDAWKG 485
Cdd:cd07139 394 DAVRIANDSDYGLSGSVWTAD---VERGLAVarrirTGT--------VGVNGFrlDFGAPFGGFKQSGIGREGGPEGLDA 462
|
....*.
gi 1199635239 486 YMRRQS 491
Cdd:cd07139 463 YLETKS 468
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
37-491 |
2.83e-80 |
|
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: 257.56 E-value: 2.83e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 37 YSPADGSELGRVRCARREDYERAAAAAEAAFLKW-REVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQ-EGLGE 114
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMtARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 115 VQEMIDVCDFAVGLSRQLYG-LTFPSERPRHRLMEQW---HPLGPIAVITAYNFP--ASVWSWNAMLAAvcGDTVIWKPS 188
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWeFDLPVPALRGGPGRRVvrrEPVGVVAAITPWNFPffLNLAKLAPALAA--GNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 189 SKTPLCAVAIQKIAcevlAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGG 268
Cdd:cd07089 160 PDTPLSALLLGEII----AETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 269 NNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVK 348
Cdd:cd07089 236 KSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 349 DFLAAVEEAKAQGGELLCGGTALPEL-GACYVSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLS 426
Cdd:cd07089 316 RVEGYIARGRDEGARLVTGGGRPAGLdKGFYVEPTLFaDVDNDMRIAQEEIFGPVLVVIPYD-DDDEAVRIANDSDYGLS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199635239 427 SSIYTTD----FREAEQFlscsgsDCGIANVNlGTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQS 491
Cdd:cd07089 395 GGVWSADvdraYRVARRI------RTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
67-476 |
2.93e-80 |
|
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: 256.81 E-value: 2.93e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 67 FLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQEMIDVCDFAVglsRQLYGLTFPSERP---- 142
Cdd:cd07095 13 FPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISI---KAYHERTGERATPmaqg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 143 ----RHRlmeqwhPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCAvaiQKIAcEVLAENGMPEGVFNL 218
Cdd:cd07095 90 ravlRHR------PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVA---ELMV-ELWEEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 219 VIGsGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTI-LELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQ 297
Cdd:cd07095 160 VQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 298 RCTTTRRVIVHESRY-EELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGA 376
Cdd:cd07095 239 RCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 377 cYVSPAIFKMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFLscSGSDCGIANVNLG 456
Cdd:cd07095 319 -FLSPGIIDVTDAADVPDEEIFGPLLQVYRYD-DFDEAIALANATRFGLSAGLLSDDEALFERFL--ARIRAGIVNWNRP 394
|
410 420
....*....|....*....|
gi 1199635239 457 TNGAEIGGAFGGEKETGGGR 476
Cdd:cd07095 395 TTGASSTAPFGGVGLSGNHR 414
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
24-476 |
9.45e-80 |
|
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: 256.46 E-value: 9.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLE 103
Cdd:cd07151 2 EWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 104 MGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERP--RHRLMEQwhPLGPIAVITAYNFP--ASVWSWNAMLAavC 179
Cdd:cd07151 82 SGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPgkENRVYRE--PLGVVGVISPWNFPlhLSMRSVAPALA--L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 180 GDTVIWKPSSKTPLCAVAIqkIAcEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRF 259
Cdd:cd07151 158 GNAVVLKPASDTPITGGLL--LA-KIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 260 GRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVG 339
Cdd:cd07151 235 KKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 340 PVADANVVKDFLAAVEEAKAQGGELLCGGTALPELgacyVSPAIFK-MSADAPLVREEKFCPILYLIPYSGGlGEAIRIH 418
Cdd:cd07151 315 PLINESQVDGLLDKIEQAVEEGATLLVGGEAEGNV----LEPTVLSdVTNDMEIAREEIFGPVAPIIKADDE-EEALELA 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199635239 419 NGVPHGLSSSIYTTDFREAEQFlsCSGSDCGIANVNLGTNGAEIGGAFGGEKETGGGR 476
Cdd:cd07151 390 NDTEYGLSGAVFTSDLERGVQF--ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGR 445
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
37-494 |
9.73e-80 |
|
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: 255.99 E-value: 9.73e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 37 YSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQ 116
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 117 EMIDVCDFAVGLSRQLYG---LTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPL 193
Cdd:cd07099 81 LALEAIDWAARNAPRVLAprkVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 194 CAVAIQkiacEVLAENGMPEGVFNLVIGSGrDVGEVMLeDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASI 273
Cdd:cd07099 161 VGELLA----EAWAAAGPPQGVLQVVTGDG-ATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 274 VTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAA 353
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 354 VEEAKAQGGELLCGGtALPELGACYVSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTT 432
Cdd:cd07099 315 VDDAVAKGAKALTGG-ARSNGGGPFYEPTVLTdVPHDMDVMREETFGPVLPVMPVA-DEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199635239 433 DFREAEQF---LscsgsDCGIANVN-LGTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQSGAI 494
Cdd:cd07099 393 DLARAEAIarrL-----EAGAVSINdVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
24-479 |
4.18e-79 |
|
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: 254.73 E-value: 4.18e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLE 103
Cdd:cd07138 6 AWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 104 MG---KILQE-----GLGEVQEMIDVCDfavglsrqlyglTFPSERPRHRLMEQWHPLGPIAVITAYNFP-----ASVws 170
Cdd:cd07138 86 MGapiTLARAaqvglGIGHLRAAADALK------------DFEFEERRGNSLVVREPIGVCGLITPWNWPlnqivLKV-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 171 wNAMLAAVCgdTVIWKPSSKTPLCAVaiqkIACEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRH 250
Cdd:cd07138 152 -APALAAGC--TVVLKPSEVAPLSAI----ILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 251 VGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGN 330
Cdd:cd07138 225 VAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 331 PLEEGVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPEL--GACYVSPAIF-KMSADAPLVREEKFCPILYLIPY 407
Cdd:cd07138 305 PRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEGleRGYFVKPTVFaDVTPDMTIAREEIFGPVLSIIPY 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199635239 408 SgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFlsCSGSDCGIANVNLGtnGAEIGGAFGGEKETGGGRECG 479
Cdd:cd07138 385 D-DEDEAIAIANDTPYGLAGYVWSADPERARAV--ARRLRAGQVHINGA--AFNPGAPFGGYKQSGNGREWG 451
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
39-477 |
2.45e-78 |
|
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: 252.28 E-value: 2.45e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 39 PADGSELGRVRCARREDYERAAAAAeaafLKWREVPAPV-RGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQE 117
Cdd:cd07146 6 PYTGEVVGTVPAGTEEALREALALA----ASYRSTLTRYqRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 118 MIDVCDFAVGLSRQLYGLTFPSE----RPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPL 193
Cdd:cd07146 82 AADVLRFAAAEALRDDGESFSCDltanGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 194 CAVAIqkiaCEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRfgRTILELGGNNASI 273
Cdd:cd07146 162 SAIYL----ADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--RQLLELGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 274 VTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAA 353
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 354 VEEAKAQGGELLCGGTalpELGACYvSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTT 432
Cdd:cd07146 316 VEEAIAQGARVLLGNQ---RQGALY-APTVLdHVPPDAELVTEETFGPVAPVIRVK-DLDEAIAISNSTAYGLSSGVCTN 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1199635239 433 DFREAEQFLscSGSDCGIANVNlgtngaEIGG------AFGGEKETG-GGRE 477
Cdd:cd07146 391 DLDTIKRLV--ERLDVGTVNVN------EVPGfrselsPFGGVKDSGlGGKE 434
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
37-437 |
1.84e-77 |
|
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: 249.94 E-value: 1.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 37 YSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGL-GEV 115
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 116 QEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFP--ASVWSWNAMLAAvcGDTVIWKPSSKTPL 193
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPlmMAAWKIAPALAA--GNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 194 CAVAIQKIACEVLaengmPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASI 273
Cdd:cd07092 160 TTLLLAELAAEVL-----PPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 274 VTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAA 353
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 354 VEEAKaQGGELLCGGTALPELGACYVSPAIFKMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTD 433
Cdd:cd07092 315 VERAP-AHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFD-DEDEAIELANDVEYGLASSVWTRD 392
|
....
gi 1199635239 434 FREA 437
Cdd:cd07092 393 VGRA 396
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
36-494 |
1.34e-76 |
|
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: 247.92 E-value: 1.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 36 SYSPADGSELGRVRCARREDYERAAAAAEAAFLK-WREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGE 114
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 115 VQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQwHPLGPIAVITAYNFPASVW--SWNAMLAAvcGDTVIWKPSSKTP 192
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVR-EPHGVTGHIIPWNYPLQITgrSVAPALAA--GNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 193 LCAVAIQKIACEVlaenGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNAS 272
Cdd:cd07109 158 LTALRLAELAEEA----GLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 273 IVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGnPLEEGVHVGPVADANVVKDFLA 352
Cdd:cd07109 234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 353 AVEEAKAQGGELLCGGTALPEL--GACYVSPAIFK-MSADAPLVREEKFCPILYLIPYsGGLGEAIRIHNGVPHGLSSSI 429
Cdd:cd07109 313 FVARARARGARIVAGGRIAEGApaGGYFVAPTLLDdVPPDSRLAQEEIFGPVLAVMPF-DDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199635239 430 YTTDFREAEQFlsCSGSDCGIANVNLGTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQSGAI 494
Cdd:cd07109 392 WTRDGDRALRV--ARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
24-477 |
1.73e-76 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 248.67 E-value: 1.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLE 103
Cdd:PRK11241 18 EWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 104 MGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTV 183
Cdd:PRK11241 98 QGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 184 IWKPSSKTPLCAVAIQKIAcevlAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTI 263
Cdd:PRK11241 178 VLKPASQTPFSALALAELA----IRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 264 LELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVAD 343
Cdd:PRK11241 254 LELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLID 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 344 ANVVKDFLAAVEEAKAQGGELLCGGTAlPELGACYVSPAIF-KMSADAPLVREEKFCPILYLIPYSGGlGEAIRIHNGVP 422
Cdd:PRK11241 334 EKAVAKVEEHIADALEKGARVVCGGKA-HELGGNFFQPTILvDVPANAKVAKEETFGPLAPLFRFKDE-ADVIAQANDTE 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199635239 423 HGLSSSIYTTD----FREAEQFlscsgsDCGIANVNLGTNGAEIgGAFGGEKETGGGRE 477
Cdd:PRK11241 412 FGLAAYFYARDlsrvFRVGEAL------EYGIVGINTGIISNEV-APFGGIKASGLGRE 463
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
24-456 |
3.74e-76 |
|
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: 247.43 E-value: 3.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLE 103
Cdd:cd07085 8 EWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 104 MGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTV 183
Cdd:cd07085 88 HGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 184 IWKPSSKTPLCAVaiqKIAcEVLAENGMPEGVFNLVIGsGRDVGEVMLEDARVRLVSFTGSTETGRHVgVAVARRFGRTI 263
Cdd:cd07085 168 VLKPSERVPGAAM---RLA-ELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYI-YERAAANGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 264 LELGG-NNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVA 342
Cdd:cd07085 242 QALGGaKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 343 DANVVKDFLAAVEEAKAQGGELLCGG---TALPELGACYVSPAIF-KMSADAPLVREEKFCPILYLIpYSGGLGEAIRIH 418
Cdd:cd07085 322 SPAAKERIEGLIESGVEEGAKLVLDGrgvKVPGYENGNFVGPTILdNVTPDMKIYKEEIFGPVLSIV-RVDTLDEAIAII 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 1199635239 419 NGVPHGLSSSIYTTDFREAEQFLscSGSDCGIANVNLG 456
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQ--REVDAGMVGINVP 436
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
24-495 |
7.15e-76 |
|
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: 246.71 E-value: 7.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGaKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKW-REVPAPVRGEIVRQIGVRLREKKEALGRLVSL 102
Cdd:cd07082 9 EWKESSG-KTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWwPTMPLEERIDCLHKFADLLKENKEEVANLLMW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 103 EMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRL----MEQWHPLGPIAVITAYNFPASVwSWNAML-AA 177
Cdd:cd07082 88 EIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaQVRREPLGVVLAIGPFNYPLNL-TVSKLIpAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 178 VCGDTVIWKPSSKTPLCAVaiqKIAcEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVAR 257
Cdd:cd07082 167 IMGNTVVFKPATQGVLLGI---PLA-EAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 258 RfgRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVH 337
Cdd:cd07082 243 K--RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 338 VGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPElgaCYVSPA-IFKMSADAPLVREEKFCPILYLIPYSGgLGEAIR 416
Cdd:cd07082 321 ITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGG---NLIYPTlLDPVTPDMRLAWEEPFGPVLPIIRVND-IEEAIE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 417 IHNGVPHGLSSSIYTTD----FREAEQFLSCSgsdcgianVNLgtNGAEIGG----AFGGEKETGGGRECGSDAWKGYMR 488
Cdd:cd07082 397 LANKSNYGLQASIFTKDinkaRKLADALEVGT--------VNI--NSKCQRGpdhfPFLGRKDSGIGTQGIGDALRSMTR 466
|
....*..
gi 1199635239 489 RQSGAIN 495
Cdd:cd07082 467 RKGIVIN 473
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
24-497 |
1.15e-75 |
|
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: 246.45 E-value: 1.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLK--WREVPAPVRGEIVRQIGVRLREKKEALGRLVS 101
Cdd:cd07119 5 EWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLET 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 102 LEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSerPRHRLMEQWH-PLGPIAVITAYNFPASVWSWNAMLAAVCG 180
Cdd:cd07119 85 LNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDV--PPHVISRTVRePVGVCGLITPWNYPLLQAAWKLAPALAAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 181 DTVIWKPSSKTPLCAVAIQKIacevLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFG 260
Cdd:cd07119 163 NTVVIKPSEVTPLTTIALFEL----IEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 261 RTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGP 340
Cdd:cd07119 239 KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 341 VADANVVKDFLAAVEEAKAQGGELLCGGTAlPELGAC----YVSPAIF-KMSADAPLVREEKFCPILYLIPYSGGlGEAI 415
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKR-PTGDELakgyFVEPTIFdDVDRTMRIVQEEIFGPVLTVERFDTE-EEAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 416 RIHNGVPHGLSSSIYTTDFREAEQFLscSGSDCGIANVN---LGTNGAEiggaFGGEKETGGGRECGSDAWKGYMRRQSG 492
Cdd:cd07119 397 RLANDTPYGLAGAVWTKDIARANRVA--RRLRAGTVWINdyhPYFAEAP----WGGYKQSGIGRELGPTGLEEYQETKHI 470
|
....*
gi 1199635239 493 AINFS 497
Cdd:cd07119 471 NINLS 475
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
34-477 |
2.44e-75 |
|
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: 244.46 E-value: 2.44e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 34 LVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLG 113
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 114 EVQEMIDVCDFAVGLSRQLYGLTFP---SERPRHRL-MEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSS 189
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldiSARGEGRQgLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 190 KTPLCAVaiqKIAcEVLAENGMPEGVFNlVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRfgRTILELGGN 269
Cdd:cd07147 161 RTPLSAL---ILG-EVLAETGLPKGAFS-VLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 270 NASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKD 349
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 350 FLAAVEEAKAQGGELLCGGTalpELGACYVSPAIFKMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSI 429
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYD-DFDEALAAVNDSKFGLQAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199635239 430 YTTDFREAEQFLscsgsdcgianvnlgtNGAEIGGAF--------------GGEKETGGGRE 477
Cdd:cd07147 390 FTRDLEKALRAW----------------DELEVGGVVindvptfrvdhmpyGGVKDSGIGRE 435
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
24-488 |
3.69e-75 |
|
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: 244.81 E-value: 3.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAF--LKWREVPAPVRGEIVRQIGVRLREKKEALGRLVS 101
Cdd:cd07091 11 EFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFetGWWRKMDPRERGRLLNKLADLIERDRDELAALES 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 102 LEMGKILQEGL-GEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQwHPLGPIAVITAYNFPASVWSWNAMLAAVCG 180
Cdd:cd07091 91 LDNGKPLEESAkGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRR-EPIGVCGQIIPWNFPLLMLAWKLAPALAAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 181 DTVIWKPSSKTPLCAVAiqkiACEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARR-F 259
Cdd:cd07091 170 NTVVLKPAEQTPLSALY----LAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSnL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 260 GRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVG 339
Cdd:cd07091 246 KKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 340 PVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGAcYVSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIH 418
Cdd:cd07091 326 PQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGY-FIQPTVFtDVKDDMKIAKEEIFGPVVTILKFK-TEDEVIERA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199635239 419 NGVPHGLSSSIYTTDFREAEQFlscsgsdcgIANVNLGT---NGAEIGGA---FGGEKETGGGRECGSDAWKGYMR 488
Cdd:cd07091 404 NDTEYGLAAGVFTKDINKALRV---------SRALKAGTvwvNTYNVFDAavpFGGFKQSGFGRELGEEGLEEYTQ 470
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
42-490 |
1.92e-74 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 241.81 E-value: 1.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 42 GSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQEMIDV 121
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 122 CDFAVGLSRQLYGLTFPSERPRHRLMEQwHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCAVAIqkI 201
Cdd:cd07152 81 LHEAAGLPTQPQGEILPSAPGRLSLARR-VPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVV--I 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 202 AcEVLAENGMPEGVFNLVIGsGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMK 281
Cdd:cd07152 158 A-RLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 282 QAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAAVEEAKAQG 361
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 362 GELLCGGTAlpeLGACYVSPAIFKMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDF----REA 437
Cdd:cd07152 316 ARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFD-SDEEAVALANDTEYGLSAGIISRDVgramALA 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1199635239 438 EQFlscsgsDCGIANVNLGTNGAEIGGAFGGEKETG-GGRECGSDAWKGYMRRQ 490
Cdd:cd07152 392 DRL------RTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFTQWQ 439
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
39-479 |
2.66e-74 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 241.87 E-value: 2.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 39 PADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQEM 118
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 119 IDVCDFAVGLSRQLY-----GLTFPSERPRHRLMEQwhPLGPIAVITAYNFP--ASVWSWNAMLAAVCgdTVIWKPSSKT 191
Cdd:cd07110 84 AGCFEYYADLAEQLDakaerAVPLPSEDFKARVRRE--PVGVVGLITPWNFPllMAAWKVAPALAAGC--TVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 192 PLCAVAIQKIACEVlaenGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNA 271
Cdd:cd07110 160 SLTELELAEIAAEA----GLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 272 SIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFL 351
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 352 AAVEEAKAQGGELLCGGTALPELGACY-VSPAIF-KMSADAPLVREEKFCPILYLIPYSGGlGEAIRIHNGVPHGLSSSI 429
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAHLEKGYfIAPTVFaDVPTDSRIWREEIFGPVLCVRSFATE-DEAIALANDSEYGLAAAV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1199635239 430 YTTDFREAEQFlsCSGSDCGIANVNlGTNGAEIGGAFGGEKETGGGRECG 479
Cdd:cd07110 395 ISRDAERCDRV--AEALEAGIVWIN-CSQPCFPQAPWGGYKRSGIGRELG 441
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
36-482 |
1.14e-73 |
|
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: 240.32 E-value: 1.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 36 SYSPADGSELGRVRCARREDYERAAAAAEAAFLK--WREVPApVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLG 113
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 114 EVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQwHPLGPIAVITAYNFPA--SVWSWNAMLAAVCgdTVIWKPSSKT 191
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLR-EPMGVAGIIVPWNSPVvlLVRSLAPALAAGC--TVVVKPAGQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 192 PLCAVAIQKIACEVlaeNGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNA 271
Cdd:cd07120 157 AQINAAIIRILAEI---PSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 272 SIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFL 351
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 352 AAVEEAKAQGGELLCGGTALPEL---GACYvSPAIFKMS-ADAPLVREEKFCPILYLIPYSGGlGEAIRIHNGVPHGLSS 427
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEGlakGAFL-RPTLLEVDdPDADIVQEEIFGPVLTLETFDDE-AEAVALANDTDYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199635239 428 SIYTTD----FREAEqflscsgsdcGIAN--VNLGTNGAEIGGA-FGGEKETGGGRECGSDA 482
Cdd:cd07120 392 SVWTRDlaraMRVAR----------AIRAgtVWINDWNKLFAEAeEGGYRQSGLGRLHGVAA 443
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
27-496 |
5.55e-72 |
|
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: 236.57 E-value: 5.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 27 ASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFL-KWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMG 105
Cdd:cd07113 10 AGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 106 KI--LQEGLgEVQEMIDVCDFAVGLSRQLYGLT----FPS-ERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAV 178
Cdd:cd07113 90 KSihLSRAF-EVGQSANFLRYFAGWATKINGETlapsIPSmQGERYTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 179 CGDTVIWKPSSKTPLcavAIQKIAcEVLAENGMPEGVFNLVIGSGrDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARR 258
Cdd:cd07113 169 TGCTIVIKPSEFTPL---TLLRVA-ELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQAASD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 259 FGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHV 338
Cdd:cd07113 244 LTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 339 GPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGAcYVSPAIFKM-SADAPLVREEKFCPILYLIPYSGGlGEAIRI 417
Cdd:cd07113 324 GPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGY-FVQPTLVLArSADSRLMREETFGPVVSFVPYEDE-EELIQL 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199635239 418 HNGVPHGLSSSIYTTDFREAEQFLscSGSDCGIANVNLGTNgAEIGGAFGGEKETGGGRECGSDAWKGYMRRQSGAINF 496
Cdd:cd07113 402 INDTPFGLTASVWTNNLSKALRYI--PRIEAGTVWVNMHTF-LDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY 477
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
22-433 |
1.09e-71 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 235.57 E-value: 1.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 22 GKEWFASDGAKELVsYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVS 101
Cdd:PRK13473 8 NGELVAGEGEKQPV-YNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLES 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 102 LEMGKILQEGLG-EVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFP--ASVWSWNAMLAAv 178
Cdd:PRK13473 87 LNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPlmMAAWKLAPALAA- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 179 cGDTVIWKPSSKTPLCAVAIQKIACEVLaengmPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARR 258
Cdd:PRK13473 166 -GNTVVLKPSEITPLTALKLAELAADIL-----PPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 259 FGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHV 338
Cdd:PRK13473 240 VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 339 GPVADANVVKDFLAAVEEAKAQG-GELLCGGTAlPELGACYVSPAIFkmsADAP----LVREEKFCPILYLIPYSgGLGE 413
Cdd:PRK13473 320 GPLISAAHRDRVAGFVERAKALGhIRVVTGGEA-PDGKGYYYEPTLL---AGARqddeIVQREVFGPVVSVTPFD-DEDQ 394
|
410 420
....*....|....*....|
gi 1199635239 414 AIRIHNGVPHGLSSSIYTTD 433
Cdd:PRK13473 395 AVRWANDSDYGLASSVWTRD 414
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
24-496 |
1.83e-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: 235.38 E-value: 1.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLK-WREVPAPVRGEIVRQIGVRLREKKEALGRLVSL 102
Cdd:cd07144 15 EFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAIEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 103 EMGKILQEG-LGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQwHPLGPIAVITAYNFPASVWSWNAMLAAVCGD 181
Cdd:cd07144 95 DSGKPYHSNaLGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLH-EPYGVCGQIIPWNYPLAMAAWKLAPALAAGN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 182 TVIWKPSSKTPLCAVAIqkiaCEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGR 261
Cdd:cd07144 174 TVVIKPAENTPLSLLYF----ANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 262 TILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYG-RLKIGNPLEEGVHVGP 340
Cdd:cd07144 250 VTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 341 VADANVVKDFLAAVEEAKAQGGELLCGGTALPELGA--CYVSPAIFkmsADAP----LVREEKFCPILYLIPYSgGLGEA 414
Cdd:cd07144 330 QVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGkgYFIPPTIF---TDVPqdmrIVKEEIFGPVVVISKFK-TYEEA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 415 IRIHNGVPHGLSSSIYTTDFREAEQFlsCSGSDCGIANVNlGTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQSGAI 494
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRV--ARELEAGMVWIN-SSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
..
gi 1199635239 495 NF 496
Cdd:cd07144 483 NL 484
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
38-487 |
2.09e-71 |
|
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: 234.42 E-value: 2.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 38 SPADGSELGRVRCARREDYERAAAAAEAAFLK--WREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGK-ILQEGLGE 114
Cdd:cd07112 8 NPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKpISDALAVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 115 VQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQwHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLC 194
Cdd:cd07112 88 VPSAANTFRWYAEAIDKVYGEVAPTGPDALALITR-EPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 195 AVAIQKIAcevlAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVAR-RFGRTILELGGNNASI 273
Cdd:cd07112 167 ALRLAELA----LEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 274 VTE-HADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLA 352
Cdd:cd07112 243 VFAdAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 353 AVEEAKAQGGELLCGGTA-LPELGACYVSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIY 430
Cdd:cd07112 323 YIESGKAEGARLVAGGKRvLTETGGFFVEPTVFDgVTPDMRIAREEIFGPVLSVITFD-SEEEAVALANDSVYGLAASVW 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199635239 431 TTDFREAEQFlsCSGSDCGIANVNlGTNGAEIGGAFGGEKETGGGRECGSDAWKGYM 487
Cdd:cd07112 402 TSDLSRAHRV--ARRLRAGTVWVN-CFDEGDITTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
29-433 |
9.72e-71 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 234.44 E-value: 9.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 29 DGAKELVSYSPADGSEL-GRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKI 107
Cdd:PRK03137 47 TTEDKIVSINPANKSEVvGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 108 LQEGLGEVQEMIDVCDFavgLSRQLYGLTFPSE---RP--RHRLMEQwhPLGPIAVITAYNFPASVWSWNAMLAAVCGDT 182
Cdd:PRK03137 127 WAEADADTAEAIDFLEY---YARQMLKLADGKPvesRPgeHNRYFYI--PLGVGVVISPWNFPFAIMAGMTLAAIVAGNT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 183 VIWKPSSKTPLCAVaiqKIAcEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVAR----- 257
Cdd:PRK03137 202 VLLKPASDTPVIAA---KFV-EVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKvqpgq 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 258 -RFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPlEEGV 336
Cdd:PRK03137 278 iWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 337 HVGPVADANVVKDFLAAVEEAKaQGGELLCGGTALPELGAcYVSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAI 415
Cdd:PRK03137 357 YMGPVINQASFDKIMSYIEIGK-EEGRLVLGGEGDDSKGY-FIQPTIFAdVDPKARIMQEEIFGPVVAFIKAK-DFDHAL 433
|
410
....*....|....*...
gi 1199635239 416 RIHNGVPHGLSSSIYTTD 433
Cdd:PRK03137 434 EIANNTEYGLTGAVISNN 451
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
37-479 |
1.06e-69 |
|
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: 231.70 E-value: 1.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 37 YSPADGSE-LGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEV 115
Cdd:cd07125 51 IDPADHERtIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 116 QEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSwNAMLAA-VCGDTVIWKPSSKTPLC 194
Cdd:cd07125 131 REAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFT-GQIAAAlAAGNTVIAKPAEQTPLI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 195 AVAiqkiACEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRT---ILELGGNNA 271
Cdd:cd07125 210 AAR----AVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPIlplIAETGGKNA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 272 SIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFL 351
Cdd:cd07125 286 MIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 352 AAVEEAKAQgGELLCgGTALPELGACYVSPAIFKMSADAPLvREEKFCPILYLIPYSGG-LGEAIRIHNGVPHGLSSSIY 430
Cdd:cd07125 366 AHTELMRGE-AWLIA-PAPLDDGNGYFVAPGIIEIVGIFDL-TTEVFGPILHVIRFKAEdLDEAIEDINATGYGLTLGIH 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1199635239 431 TTDFREAEQFLscsgSDCGIAN--VNLGTNGAeIGGA--FGGEKETGGGRECG 479
Cdd:cd07125 443 SRDEREIEYWR----ERVEAGNlyINRNITGA-IVGRqpFGGWGLSGTGPKAG 490
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
38-490 |
1.82e-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: 229.12 E-value: 1.82e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 38 SPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQE 117
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 118 MIDVCDFavglsrqlYGLTFPSE-RPRHR------LM---EQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKP 187
Cdd:cd07101 82 VAIVARY--------YARRAERLlKPRRRrgaipvLTrttVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 188 SSKTPLCAVaiqkIACEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARvrLVSFTGSTETGRHVGVAVARRFGRTILELG 267
Cdd:cd07101 154 DSQTALTAL----WAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD--YVMFTGSTATGRVVAERAGRRLIGCSLELG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 268 GNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVV 347
Cdd:cd07101 228 GKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 348 KDFLAAVEEAKAQGGELLCGGTALPELGACYVSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLS 426
Cdd:cd07101 308 DRVTAHVDDAVAKGATVLAGGRARPDLGPYFYEPTVLTgVTEDMELFAEETFGPVVSIYRVA-DDDEAIELANDTDYGLN 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 427 SSIYTTDFRE----AEQFlscsgsDCGIANVNLG--TNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQ 490
Cdd:cd07101 387 ASVWTRDGARgrriAARL------RAGTVNVNEGyaAAWASIDAPMGGMKDSGLGRRHGAEGLLKYTETQ 450
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
37-441 |
4.93e-69 |
|
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: 227.90 E-value: 4.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 37 YSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQ 116
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 117 EMIDVCDFAVGLSRQ-LYGLTFPSERPRHRLMEQwHPLGPIAVITAYNFPASVwSWNAMLAAV-CGDTVIWKPSSKTPLC 194
Cdd:cd07102 81 GMLERARYMISIAEEaLADIRVPEKDGFERYIRR-EPLGVVLIIAPWNYPYLT-AVNAVIPALlAGNAVILKHSPQTPLC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 195 AVAIQKIacevLAENGMPEGVFNLVIGSGrDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIV 274
Cdd:cd07102 159 GERFAAA----FAEAGLPEGVFQVLHLSH-ETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 275 TEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYE---ELAQKLTSAYgrlKIGNPLEEGVHVGPVADANVVKDFL 351
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDafvEAFVAVVKGY---KLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 352 AAVEEAKAQGGELLCGGTALPEL--GACYVSPAIF-KMSADAPLVREEKFCPILYLIPYSGGlGEAIRIHNGVPHGLSSS 428
Cdd:cd07102 311 AQIADAIAKGARALIDGALFPEDkaGGAYLAPTVLtNVDHSMRVMREETFGPVVGIMKVKSD-AEAIALMNDSEYGLTAS 389
|
410
....*....|...
gi 1199635239 429 IYTTDFREAEQFL 441
Cdd:cd07102 390 VWTKDIARAEALG 402
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
24-491 |
1.30e-68 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 227.84 E-value: 1.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLE 103
Cdd:PRK13252 14 AYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 104 MGKILQEGL-GEVQEMIDVCDFAVGL-------SRQLYGLTFPSERpRhrlmeqwHPLGPIAVITAYNFPASVWSWNAML 175
Cdd:PRK13252 94 TGKPIQETSvVDIVTGADVLEYYAGLapalegeQIPLRGGSFVYTR-R-------EPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 176 AAVCGDTVIWKPSSKTPLCAVaiqKIAcEVLAENGMPEGVFNLVIGSGRdVGEVMLEDARVRLVSFTGSTETGRHVGVAV 255
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTAL---KLA-EIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 256 ARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEG 335
Cdd:PRK13252 241 AASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 336 VHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGA---CYVSPAIF-KMSADAPLVREEKFCPILYLIPYSGGl 411
Cdd:PRK13252 321 TNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFangAFVAPTVFtDCTDDMTIVREEIFGPVMSVLTFDDE- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 412 GEAIRIHNGVPHGLSSSIYTTDFREAEQFLscSGSDCGIANVN-LGTNGAEIggAFGGEKETGGGRECGSDAWKGYMRRQ 490
Cdd:PRK13252 400 DEVIARANDTEYGLAAGVFTADLSRAHRVI--HQLEAGICWINtWGESPAEM--PVGGYKQSGIGRENGIATLEHYTQIK 475
|
.
gi 1199635239 491 S 491
Cdd:PRK13252 476 S 476
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
27-481 |
2.80e-68 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 228.22 E-value: 2.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 27 ASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGK 106
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 107 ILQEGLGEVQEMIDVCDFavglsrqlYGLTFPSE-RPRHR-----LM----EQWHPLGPIAVITAYNFPASVWSWNAMLA 176
Cdd:PRK09407 107 ARRHAFEEVLDVALTARY--------YARRAPKLlAPRRRagalpVLtkttELRQPKGVVGVISPWNYPLTLAVSDAIPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 177 AVCGDTVIWKPSSKTPLCAVAiqkiACEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARvrLVSFTGSTETGRHVGVAVA 256
Cdd:PRK09407 179 LLAGNAVVLKPDSQTPLTALA----AVELLYEAGLPRDLWQVVTGPGPVVGTALVDNAD--YLMFTGSTATGRVLAEQAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 257 RRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGV 336
Cdd:PRK09407 253 RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 337 HVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGACYVSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAI 415
Cdd:PRK09407 333 DMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGPLFYEPTVLTgVTPDMELAREETFGPVVSVYPVA-DVDEAV 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199635239 416 RIHNGVPHGLSSSIYTTDFREAEQFlsCSGSDCGIANVN--LGTNGAEIGGAFGGEKETGGGRECGSD 481
Cdd:PRK09407 412 ERANDTPYGLNASVWTGDTARGRAI--AARIRAGTVNVNegYAAAWGSVDAPMGGMKDSGLGRRHGAE 477
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
22-487 |
1.48e-67 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 225.77 E-value: 1.48e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 22 GKEWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLK-----WREVPAPVRGEIVRQIGVRLREKKEAL 96
Cdd:PLN02467 13 GGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKSEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 97 GRLVSLEMGKILQEGLGEvqeMIDV--C-----DFAVGL-SRQLYGLTFPSERPRHRLMeqWHPLGPIAVITAYNFP--A 166
Cdd:PLN02467 93 AKLETLDCGKPLDEAAWD---MDDVagCfeyyaDLAEALdAKQKAPVSLPMETFKGYVL--KEPLGVVGLITPWNYPllM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 167 SVWSWNAMLAAVCgdTVIWKPSSktpLCAVAIQKIAcEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTE 246
Cdd:PLN02467 168 ATWKVAPALAAGC--TAVLKPSE---LASVTCLELA-DICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 247 TGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRL 326
Cdd:PLN02467 242 TGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 327 KIGNPLEEGVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGACY-VSPAIF-KMSADAPLVREEKFCPILYL 404
Cdd:PLN02467 322 KISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKGFfIEPTIItDVTTSMQIWREEVFGPVLCV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 405 IPYSGGlGEAIRIHNGVPHGLSSSIYTTDF----REAEQFlscsgsDCGIANVNLgTNGAEIGGAFGGEKETGGGRECGS 480
Cdd:PLN02467 402 KTFSTE-DEAIELANDSHYGLAGAVISNDLerceRVSEAF------QAGIVWINC-SQPCFCQAPWGGIKRSGFGRELGE 473
|
....*..
gi 1199635239 481 DAWKGYM 487
Cdd:PLN02467 474 WGLENYL 480
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
83-454 |
7.77e-67 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 221.15 E-value: 7.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 83 RQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAY 162
Cdd:PRK10090 2 RKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 163 NFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCAVAIQKIACEVlaenGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFT 242
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI----GLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 243 GSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSA 322
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 323 YGRLKIGNPLEEG-VHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGACYVSPAIFKMSADAPLVREEKFCPI 401
Cdd:PRK10090 238 MQAVQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1199635239 402 LYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAeqFLSCSGSDCGIANVN 454
Cdd:PRK10090 318 LPVVAFD-TLEEAIAMANDSDYGLTSSIYTQNLNVA--MKAIKGLKFGETYIN 367
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
24-477 |
5.87e-65 |
|
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: 218.09 E-value: 5.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLE 103
Cdd:cd07117 8 EWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 104 MGKILQEGLGevqemIDVcDFAVGLSRQLYGLTFPSERPRHRLMEQW------HPLGPIAVITAYNFPASVWSWNAMLAA 177
Cdd:cd07117 88 NGKPIRETRA-----VDI-PLAADHFRYFAGVIRAEEGSANMIDEDTlsivlrEPIGVVGQIIPWNFPFLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 178 VCGDTVIWKPSSKTPLCAVAIQKIACEVLaengmPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVAR 257
Cdd:cd07117 162 AAGNTVVIKPSSTTSLSLLELAKIIQDVL-----PKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 258 RFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVH 337
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 338 VGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGA---CYVSPA-IFKMSADAPLVREEKFCPILYLIPYSgGLGE 413
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLdkgFFIEPTlIVNVTNDMRVAQEEIFGPVATVIKFK-TEDE 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199635239 414 AIRIHNGVPHGLSSSIYTTDFREAEQFlsCSGSDCGIANVNLgTNGAEIGGAFGGEKETGGGRE 477
Cdd:cd07117 396 VIDMANDSEYGLGGGVFTKDINRALRV--ARAVETGRVWVNT-YNQIPAGAPFGGYKKSGIGRE 456
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
24-491 |
1.40e-64 |
|
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: 216.98 E-value: 1.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLK--WREVPAPVRGEIVRQIGVRLREKKEALGRLVS 101
Cdd:cd07142 11 QFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALET 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 102 LEMGKILQEG-LGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRH--RLMEqwhPLGPIAVITAYNFPASVWSWNAMLAAV 178
Cdd:cd07142 91 WDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHvyTLHE---PIGVVGQIIPWNFPLLMFAWKVGPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 179 CGDTVIWKPSSKTPLCAVAIQKIAcevlAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHV-GVAVAR 257
Cdd:cd07142 168 CGNTIVLKPAEQTPLSALLAAKLA----AEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIImQLAAKS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 258 RFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVH 337
Cdd:cd07142 244 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 338 VGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGAcYVSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIR 416
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGY-YIQPTIFsDVKDDMKIARDEIFGPVQSILKFK-TVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199635239 417 IHNGVPHGLSSSIYTTDFREAEQFLscSGSDCGIANVNLgTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQS 491
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLS--RALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKA 473
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
24-468 |
2.12e-64 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 216.75 E-value: 2.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAkELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLE 103
Cdd:PRK09457 8 DWIAGQGE-AFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 104 MGKILQEGLGEVQEMIDvcdfAVGLSRQLYG-LTFPSERP--------RHRlmeqwhPLGPIAVITAYNFPASVWSWNAM 174
Cdd:PRK09457 87 TGKPLWEAATEVTAMIN----KIAISIQAYHeRTGEKRSEmadgaavlRHR------PHGVVAVFGPYNFPGHLPNGHIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 175 LAAVCGDTVIWKPSSKTPLCAVAIQKIacevLAENGMPEGVFNLVIGsGRDVGEVMLEDARVRLVSFTGSTETGRHVGVA 254
Cdd:PRK09457 157 PALLAGNTVVFKPSELTPWVAELTVKL----WQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 255 VARRFGRTI-LELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRY-EELAQKLTSAYGRLKIGNPL 332
Cdd:PRK09457 232 FAGQPEKILaLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 333 EE-GVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTaLPELGACYVSPAIFKMSADAPLVREEKFCPILYLIPYSgGL 411
Cdd:PRK09457 312 AEpQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMT-QLQAGTGLLTPGIIDVTGVAELPDEEYFGPLLQVVRYD-DF 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199635239 412 GEAIRIHNGVPHGLSSSIYTTDFREAEQFLscSGSDCGIANVNLGTNGAEIGGAFGG 468
Cdd:PRK09457 390 DEAIRLANNTRFGLSAGLLSDDREDYDQFL--LEIRAGIVNWNKPLTGASSAAPFGG 444
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
22-479 |
2.43e-64 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 217.06 E-value: 2.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 22 GKEWFasDGAKELVSYSPADGSE-LGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLV 100
Cdd:cd07083 24 GGEWV--DTKERMVSVSPFAPSEvVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 101 SLEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWH-PLGPIAVITAYNFPASVWSWNAMLAAVC 179
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYvGLGAGVVISPWNFPVAIFTGMIVAPVAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 180 GDTVIWKPSSKTPLCAVAiqkiACEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARR- 258
Cdd:cd07083 182 GNTVIAKPAEDAVVVGYK----VFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLa 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 259 -----FGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLE 333
Cdd:cd07083 258 pgqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 334 EGVHVGPVADANVVKDFLAAVEEAKaQGGELLCGGTaLPELGACYVSPAIFKM-SADAPLVREEKFCPILYLIPYSGG-L 411
Cdd:cd07083 338 NGTDLGPVIDAEQEAKVLSYIEHGK-NEGQLVLGGK-RLEGEGYFVAPTVVEEvPPKARIAQEEIFGPVLSVIRYKDDdF 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 412 GEAIRIHNGVPHGLSSSIYttdFREAEQFLSCSGS-DCGIANVNLGTNGAEIG-GAFGGEKETGGGRECG 479
Cdd:cd07083 416 AEALEVANSTPYGLTGGVY---SRKREHLEEARREfHVGNLYINRKITGALVGvQPFGGFKLSGTNAKTG 482
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
24-489 |
8.35e-63 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 212.64 E-value: 8.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLE 103
Cdd:cd07111 29 KWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 104 MGKILQEglgevqemidVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTV 183
Cdd:cd07111 109 NGKPIRE----------SRDCDIPLVARHFYHHAGWAQLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 184 IWKPSSKTPLCAVAIQKIAcevlAENGMPEGVFNLVIGSGrDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTI 263
Cdd:cd07111 179 VLKPAEYTPLTALLFAEIC----AEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 264 LELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVAD 343
Cdd:cd07111 254 LELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 344 ANVVKDFLAAVEEAKAQGGELLCGGTALPELGaCYVSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVP 422
Cdd:cd07111 334 PAQLKRIRELVEEGRAEGADVFQPGADLPSKG-PFYPPTLFTnVPPASRIAQEEIFGPVLVVLTFR-TAKEAVALANNTP 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199635239 423 HGLSSSIYTTDFREAeqfLSCSGS-DCGIANVNlGTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRR 489
Cdd:cd07111 412 YGLAASVWSENLSLA---LEVALSlKAGVVWIN-GHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRP 475
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
22-477 |
6.49e-61 |
|
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: 207.58 E-value: 6.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 22 GKEWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVS 101
Cdd:cd07559 6 NGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 102 LEMGKILQEGLGevqemIDVcDFAVGLSRQLYGLTFPSERPRHRLMEQ------WHPLGPIAVITAYNFP--ASVWSWNA 173
Cdd:cd07559 86 LDNGKPIRETLA-----ADI-PLAIDHFRYFAGVIRAQEGSLSEIDEDtlsyhfHEPLGVVGQIIPWNFPllMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 174 MLAAvcGDTVIWKPSSKTPLCAVAIQKIACEVLaengmPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGV 253
Cdd:cd07559 160 ALAA--GNTVVLKPASQTPLSILVLMELIGDLL-----PKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 254 AVARRFGRTILELGGNNASIV-----TEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKI 328
Cdd:cd07559 233 YAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 329 GNPLEEGVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPEL----GACYVSPAIFKMSADAPLVREEKFCPILYL 404
Cdd:cd07559 313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199635239 405 IPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFLScsgsdcGIANVNLGTNGAEI---GGAFGGEKETGGGRE 477
Cdd:cd07559 393 ITFK-DEEEAIAIANDTEYGLGGGVWTRDINRALRVAR------GIQTGRVWVNCYHQypaHAPFGGYKKSGIGRE 461
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
18-495 |
2.11e-60 |
|
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: 206.23 E-value: 2.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 18 GVSTGKEWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAF-LKW-REVPAPVRGEIVRQIGVRLREKKEA 95
Cdd:cd07143 8 GLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFeTDWgLKVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 96 LGRLVSLEMGK-ILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFpsERPRHRLMEQWH-PLGPIAVITAYNFPASVWSWNA 173
Cdd:cd07143 88 LASIEALDNGKtFGTAKRVDVQASADTFRYYGGWADKIHGQVI--ETDIKKLTYTRHePIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 174 MLAAVCGDTVIWKPSSKTPLCAVAiqkiACEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGV 253
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALY----MTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVME 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 254 AVAR-RFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPL 332
Cdd:cd07143 242 AAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 333 EEGVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGAcYVSPAIF-KMSADAPLVREEKFCPILYLIPYSGGl 411
Cdd:cd07143 322 AEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY-FIEPTIFtDVTEDMKIVKEEIFGPVVAVIKFKTE- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 412 GEAIRIHNGVPHGLSSSIYTTDFREAEQflSCSGSDCGIANVNLgTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQS 491
Cdd:cd07143 400 EEAIKRANDSTYGLAAAVFTNNINNAIR--VANALKAGTVWVNC-YNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKA 476
|
....
gi 1199635239 492 GAIN 495
Cdd:cd07143 477 VHIN 480
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
67-476 |
2.11e-59 |
|
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: 202.04 E-value: 2.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 67 FLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGkiLQEGLGE--VQEMIDVCDFAVGLSRQLYGLTFPSERPRH 144
Cdd:cd07105 13 FPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG--ATAAWAGfnVDLAAGMLREAASLITQIIGGSIPSDKPGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 145 RLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCAVAIqkiaCEVLAENGMPEGVFNLVIGSGR 224
Cdd:cd07105 91 LAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLI----GRVFHEAGLPKGVLNVVTHSPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 225 DVGEV---MLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTT 301
Cdd:cd07105 167 DAPEVveaLIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 302 TRRVIVHESRYEELAQKLTSAYGRLKIGnpleeGVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGACYVSP 381
Cdd:cd07105 247 TERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPSGTSMPP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 382 AIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAeqfLSCSGS-DCGIANVNLGTNG 459
Cdd:cd07105 322 TILDnVTPDMDIYSEESFGPVVSIIRVK-DEEEAVRIANDSEYGLSAAVFTRDLARA---LAVAKRiESGAVHINGMTVH 397
|
410
....*....|....*..
gi 1199635239 460 AEIGGAFGGEKETGGGR 476
Cdd:cd07105 398 DEPTLPHGGVKSSGYGR 414
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
24-486 |
4.02e-59 |
|
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: 202.58 E-value: 4.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLK---WREVPAPVRGEIVRQIGVRLREKKEALGRLV 100
Cdd:cd07141 14 EWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 101 SLEMGKILQEG-LGEVQEMIDVCDFAVGLSRQLYGLTFPSERP-----RHRlmeqwhPLGPIAVITAYNFPASVWSWNAM 174
Cdd:cd07141 94 TLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDfftytRHE------PVGVCGQIIPWNFPLLMAAWKLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 175 LAAVCGDTVIWKPSSKTPLCAVAIqkiaCEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVA 254
Cdd:cd07141 168 PALACGNTVVLKPAEQTPLTALYL----ASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 255 VAR-RFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLE 333
Cdd:cd07141 244 AGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 334 EGVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGAcYVSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLG 412
Cdd:cd07141 324 PKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGY-FIQPTVFSdVTDDMRIAKEEIFGPVQQIFKFK-TID 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199635239 413 EAIRIHNGVPHGLSSSIYTTDFREAEQFlsCSGSDCGIANVNLgTNGAEIGGAFGGEKETGGGRECGSDAWKGY 486
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITF--SNALRAGTVWVNC-YNVVSPQAPFGGYKMSGNGRELGEYGLQEY 472
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
31-477 |
1.58e-56 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 195.47 E-value: 1.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 31 AKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQE 110
Cdd:PRK13968 6 ATHAISVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 111 GLGEVQEMIDVCDFavglsrqlYGLTFPSE-RPRHRLME------QWHPLGPIAVITAYNFPAsvwsWNAMLAAV----C 179
Cdd:PRK13968 86 ARAEVAKSANLCDW--------YAEHGPAMlKAEPTLVEnqqaviEYRPLGTILAIMPWNFPL----WQVMRGAVpillA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 180 GDTVIWKPSSKTPLCAVAIQkiacEVLAENGMPEGVFNLVIGSGRDVGEvMLEDARVRLVSFTGSTETGRHVGVAVARRF 259
Cdd:PRK13968 154 GNGYLLKHAPNVMGCAQLIA----QVFKDAGIPQGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAGAAIGAQAGAAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 260 GRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVG 339
Cdd:PRK13968 229 KKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 340 PVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGACYVSPAIFKMSADAPLVREEKFCPILyLIPYSGGLGEAIRIHN 419
Cdd:PRK13968 309 PMARFDLRDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVA-AITVAKDAEHALELAN 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199635239 420 GVPHGLSSSIYTTDFREAEQFlsCSGSDCGIANVNlGTNGAEIGGAFGGEKETGGGRE 477
Cdd:PRK13968 388 DSEFGLSATIFTTDETQARQM--AARLECGGVFIN-GYCASDARVAFGGVKKSGFGRE 442
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
24-496 |
1.64e-55 |
|
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: 193.10 E-value: 1.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLK--WREVPAPVRGEIVRQIGVRLREKKEALGRLVS 101
Cdd:cd07140 13 EFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIES 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 102 LEMGKILQEGLG-EVQEMIDVCDFAVGLSRQLYGLTFP--SERPRHRL-MEQWHPLGPIAVITAYNFPASVWSWN--AML 175
Cdd:cd07140 93 LDSGAVYTLALKtHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLAWKmaACL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 176 AAvcGDTVIWKPSSKTPLCAVaiqKIAcEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAV 255
Cdd:cd07140 173 AA--GNTVVLKPAQVTPLTAL---KFA-ELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 256 A-RRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEE 334
Cdd:cd07140 247 AvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 335 GVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELGAcYVSPAIFKMSADAPLV-REEKFCPILYLIPYSGGLGE 413
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF-FFEPTVFTDVEDHMFIaKEESFGPIMIISKFDDGDVD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 414 AI-RIHNGVPHGLSSSIYTTDFREAeqfLSCSGS-DCGIANVNLgTNGAEIGGAFGGEKETGGGRECGSDAWKGYMRRQS 491
Cdd:cd07140 406 GVlQRANDTEYGLASGVFTKDINKA---LYVSDKlEAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKT 481
|
....*
gi 1199635239 492 GAINF 496
Cdd:cd07140 482 VTIEY 486
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
39-477 |
4.19e-55 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 191.49 E-value: 4.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 39 PADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQEM 118
Cdd:PRK09406 8 PATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 119 IDVCDFAVGLSRQLYGlTFPSERPR---HRLMEQWHPLGPIAVITAYNFPAsvwsWNAML----AAVCGDTVIWKPSSKT 191
Cdd:PRK09406 88 AKGFRYYAEHAEALLA-DEPADAAAvgaSRAYVRYQPLGVVLAVMPWNFPL----WQVVRfaapALMAGNVGLLKHASNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 192 PLCAVAIQkiacEVLAENGMPEGVF-NLVIGSGrdVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNN 270
Cdd:PRK09406 163 PQTALYLA----DLFRRAGFPDGCFqTLLVGSG--AVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 271 ASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDF 350
Cdd:PRK09406 237 PFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 351 LAAVEEAKAQGGELLCGGTALPELGACYVSPAIFKMSADAPLVREEKFCPI--LYLIpysGGLGEAIRIHNGVPHGLSSS 428
Cdd:PRK09406 317 EKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVasLYRV---ADIDEAIEIANATTFGLGSN 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1199635239 429 IYTTDFREAEQFLscSGSDCGIANVN-LGTNGAEIGgaFGGEKETGGGRE 477
Cdd:PRK09406 394 AWTRDEAEQERFI--DDLEAGQVFINgMTVSYPELP--FGGVKRSGYGRE 439
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
28-440 |
6.06e-54 |
|
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: 188.94 E-value: 6.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 28 SDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKI 107
Cdd:TIGR01722 12 GASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 108 LQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKP 187
Cdd:TIGR01722 92 HSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 188 SSKTPLCAVAIqkiaCEVLAENGMPEGVFNLVIGsGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELG 267
Cdd:TIGR01722 172 SEKVPSAAVKL----AELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 268 GNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVI-VHESRyeELAQKLTSAYGRLKIGNPLEEGVHVGPVADANV 346
Cdd:TIGR01722 247 AKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVlVGAAD--EWVPEIRERAEKIRIGPGDDPGAEMGPLITPQA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 347 VKDFLAAVEEAKAQGGELLCGGTALPELG---ACYVSPAIF-KMSADAPLVREEKFCPILYLIPySGGLGEAIRIHNGVP 422
Cdd:TIGR01722 325 KDRVASLIAGGAAEGAEVLLDGRGYKVDGyeeGNWVGPTLLeRVPPTMKAYQEEIFGPVLCVLE-ADTLEEAIALINASP 403
|
410
....*....|....*...
gi 1199635239 423 HGLSSSIYTTDFREAEQF 440
Cdd:TIGR01722 404 YGNGTAIFTRDGAAARRF 421
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
21-415 |
6.95e-50 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 184.25 E-value: 6.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 21 TGKEWFAS-----DGAKELVsYSPADGSE-LGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKE 94
Cdd:PRK11904 547 LEKQWQAGpiingEGEARPV-VSPADRRRvVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRA 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 95 ALGRLVSLEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYG----LTFPS-ERPRHRLmeqwHPLGPIAVITAYNFPASVW 169
Cdd:PRK11904 626 ELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGapekLPGPTgESNELRL----HGRGVFVCISPWNFPLAIF 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 170 SWNAMLAAVCGDTVIWKPSSKTPLCAVAiqkiACEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGR 249
Cdd:PRK11904 702 LGQVAAALAAGNTVIAKPAEQTPLIAAE----AVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETAR 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 250 HVGVAVARRFGRT---ILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRL 326
Cdd:PRK11904 778 IINRTLAARDGPIvplIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAEL 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 327 KIGNPLEEGVHVGPVADANvVKDFLAAVEEAKAQGGELLCGGTaLPELGA--CYVSPAIFKMSaDAPLVREEKFCPILYL 404
Cdd:PRK11904 858 KVGDPRLLSTDVGPVIDAE-AKANLDAHIERMKREARLLAQLP-LPAGTEngHFVAPTAFEID-SISQLEREVFGPILHV 934
|
410
....*....|..
gi 1199635239 405 IPY-SGGLGEAI 415
Cdd:PRK11904 935 IRYkASDLDKVI 946
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
38-433 |
1.24e-48 |
|
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: 173.76 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 38 SPADGSELGRVRCARREDYERAAAAAEAAFL---KWreVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGE 114
Cdd:cd07148 5 NPFDLKPIGEVPTVDWAAIDKALDTAHALFLdrnNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 115 VQEMIDVCDFAVGLSRQLYG------LTFPSERPRHRLMEQwhPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPS 188
Cdd:cd07148 83 VTRAIDGVELAADELGQLGGreipmgLTPASAGRIAFTTRE--PIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 189 SKTPLCAVAIQKIacevLAENGMPEGVFNLVIgSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRfGRTILELGG 268
Cdd:cd07148 161 LATPLSCLAFVDL----LHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 269 NNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVK 348
Cdd:cd07148 235 AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 349 DFLAAVEEAKAQGGELLCGGTALPElgACYVSPAIFKMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSS 428
Cdd:cd07148 315 RVEEWVNEAVAAGARLLCGGKRLSD--TTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYD-DLDEAIAQANSLPVAFQAA 391
|
....*
gi 1199635239 429 IYTTD 433
Cdd:cd07148 392 VFTKD 396
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
38-479 |
2.37e-48 |
|
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: 174.33 E-value: 2.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 38 SPADGSE-LGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQ 116
Cdd:TIGR01238 57 NPADRRDiVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 117 EMIDVCDFAVGLSRQlyglTFPSERPRhrlmeqwhPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCAV 196
Cdd:TIGR01238 137 EAVDFCRYYAKQVRD----VLGEFSVE--------SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAY 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 197 AiqkiACEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRF---GRTILELGGNNASI 273
Cdd:TIGR01238 205 R----AVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 274 VTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAA 353
Cdd:TIGR01238 281 VDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAH 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 354 VEEAKAQG---GELLCGGTALPELGAcYVSPAIFKMSADAPLvREEKFCPILYLIPYSGG-LGEAIRIHN----GVPHGL 425
Cdd:TIGR01238 361 IEHMSQTQkkiAQLTLDDSRACQHGT-FVAPTLFELDDIAEL-SEEVFGPVLHVVRYKAReLDQIVDQINqtgyGLTMGV 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1199635239 426 SSSIYTTdFREAEqflscSGSDCGIANVNLGTNGAEIG-GAFGGEKETGGGRECG 479
Cdd:TIGR01238 439 HSRIETT-YRWIE-----KHARVGNCYVNRNQVGAVVGvQPFGGQGLSGTGPKAG 487
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
20-410 |
1.65e-47 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 177.05 E-value: 1.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 20 STGKEWFA--------SDGAKELVsYSPADGSE-LGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLR 90
Cdd:COG4230 551 AAEKQWQAapliageaASGEARPV-RNPADHSDvVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLE 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 91 EKKEALGRLVSLEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGltfpsERPRHrlmeqwHPLGPIAVITAYNFP----- 165
Cdd:COG4230 630 AHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFA-----APTVL------RGRGVFVCISPWNFPlaift 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 166 ---AsvwswnAMLAAvcGDTVIWKPSSKTPLCAVAiqkiACEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFT 242
Cdd:COG4230 699 gqvA------AALAA--GNTVLAKPAEQTPLIAAR----AVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFT 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 243 GSTETGRHVGVAVARRFGRT---ILELGGNNASIV-----TEhadmkQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEE 314
Cdd:COG4230 767 GSTETARLINRTLAARDGPIvplIAETGGQNAMIVdssalPE-----QVVDDVLASAFDSAGQRCSALRVLCVQEDIADR 841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 315 LAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAAVEEAKAQGGelLCGGTALPELGA--CYVSPAIFKMSADAPL 392
Cdd:COG4230 842 VLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGR--LVHQLPLPEECAngTFVAPTLIEIDSISDL 919
|
410
....*....|....*...
gi 1199635239 393 vREEKFCPILYLIPYSGG 410
Cdd:COG4230 920 -EREVFGPVLHVVRYKAD 936
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
32-488 |
1.88e-47 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 172.68 E-value: 1.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 32 KELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLK--WREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQ 109
Cdd:PLN02466 73 KTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 110 EGLG-EVQEMIDVCDFAVGLSRQLYGLTFPSERPRHrlMEQWH-PLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKP 187
Cdd:PLN02466 153 QSAKaELPMFARLFRYYAGWADKIHGLTVPADGPHH--VQTLHePIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 188 SSKTPLCAVaiqkIACEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHV-GVAVARRFGRTILEL 266
Cdd:PLN02466 231 AEQTPLSAL----YAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVlELAAKSNLKPVTLEL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 267 GGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANV 346
Cdd:PLN02466 307 GGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQ 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 347 VKDFLAAVEEAKAQGGELLCGGTALPELGAcYVSPAIFKMSADAPLV-REEKFCPILYLIPYSgGLGEAIRIHNGVPHGL 425
Cdd:PLN02466 387 FEKILRYIKSGVESGATLECGGDRFGSKGY-YIQPTVFSNVQDDMLIaQDEIFGPVQSILKFK-DLDEVIRRANNTRYGL 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199635239 426 SSSIYTTDFREAEQFLSCsgsdcgianVNLGT---NGAEIGGA---FGGEKETGGGRECGSDAWKGYMR 488
Cdd:PLN02466 465 AAGVFTQNLDTANTLSRA---------LRVGTvwvNCFDVFDAaipFGGYKMSGIGREKGIYSLNNYLQ 524
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
39-491 |
1.83e-46 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 169.23 E-value: 1.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 39 PADGSELGRVRCARREDYERAAAAAEAAFL--KWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEG-LGEV 115
Cdd:PLN02766 43 PRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGkAVDI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 116 QEMIDVCDFAVGLSRQLYGLTFPSERPRH--RLMEqwhPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPL 193
Cdd:PLN02766 123 PAAAGLLRYYAGAADKIHGETLKMSRQLQgyTLKE---PIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 194 CAVAIQKIAcevlAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTI-LELGGNNAS 272
Cdd:PLN02766 200 SALFYAHLA----KLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNLKQVsLELGGKSPL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 273 IVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLA 352
Cdd:PLN02766 276 LIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 353 AVEEAKAQGGELLCGGTALPELGAcYVSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYT 431
Cdd:PLN02766 356 YIEHGKREGATLLTGGKPCGDKGY-YIEPTIFtDVTEDMKIAQDEIFGPVMSLMKFK-TVEEAIKKANNTKYGLAAGIVT 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199635239 432 TDF----------REAEQFLSCS---GSDCgianvnlgtngaeiggAFGGEKETGGGRECGSDAWKGYMRRQS 491
Cdd:PLN02766 434 KDLdvantvsrsiRAGTIWVNCYfafDPDC----------------PFGGYKMSGFGRDQGMDALDKYLQVKS 490
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
20-407 |
7.71e-45 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 169.28 E-value: 7.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 20 STGKEWFA--------SDGAKELVsYSPADGSEL-GRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLR 90
Cdd:PRK11905 548 FAAKTWHAapllaggdVDGGTRPV-LNPADHDDVvGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLME 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 91 EKKEALGRLVSLEMGKILQEGLGEVQEMIDVCDFavglsrqlYGltfpsERPRHRLMEQWH-PLGPIAVITAYNFPASVW 169
Cdd:PRK11905 627 AHMPELFALAVREAGKTLANAIAEVREAVDFLRY--------YA-----AQARRLLNGPGHkPLGPVVCISPWNFPLAIF 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 170 SWNAMLAAVCGDTVIWKPSSKTPLCAVAiqkiACEVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGR 249
Cdd:PRK11905 694 TGQIAAALVAGNTVLAKPAEQTPLIAAR----AVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVAR 769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 250 HVGVAVARRFGRT---ILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRL 326
Cdd:PRK11905 770 LIQRTLAKRSGPPvplIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDEL 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 327 KIGNPLEEGVHVGPVADANVVKDFLAAVEEAKAQGGelLCGGTALPEL--GACYVSPAIFKMSADAPLVReEKFCPILYL 404
Cdd:PRK11905 850 RIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGR--LVHQLPLPAEteKGTFVAPTLIEIDSISDLER-EVFGPVLHV 926
|
...
gi 1199635239 405 IPY 407
Cdd:PRK11905 927 VRF 929
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
37-476 |
1.54e-42 |
|
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: 157.46 E-value: 1.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 37 YSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEG-LGEV 115
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 116 qemIDVCDFAVGLSRqlYGLTF--PSERPRHRLME------QWHPLGPIAVITAYNFP-ASVWSwnAMLAAV-CGDTVIW 185
Cdd:cd07098 81 ---LVTCEKIRWTLK--HGEKAlrPESRPGGLLMFykrarvEYEPLGVVGAIVSWNYPfHNLLG--PIIAALfAGNAIVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 186 KPSSKTPLCAVAIQKIACEVLAENGMPEGVFNLVIGSGrDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILE 265
Cdd:cd07098 154 KVSEQVAWSSGFFLSIIRECLAACGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 266 LGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADAN 345
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 346 VVKDFLAAVEEAKAQGGELLCGGT--ALPEL-GACYVSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGV 421
Cdd:cd07098 313 RFDRLEELVADAVEKGARLLAGGKryPHPEYpQGHYFPPTLLvDVTPDMKIAQEEVFGPVMVVMKAS-DDEEAVEIANST 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199635239 422 PHGLSSSIYTTDFREAEQFlsCSGSDCGIANVN-LGTNGAEIGGAFGGEKETGGGR 476
Cdd:cd07098 392 EYGLGASVFGKDIKRARRI--ASQLETGMVAINdFGVNYYVQQLPFGGVKGSGFGR 445
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
22-477 |
1.50e-41 |
|
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: 155.30 E-value: 1.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 22 GKEWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVS 101
Cdd:cd07116 6 GGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 102 LEMGKILQEGLG-EVQEMIDVCDFAVGLSRQLYGLTfpSERPRHRLMEQWH-PLGPIAVITAYNFPASVWSWNAMLAAVC 179
Cdd:cd07116 86 WDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSI--SEIDENTVAYHFHePLGVVGQIIPWNFPLLMATWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 180 GDTVIWKPSSKTPLCAVAIQKIACEVLaengmPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARRF 259
Cdd:cd07116 164 GNCVVLKPAEQTPASILVLMELIGDLL-----PPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 260 GRTILELGGNNASI----VTEHAD--MKQAVPGIVFGAAgTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLE 333
Cdd:cd07116 239 IPVTLELGGKSPNIffadVMDADDafFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 334 EGVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTA--LP-ELGACYVSPAIFKMSADAPLVREEKFCPILYLIPYSgG 410
Cdd:cd07116 318 TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERneLGgLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTFK-D 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 411 LGEAIRIHNGVPHGLSSSIYTTDFREAEQFLScsgsdcGIANVNLGTNGAEI---GGAFGGEKETGGGRE 477
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGR------GIQAGRVWTNCYHLypaHAAFGGYKQSGIGRE 460
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
39-477 |
2.03e-39 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 149.66 E-value: 2.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 39 PADGSELGRVRCARREDYERAAAAAEAAFLK--WREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGL-GEV 115
Cdd:PRK09847 42 PVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLrDDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 116 QEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQwHPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCA 195
Cdd:PRK09847 122 PGAARAIRWYAEAIDKVYGEVATTSSHELAMIVR-EPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 196 VAIQKIAcevlAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGV-AVARRFGRTILELGGNNASIV 274
Cdd:PRK09847 201 IRLAGLA----KEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 275 -TEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVAD---ANVVKDF 350
Cdd:PRK09847 277 fADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDcahADSVHSF 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 351 laaVEEAKAQGGELLCG-GTALPelgaCYVSPAIF-KMSADAPLVREEKFCPILYLIPYSGGlGEAIRIHNGVPHGLSSS 428
Cdd:PRK09847 357 ---IREGESKGQLLLDGrNAGLA----AAIGPTIFvDVDPNASLSREEIFGPVLVVTRFTSE-EQALQLANDSQYGLGAA 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1199635239 429 IYTTDFREAEQFlsCSGSDCGIANVNlGTNGAEIGGAFGGEKETGGGRE 477
Cdd:PRK09847 429 VWTRDLSRAHRM--SRRLKAGSVFVN-NYNDGDMTVPFGGYKQSGNGRD 474
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
3-440 |
6.54e-39 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 149.90 E-value: 6.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 3 KNSWLESLGVAGTCPGVS------TGKEWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAP 76
Cdd:PLN02419 94 RSSWLSTSPEQSTQPQMPprvpnlIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPIT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 77 VRGEIVRQIGVRLREKKEALGRLVSLEMGKILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHRLMEQWHPLGPI 156
Cdd:PLN02419 174 TRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVC 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 157 AVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCAVAIQKIACEVlaenGMPEGVFNLVIGSGrDVGEVMLEDARV 236
Cdd:PLN02419 254 AGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEA----GLPDGVLNIVHGTN-DTVNAICDDEDI 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 237 RLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVI-VHESRYEEl 315
Cdd:PLN02419 329 RAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVfVGDAKSWE- 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 316 aQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAAVEEAKAQGGELLCGGTALPELG---ACYVSPAIFK-MSADAP 391
Cdd:PLN02419 408 -DKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGyekGNFIGPTILSgVTPDME 486
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1199635239 392 LVREEKFCPILYLIPySGGLGEAIRIHNGVPHGLSSSIYTTDFREAEQF 440
Cdd:PLN02419 487 CYKEEIFGPVLVCMQ-ANSFDEAISIINKNKYGNGAAIFTSSGAAARKF 534
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
117-473 |
1.29e-37 |
|
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: 145.04 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 117 EMIDVCDFAVGLSRQLYGLTFPSERP--RHRLmeQWHPL-GPIAVITAYNFPASvwswNAMLA---AVCGDTVIWKPSSK 190
Cdd:cd07123 134 ELIDFLRFNVKYAEELYAQQPLSSPAgvWNRL--EYRPLeGFVYAVSPFNFTAI----GGNLAgapALMGNVVLWKPSDT 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 191 TPLCAVAIQKIacevLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRH------VGVAVARRFGRTIL 264
Cdd:cd07123 208 AVLSNYLVYKI----LEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSlwkqigENLDRYRTYPRIVG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 265 ELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADA 344
Cdd:cd07123 284 ETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 345 NVVKDFLAAVEEAKAQGG-ELLCGGTALPELGAcYVSPAIFKMSA-DAPLVREEKFCPIL--YLIPYSgGLGEAIR-IHN 419
Cdd:cd07123 364 KAFDRIKGYIDHAKSDPEaEIIAGGKCDDSVGY-FVEPTVIETTDpKHKLMTEEIFGPVLtvYVYPDS-DFEETLElVDT 441
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199635239 420 GVPHGLSSSIYTTD---FREAEQFLSCSgsdCGIANVNLGTNGAEIGG-AFGGEKETG 473
Cdd:cd07123 442 TSPYALTGAIFAQDrkaIREATDALRNA---AGNFYINDKPTGAVVGQqPFGGARASG 496
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
20-479 |
3.04e-36 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 143.58 E-value: 3.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 20 STGKEWFA--------SDGAKELVSySPADGSEL-GRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLR 90
Cdd:PRK11809 640 SAHQKWQAapmledpvAAGEMSPVI-NPADPRDIvGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLME 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 91 EKKEALGRLVSLEMGKILQEGLGEVQEMIDVCDFAVGLSRQlyglTFPSERprHRlmeqwhPLGPIAVITAYNFPASVWS 170
Cdd:PRK11809 719 AQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRD----DFDNDT--HR------PLGPVVCISPWNFPLAIFT 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 171 WN--AMLAAvcGDTVIWKPSSKTPLcaVAIQKIAceVLAENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETG 248
Cdd:PRK11809 787 GQvaAALAA--GNSVLAKPAEQTPL--IAAQAVR--ILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVA 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 249 RHVGVAVARRF---GRT---ILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSA 322
Cdd:PRK11809 861 RLLQRNLAGRLdpqGRPiplIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGA 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 323 YGRLKIGNPLEEGVHVGPVADANVVKDFLAAVEEAKAQGGELLcgGTALPELGAC----YVSPAIFKMSADAPLVReEKF 398
Cdd:PRK11809 941 MAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVF--QAARENSEDWqsgtFVPPTLIELDSFDELKR-EVF 1017
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 399 CPILYLIPY-SGGLGEAIRIHNGVPHGLSSSIYTtdfREAEQFLSCSGSdcgiANV-NLGTN----GAEIG-GAFGGEKE 471
Cdd:PRK11809 1018 GPVLHVVRYnRNQLDELIEQINASGYGLTLGVHT---RIDETIAQVTGS----AHVgNLYVNrnmvGAVVGvQPFGGEGL 1090
|
....*...
gi 1199635239 472 TGGGRECG 479
Cdd:PRK11809 1091 SGTGPKAG 1098
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
151-448 |
2.77e-34 |
|
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: 133.81 E-value: 2.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 151 HPLGPIAVITAYNFPASVwSWNAMLAAV-CGDTVIWKPSSKTPLCAVAIQKiacevLAENGMPEGVFnLVIGSGRDVGEV 229
Cdd:cd07087 99 EPLGVVLIIGPWNYPLQL-ALAPLIGAIaAGNTVVLKPSELAPATSALLAK-----LIPKYFDPEAV-AVVEGGVEVATA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 230 MLEdARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHE 309
Cdd:cd07087 172 LLA-EPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 310 SRYEELAQKLTSA----YGRlkigNPLEEgvhvgpvadanvvKDFLAAVEEAKAQ-------GGELLCGGTALPElgACY 378
Cdd:cd07087 251 SIKDELIEELKKAikefYGE----DPKES-------------PDYGRIINERHFDrlaslldDGKVVIGGQVDKE--ERY 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199635239 379 VSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFLS--CSGSDC 448
Cdd:cd07087 312 IAPTILdDVSPDSPLMQEEIFGPILPILTYD-DLDEAIEFINSRPKPLALYLFSEDKAVQERVLAetSSGGVC 383
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
152-499 |
9.97e-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: 129.65 E-value: 9.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 152 PLGPIAVITAYNFPASVwSWNAMLAAVC-GDTVIWKPSSKTPLCAVAIQKIAcevlaENGMPEGVFNLVIGSGRDVGEVM 230
Cdd:cd07135 108 PLGVVLIIGPWNYPVLL-ALSPLVGAIAaGCTVVLKPSELTPHTAALLAELV-----PKYLDPDAFQVVQGGVPETTALL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 231 leDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHES 310
Cdd:cd07135 182 --EQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 311 RYEELAQKLTSAYGRLKIG--NPLEEGVHVgpVADANvvkdFLAAVEEAKAQGGELLCGGTAlpELGACYVSPAI-FKMS 387
Cdd:cd07135 260 VYDEFVEELKKVLDEFYPGgaNASPDYTRI--VNPRH----FNRLKSLLDTTKGKVVIGGEM--DEATRFIPPTIvSDVS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 388 ADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFL------SCSGSDCGIAnvnLGTNGAe 461
Cdd:cd07135 332 WDDSLMSEELFGPVLPIIKVD-DLDEAIKVINSRDTPLALYIFTDDKSEIDHILtrtrsgGVVINDTLIH---VGVDNA- 406
|
330 340 350
....*....|....*....|....*....|....*...
gi 1199635239 462 iggAFGGEKETGGGRECGSDAWKgymrrqsgaiNFSHE 499
Cdd:cd07135 407 ---PFGGVGDSGYGAYHGKYGFD----------TFTHE 431
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
70-489 |
1.12e-29 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 121.19 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 70 WREVPAPVRGEIVRQIGVRLREKKEALGRLVSLEMGK----ILQEGLGEVQEMIDVCDFAVGLSRQLYGLTFPSERPRHR 145
Cdd:cd07084 15 ARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKgwmfAENICGDQVQLRARAFVIYSYRIPHEPGNHLGQGLKQQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 146 LMEQWhPLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCAVAIQKIACEVLAengMPEGVFNLVIGSGRd 225
Cdd:cd07084 95 HGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGL---LPPEDVTLINGDGK- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 226 VGEVMLEDARVRLVSFTGSTETGRhvGVAVARRFGRTILELGGNNASIVTEHADMKQAVP-GIVFGAAGTAGQRCTTTRR 304
Cdd:cd07084 170 TMQALLLHPNPKMVLFTGSSRVAE--KLALDAKQARIYLELAGFNWKVLGPDAQAVDYVAwQCVQDMTACSGQKCTAQSM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 305 VIVHES-RYEELAQKLTSAYGRLKIGNPLeegvhVGPVADANVvkdfLAAVEEAKAQGG-ELLCGGTALPEL------GA 376
Cdd:cd07084 248 LFVPENwSKTPLVEKLKALLARRKLEDLL-----LGPVQTFTT----LAMIAHMENLLGsVLLFSGKELKNHsipsiyGA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 377 CyVSPAIFKMSADA----PLVREEKFCPILYLIPYSGG----LGEAIRIHNGvphGLSSSIYTTDFREAEQFLSCSGSDC 448
Cdd:cd07084 319 C-VASALFVPIDEIlktyELVTEEIFGPFAIVVEYKKDqlalVLELLERMHG---SLTAAIYSNDPIFLQELIGNLWVAG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1199635239 449 GIANVNLGTNGAEIGG--AFGGEKETGGGRECGSDAWKGYMRR 489
Cdd:cd07084 395 RTYAILRGRTGVAPNQnhGGGPAADPRGAGIGGPEAIKLVWRC 437
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
24-437 |
7.36e-29 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 119.48 E-value: 7.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 24 EWFASDGAKELVSYSPADGSELGRVRCARREDYERAAAAAEAAFLKWREVPAPVRGEIVRQIGVRLREKKEALGRLVSLE 103
Cdd:PLN00412 23 EWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 104 MGKILQEGLGEVQEMIDVCDFA-------VGLSRQLYGLTFP-SERPRHRLMEQWhPLGPIAVITAYNFPASVWSWNAML 175
Cdd:PLN00412 103 IAKPAKDAVTEVVRSGDLISYTaeegvriLGEGKFLVSDSFPgNERNKYCLTSKI-PLGVVLAIPPFNYPVNLAVSKIAP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 176 AAVCGDTVIWKPssKTPLCAVAIQKIACEVLAenGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGStETGrhvgVAV 255
Cdd:PLN00412 182 ALIAGNAVVLKP--PTQGAVAALHMVHCFHLA--GFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTG----IAI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 256 ARRFGRTIL--ELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPlE 333
Cdd:PLN00412 253 SKKAGMVPLqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-E 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 334 EGVHVGPV---ADANVVKDFlaaVEEAKAQGGELLC-----GGTALPELgacyvspaIFKMSADAPLVREEKFCPILYLI 405
Cdd:PLN00412 332 DDCDITPVvseSSANFIEGL---VMDAKEKGATFCQewkreGNLIWPLL--------LDNVRPDMRIAWEEPFGPVLPVI 400
|
410 420 430
....*....|....*....|....*....|..
gi 1199635239 406 PYSgGLGEAIRIHNGVPHGLSSSIYTTDFREA 437
Cdd:PLN00412 401 RIN-SVEEGIHHCNASNFGLQGCVFTRDINKA 431
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
128-489 |
3.56e-27 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 114.67 E-value: 3.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 128 LSRqlyGLTFpseRPRHRLMeqwhPLGPIAV-ITAYNFPasVWswnAML-----AAVCGDTVIWKPSSKTPLCAVAIQKI 201
Cdd:cd07128 129 LSK---DGTF---VGQHILT----PRRGVAVhINAFNFP--VW---GMLekfapALLAGVPVIVKPATATAYLTEAVVKD 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 202 aceVLAENGMPEGVFNLVIGSGRDvgevMLEDARVR-LVSFTGSTETGRHVGV--AVARRFGRTILELGGNNASIVTEHA 278
Cdd:cd07128 194 ---IVESGLLPEGALQLICGSVGD----LLDHLGEQdVVAFTGSAATAAKLRAhpNIVARSIRFNAEADSLNAAILGPDA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 279 DMKQA-----VPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHVGPVADANVVKDFLAA 353
Cdd:cd07128 267 TPGTPefdlfVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAA 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 354 VEEAKAqGGELLCGGTALPEL------GACYVSPAIFKMS--ADAPLVRE-EKFCPILYLIPYSgGLGEAIRIHNGVPHG 424
Cdd:cd07128 347 VATLLA-EAEVVFGGPDRFEVvgadaeKGAFFPPTLLLCDdpDAATAVHDvEAFGPVATLMPYD-SLAEAIELAARGRGS 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199635239 425 LSSSIYTTDFREAEQFLSCSGSDCGIANVNLGTNGAEIGG--------AFGGEKETGGGRECGS-DAWKGYMRR 489
Cdd:cd07128 425 LVASVVTNDPAFARELVLGAAPYHGRLLVLNRDSAKESTGhgsplpqlVHGGPGRAGGGEELGGlRGVKHYMQR 498
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
175-467 |
4.04e-26 |
|
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: 110.39 E-value: 4.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 175 LAAvcGDTVIWKPSSKTPLCAVAIQKIACEVLAEN--GMPEGvfnlvigsGRDVGEVMLeDARVRLVSFTGSTETGRHVG 252
Cdd:cd07134 125 IAA--GNTAILKPSELTPHTSAVIAKIIREAFDEDevAVFEG--------DAEVAQALL-ELPFDHIFFTGSPAVGKIVM 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 253 VAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSA----YGRlki 328
Cdd:cd07134 194 AAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEiekfYGK--- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 329 gnplEEGVHVGP-----VADANV--VKDFLaavEEAKAQGGELLCGGTALPElgACYVSPAIFK-MSADAPLVREEKFCP 400
Cdd:cd07134 271 ----DAARKASPdlariVNDRHFdrLKGLL---DDAVAKGAKVEFGGQFDAA--QRYIAPTVLTnVTPDMKIMQEEIFGP 341
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199635239 401 ILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFL--SCSGSDC------GIANVNL---GTNGAEIGGAFG 467
Cdd:cd07134 342 VLPIITYE-DLDEVIEYINAKPKPLALYVFSKDKANVNKVLarTSSGGVVvndvvlHFLNPNLpfgGVNNSGIGSYHG 418
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
152-468 |
4.30e-26 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 111.27 E-value: 4.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 152 PLGPIAVITAYNFPASVwSWNAMLAAV-CGDTVIWKPSSKTPLCAVAIQKiacevLAENGMPEGVFNLVIGsGRDVGEVM 230
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNL-TLIPLAGAIaAGNTVVLKPSELSPHTSKLMAK-----LLTKYLDPSYVRVIEG-GVEVTTEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 231 LEdARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHES 310
Cdd:PTZ00381 182 LK-EPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 311 ----RYEELAQKLTSAYGRlkigNPLEEGvhvgpvadanvvkDFLAAVEEAKAQ---------GGELLCGGTAlpELGAC 377
Cdd:PTZ00381 261 ikdkFIEALKEAIKEFFGE----DPKKSE-------------DYSRIVNEFHTKrlaelikdhGGKVVYGGEV--DIENK 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 378 YVSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFLS--CSGS----DC-- 448
Cdd:PTZ00381 322 YVAPTIIvNPDLDSPLMQEEIFGPILPILTYE-NIDEVLEFINSRPKPLALYYFGEDKRHKELVLEntSSGAvvinDCvf 400
|
330 340
....*....|....*....|..
gi 1199635239 449 GIANVNL--GTNGAEIGGAFGG 468
Cdd:PTZ00381 401 HLLNPNLpfGGVGNSGMGAYHG 422
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
152-510 |
1.51e-25 |
|
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: 109.13 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 152 PLGPIAVITAYNFPAsvwswnaML-------AAVCGDTVIWKPSSKTPLCAVAIQKIACEVLAENgmpegvFNLVIGSGR 224
Cdd:cd07136 100 PYGVVLIIAPWNYPF-------QLalapligAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEE------YVAVVEGGV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 225 DVGEVMLeDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRR 304
Cdd:cd07136 167 EENQELL-DQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 305 VIVHESRYEELAQKL----TSAYGRlkigNPLEEGVHVGPVADANV--VKDFLaaveeakaQGGELLCGGTALPElgACY 378
Cdd:cd07136 246 VLVHESVKEKFIKELkeeiKKFYGE----DPLESPDYGRIINEKHFdrLAGLL--------DNGKIVFGGNTDRE--TLY 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 379 VSPAIFK-MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFL-SCS-GSDC------G 449
Cdd:cd07136 312 IEPTILDnVTWDDPVMQEEIFGPILPVLTYD-TLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLeNLSfGGGCindtimH 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199635239 450 IANVNLGtngaeiggaFGGEKETGGGrecgsdAWKGYmrrqSGAINFSHEMP-LAQGIKFEF 510
Cdd:cd07136 391 LANPYLP---------FGGVGNSGMG------SYHGK----YSFDTFSHKKSiLKKSTWFDL 433
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
138-433 |
2.70e-25 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 108.40 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 138 PSERPRHRLMEQwhPLGPIAVITAYNFP----------ASVwswnamLAAVCgdTVIWKPSSKTPLCAVAIQKIACEVLA 207
Cdd:cd07129 93 PLPRPDLRRMLV--PLGPVAVFGASNFPlafsvaggdtASA------LAAGC--PVVVKAHPAHPGTSELVARAIRAALR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 208 ENGMPEGVFNLVIGSGRDVGEVMLEDARVRLVSFTGSTETGRHVGVAVARR------FGrtilELGGNNASIVTEHAdMK 281
Cdd:cd07129 163 ATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARpepipfYA----ELGSVNPVFILPGA-LA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 282 QAVPGIVFGAAGT----AGQRCTTTRRVIVHES-RYEELAQKLTSAYGRLKIGNPLEEGVHvgpvadanvvKDFLAAVEE 356
Cdd:cd07129 238 ERGEAIAQGFVGSltlgAGQFCTNPGLVLVPAGpAGDAFIAALAEALAAAPAQTMLTPGIA----------EAYRQGVEA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 357 AKAQGGELLCGGTALPElGACYVSPAIFKMSADA----PLVREEKFCPILYLIPYsGGLGEAIRIHNGVPHGLSSSIYTT 432
Cdd:cd07129 308 LAAAPGVRVLAGGAAAE-GGNQAAPTLFKVDAAAfladPALQEEVFGPASLVVRY-DDAAELLAVAEALEGQLTATIHGE 385
|
.
gi 1199635239 433 D 433
Cdd:cd07129 386 E 386
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
112-433 |
3.29e-25 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 108.64 E-value: 3.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 112 LGEVQEMIDvcDFAVGLSRQlygltfPSERPRHRLMeqwhPLGPIAV-ITAYNFPAsvWS-W-NAMLAAVCGDTVIWKPS 188
Cdd:PRK11903 119 LGDARLLRD--GEAVQLGKD------PAFQGQHVLV----PTRGVALfINAFNFPA--WGlWeKAAPALLAGVPVIVKPA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 189 SKTPLCAvaiQKIACEVLAENGMPEGVFNLVIGSGRDV-GEVMLEDarvrLVSFTGSTETGRHVGV--AVARRFGRTILE 265
Cdd:PRK11903 185 TATAWLT---QRMVKDVVAAGILPAGALSVVCGSSAGLlDHLQPFD----VVSFTGSAETAAVLRShpAVVQRSVRVNVE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 266 LGGNNASIV-------TEHADMkqAVPGIVFGAAGTAGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGVHV 338
Cdd:PRK11903 258 ADSLNSALLgpdaapgSEAFDL--FVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRM 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 339 GPVADANVVKDFLAAVEEAKAQgGELLCGGTALPELGA-----CYVSPAIFKMS-AD-APLVRE-EKFCPILYLIPYSgG 410
Cdd:PRK11903 336 GPLVSRAQLAAVRAGLAALRAQ-AEVLFDGGGFALVDAdpavaACVGPTLLGASdPDaATAVHDvEVFGPVATLLPYR-D 413
|
330 340
....*....|....*....|...
gi 1199635239 411 LGEAIRIHNGVPHGLSSSIYTTD 433
Cdd:PRK11903 414 AAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
149-442 |
5.44e-25 |
|
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: 107.19 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 149 QWHPLGPIAVITAYNFPA--SVWSWNAMLAAvcGDTVIWKPSSKTPLCAVAIQkiacEVLAENGMPEGVfnLVIGSGRDV 226
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLylALGPLIAALAA--GNRVMIKPSEFTPRTSALLA----ELLAEYFDEDEV--AVVTGGADV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 227 GEvmledARVRL----VSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTT 302
Cdd:cd07133 170 AA-----AFSSLpfdhLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 303 RRVIVHESRYEELAQKLTSAYGRL---KIGNPleegvHVGPVADANVVKDFLAAVEEAKAQGGELL-CGGTALPELGACY 378
Cdd:cd07133 245 DYVLVPEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIeLNPAGEDFAATRK 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199635239 379 VSP-AIFKMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFLS 442
Cdd:cd07133 320 LPPtLVLNVTDDMRVMQEEIFGPILPILTYD-SLDEAIDYINARPRPLALYYFGEDKAEQDRVLR 383
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
145-458 |
1.93e-17 |
|
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: 85.22 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 145 RLMEQWH--PLGPIAVITAYNFPAsvW-SWNAMLAA-VCGDTVIWKPSSKTPLCAVAIQKIACEVLAENGMPEGVFNLVI 220
Cdd:cd07127 184 AMEKTFTvvPRGVALVIGCSTFPT--WnGYPGLFASlATGNPVIVKPHPAAILPLAITVQVAREVLAEAGFDPNLVTLAA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 221 GS-GRDVGEVMLEDARVRLVSFTGSTETGRHVgVAVARRfGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRC 299
Cdd:cd07127 262 DTpEEPIAQTLATRPEVRIIDFTGSNAFGDWL-EANARQ-AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMC 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 300 TTTRRVIV----------HESrYEELAQKLTSAYGRLkIGNPLEEGVHVGPVADANVvkdfLAAVEEAkAQGGELLCGGT 369
Cdd:cd07127 340 TTPQNIYVprdgiqtddgRKS-FDEVAADLAAAIDGL-LADPARAAALLGAIQSPDT----LARIAEA-RQLGEVLLASE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 370 AL--PEL-GACYVSPAIFKM-SADAPLVREEKFCPILYLIPYSGGlGEAIRIHNGV--PHG-LSSSIYTTDfreaEQFLS 442
Cdd:cd07127 413 AVahPEFpDARVRTPLLLKLdASDEAAYAEERFGPIAFVVATDST-DHSIELARESvrEHGaMTVGVYSTD----PEVVE 487
|
330
....*....|....*.
gi 1199635239 443 CSGSDCGIANVNLGTN 458
Cdd:cd07127 488 RVQEAALDAGVALSIN 503
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
135-476 |
5.95e-16 |
|
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: 79.76 E-value: 5.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 135 LTFPSerpRHRLMEQwhPLGPIAVITAYNFPASVwSWNAMLAAV-CGDTVIWKPSSKTPLCAVAIQKIACEVLAENGMPe 213
Cdd:cd07137 89 TTFPA---KAEIVSE--PLGVVLVISAWNFPFLL-SLEPVIGAIaAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIK- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 214 gvfnlVIGSGRDVGEVMLEDaRVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAG 293
Cdd:cd07137 162 -----VIEGGVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 294 T-AGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGvHVGPVADANVVKDFLAAVEEAKAQgGELLCGGTALP 372
Cdd:cd07137 236 CnNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGGERDE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 373 ElgACYVSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFLS--CSGS--- 446
Cdd:cd07137 314 K--NLYIEPTILlDPPLDSSIMTEEIFGPLLPIITVK-KIEESIEIINSRPKPLAAYVFTKNKELKRRIVAetSSGGvtf 390
|
330 340 350
....*....|....*....|....*....|.
gi 1199635239 447 -DCGIANVNLGTngaeiggAFGGEKETGGGR 476
Cdd:cd07137 391 nDTVVQYAIDTL-------PFGGVGESGFGA 414
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
135-476 |
8.76e-15 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 76.69 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 135 LTFPSerpRHRLMEQwhPLGPIAVITAYNFPASVwSWNAMLAAV-CGDTVIWKPSSKTPLCAVAIQKIACEVLAENGMPe 213
Cdd:PLN02203 96 VAFPA---TAEVVPE--PLGVVLIFSSWNFPIGL-SLEPLIGAIaAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVK- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 214 gvfnlVIGSGRDVGEVMLEDaRVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHA---DMKQAVPGIVFG 290
Cdd:PLN02203 169 -----VIEGGPAVGEQLLQH-KWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSLSssrDTKVAVNRIVGG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 291 AAGT-AGQRCTTTRRVIVHESRYEELAQKLTSAYGRLKIGNPLEEGvHVGPVADANVVKDFLAAVEEAKAQgGELLCGGT 369
Cdd:PLN02203 243 KWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVA-ASIVHGGS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 370 ALPElgACYVSPAIF-KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFLS--CSGS 446
Cdd:PLN02203 321 IDEK--KLFIEPTILlNPPLDSDIMTEEIFGPLLPIITVK-KIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSetSSGS 397
|
330 340 350
....*....|....*....|....*....|....*
gi 1199635239 447 dcgianvnLGTNGAEIGGA-----FGGEKETGGGR 476
Cdd:PLN02203 398 --------VTFNDAIIQYAcdslpFGGVGESGFGR 424
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
149-449 |
2.86e-14 |
|
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: 74.95 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 149 QWHPLGPIAVITAYNFPASVwSWNAMLAAVC-GDTVIWKPSSKTPLCAVAIQKIACEVLAENgmpegVFNLVIGSGRDVG 227
Cdd:cd07132 97 YKEPLGVVLIIGAWNYPLQL-TLVPLVGAIAaGNCVVIKPSEVSPATAKLLAELIPKYLDKE-----CYPVVLGGVEETT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 228 EvmLEDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIV 307
Cdd:cd07132 171 E--LLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLC 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 308 HESRYEELAQKLTSAygrLK--IGNPLEEGVHVGPVADA---NVVKDFLaaveeakaQGGELLCGGTALPelGACYVSPA 382
Cdd:cd07132 249 TPEVQEKFVEALKKT---LKefYGEDPKESPDYGRIINDrhfQRLKKLL--------SGGKVAIGGQTDE--KERYIAPT 315
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 383 IFK-MSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFLS--CSGSDCG 449
Cdd:cd07132 316 VLTdVKPSDPVMQEEIFGPILPIVTVN-NLDEAIEFINSREKPLALYVFSNNKKVINKILSntSSGGVCV 384
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
152-491 |
4.81e-14 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 74.31 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 152 PLGPIAVITAYNFPAsVWSWNAMLAAV-CGDTVIWKPSSKTPLCAVAIQKiacevLAENGMPEGVFNLVIGSGRDVGEVM 230
Cdd:PLN02174 112 PLGVVLVISAWNYPF-LLSIDPVIGAIsAGNAVVLKPSELAPASSALLAK-----LLEQYLDSSAVRVVEGAVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 231 leDARVRLVSFTGSTETGRHVGVAVARRFGRTILELGGNNASIVTEHADMKQAVPGIVFGAAG-TAGQRCTTTRRVIVHE 309
Cdd:PLN02174 186 --EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 310 SR----YEELAQKLTSAYGRlkigNPLEEGvHVGPVADANVVkDFLAAVEEAKAQGGELLCGGTALPElgACYVSPAI-F 384
Cdd:PLN02174 264 EYapkvIDAMKKELETFYGK----NPMESK-DMSRIVNSTHF-DRLSKLLDEKEVSDKIVYGGEKDRE--NLKIAPTIlL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 385 KMSADAPLVREEKFCPILYLIPYSgGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFlSCSGSDCGIANVNLGTNGAEIGG 464
Cdd:PLN02174 336 DVPLDSLIMSEEIFGPLLPILTLN-NLEESFDVIRSRPKPLAAYLFTHNKKLKERF-AATVSAGGIVVNDIAVHLALHTL 413
|
330 340
....*....|....*....|....*..
gi 1199635239 465 AFGGEKETGGGRECGSDAWKGYMRRQS 491
Cdd:PLN02174 414 PFGGVGESGMGAYHGKFSFDAFSHKKA 440
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
152-467 |
1.85e-09 |
|
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: 59.82 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 152 PLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLcaVAIQKIacEVLAENGMPEGVFNLVIGSGRDVGEVML 231
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSV--VMEQFL--RLLHLCGMPATDVDLIHSDGPTMNKILL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 232 EdARVRLVSFTGSTETGRHVGVAVArrfGRTILELGG----------NNASIVTEHADMKqavpgivfgAAGTAGQRCTT 301
Cdd:cd07126 218 E-ANPRMTLFTGSSKVAERLALELH---GKVKLEDAGfdwkilgpdvSDVDYVAWQCDQD---------AYACSGQKCSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 302 TRRVIVHESRYEE-LAQKLTSAYGRLKIgnpleEGVHVGPVADANVVK-----DFLAAVEEAKAQ-GGELLCGGTaLPEL 374
Cdd:cd07126 285 QSILFAHENWVQAgILDKLKALAEQRKL-----EDLTIGPVLTWTTERildhvDKLLAIPGAKVLfGGKPLTNHS-IPSI 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 375 GACYVSPAIF------KMSADAPLVREEKFCPILYLIPY-SGGLGEAIRIHNGVPHGLSSSIYTTDFREAEQFLSCSGSD 447
Cdd:cd07126 359 YGAYEPTAVFvpleeiAIEENFELVTTEVFGPFQVVTEYkDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNG 438
|
330 340
....*....|....*....|
gi 1199635239 448 CGIANVNLGTNGAEIGGAFG 467
Cdd:cd07126 439 TTYAGIRARTTGAPQNHWFG 458
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
152-334 |
1.86e-07 |
|
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: 53.42 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 152 PLGPIAVITAYNFPASVWSWNAMLAAVCGDTVIWKPSSKTPLCAVAIQKIACEVLAENGMPEGVFNLVIGSGRDVGEVML 231
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 232 EDARVRLVSFTGSTETgrhvgVAVARRFGRTILELG-GNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVIVHES 310
Cdd:cd07081 175 KFPGIGLLLATGGPAV-----VKAAYSSGKPAIGVGaGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDS 249
|
170 180
....*....|....*....|....
gi 1199635239 311 RYEELAQKLTSAYGRLKIGNPLEE 334
Cdd:cd07081 250 VYDEVMRLFEGQGAYKLTAEELQQ 273
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
152-322 |
5.95e-04 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 42.22 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 152 PLGPIAVITAYNFPASVWSWNA--MLAAvcGDTVIWK--PSSKTpLCAVAIQKIAcEVLAENGMPEGVFNLVIGSGRDVG 227
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSisMLAA--GNAVVFNphPGAKK-VSAYAVELIN-KAIAEAGGPDNLVVTVEEPTIETT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199635239 228 EVMLEDARVRLVSFTGstetGRHVgVAVARRFGRTILELG-GNNASIVTEHADMKQAVPGIVFGAAGTAGQRCTTTRRVI 306
Cdd:cd07121 173 NELMAHPDINLLVVTG----GPAV-VKAALSSGKKAIGAGaGNPPVVVDETADIEKAARDIVQGASFDNNLPCIAEKEVI 247
|
170
....*....|....*.
gi 1199635239 307 VHESRYEELAQKLTSA 322
Cdd:cd07121 248 AVDSVADYLIAAMQRN 263
|
|
| |
