|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
53-463 |
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: 828.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 53 GVYNGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:cd07130 1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 133 SLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICG 212
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 213 NVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGR 292
Cdd:cd07130 161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 293 SLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL------------------------------------ 336
Cdd:cd07130 241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLivhesiydevlerlkkaykqvrigdplddgtlvgpl 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 337 ----------------------------VMDRPGNYVEPTIVTGLgHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 388
Cdd:cd07130 321 htkaavdnylaaieeaksqggtvlfggkVIDGPGNYVEPTIVEGL-SDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVP 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 982742419 389 QGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYS 463
Cdd:cd07130 400 QGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
53-463 |
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: 769.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 53 GVYNGSWGGRG-EVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07086 1 GVIGGEWVGSGgETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 132 VSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMIC 211
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 212 GNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFG 291
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL----------------------------------- 336
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLivhesvydeflerlvkaykqvrigdpldegtlvgp 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 337 -----------------------------VMDR--PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNN 385
Cdd:cd07086 321 linqaavekylnaieiaksqggtvltggkRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 982742419 386 EVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYS 463
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
36-474 |
0e+00 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 623.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 36 QPQYAWLKELGLREENEGVY-NGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIV 114
Cdd:PLN02315 5 RKEYEFLSEIGLSSRNLGCYvGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 115 RQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAF 194
Cdd:PLN02315 85 RQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 195 NFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTG 274
Cdd:PLN02315 165 NFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 275 STQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL------------------ 336
Cdd:PLN02315 245 SSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLllhesiyddvleqlltvy 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 337 ----------------------------------------------VMDRPGNYVEPTIVTgLGHDASIAHTETFAPILY 370
Cdd:PLN02315 325 kqvkigdplekgtllgplhtpeskknfekgieiiksqggkiltggsAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 371 VFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWK 450
Cdd:PLN02315 404 VMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWK 483
|
490 500
....*....|....*....|....
gi 982742419 451 QYMRRSTCTINYSKDLPLAQGIKF 474
Cdd:PLN02315 484 QYMRRSTCTINYGNELPLAQGINF 507
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
89-460 |
2.98e-129 |
|
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: 381.56 E-value: 2.98e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 89 EETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPI 168
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 169 LPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLednkLPGAIC 248
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAG----LPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 249 SLTCGGAD-IGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAG 327
Cdd:cd07078 157 NVVTGDGDeVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 328 QRCTTARRL---------VMDR--------------------------------------------------------PG 342
Cdd:cd07078 237 QVCTAASRLlvhesiydeFVERlvervkalkvgnpldpdtdmgplisaaqldrvlayiedakaegakllcggkrleggKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 343 NYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIP 422
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVA--ERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 982742419 423 TSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 460
Cdd:cd07078 395 SVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
61-457 |
5.82e-129 |
|
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: 381.88 E-value: 5.82e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 61 GRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 141 VEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIeQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGA 220
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYT-RREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 221 PTTSLISVAvtkiIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGG 299
Cdd:pfam00171 163 ELTPLTALL----LAELFEEAGLPaGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 300 NNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLV------------------------------------------ 337
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLvhesiydefveklveaakklkvgdpldpdtdmgpliskaqle 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 338 ----------------------MDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSI 395
Cdd:pfam00171 319 rvlkyvedakeegaklltggeaGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982742419 396 FTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRST 457
Cdd:pfam00171 399 FTSDLERALRVA--RRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
56-462 |
2.08e-126 |
|
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: 376.00 E-value: 2.08e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:COG1012 11 GGEWvaAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 134 LEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGN 213
Cdd:COG1012 91 LETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 214 VCLWKGAPTTSLISVAvtkiIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGR 292
Cdd:COG1012 171 TVVLKPAEQTPLSALL----LAELLEEAGLPaGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 293 SLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLV----------------------------------- 337
Cdd:COG1012 247 VTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLvhesiydefverlvaaakalkvgdpldpgtdmgpl 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 338 -----MDR-------------------------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEV 387
Cdd:COG1012 327 iseaqLERvlayiedavaegaelltggrrpdgeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDT 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 982742419 388 KQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 462
Cdd:COG1012 407 EYGLAASVFTRDLARARRVA--RRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
93-460 |
9.95e-125 |
|
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: 367.71 E-value: 9.95e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 93 KKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSE 172
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 173 RSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLednkLPGAICSLTC 252
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG----LPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 253 GGAD-IGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCT 331
Cdd:cd06534 157 GGGDeVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 332 TARRLvmdrpgnYVEP-----------TIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 400
Cdd:cd06534 237 AASRL-------LVHEsiydefveklvTVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDL 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 401 GRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 460
Cdd:cd06534 310 NRALRVA--ERLRAGTVYINDSSIGVGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
56-463 |
1.78e-102 |
|
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: 314.67 E-value: 1.78e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSWGGR--GEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:cd07131 4 GGEWVDSasGETFDSRNPADlEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 133 SLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICG 212
Cdd:cd07131 84 TREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 213 NVCLWKGAPTTSlisvAVTKIIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFG 291
Cdd:cd07131 164 NTVVFKPAEDTP----ACALKLVELFAEAGLPpGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVMDR------------------------------- 340
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHEsvydeflkrfverakrlrvgdgldeetdmgp 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 341 -------------------------------------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAW 383
Cdd:cd07131 320 lineaqlekvlnyneigkeegatlllggerltgggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 384 NNEVKQGLSSSIFTKDLGRIFRWLGpkgsDC--GIVNVNIPTSGAEIGGAFGGEKHTGGG-RESGSDAWKQYMRRSTCTI 460
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARR----DLeaGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
...
gi 982742419 461 NYS 463
Cdd:cd07131 476 DYS 478
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
52-448 |
5.48e-87 |
|
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: 274.51 E-value: 5.48e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 52 EGVYNGSWGGRGEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGS 130
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 131 LVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMI 210
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 211 CGNVCLWKGAPTTSLISVAvtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQER 289
Cdd:cd07097 162 YGNTVVFKPAELTPASAWA----LVEILEEAGLPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 290 FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLV-------------------------------- 337
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIvtegihdrfvealvertkalkvgdaldegvdi 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 338 ----------------------------------MDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAW 383
Cdd:cd07097 318 gpvvserqlekdlryieiarsegaklvyggerlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 982742419 384 NNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSDA 448
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFK--RRVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEAA 461
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
71-453 |
1.13e-77 |
|
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: 249.66 E-value: 1.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVqey 150
Cdd:cd07103 4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 151 vdicDYAVGL-------SRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPvavygwnnaIAMI---------CGNV 214
Cdd:cd07103 81 ----DYAASFlewfaeeARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFP---------AAMItrkiapalaAGCT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 215 CLWKGAPTTSLISVAvtkiIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQ--ERFG 291
Cdd:cd07103 148 VVLKPAEETPLSALA----LAELAEEAGLPaGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKL--LMAQaaDTVK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTA-------------------------------------- 333
Cdd:cd07103 222 RVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCAnriyvhesiydefveklvervkklkvgngldegtdmgp 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 334 ----------RRLVMD----------------RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEV 387
Cdd:cd07103 302 lineravekvEALVEDavakgakvltggkrlgLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDT 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 982742419 388 KQGLSSSIFTKDLGRIFRwLGpKGSDCGIVNVNIPT-SGAEIggAFGGEKHTGGGRESGSDAWKQYM 453
Cdd:cd07103 382 PYGLAAYVFTRDLARAWR-VA-EALEAGMVGINTGLiSDAEA--PFGGVKESGLGREGGKEGLEEYL 444
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
87-452 |
2.39e-71 |
|
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: 232.42 E-value: 2.39e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 87 DYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGG 166
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 167 PILPSERSGHALIEQWNPVGLVGIITAFNFPV-----AVygwnnAIAMICGNVCLWKGAPTTslisvAVTK--IIAKVLE 239
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLilamrSV-----APALALGNAVVLKPDSRT-----PVTGglLIAEIFE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 240 DNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGlmvqERFGRSL----LELGGNNAIIAFEDADLSLV 314
Cdd:cd07104 151 EAGLPkGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIG----ELAGRHLkkvaLELGGNNPLIVLDDADLDLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 315 VPSALFAAVGTAGQRCTTARRLVMDRP----------------------------------------------------- 341
Cdd:cd07104 227 VSAAAFGAFLHQGQICMAAGRILVHESvydefveklvakakalpvgdprdpdtvigplinerqvdrvhaivedavaagar 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 --------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRwLGpKGSD 413
Cdd:cd07104 307 lltggtyeGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMA-FA-ERLE 384
|
410 420 430
....*....|....*....|....*....|....*....
gi 982742419 414 CGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQY 452
Cdd:cd07104 385 TGMVHINDQTVNDEPHVPFGGVKASGGGRFGGPASLEEF 423
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
63-405 |
3.78e-70 |
|
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: 230.23 E-value: 3.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVE 142
Cdd:cd07088 12 GETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 143 GVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPT 222
Cdd:cd07088 92 ARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 223 TSLISVAVTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN 301
Cdd:cd07088 172 TPLNALEFAELVDEA----GLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 302 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVMD------------------------------------------ 339
Cdd:cd07088 248 PAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHediydefmeklvekmkavkvgdpfdaatdmgplvneaaldkv 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 340 -----------------------RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIF 396
Cdd:cd07088 328 eemveraveagatlltggkrpegEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIY 407
|
....*....
gi 982742419 397 TKDLGRIFR 405
Cdd:cd07088 408 TENLNTAMR 416
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
71-446 |
7.27e-69 |
|
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: 226.44 E-value: 7.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07150 6 PADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 151 VDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVav 230
Cdd:cd07150 86 PELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 231 tkIIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKqvglMVQERFGRSL----LELGGNNAIIA 305
Cdd:cd07150 164 --KIAEIMEEAGLPkGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGR----EIAEKAGRHLkkitLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 306 FEDADLSLVVPSALFAAVGTAGQRCTTARRLVMDRP-------------------------------------------- 341
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPvydefvkkfvarasklkvgdprdpdtvigplisprqverikrqv 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 -----------------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIF 404
Cdd:cd07150 318 edavakgaklltggkydGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAF 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 982742419 405 RWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGS 446
Cdd:cd07150 398 KL--AERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGE 437
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
71-454 |
2.63e-67 |
|
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: 222.81 E-value: 2.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWK--IWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQ 148
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 149 EYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISV 228
Cdd:cd07114 84 YLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 229 AVTKIiakVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFED 308
Cdd:cd07114 164 ELAKL---AEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 309 ADLSLVVPSALFAAVGTAGQRCTT---------------------ARRLVMDRP-------------------------- 341
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAgsrllvqrsiydefverlvarARAIRVGDPldpetqmgplaterqlekveryvara 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 ---------------------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 400
Cdd:cd07114 321 reegarvltggerpsgadlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 982742419 401 GRIFRWlgPKGSDCGIVNVNI-----PTSgaeiggAFGGEKHTGGGRESGSDAWKQYMR 454
Cdd:cd07114 401 ARAHRV--ARAIEAGTVWVNTyralsPSS------PFGGFKDSGIGRENGIEAIREYTQ 451
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
57-445 |
7.20e-63 |
|
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: 211.39 E-value: 7.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 57 GSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSL 134
Cdd:cd07151 1 GEWrdGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 135 EMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNV 214
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 215 CLWKGAPTTslisvAVTK--IIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFG 291
Cdd:cd07151 161 VVLKPASDT-----PITGglLLAKIFEEAGLPKGVLNVVVGaGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVMDRP------------------------------ 341
Cdd:cd07151 236 KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDvydefvekfvervkalpygdpsdpdtvvgp 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 -------------------------------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQG 390
Cdd:cd07151 316 linesqvdglldkieqaveegatllvggeaeGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 982742419 391 LSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESG 445
Cdd:cd07151 396 LSGAVFTSDLERGVQF--ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNG 448
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
71-452 |
4.25e-61 |
|
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: 206.14 E-value: 4.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG-EVQE 149
Cdd:cd07115 4 PATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 150 YVDICDYAVGLSRMIGGPILPSeRSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07115 84 AADTFRYYAGWADKIEGEVIPV-RGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 230 VTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFED 308
Cdd:cd07115 163 IAELMAEA----GFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 309 ADLSLVVPSALFAAVGTAGQRCTTARRLV----------------------------------------MDR-------- 340
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLvhesiydeflerftslarslrpgdpldpktqmgplvsqaqFDRvldyvdvg 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 341 ----------------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIF 404
Cdd:cd07115 319 reegarlltggkrpgaRGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 982742419 405 RWlgPKGSDCGIVNVNipTSGA-EIGGAFGGEKHTGGGRESGSDAWKQY 452
Cdd:cd07115 399 RV--AAALKAGTVWIN--TYNRfDPGSPFGGYKQSGFGREMGREALDEY 443
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
71-457 |
2.63e-60 |
|
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: 203.91 E-value: 2.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 151 VDICDYAVGLSrmiggpiLPSER----SGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLI 226
Cdd:cd07106 84 VAWLRYTASLD-------LPDEVieddDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 227 SVAVTKIIAKVLEdnklPGAICSLTcGGADIGTAMAKDERVNLLSFTGSTQVGKQVglMVQ--ERFGRSLLELGGNNAII 304
Cdd:cd07106 157 TLKLGELAQEVLP----PGVLNVVS-GGDELGPALTSHPDIRKISFTGSTATGKKV--MASaaKTLKRVTLELGGNDAAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 305 AFEDADLSLVVPSALFAAVGTAGQRCTTARRL------------------------------------------------ 336
Cdd:cd07106 230 VLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLyvhesiydefcealvalakaavvgdgldpgttlgpvqnkmqydkvkel 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 337 ----------------VMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 400
Cdd:cd07106 310 vedakakgakvlaggePLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 982742419 401 GRIFRwLGPKgSDCGIVNVNiptSGAEIGGA--FGGEKHTGGGRESGSDAWKQYMRRST 457
Cdd:cd07106 390 ERAEA-VARR-LEAGTVWIN---THGALDPDapFGGHKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
66-444 |
3.08e-60 |
|
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: 204.12 E-value: 3.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 66 ITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 146 EVQEYVDICDYAVGLSRMIGGPILPSE----RSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 222 TTSLISVAVTKIIAKVlednKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGN 300
Cdd:cd07145 161 NTPLTAIELAKILEEA----GLPpGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 301 NAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVMDR---------------------------------------- 340
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEevydkflkllvekvkklkvgdpldestdlgplispeaver 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 341 ----------------------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTK 398
Cdd:cd07145 317 menlvndavekggkilyggkrdEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTN 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 982742419 399 DLGRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 444
Cdd:cd07145 397 DINRALKV--ARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREG 440
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
71-454 |
6.35e-60 |
|
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: 202.94 E-value: 6.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGV-GEVQE 149
Cdd:cd07092 4 PATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 150 YVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07092 84 AVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 230 VTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDA 309
Cdd:cd07092 164 LAELAAEVLP----PGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 310 DLSLVVPSALFAAVGTAGQRCTTARRLVM--------------------------------------------------- 338
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVhesvydefvaalveavsairvgdpddedtemgplnsaaqrervagfverap 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 339 ------------DRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRW 406
Cdd:cd07092 320 aharvltggrraEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 982742419 407 LGPKGSDCGIVNVNIPTSgAEIggAFGGEKHTGGGRESGSDAWKQYMR 454
Cdd:cd07092 400 SARLDFGTVWVNTHIPLA-AEM--PHGGFKQSGYGKDLSIYALEDYTR 444
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
68-448 |
1.50e-59 |
|
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: 202.02 E-value: 1.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 68 TYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGev 147
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 148 qeyVDI----------CDYAVGLsrmiGGPILPSERsGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLW 217
Cdd:cd07093 79 ---RDIpraaanfrffADYILQL----DGESYPQDG-GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 218 KGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLE 296
Cdd:cd07093 151 KPSEWTPLTAW----LLAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 297 LGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVMDRP----------------------------------- 341
Cdd:cd07093 227 LGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSiydeflerfverakalkvgdpldpdtevgpliske 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 ---------------------------------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 388
Cdd:cd07093 307 hlekvlgyvelaraegatiltgggrpelpdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTP 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 982742419 389 QGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN------IPTsgaeiggAFGGEKHTGGGRESGSDA 448
Cdd:cd07093 387 YGLAAYVWTRDLGRAHRV--ARRLEAGTVWVNcwlvrdLRT-------PFGGVKASGIGREGGDYS 443
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
52-453 |
5.13e-59 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 201.84 E-value: 5.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 52 EGVYNGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLG 129
Cdd:PLN02278 26 QGLIGGKWtdAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 130 SLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAM 209
Cdd:PLN02278 106 QLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 210 ICGNVCLWKGAPTTSLISVAVTKIiakVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQ-- 287
Cdd:PLN02278 186 AAGCTVVVKPSELTPLTALAAAEL---ALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKK--LMAGaa 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 288 ERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARR-------------------------------- 335
Cdd:PLN02278 261 ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRilvqegiydkfaeafskavqklvvgdgfeegv 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 336 ----------------LVMD----------------RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAW 383
Cdd:PLN02278 341 tqgplineaavqkvesHVQDavskgakvllggkrhsLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAI 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 982742419 384 NNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN---IPTSGAeiggAFGGEKHTGGGRESGSDAWKQYM 453
Cdd:PLN02278 421 ANDTEAGLAAYIFTRDLQRAWRV--SEALEYGIVGVNeglISTEVA----PFGGVKQSGLGREGSKYGIDEYL 487
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
66-443 |
2.22e-57 |
|
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: 196.28 E-value: 2.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 66 ITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 146 EVQEYVDICDYAVGLSRMIGGPILPSE-------RSGHALIEqwnPVGLVGIITAFNFPVavygwnN--------AIAmi 210
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFDaspggegRIGFTIRE---PIGVVAAITPFNFPL------NlvahkvgpAIA-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 211 CGNVCLWKGAPTTSLISVAvtkiIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVglmvQER 289
Cdd:cd07149 150 AGNAVVLKPASQTPLSALK----LAELLLEAGLPkGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAI----ARK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 290 FG--RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL-----VMD----------------------- 339
Cdd:cd07149 222 AGlkKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIfvhedIYDeflerfvaatkklvvgdpldedt 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 340 ---------------------------------RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNE 386
Cdd:cd07149 302 dvgpmiseaeaerieewveeaveggarlltggkRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMAND 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 982742419 387 VKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 443
Cdd:cd07149 382 SPYGLQAGVFTNDLQKALKAA--RELEVGGVMINdSSTFRVD-HMPYGGVKESGTGRE 436
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
68-454 |
5.84e-57 |
|
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: 195.22 E-value: 5.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 68 TYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEV 147
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 148 QEYVDICDYAVGL-SRMIGGPI-LPSERSGHALIEqwnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSL 225
Cdd:cd07090 81 DSSADCLEYYAGLaPTLSGEHVpLPGGSFAYTRRE---PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 226 ISVavtkIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIA 305
Cdd:cd07090 158 TAL----LLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 306 FEDADLSLVVPSALFAAVGTAGQRCTTARRL-------------VMDRP------------------------------- 341
Cdd:cd07090 234 FDDADLENAVNGAMMANFLSQGQVCSNGTRVfvqrsikdefterLVERTkkirigdpldedtqmgaliseehlekvlgyi 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 -------------------------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIF 396
Cdd:cd07090 314 esakqegakvlcggervvpedglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVF 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 982742419 397 TKDLGRIFRWLGP-KGSDCGIVNVNIptSGAEIggAFGGEKHTGGGRESGSDAWKQYMR 454
Cdd:cd07090 394 TRDLQRAHRVIAQlQAGTCWINTYNI--SPVEV--PFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
54-462 |
7.41e-57 |
|
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: 196.29 E-value: 7.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 54 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 133 SLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPIL---PSERSGHALIeqwnPVGLVGIITAFNFPVAVYGWNNAIAM 209
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVemvPGEDNRYVYR----PLGVGAVISPWNFPLAILAGMTTAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 210 ICGNVCLWKGAPTTSLISVAVtkiiAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGStqvgKQVGLMVQE 288
Cdd:cd07124 192 VTGNTVVLKPAEDTPVIAAKL----VEILEEAGLPpGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGS----REVGLRIYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 289 RFG----------RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLV--------------------- 337
Cdd:cd07124 264 RAAkvqpgqkwlkRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIvhesvydeflerlvertkalk 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 338 -------------------MDR-------------------------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFK 373
Cdd:cd07124 344 vgdpedpevymgpvidkgaRDRirryieigksegrlllggevlelaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 374 FKNEEEVFAWNNEVKQGLSSSIFTKDLGRI--FRwlgpKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTG-GGRESGSDAW 449
Cdd:cd07124 424 AKDFDEALEIANDTEYGLTGGVFSRSPEHLerAR----REFEVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDYL 499
|
490
....*....|...
gi 982742419 450 KQYMRRSTCTINY 462
Cdd:cd07124 500 LQFMQPKTVTENF 512
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
71-462 |
1.41e-56 |
|
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: 194.52 E-value: 1.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07107 4 PATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 151 VDICDYAVGLSRMIGGPILP-SERSGHALIEQwnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07107 84 AALLDYFAGLVTELKGETIPvGGRNLHYTLRE--PYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 230 VTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDA 309
Cdd:cd07107 162 LAELAREVLP----PGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 310 DLSLVVPSALFAA-VGTAGQRCTTARRL--------------------------------------------VMD----- 339
Cdd:cd07107 238 DPEAAADAAVAGMnFTWCGQSCGSTSRLfvhesiydevlarvvervaaikvgdptdpattmgplvsrqqydrVMHyidsa 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 340 ------------RP-------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 400
Cdd:cd07107 318 kregarlvtgggRPegpalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982742419 401 GRIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 462
Cdd:cd07107 398 SQAHR--TARRVEAGYVWIN-GSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
56-453 |
3.24e-56 |
|
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: 194.07 E-value: 3.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAW--KIWADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07119 3 DGEWveAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 132 VSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMIC 211
Cdd:cd07119 83 ETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVR-EPVGVCGLITPWNYPLLQAAWKLAPALAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 212 GNVCLWKGAPTTSLISVAVTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERF 290
Cdd:cd07119 162 GNTVVIKPSEVTPLTTIALFELIEEA----GLPAGVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 291 GRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVMDRP----------------------------- 341
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESihdkfvaalaerakkiklgngldadtemg 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 ---------------------------------------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFA 382
Cdd:cd07119 318 plvsaehrekvlsyiqlgkeegarlvcggkrptgdelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 982742419 383 WNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN---IPTSGAEiggaFGGEKHTGGGRESGSDAWKQYM 453
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVA--RRLRAGTVWINdyhPYFAEAP----WGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
69-454 |
7.38e-55 |
|
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: 189.74 E-value: 7.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 69 YCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQ 148
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 149 EYVDICDYAVGLSrmigGPILPSER-------SGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:cd07099 81 LALEAIDWAARNA----PRVLAPRKvptgllmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 222 TTSLISVAVTKIIAKVLednkLPGAICSLTCGGADIGTAMAkDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN 301
Cdd:cd07099 157 VTPLVGELLAEAWAAAG----PPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 302 AIIAFEDADLSLVVPSALFAAVGTAGQRC------------------------------------------TTARRL--- 336
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCisvervyvhesvydefvarlvakaralrpgaddigdadigpmTTARQLdiv 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 337 -------------------VMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT 397
Cdd:cd07099 312 rrhvddavakgakaltggaRSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982742419 398 KDL---GRIFRWLgpkgsDCGIVNVNIPTSGAEIGGA-FGGEKHTGGGRESGSDAWKQYMR 454
Cdd:cd07099 392 RDLaraEAIARRL-----EAGAVSINDVLLTAGIPALpFGGVKDSGGGRRHGAEGLREFCR 447
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
89-443 |
1.14e-54 |
|
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: 188.44 E-value: 1.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 89 EETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICD-YAVGLSRMIGGP 167
Cdd:cd07100 2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRyYAENAEAFLADE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 168 ILPSErSGHALIeQWNPVGLVGIITAFNFP---VAVYGwnnAIAMICGNVCLWKGAPTTSLISVAvtkiIAKVLEDNKLP 244
Cdd:cd07100 82 PIETD-AGKAYV-RYEPLGVVLGIMPWNFPfwqVFRFA---APNLMAGNTVLLKHASNVPGCALA----IEELFREAGFP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 245 -GAICSLTCGGADIGTAMAkDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAV 323
Cdd:cd07100 153 eGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 324 GTAGQRCTTARRL----------------------------------------------------------------VMD 339
Cdd:cd07100 232 QNAGQSCIAAKRFivhedvydeflekfveamaalkvgdpmdedtdlgplarkdlrdelheqveeavaagatlllggkRPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 340 RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLG---RIFRWLgpkgsDCGI 416
Cdd:cd07100 312 GPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLEraeRVARRL-----EAGM 386
|
410 420
....*....|....*....|....*...
gi 982742419 417 VNVNIPT-SGAEIggAFGGEKHTGGGRE 443
Cdd:cd07100 387 VFINGMVkSDPRL--PFGGVKRSGYGRE 412
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
71-443 |
1.91e-54 |
|
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: 188.72 E-value: 1.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL-VEGVGEVQE 149
Cdd:cd07108 4 PATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 150 YVDICDYAVGLSRMIGGPILPSeRSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07108 84 LADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 230 VTKIIAKVLednklPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFED 308
Cdd:cd07108 163 LAEILAQVL-----PAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 309 ADLSLVVPSALFAAVGT-AGQRCTTARRL---------VMDR-------------------------------------- 340
Cdd:cd07108 238 ADLDDAVDGAIAGMRFTrQGQSCTAGSRLfvhediydaFLEKlvaklsklkigdpldeatdigaiisekqfakvcgyidl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 341 ----------------------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTK 398
Cdd:cd07108 318 glstsgatvlrggplpgegplaDGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 982742419 399 DLGRIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRE 443
Cdd:cd07108 398 DLGRALR--AAHALEAGWVQVN-QGGGQQPGQSYGGFKQSGLGRE 439
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
71-460 |
2.19e-54 |
|
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: 188.60 E-value: 2.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKIWA-DIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQE 149
Cdd:cd07109 4 PSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 150 YVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07109 84 AARYFEYYGGAADKLHGETIPLGPGYFVYTVR-EPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 230 vtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFED 308
Cdd:cd07109 163 ----LAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 309 ADLSLVVPSALFAAVGTAGQRCTTARRLVMDRP----------------------------------------------- 341
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSiydevlerlverfralrvgpgledpdlgplisakqldrvegfvarar 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 -------------------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGR 402
Cdd:cd07109 319 argarivaggriaegapagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 982742419 403 IFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 460
Cdd:cd07109 399 ALRV--ARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
66-443 |
2.48e-54 |
|
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: 188.22 E-value: 2.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 66 ITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 146 EVQEYVDICDYAVGLSRMIGGPILP---SERS-GH-ALIEQWnPVGLVGIITAFNFPV--AVYGWNNAIAMicGNVCLWK 218
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldiSARGeGRqGLVRRF-PIGPVSAITPFNFPLnlVAHKVAPAIAA--GCPFVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 219 GAPTTSLISVavtkIIAKVLEDNKLP-GAICSLTCgGADIGTAMAKDERVNLLSFTGStqvgKQVGLMVQERFGRS--LL 295
Cdd:cd07147 158 PASRTPLSAL----ILGEVLAETGLPkGAFSVLPC-SRDDADLLVTDERIKLLSFTGS----PAVGWDLKARAGKKkvVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 296 ELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVMDRP---------------------------------- 341
Cdd:cd07147 229 ELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSvydefksrlvarvkalktgdpkddatdvgpmise 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 ---------------------------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSS 394
Cdd:cd07147 309 seaervegwvneavdagaklltggkrdGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 982742419 395 IFTKDLGRIFR-WlgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 443
Cdd:cd07147 389 VFTRDLEKALRaW---DELEVGGVVINdVPTFRVD-HMPYGGVKDSGIGRE 435
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
71-460 |
5.79e-53 |
|
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: 184.85 E-value: 5.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKI--WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQ 148
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 149 EYVDICDYAVGLSRMIGGPI---LPSERSGHALIEqwnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSl 225
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSynnLGDDMLGLVLRE---PIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 226 isvAVTKIIAKVLEDNKLPGAICS-LTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAII 304
Cdd:cd07118 160 ---GTTLMLAELLIEAGLPAGVVNiVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 305 AFEDADLSLVVPSALFAAVGTAGQRCTTARRLVMDR-------------------------------------------- 340
Cdd:cd07118 237 VFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHEsiadafvaavvarsrkvrvgdpldpetkvgaiineaqlakitdy 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 341 ---------------------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 399
Cdd:cd07118 317 vdagraegatlllggerlasaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982742419 400 LGRIFrwLGPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 460
Cdd:cd07118 397 IDTAL--TVARRIRAGTVWVNtFLDGSPEL--PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
69-453 |
1.63e-52 |
|
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: 183.60 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 69 YCPANNEPIARVRQASVADYEETVKKAREAWKIWA-DIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILV-EGVGE 146
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMtARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 147 VQEYVDICDYAVGLSRM------IGGPILPSERSGHALIEQwnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGA 220
Cdd:cd07089 82 VDGPIGHLRYFADLADSfpwefdLPVPALRGGPGRRVVRRE--PVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 221 PTTSLISVAVTKIIAkvlEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGN 300
Cdd:cd07089 160 PDTPLSALLLGEIIA---ETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 301 NAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVMDR------------------------PGN------------- 343
Cdd:cd07089 237 SANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRsrydevvealaaafealpvgdpadPGTvmgplisaaqrdr 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 344 -----------------------------YVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSS 394
Cdd:cd07089 317 vegyiargrdegarlvtgggrpagldkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982742419 395 IFTKDLGR---IFRWLgpkgsDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 453
Cdd:cd07089 397 VWSADVDRayrVARRI-----RTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
56-444 |
5.41e-52 |
|
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: 182.65 E-value: 5.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07117 6 NGEWvkGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 134 LEMGKILVEGVGevqeyVDIcDYAVGLSRMIGGPILPSERSGHALIEQW------NPVGLVGIITAFNFPVAVYGWNNAI 207
Cdd:cd07117 86 LDNGKPIRETRA-----VDI-PLAADHFRYFAGVIRAEEGSANMIDEDTlsivlrEPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 208 AMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDnklpGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQ 287
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPK----GVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 288 ERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLV------------------------------ 337
Cdd:cd07117 236 KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFvqegiydefvaklkekfenvkvgnpldpdt 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 338 ----------MDR----------------------------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEE 379
Cdd:cd07117 316 qmgaqvnkdqLDKilsyvdiakeegakiltgghrltengldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDE 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 982742419 380 VFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRES 444
Cdd:cd07117 396 VIDMANDSEYGLGGGVFTKDINRALRV--ARAVETGRVWVNtynqIPA-----GAPFGGYKKSGIGRET 457
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
56-454 |
9.77e-52 |
|
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: 181.92 E-value: 9.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKI--WADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07142 9 NGQFvdAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 132 VSLEMGKILVEG-VGEVQEYVDICDYAVGLSRMIGGPILPSERSGHA--LIEqwnPVGLVGIITAFNFPVAVYGWNNAIA 208
Cdd:cd07142 89 ETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVytLHE---PIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 209 MICGNVCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQV-GLMV 286
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSAL----LAAKLAAEAGLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIImQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 287 QERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVM---------------------------- 338
Cdd:cd07142 242 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVhesiydefvekakaralkrvvgdpfrkg 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 339 ---------------------------------DRPGN---YVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFA 382
Cdd:cd07142 322 veqgpqvdkeqfekilsyiehgkeegatlitggDRIGSkgyYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982742419 383 WNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMR 454
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLS--RALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
77-453 |
1.45e-51 |
|
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: 180.57 E-value: 1.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 77 IARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDY 156
Cdd:cd07152 4 LGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 157 AVGLSRMIGGPILPSERsGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTslisvAVTK--II 234
Cdd:cd07152 84 AAGLPTQPQGEILPSAP-GRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRT-----PVSGgvVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 235 AKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGlmvqERFGRSL----LELGGNNAIIAFEDAD 310
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVG----EAAGRHLkkvsLELGGKNALIVLDDAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 311 LSLVVPSALFAAVGTAGQRCTTARRL-----VMD---------------------------------------------- 339
Cdd:cd07152 234 LDLAASNGAWGAFLHQGQICMAAGRHlvhesVADaytaklaakakhlpvgdpatgqvalgplinarqldrvhaivddsva 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 340 ----------RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRwLGP 409
Cdd:cd07152 314 agarleaggtYDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA-LAD 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 982742419 410 KgSDCGIVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSDAWKQYM 453
Cdd:cd07152 393 R-LRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFT 436
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
66-443 |
1.06e-50 |
|
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: 178.78 E-value: 1.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 66 ITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 146 EVQEYVDICDYAVGLSRMIGGPILP---SERSGHALIeqW---NPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKG 219
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPldaTQGSDNRLA--WtirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 220 APTTSLISVAVTKIIakvLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQERFGRSLLELGG 299
Cdd:cd07094 159 ASKTPLSALELAKIL---VEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEA--LRANAGGKRIALELGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 300 NNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVMD---------------------------------------- 339
Cdd:cd07094 234 NAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHeelydefieafvaavkklkvgdpldedtdvgpliseeaae 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 340 ---------------------RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTK 398
Cdd:cd07094 314 rverwveeaveagarllcggeRDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 982742419 399 DLGRIFRwlGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRE 443
Cdd:cd07094 394 DLNVAFK--AAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGRE 436
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
56-405 |
1.37e-50 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 178.95 E-value: 1.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW-GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSL 134
Cdd:PRK13473 8 NGELvAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 135 EMGK-ILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGN 213
Cdd:PRK13473 88 NCGKpLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 214 VCLWKGAPTTSLISVAVTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRS 293
Cdd:PRK13473 168 TVVLKPSEITPLTALKLAELAADILP----PGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 294 LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL------------------------------------- 336
Cdd:PRK13473 244 HLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIyaqrgiyddlvaklaaavatlkvgdpddedtelgpli 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 337 ----------------------------VMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 388
Cdd:PRK13473 324 saahrdrvagfverakalghirvvtggeAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSD 403
|
410
....*....|....*..
gi 982742419 389 QGLSSSIFTKDLGRIFR 405
Cdd:PRK13473 404 YGLASSVWTRDVGRAHR 420
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
56-445 |
2.16e-50 |
|
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: 178.15 E-value: 2.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAW--KIWADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07139 4 GGRWvaPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 132 VSLEMGK-ILVEGVGEVQEYVDICDYAVGLSRmigGPILPSERS----GHALIEQwNPVGLVGIITAFNFPVAVYGWNNA 206
Cdd:cd07139 84 WTAENGMpISWSRRAQGPGPAALLRYYAALAR---DFPFEERRPgsggGHVLVRR-EPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 207 IAMICGNVCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMV 286
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAY----LLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 287 QERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARR------------------------------- 335
Cdd:cd07139 236 GERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRilvprsrydevvealaaavaalkvgdpldpa 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 336 -----LVMDR------------------------------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEV 380
Cdd:cd07139 316 tqigpLASARqrervegyiakgraegarlvtgggrpagldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 982742419 381 FAWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVNIPTSgaEIGGAFGGEKHTGGGRESG 445
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERglaVARRI-----RTGTVGVNGFRL--DFGAPFGGFKQSGIGREGG 456
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
71-460 |
3.66e-50 |
|
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: 177.17 E-value: 3.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRqasvADYEETVKKARE-AWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQE 149
Cdd:cd07146 6 PYTGEVVGTVP----AGTEEALREALAlAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 150 YVDICDYAVGLSRMIGGPILPSERSGHA----LIEQWNPVGLVGIITAFNFPVavygwNNAIAMIC-----GNVCLWKGA 220
Cdd:cd07146 82 AADVLRFAAAEALRDDGESFSCDLTANGkarkIFTLREPLGVVLAITPFNHPL-----NQVAHKIApaiaaNNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 221 PTTSLISVAvtkiIAKVLEDNKLPGAICSLTCGG-ADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERfgRSLLELGG 299
Cdd:cd07146 157 EKTPLSAIY----LADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--RQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 300 NNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL-----------------------------------VMDRP--- 341
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRIlvhesvadefvdllveksaalvvgdpmdpatdmgtVIDEEaai 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 -----------------------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTK 398
Cdd:cd07146 311 qienrveeaiaqgarvllgnqrqGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTN 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 982742419 399 DLGRIFRWLgpKGSDCGIVNVN------IPTSgaeiggAFGGEKHTG-GGRESGSDAWKQYMRRSTCTI 460
Cdd:cd07146 391 DLDTIKRLV--ERLDVGTVNVNevpgfrSELS------PFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
56-453 |
4.15e-50 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 177.79 E-value: 4.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:PRK11241 16 NGEWldANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 134 LEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGN 213
Cdd:PRK11241 96 LEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 214 VCLWKGAPTTSLISVAvtkiIAKVLEDNKLPGAICSLTCGGA-DIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGR 292
Cdd:PRK11241 176 TMVLKPASQTPFSALA----LAELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 293 SLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL-----VMDR--------------------------- 340
Cdd:PRK11241 252 VSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLyvqdgVYDRfaeklqqavsklhigdglekgvtigpl 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 341 --------------------------------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 388
Cdd:PRK11241 332 idekavakveehiadalekgarvvcggkahelGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTE 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 982742419 389 QGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIgGAFGGEKHTGGGRESGSDAWKQYM 453
Cdd:PRK11241 412 FGLAAYFYARDLSRVFRV--GEALEYGIVGINTGIISNEV-APFGGIKASGLGREGSKYGIEDYL 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
68-453 |
4.50e-50 |
|
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: 177.15 E-value: 4.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 68 TYCPANNEPIARVRQASVADYEETVKKAREAWK--IWADIPApKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 146 EVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSL 225
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLR-EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 226 ISVAVTKIIAKVLEdnkLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAII 304
Cdd:cd07120 159 INAAIIRILAEIPS---LPaGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 305 AFEDADLSLVVPSALFAAVGTAGQRCTTARRL---------VMDR-----------PG--------------------NY 344
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVlvqrsiadeVRDRlaarlaavkvgPGldpasdmgplidranvdrvdRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 345 VE---------------------------PTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT 397
Cdd:cd07120 316 VEraiaagaevvlrggpvteglakgaflrPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 982742419 398 KDLGRIFRWlgPKGSDCGIVNVNipTSGAEIGGA-FGGEKHTGGGRESGSDAWKQYM 453
Cdd:cd07120 396 RDLARAMRV--ARAIRAGTVWIN--DWNKLFAEAeEGGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
56-460 |
1.40e-49 |
|
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: 176.25 E-value: 1.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKI--WADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07091 9 NNEFvdSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 132 VSLEMGKILVEG-VGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMI 210
Cdd:cd07091 89 ESLDNGKPLEESaKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRR-EPIGVCGQIIPWNFPLLMLAWKLAPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 211 CGNVCLWKGAPTTSLISVAVTKIIAKVLednkLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVglMV--- 286
Cdd:cd07091 168 AGNTVVLKPAEQTPLSALYLAELIKEAG----FPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTI--MEaaa 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 287 QERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL------------------------------ 336
Cdd:cd07091 242 KSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIfvqesiydefvekfkaraekrvvgdpfdpd 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 337 --------------VMD--------------------RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFA 382
Cdd:cd07091 322 tfqgpqvskaqfdkILSyiesgkkegatlltggerhgSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 383 WNNEVKQGLSSSIFTKDLGRIFR----------WLgpkgsDC-GIVNVNIPtsgaeiggaFGGEKHTGGGRESGSDAWKQ 451
Cdd:cd07091 402 RANDTEYGLAAGVFTKDINKALRvsralkagtvWV-----NTyNVFDAAVP---------FGGFKQSGFGRELGEEGLEE 467
|
....*....
gi 982742419 452 YMRRSTCTI 460
Cdd:cd07091 468 YTQVKAVTI 476
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
56-422 |
6.47e-49 |
|
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: 174.24 E-value: 6.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07085 6 NGEWveSKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLIT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 134 LEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGN 213
Cdd:cd07085 86 LEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 214 VCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvglmVQER---F 290
Cdd:cd07085 166 TFVLKPSERVPGAAM----RLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEY----IYERaaaN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 291 GRSLLELGG-NNAIIAFEDADLSLVVPSALFAAVGTAGQRC----------TTAR------------------------- 334
Cdd:cd07085 238 GKRVQALGGaKNHAVVMPDADLEQTANALVGAAFGAAGQRCmalsvavavgDEADewipklverakklkvgagddpgadm 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 335 ------------------------RLVMD---------RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVF 381
Cdd:cd07085 318 gpvispaakeriegliesgveegaKLVLDgrgvkvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 982742419 382 AWNNEVKQGLSSSIFTKD--LGRIFRwlgpKGSDCGIVNVNIP 422
Cdd:cd07085 398 AIINANPYGNGAAIFTRSgaAARKFQ----REVDAGMVGINVP 436
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
35-461 |
2.91e-48 |
|
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: 172.59 E-value: 2.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 35 NQPqyawlkeLGLREENEGVYNGSwggrGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWK-IWADIPAPKRGEI 113
Cdd:cd07144 5 DQP-------TGLFINNEFVKSSD----GETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFEsWWSKVTGEERGEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 114 VRQIGDALREKIQVLGSLVSLEMGKIL-VEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIIT 192
Cdd:cd07144 74 LDKLADLVEKNRDLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLH-EPYGVCGQII 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 193 AFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLiSVAVtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLS 271
Cdd:cd07144 153 PWNYPLAMAAWKLAPALAAGNTVVIKPAENTPL-SLLY---FANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 272 FTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCT-TARRLV------------- 337
Cdd:cd07144 229 FTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTaTSRIYVqesiydkfvekfv 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 338 ---------------------------MDR---------------------------PGNYVEPTIVTGLGHDASIAHTE 363
Cdd:cd07144 309 ehvkqnykvgspfdddtvvgpqvsktqYDRvlsyiekgkkegaklvyggekapeglgKGYFIPPTIFTDVPQDMRIVKEE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 364 TFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRE 443
Cdd:cd07144 389 IFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVA--RELEAGMVWIN-SSNDSDVGVPFGGFKMSGIGRE 465
|
490
....*....|....*...
gi 982742419 444 SGSDAWKQYMRRSTCTIN 461
Cdd:cd07144 466 LGEYGLETYTQTKAVHIN 483
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
56-443 |
4.43e-48 |
|
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: 172.14 E-value: 4.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07559 6 NGEWvaPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 134 LEMGKILVEGVGevqeyVDIcDYAVGLSRMIGGPILPSERSGHALIEQ------WNPVGLVGIITAFNFPVAVYGWNNAI 207
Cdd:cd07559 86 LDNGKPIRETLA-----ADI-PLAIDHFRYFAGVIRAQEGSLSEIDEDtlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 208 AMICGNVCLWKGAPTTSLISVAVTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQ 287
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDLLP----KGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 288 ERFGRSLLELGGNNAIIAFEDADLSL--VVPSALFAAVGTA---GQRCTTARRLV---------MDR------------P 341
Cdd:cd07559 236 ENLIPVTLELGGKSPNIFFDDAMDADddFDDKAEEGQLGFAfnqGEVCTCPSRALvqesiydefIERaverfeaikvgnP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 -----------------------------------------------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKF 374
Cdd:cd07559 316 ldpetmmgaqvskdqlekilsyvdigkeegaevltggerltlggldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITF 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 982742419 375 KNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRE 443
Cdd:cd07559 396 KDEEEAIAIANDTEYGLGGGVWTRDINRALRV--ARGIQTGRVWVNcyhqYPA-----HAPFGGYKKSGIGRE 461
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
63-460 |
5.19e-48 |
|
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: 172.15 E-value: 5.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKI---WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGK- 138
Cdd:cd07141 21 GKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 139 ILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWK 218
Cdd:cd07141 101 FSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRH-EPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 219 GAPTTSLISVAVTKIIAkvlEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKqvglMVQERFGRS----- 293
Cdd:cd07141 180 PAEQTPLTALYLASLIK---EAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGK----LIQQAAGKSnlkrv 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 294 LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL------------------------------------- 336
Cdd:cd07141 253 TLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTfvqesiydefvkrsverakkrvvgnpfdpkteqgpqi 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 337 -------VMD-----------------RPGN---YVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQ 389
Cdd:cd07141 333 deeqfkkILEliesgkkegaklecggkRHGDkgyFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTY 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982742419 390 GLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAeIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 460
Cdd:cd07141 413 GLAAAVFTKDIDKAITF--SNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
70-453 |
1.00e-47 |
|
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: 170.57 E-value: 1.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 70 CPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKilvegvGEVQE 149
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGK------ARRHA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 150 YVDICDYAVGlSRMIG---GPILPSERSGHAL------IEQWNPVGLVGIITAFNFPVAVyGWNNAI-AMICGNVCLWKG 219
Cdd:cd07101 76 FEEVLDVAIV-ARYYArraERLLKPRRRRGAIpvltrtTVNRRPKGVVGVISPWNYPLTL-AVSDAIpALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 220 APTTSLISVAVTKIiakvLEDNKLPGAICSLTCG-GADIGTAMAkdERVNLLSFTGSTQVGKQVGlmvqERFGRSL---- 294
Cdd:cd07101 154 DSQTALTALWAVEL----LIEAGLPRDLWQVVTGpGSEVGGAIV--DNADYVMFTGSTATGRVVA----ERAGRRLigcs 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 295 LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL-------------------------------------- 336
Cdd:cd07101 224 LELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIyvhesvydefvrrfvartralrlgaaldygpdmgslis 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 337 ----------VMD--------------RP--GNYV-EPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQ 389
Cdd:cd07101 304 qaqldrvtahVDDavakgatvlaggraRPdlGPYFyEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDY 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 982742419 390 GLSSSIFTKDLGRIfRWLGPKgSDCGIVNVN--IPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 453
Cdd:cd07101 384 GLNASVWTRDGARG-RRIAAR-LRAGTVNVNegYAAAWASIDAPMGGMKDSGLGRRHGAEGLLKYT 447
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
71-445 |
4.34e-47 |
|
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: 169.07 E-value: 4.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 151 VDICDYAVGLS---RMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLIS 227
Cdd:cd07110 84 AGCFEYYADLAeqlDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 228 VAVTKIIAKVlednKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAF 306
Cdd:cd07110 164 LELAEIAAEA----GLPpGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 307 EDADLSLVVPSALFAAVGTAGQRCT-TARRLVMDR--------------------------------------------- 340
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSaTSRLLVHESiadaflerlataaeairvgdpleegvrlgplvsqaqyekvlsfia 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 341 --------------------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 400
Cdd:cd07110 320 rgkeegarllcggrrpahleKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 982742419 401 GRIFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRESG 445
Cdd:cd07110 400 ERCDRV--AEALEAGIVWINCSQP-CFPQAPWGGYKRSGIGRELG 441
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
56-461 |
1.62e-45 |
|
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: 165.05 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW-GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWA-DIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07082 7 NGEWkESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWpTMPLEERIDCLHKFADLLKENKEEVANLLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 134 LEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHAL----IEQWNPVGLVGIITAFNFPVavygwNNAI-- 207
Cdd:cd07082 87 WEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaQVRREPLGVVLAIGPFNYPL-----NLTVsk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 208 ---AMICGNVCLWKGAPTTSLISVavtkIIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvg 283
Cdd:cd07082 162 lipALIMGNTVVFKPATQGVLLGI----PLAEAFHDAGFPkGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNR-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 284 LMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARR---------------------------- 335
Cdd:cd07082 236 LKKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRvlvhesvadelvellkeevaklkvgmpw 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 336 --------------------LVMD--------------RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVF 381
Cdd:cd07082 316 dngvditplidpksadfvegLIDDavakgatvlngggrEGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 382 AWNNEVKQGLSSSIFTKDLGRIF---RWLgpkgsDCGIVNVNIPTS-GAEIgGAFGGEKHTGGGRESGSDAWKQYMRRST 457
Cdd:cd07082 396 ELANKSNYGLQASIFTKDINKARklaDAL-----EVGTVNINSKCQrGPDH-FPFLGRKDSGIGTQGIGDALRSMTRRKG 469
|
....
gi 982742419 458 CTIN 461
Cdd:cd07082 470 IVIN 473
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
63-454 |
1.81e-44 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 162.36 E-value: 1.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVE 142
Cdd:PRK13252 21 GETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 143 G-VGEVQEYVDICDYAVGLSRMIGGPILPSeRSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:PRK13252 101 TsVVDIVTGADVLEYYAGLAPALEGEQIPL-RGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 222 TTSLISVAvtkiIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN 301
Cdd:PRK13252 180 VTPLTALK----LAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 302 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARR------------------------------------LV----MDR- 340
Cdd:PRK13252 256 PLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRvfvqksikaafearllerveririgdpmdpatnfgpLVsfahRDKv 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 341 ---------------------------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSS 393
Cdd:PRK13252 336 lgyiekgkaegarllcggerlteggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAA 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 982742419 394 SIFTKDLGRIFRWLGpkGSDCGIVNVNipTSG---AEIggAFGGEKHTGGGRESGSDAWKQYMR 454
Cdd:PRK13252 416 GVFTADLSRAHRVIH--QLEAGICWIN--TWGespAEM--PVGGYKQSGIGRENGIATLEHYTQ 473
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
71-462 |
1.04e-43 |
|
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: 160.30 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKI-WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGK-ILVEGVGEVQ 148
Cdd:cd07113 22 PATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKsIHLSRAFEVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 149 EYVDICDYAVGLSRMIGG----PILPS---ERsgHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:cd07113 102 QSANFLRYFAGWATKINGetlaPSIPSmqgER--YTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 222 TTSLISVAvtkiIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN 301
Cdd:cd07113 180 FTPLTLLR----VAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 302 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVM------------------------------------------- 338
Cdd:cd07113 256 AAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVhrskfdelvtklkqalssfqvgspmdesvmfgplanqphfdkv 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 339 ---------------------DRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT 397
Cdd:cd07113 336 csylddaraegdeivrggealAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWT 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 982742419 398 KDLGRIFRWLgPKgSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 462
Cdd:cd07113 416 NNLSKALRYI-PR-IEAGTVWVNMHTF-LDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY 477
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
63-453 |
1.86e-43 |
|
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: 159.30 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWK--IWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 141 VEGV-GEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKG 219
Cdd:cd07112 81 SDALaVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITR-EPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 220 APTTSLisvavTKI-IAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQvgLMvqERFGRS---- 293
Cdd:cd07112 160 AEQSPL-----TALrLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRR--FL--EYSGQSnlkr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 294 -LLELGGNNAIIAFEDA-DLSLVVPSALFAAVGTAGQRCTTARRLVMDR------------------PGN---------- 343
Cdd:cd07112 231 vWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHEsikdeflekvvaaarewkPGDpldpatrmga 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 344 --------------------------------------YVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNN 385
Cdd:cd07112 311 lvseahfdkvlgyiesgkaegarlvaggkrvltetggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALAN 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 982742419 386 EVKQGLSSSIFTKDLGRIFRwlGPKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 453
Cdd:cd07112 391 DSVYGLAASVWTSDLSRAHR--VARRLRAGTVWVNC-FDEGDITTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
60-447 |
2.08e-43 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 160.43 E-value: 2.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 60 GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKI 139
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 140 LVEGVGEVQEYVDICDY----AVGL--SRMIGG--PILPSERsghaliEQWNPVGLVGIITAFNFPVAVyGWNNAI-AMI 210
Cdd:PRK09407 108 RRHAFEEVLDVALTARYyarrAPKLlaPRRRAGalPVLTKTT------ELRQPKGVVGVISPWNYPLTL-AVSDAIpALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 211 CGNVCLWKGAPTTSLISVAVtkiiAKVLEDNKLPGAICSLTCG-GADIGTAMAkdERVNLLSFTGSTQVGKQVGlmvqER 289
Cdd:PRK09407 181 AGNAVVLKPDSQTPLTALAA----VELLYEAGLPRDLWQVVTGpGPVVGTALV--DNADYLMFTGSTATGRVLA----EQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 290 FGRSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL----------------------------- 336
Cdd:PRK09407 251 AGRRLigfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIyvhesiydefvrafvaavramrlgagydy 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 337 -------------------VMD--------------RP--GNYV-EPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEV 380
Cdd:PRK09407 331 sadmgsliseaqletvsahVDDavakgatvlaggkaRPdlGPLFyEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEA 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 982742419 381 FAWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVN---IPTSGAeIGGAFGGEKHTGGGRESGSD 447
Cdd:PRK09407 411 VERANDTPYGLNASVWTGDTARgraIAARI-----RAGTVNVNegyAAAWGS-VDAPMGGMKDSGLGRRHGAE 477
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
63-462 |
2.25e-43 |
|
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: 159.58 E-value: 2.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKI--WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:cd07140 20 GKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 141 VEGVG-EVQEYVDICDYAVGLSRMIGGPILP--SERSGHAL-IEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCL 216
Cdd:cd07140 100 TLALKtHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 217 WKGAPTTSLISVAVTKIIAKVledNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVglM---VQERFGRS 293
Cdd:cd07140 180 LKPAQVTPLTALKFAELTVKA---GFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHI--MkscAVSNLKKV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 294 LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLV------------------------------------ 337
Cdd:cd07140 255 SLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFveesihdefvrrvveevkkmkigdpldrstdhgpqn 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 338 ----------------------------MDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNE--EEVFAWNNEV 387
Cdd:cd07140 335 hkahldklveycergvkegatlvyggkqVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDT 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 982742419 388 KQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 462
Cdd:cd07140 415 EYGLASGVFTKDINKALYV--SDKLEAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIEY 486
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
49-461 |
2.48e-43 |
|
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: 159.23 E-value: 2.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 49 EENEGVY-NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKI-WA-DIPAPKRGEIVRQIGDALRE 123
Cdd:cd07143 4 EQPTGLFiNGEFvdSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGlKVSGSKRGRCLSKLADLMER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 124 KIQVLGSLVSLEMGK-ILVEGVGEVQEYVDICDYAVGLSRMIGGPILP--SERSGHALIEqwnPVGLVGIITAFNFPVAV 200
Cdd:cd07143 84 NLDYLASIEALDNGKtFGTAKRVDVQASADTFRYYGGWADKIHGQVIEtdIKKLTYTRHE---PIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 201 YGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAkvlEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGK 280
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIP---EAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 281 qvglMVQERFGRS-----LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVM----------------- 338
Cdd:cd07143 238 ----KVMEAAAKSnlkkvTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVqegiydkfvkrfkekak 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 339 --------------------------------------------DRPGN---YVEPTIVTGLGHDASIAHTETFAPILYV 371
Cdd:cd07143 314 klkvgdpfaedtfqgpqvsqiqyerimsyiesgkaegatvetggKRHGNegyFIEPTIFTDVTEDMKIVKEEIFGPVVAV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 372 FKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGP-KGSDCGIVNVNIPTSGAeiggAFGGEKHTGGGRESGSDAWK 450
Cdd:cd07143 394 IKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANAlKAGTVWVNCYNLLHHQV----PFGGYKQSGIGRELGEYALE 469
|
490
....*....|.
gi 982742419 451 QYMRRSTCTIN 461
Cdd:cd07143 470 NYTQIKAVHIN 480
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
28-445 |
1.89e-42 |
|
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: 157.36 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 28 FMSTLLINQPQYAWLKE-LGLREENEG----VYNGSWGGRGEVITTYCPANNE-PIARVRQASVADYEETVKKAREAWKI 101
Cdd:cd07125 5 FVNRIFDLEVPLEALADaLKAFDEKEWeaipIINGEETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 102 WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICD-YAVGLSRMIGGPILPSERSGHALIE 180
Cdd:cd07125 85 WSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRyYAAQARELFSDPELPGPTGELNGLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 181 qWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIiakvLEDNKLPGAICSLT-CGGADIGT 259
Cdd:cd07125 165 -LHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVEL----LHEAGVPRDVLQLVpGDGEEIGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 260 AMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLL---ELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTAR-- 334
Cdd:cd07125 240 ALVAHPRIDGVIFTGSTETAKLINRALAERDGPILPliaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRll 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 335 --------------------------------------------------------RLVMDRP-----GNYVEPTIVTGl 353
Cdd:cd07125 320 ylqeeiaerfiemlkgamaslkvgdpwdlstdvgplidkpagkllrahtelmrgeaWLIAPAPlddgnGYFVAPGIIEI- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 354 ghDASIAH-TETFAPILYVFKFKNE--EEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAeIGG 430
Cdd:cd07125 399 --VGIFDLtTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWR--ERVEAGNLYINRNITGA-IVG 473
|
490
....*....|....*..
gi 982742419 431 A--FGGEKHTGGGRESG 445
Cdd:cd07125 474 RqpFGGWGLSGTGPKAG 490
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
56-453 |
9.79e-42 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 155.28 E-value: 9.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW-----GGRGEVITtycPANNEPIARVRQASVADYEETVKKAREAW-----KIWADIPAPKRGEIVRQIGDALREKI 125
Cdd:PLN02467 13 GGEWrepvlGKRIPVVN---PATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 126 QVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGG----PI-LPSER-SGHALieqWNPVGLVGIITAFNFPVA 199
Cdd:PLN02467 90 SELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkqkaPVsLPMETfKGYVL---KEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 200 VYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVlednKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQV 278
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREV----GLPpGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 279 GKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVM-------------------- 338
Cdd:PLN02467 243 GRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVheriasefleklvkwaknik 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 339 -----------------------------------------DRP-----GNYVEPTIVTGLGHDASIAHTETFAPILYVF 372
Cdd:PLN02467 323 isdpleegcrlgpvvsegqyekvlkfistaksegatilcggKRPehlkkGFFIEPTIITDVTTSMQIWREEVFGPVLCVK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 373 KFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN--------IPtsgaeiggaFGGEKHTGGGRES 444
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISNDLERCERV--SEAFQAGIVWINcsqpcfcqAP---------WGGIKRSGFGREL 471
|
....*....
gi 982742419 445 GSDAWKQYM 453
Cdd:PLN02467 472 GEWGLENYL 480
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
37-456 |
3.35e-41 |
|
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: 153.32 E-value: 3.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 37 PQYAWLKELGLREeneGVY-NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEI 113
Cdd:cd07111 10 CALAWLDAHDRSF---GHFiNGKWvkPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 114 VRQIGDALREKIQVLGSLVSLEMGKILVEgvgevqeyvdicdyavglSRMIGGPILPSERSGHALIEQ--------WNPV 185
Cdd:cd07111 87 LYRIARHIQKHQRLFAVLESLDNGKPIRE------------------SRDCDIPLVARHFYHHAGWAQlldtelagWKPV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 186 GLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVlednKLPGAICSLTCGGADIGTAMAKDE 265
Cdd:cd07111 149 GVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEA----GLPPGVLNIVTGNGSFGSALANHP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 266 RVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVMD------ 339
Cdd:cd07111 225 GVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQesvaee 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 340 ------------RPGN----------------------YVE------------------------PTIVTGLGHDASIAH 361
Cdd:cd07111 305 lirklkermshlRVGDpldkaidmgaivdpaqlkrireLVEegraegadvfqpgadlpskgpfypPTLFTNVPPASRIAQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 362 TETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRwLGPkGSDCGIVNVNI-----PTSGaeiggaFGGEK 436
Cdd:cd07111 385 EEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALE-VAL-SLKAGVVWINGhnlfdAAAG------FGGYR 456
|
490 500
....*....|....*....|
gi 982742419 437 HTGGGRESGSDAWKQYMRRS 456
Cdd:cd07111 457 ESGFGREGGKEGLYEYLRPS 476
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
56-445 |
9.58e-41 |
|
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: 151.89 E-value: 9.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW-----GGRGEVIttyCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGS 130
Cdd:cd07138 4 DGAWvapagTETIDVI---NPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 131 LVSLEMG-------KILVE-GVGEVQEYVDIC-DYAVglsrmiggpilpSERSGHALIeQWNPVGLVGIITAFNFPVavy 201
Cdd:cd07138 81 AITLEMGapitlarAAQVGlGIGHLRAAADALkDFEF------------EERRGNSLV-VREPIGVCGLITPWNWPL--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 202 gwnNAI------AMICGNVCLWKG---APTTSLIsvavtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLS 271
Cdd:cd07138 145 ---NQIvlkvapALAAGCTVVLKPsevAPLSAII-------LAEILDEAGLPAGVFNLVNGdGPVVGEALSAHPDVDMVS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 272 FTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCT-------------------- 331
Cdd:cd07138 215 FTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNaptrmlvprsryaeaeeiaa 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 332 -TARRLVMDRP----------------------------------------------GNYVEPTIVTGLGHDASIAHTET 364
Cdd:cd07138 295 aAAEAYVVGDPrdpattlgplasaaqfdrvqgyiqkgieegarlvaggpgrpeglerGYFVKPTVFADVTPDMTIAREEI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 365 FAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVNipTSGAEIGGAFGGEKHTGGG 441
Cdd:cd07138 375 FGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERaraVARRL-----RAGQVHIN--GAAFNPGAPFGGYKQSGNG 447
|
....
gi 982742419 442 RESG 445
Cdd:cd07138 448 REWG 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
87-460 |
3.81e-40 |
|
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: 149.65 E-value: 3.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 87 DYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMG------KILVEGVGEVqeyvdICDYAVGL 160
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGataawaGFNVDLAAGM-----LREAASLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 161 SRMIGGPIlPSERSGH-ALIEQwNPVGLVGIITAFNFPVAVYGwnNAIAM--ICGNVCLWKG---APTTSLIsvavtkiI 234
Cdd:cd07105 76 TQIIGGSI-PSDKPGTlAMVVK-EPVGVVLGIAPWNAPVILGT--RAIAYplAAGNTVVLKAselSPRTHWL-------I 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 235 AKVLEDNKLP-GAICSLTCGGAD---IGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDAD 310
Cdd:cd07105 145 GRVFHEAGLPkGVLNVVTHSPEDapeVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDAD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 311 LSLVVPSALFAAVGTAGQRCTTARRLVMDR-------------------------------------------------- 340
Cdd:cd07105 225 LDAAANAALFGAFLNSGQICMSTERIIVHEsiadefveklkaaaeklfagpvvlgslvsaaaadrvkelvddalskgakl 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 341 ----------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRwLGpK 410
Cdd:cd07105 305 vvggladespSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALA-VA-K 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 982742419 411 GSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 460
Cdd:cd07105 383 RIESGAVHINGMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
54-455 |
3.84e-40 |
|
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: 150.81 E-value: 3.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 54 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 133 SLEMGKILVEGVGEVQEYVDICDY-AVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMIC 211
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYyARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 212 GNVCLWKGAPTTSLISVAVTKIIAkvlEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQER-- 289
Cdd:cd07083 182 GNTVIAKPAEDAVVVGYKVFEIFH---EAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLap 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 290 ----FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLV----------------MDR--------- 340
Cdd:cd07083 259 gqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLIltqgayepvlerllkrAERlsvgppeen 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 341 --------------------------------------PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEE--EV 380
Cdd:cd07083 339 gtdlgpvidaeqeakvlsyiehgknegqlvlggkrlegEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEA 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 982742419 381 FAWNNEVKQGLSSSIFTKDLGRIfRWLGPKgSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdawKQYMRR 455
Cdd:cd07083 419 LEVANSTPYGLTGGVYSRKREHL-EEARRE-FHVGNLYINRKITGALVGvQPFGGFKLSGTNAKTGG---PHYLRR 489
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
87-448 |
4.71e-39 |
|
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: 146.65 E-value: 4.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 87 DYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRmigg 166
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYH---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 167 pilpsERSG--------HALIEQWNPVGLVGIITAFNFPVAVYgwNNAI--AMICGNVCLWKGAPTTSlisvAVTKIIAK 236
Cdd:cd07095 77 -----ERTGeratpmaqGRAVLRHRPHGVMAVFGPFNFPGHLP--NGHIvpALLAGNTVVFKPSELTP----AVAELMVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 237 VLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSL-LELGGNNAIIAFEDADLSLVV 315
Cdd:cd07095 146 LWEEAGLPPGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 316 PSALFAAVGTAGQRCTTARRLV---------------------------------------------------------- 337
Cdd:cd07095 226 YLIVQSAFLTAGQRCTCARRLIvpdgavgdaflerlveaakrlrigapdaeppfmgpliiaaaaaryllaqqdllalgge 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 338 -------MDRPGNYVEPTI--VTGLghdASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDlGRIFRWLG 408
Cdd:cd07095 306 pllamerLVAGTAFLSPGIidVTDA---ADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDD-EALFERFL 381
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 982742419 409 PKgSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDA 448
Cdd:cd07095 382 AR-IRAGIVNWNRPTTGASSTAPFGGVGLSGNHRPSAYYA 420
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
71-402 |
6.59e-39 |
|
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: 146.62 E-value: 6.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 151 VDICDYAVGLSRMIGGPILPSERSG-HALIEQwNPVGLVGIITAFNFP--VAVygwnNAI--AMICGNVCLWKGAPTTSL 225
Cdd:cd07102 83 LERARYMISIAEEALADIRVPEKDGfERYIRR-EPLGVVLIIAPWNYPylTAV----NAVipALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 226 ISVAvtkiIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIA 305
Cdd:cd07102 158 CGER----FAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 306 FEDADLSLVVPSALFAAVGTAGQRC------------------------------------TT----------------- 332
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCcsieriyvhesiydafveafvavvkgyklgdpldpsTTlgpvvsaraadfvraqi 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 333 -------ARRL-------VMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTK 398
Cdd:cd07102 314 adaiakgARALidgalfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
....
gi 982742419 399 DLGR 402
Cdd:cd07102 394 DIAR 397
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
63-454 |
8.96e-38 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 144.95 E-value: 8.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWK--IWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:PLN02466 72 GKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 141 VEGVG-EVQEYVDICDYAVGLSRMIGGPILPSErSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKG 219
Cdd:PLN02466 152 EQSAKaELPMFARLFRYYAGWADKIHGLTVPAD-GPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 220 APTTSLISVAVtkiiAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQV-GLMVQERFGRSLLEL 297
Cdd:PLN02466 231 AEQTPLSALYA----AKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVlELAAKSNLKPVTLEL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 298 GGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTA----------------------RRLVMD---------------- 339
Cdd:PLN02466 307 GGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGsrtfvhervydefvekakaralKRVVGDpfkkgveqgpqidseq 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 340 --------------------------RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSS 393
Cdd:PLN02466 387 fekilryiksgvesgatlecggdrfgSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAA 466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982742419 394 SIFTKDL---GRIFRWLgpkgsDCGIVNVN--------IPtsgaeiggaFGGEKHTGGGRESGSDAWKQYMR 454
Cdd:PLN02466 467 GVFTQNLdtaNTLSRAL-----RVGTVWVNcfdvfdaaIP---------FGGYKMSGIGREKGIYSLNNYLQ 524
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
54-405 |
1.99e-36 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 140.84 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 54 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:PRK03137 40 IIGGERITTEDKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 133 SLEMGKILVEGVGEVQEYVDICDY----AVGLSRmiGGPIL--PSERSGHALIeqwnPVGLVGIITAFNFPVAVYGWNNA 206
Cdd:PRK03137 120 VKEAGKPWAEADADTAEAIDFLEYyarqMLKLAD--GKPVEsrPGEHNRYFYI----PLGVGVVISPWNFPFAIMAGMTL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 207 IAMICGNVCLWKGAPTTSLISVAVtkiiAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGStqvgKQVGLM 285
Cdd:PRK03137 194 AAIVAGNTVLLKPASDTPVIAAKF----VEVLEEAGLPaGVVNFVPGSGSEVGDYLVDHPKTRFITFTGS----REVGLR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 286 VQER----------FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVM----------------- 338
Cdd:PRK03137 266 IYERaakvqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVhedvydevlekvveltk 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 339 ---------------------------------------------DRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFK 373
Cdd:PRK03137 346 eltvgnpednaymgpvinqasfdkimsyieigkeegrlvlggegdDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIK 425
|
410 420 430
....*....|....*....|....*....|..
gi 982742419 374 FKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 405
Cdd:PRK03137 426 AKDFDHALEIANNTEYGLTGAVISNNREHLEK 457
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
63-454 |
4.40e-36 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 139.57 E-value: 4.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWK--IWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:PLN02766 35 GKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 141 VEGvgevqEYVDI------CDYAVGLSRMIGGPILPSERS--GHALIEqwnPVGLVGIITAFNFPVAVYGWNNAIAMICG 212
Cdd:PLN02766 115 ALG-----KAVDIpaaaglLRYYAGAADKIHGETLKMSRQlqGYTLKE---PIGVVGHIIPWNFPSTMFFMKVAPALAAG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 213 NVCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKqvglMVQERFG 291
Cdd:PLN02766 187 CTMVVKPAEQTPLSAL----FYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGR----KIMQAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 292 RS-----LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL---------------------VMDRP---- 341
Cdd:PLN02766 259 TSnlkqvSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVyvqegiydefvkklvekakdwVVGDPfdpr 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 ---------------------------------------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFA 382
Cdd:PLN02766 339 arqgpqvdkqqfekilsyiehgkregatlltggkpcgdkGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIK 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 982742419 383 WNNEVKQGLSSSIFTKDL---GRIFRWLgpkgsDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMR 454
Cdd:PLN02766 419 KANNTKYGLAAGIVTKDLdvaNTVSRSI-----RAGTIWVNC-YFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
60-459 |
3.56e-35 |
|
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: 136.55 E-value: 3.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 60 GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKI 139
Cdd:TIGR01722 12 GASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 140 LVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKG 219
Cdd:TIGR01722 92 HSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 220 APTTSLISVAVtkiiAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVgLMVQERFGRSLLELGG 299
Cdd:TIGR01722 172 SEKVPSAAVKL----AELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYI-HTTGSAHGKRVQALGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 300 -NNAIIAFEDADLSLVVPSALFAAVGTAGQRCTT---------ARRLV--------------MDRP-------------- 341
Cdd:TIGR01722 247 aKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAisaavlvgaADEWVpeireraekirigpGDDPgaemgplitpqakd 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 ------------------------------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGL 391
Cdd:TIGR01722 327 rvasliaggaaegaevlldgrgykvdgyeeGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGN 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 982742419 392 SSSIFTKDLG--RIFRWLgpkgSDCGIVNVNIPTSGAEIGGAFGGEKHT--GGGRESGSDAWKQYMRRSTCT 459
Cdd:TIGR01722 407 GTAIFTRDGAaaRRFQHE----IEVGQVGVNVPIPVPLPYFSFTGWKDSffGDHHIYGKQGTHFYTRGKTVT 474
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
71-443 |
1.92e-34 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 134.22 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:PRK13968 14 PATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 151 VDICD-YAV-GLSRMIGGPILPSERsgHALIEqWNPVGLVGIITAFNFPVavygWN---NAIAMI-CGNVCLWKGAPTTs 224
Cdd:PRK13968 94 ANLCDwYAEhGPAMLKAEPTLVENQ--QAVIE-YRPLGTILAIMPWNFPL----WQvmrGAVPILlAGNGYLLKHAPNV- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 225 lisVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAII 304
Cdd:PRK13968 166 ---MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 305 AFEDADLSLVVPSALFAAVGTAGQRCTTARRLV---------------------MDRP---------------------- 341
Cdd:PRK13968 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIieegiasafterfvaaaaalkMGDPrdeenalgpmarfdlrdelhhq 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 ---------------------GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 400
Cdd:PRK13968 323 veatlaegarlllggekiagaGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDE 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 982742419 401 GRIFRWlgPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRE 443
Cdd:PRK13968 403 TQARQM--AARLECGGVFINgYCASDARV--AFGGVKKSGFGRE 442
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
115-405 |
1.69e-33 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 130.63 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 115 RQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAF 194
Cdd:PRK10090 2 RKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 195 NFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVNLLSFT 273
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI----GLPKGVFNLVLGrGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 274 GSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL-----VMDR-------- 340
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVyvqkgIYDQfvnrlgea 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 341 ----------------------------------------------------PGNYVEPTIVTGLGHDASIAHTETFAPI 368
Cdd:PRK10090 238 mqavqfgnpaerndiamgplinaaalerveqkvaraveegarvalggkavegKGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 982742419 369 LYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 405
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMK 354
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
38-460 |
2.00e-32 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 129.25 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 38 QYAWLKELGLREENEGVYNGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWK--IWADIPAPKRGEI 113
Cdd:PRK09847 7 AYWQDKALSLAIENRLFINGEYtaAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 114 VRQIGDALREKIQVLGSLVSLEMGKIL-------VEGVGEVQEYvdicdYAVGLSRMIGgPILPSERSGHALIEQwNPVG 186
Cdd:PRK09847 87 LNKLADLMEAHAEELALLETLDTGKPIrhslrddIPGAARAIRW-----YAEAIDKVYG-EVATTSSHELAMIVR-EPVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 187 LVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAvtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDE 265
Cdd:PRK09847 160 VIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIR----LAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 266 RVNLLSFTGSTQVGKQvgLMV---QERFGRSLLELGGNNAIIAFEDA-DLSLVVPSALFAAVGTAGQRCTTARRLVMD-- 339
Cdd:PRK09847 236 DIDAIAFTGSTRTGKQ--LLKdagDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEes 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 340 ----------------RPGN--------------------------------------------YVEPTIVTGLGHDASI 359
Cdd:PRK09847 314 iadeflallkqqaqnwQPGHpldpattmgtlidcahadsvhsfiregeskgqllldgrnaglaaAIGPTIFVDVDPNASL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 360 AHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGaEIGGAFGGEKHTG 439
Cdd:PRK09847 394 SREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRM--SRRLKAGSVFVNNYNDG-DMTVPFGGYKQSG 470
|
490 500
....*....|....*....|.
gi 982742419 440 GGRESGSDAWKQYMRRSTCTI 460
Cdd:PRK09847 471 NGRDKSLHALEKFTELKTIWI 491
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
69-445 |
2.46e-31 |
|
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: 125.49 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 69 YCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGV-GEV 147
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 148 qeyVDICDYAVGLSRMIGGPILPSERSGHALIE------QWNPVGLVGIITAFNFPvavygWNNAI-----AMICGNVCL 216
Cdd:cd07098 81 ---LVTCEKIRWTLKHGEKALRPESRPGGLLMFykrarvEYEPLGVVGAIVSWNYP-----FHNLLgpiiaALFAGNAIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 217 WKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLE 296
Cdd:cd07098 153 VKVSEQVAWSSGFFLSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 297 LGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARR----------------------------------------- 335
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERvivhekiydklleiltdrvqalrqgppldgdvdvgamispa 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 336 -------LVMD--------------------RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 388
Cdd:cd07098 313 rfdrleeLVADavekgarllaggkryphpeyPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 982742419 389 QGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNiptsgaEIGGA-------FGGEKHTGGGRESG 445
Cdd:cd07098 393 YGLGASVFGKDIKRARRIA--SQLETGMVAIN------DFGVNyyvqqlpFGGVKGSGFGRFAG 448
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
56-444 |
3.96e-31 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 125.46 E-value: 3.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW-GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSL 134
Cdd:PRK09457 6 NGDWiAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 135 EMGKILVEGVGEVQEYVDicdyAVGLSrmiggpILP-SERSGHALIE--------QWNPVGLVGIITAFNFPVAVYgwNN 205
Cdd:PRK09457 86 ETGKPLWEAATEVTAMIN----KIAIS------IQAyHERTGEKRSEmadgaavlRHRPHGVVAVFGPYNFPGHLP--NG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 206 AI--AMICGNVCLWKGAPTTSlisvAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVG 283
Cdd:PRK09457 154 HIvpALLAGNTVVFKPSELTP----WVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 284 LMVQERFGRSL-LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLV------------------------- 337
Cdd:PRK09457 230 RQFAGQPEKILaLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLvpqgaqgdaflarlvavakrltvgr 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 338 --------------------------------------MDRP---GNYVEPTI--VTGLghdASIAHTETFAPILYVFKF 374
Cdd:PRK09457 310 wdaepqpfmgaviseqaaqglvaaqaqllalggkslleMTQLqagTGLLTPGIidVTGV---AELPDEEYFGPLLQVVRY 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 375 KNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 444
Cdd:PRK09457 387 DDFDEAIRLANNTRFGLSAGLLSDDREDYDQFL--LEIRAGIVNWNKPLTGASSAAPFGGVGASGNHRPS 454
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
56-456 |
5.62e-30 |
|
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: 122.33 E-value: 5.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSWGGRGEVITTYCPANNEPI-ARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSL 134
Cdd:TIGR01238 43 GHSYKADGEAQPVTNPADRRDIvGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 135 EMGKILVEGVGEVQEYVDICDYAVGLSRmiggPILPSERSghalieqwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNV 214
Cdd:TIGR01238 123 EAGKTIHNAIAEVREAVDFCRYYAKQVR----DVLGEFSV--------ESRGVFVCISPWNFPLAIFTGQISAALAAGNT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 215 CLWKGAPTTSLISvavTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERF---G 291
Cdd:TIGR01238 191 VIAKPAEQTSLIA---YRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdapV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTAR---------------------RLVMDRPGNY---VEP 347
Cdd:TIGR01238 268 PLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRvlcvqedvadrvltmiqgamqELKVGVPHLLttdVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 348 TI---------------------VTGLGHDASIA--------------------HTETFAPILYVFKFKNEE--EVFAWN 384
Cdd:TIGR01238 348 VIdaeakqnllahiehmsqtqkkIAQLTLDDSRAcqhgtfvaptlfelddiaelSEEVFGPVLHVVRYKAREldQIVDQI 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 982742419 385 NEVKQGLSSSIFTKDLGRIfRWLgPKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSDAWKQYMRRS 456
Cdd:TIGR01238 428 NQTGYGLTMGVHSRIETTY-RWI-EKHARVGNCYVNRNQVGAVVGvQPFGGQGLSGTGPKAGGPHYLYRLTQV 498
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
60-336 |
1.62e-29 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 122.61 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 60 GGRGEVITTYCPANNE-PIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGK 138
Cdd:PRK11904 558 NGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGK 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 139 ILVEGVGEVQEYVDICD-YAVGLSRMIGGPI-LPSersghalieqwnPVG------LVG-----IITAFNFPVAVYGWNN 205
Cdd:PRK11904 638 TLQDAIAEVREAVDFCRyYAAQARRLFGAPEkLPG------------PTGesnelrLHGrgvfvCISPWNFPLAIFLGQV 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 206 AIAMICGNVCLWKGAPTTSLISVAVTKIiakvLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGL 284
Cdd:PRK11904 706 AAALAAGNTVIAKPAEQTPLIAAEAVKL----LHEAGIPKDVLQLLPGdGATVGAALTADPRIAGVAFTGSTETARIINR 781
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 982742419 285 MVQERFGRSL---LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL 336
Cdd:PRK11904 782 TLAARDGPIVpliAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVL 836
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
71-336 |
2.13e-29 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 122.28 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQE 149
Cdd:PRK11905 574 PADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVRE 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 150 YVDICD-YAVGLSRMIGGPILPsersghalieqwnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLI-S 227
Cdd:PRK11905 654 AVDFLRyYAAQARRLLNGPGHK-------------PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIaA 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 228 VAVtkiiaKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLL---ELGGNNAI 303
Cdd:PRK11905 721 RAV-----RLLHEAGVPKDALQLLPGdGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAM 795
|
250 260 270
....*....|....*....|....*....|...
gi 982742419 304 IAFEDADLSLVVPSALFAAVGTAGQRCTTARRL 336
Cdd:PRK11905 796 IVDSSALPEQVVADVIASAFDSAGQRCSALRVL 828
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
17-467 |
4.12e-29 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 120.62 E-value: 4.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 17 KLSGPWSRPA-----AFMSTLLINQPQYAWLKELGLREENegVYNGSW--GGRGEVITTYCPANNEPIARVRQASVADYE 89
Cdd:PLN02419 77 RISGNNLRPLrpqflALRSSWLSTSPEQSTQPQMPPRVPN--LIGGSFveSQSSSFIDVINPATQEVVSKVPLTTNEEFK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 90 ETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPIL 169
Cdd:PLN02419 155 AAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 170 PSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICS 249
Cdd:PLN02419 235 PNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASV----ILAELAMEAGLPDGVLN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 250 LTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQR 329
Cdd:PLN02419 311 IVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQR 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 330 CTT----------------------------------------------------------ARRLVMD---------RPG 342
Cdd:PLN02419 391 CMAlstvvfvgdakswedklverakalkvtcgsepdadlgpviskqakericrliqsgvddGAKLLLDgrdivvpgyEKG 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 343 NYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD--LGRIFRwlgpKGSDCGIVNVN 420
Cdd:PLN02419 471 NFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSgaAARKFQ----MDIEAGQIGIN 546
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 982742419 421 IPTSGAEIGGAFGGEKHTGGGR-----ESGSDAWKQYmrrSTCTINYsKDLP 467
Cdd:PLN02419 547 VPIPVPLPFFSFTGNKASFAGDlnfygKAGVDFFTQI---KLVTQKQ-KDIH 594
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
63-330 |
3.58e-28 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 118.50 E-value: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 63 GEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILV 141
Cdd:COG4230 569 GEARPVRNPADhSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLP 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 142 EGVGEVQEYVDICD-YAVGLSRMIGGPilpsersghaliEQWNPVGLVGIITAFNFPVA-----VygwnnAIAMICGNVC 215
Cdd:COG4230 649 DAIAEVREAVDFCRyYAAQARRLFAAP------------TVLRGRGVFVCISPWNFPLAiftgqV-----AAALAAGNTV 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 216 LWKGAPTTSLI-SVAVtkiiaKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRS 293
Cdd:COG4230 712 LAKPAEQTPLIaARAV-----RLLHEAGVPADVLQLLPGdGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPI 786
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 982742419 294 LL---ELGGNNAIIafedADLS-L---VVPSALFAAVGTAGQRC 330
Cdd:COG4230 787 VPliaETGGQNAMI----VDSSaLpeqVVDDVLASAFDSAGQRC 826
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
56-402 |
5.29e-27 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 113.31 E-value: 5.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:PLN00412 21 DGEWrtSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 134 LEMGKILVEGVGEVQEYVDICDYAV--GLSRMIGGPILPS------ERSGHALIEQWnPVGLVGIITAFNFPVAVYGWNN 205
Cdd:PLN00412 101 KEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFLVSdsfpgnERNKYCLTSKI-PLGVVLAIPPFNYPVNLAVSKI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 206 AIAMICGNVCLWKgAPTTSliSVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGStqvgkQVGLM 285
Cdd:PLN00412 180 APALIAGNAVVLK-PPTQG--AVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-----DTGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 286 VQERFGRSLL--ELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTAR----------------------------- 334
Cdd:PLN00412 252 ISKKAGMVPLqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKvvlvmesvadalvekvnakvakltvgppe 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 335 ------------------RLVMD-------------RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAW 383
Cdd:PLN00412 332 ddcditpvvsessanfieGLVMDakekgatfcqewkREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHH 411
|
410
....*....|....*....
gi 982742419 384 NNEVKQGLSSSIFTKDLGR 402
Cdd:PLN00412 412 CNASNFGLQGCVFTRDINK 430
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
56-444 |
6.10e-26 |
|
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: 110.23 E-value: 6.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSWGG--RGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07116 6 GGEWVApvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 134 LEMGKILVEGVG-EVQEYVDICDYAVGLSRMIGGPI--LPSERSGHALIEqwnPVGLVGIITAFNFPVAVYGWNNAIAMI 210
Cdd:cd07116 86 WDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSIseIDENTVAYHFHE---PLGVVGQIIPWNFPLLMATWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 211 CGNVCLWKGAPTTSLISVAVTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERF 290
Cdd:cd07116 163 AGNCVVLKPAEQTPASILVLMELIGDLLP----PGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 291 GRSLLELGGNNAIIAFED---ADLSLVVPS----ALFAAvgTAGQRCTTARRLV---------MDRP------------- 341
Cdd:cd07116 239 IPVTLELGGKSPNIFFADvmdADDAFFDKAlegfVMFAL--NQGEVCTCPSRALiqesiydrfMERAlervkaikqgnpl 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 342 ----------------------------------------------GNYVEPTIVTGlGHDASIAHTETFAPILYVFKFK 375
Cdd:cd07116 317 dtetmigaqasleqlekilsyidigkeegaevltggernelggllgGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 982742419 376 NEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRES 444
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRM--GRGIQAGRVWTNcyhlYPA-----HAAFGGYKQSGIGREN 461
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
77-336 |
3.22e-23 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 103.51 E-value: 3.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 77 IARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDY 156
Cdd:PRK11809 673 VGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRY 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 157 AVGLSRmiggpilpsersGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIak 236
Cdd:PRK11809 753 YAGQVR------------DDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRIL-- 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 237 vLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERF---GRS---LLELGGNNAIIAFEDAD 310
Cdd:PRK11809 819 -LEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqGRPiplIAETGGQNAMIVDSSAL 897
|
250 260
....*....|....*....|....*.
gi 982742419 311 LSLVVPSALFAAVGTAGQRCTTARRL 336
Cdd:PRK11809 898 TEQVVADVLASAFDSAGQRCSALRVL 923
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
66-443 |
4.70e-22 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 98.27 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 66 ITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 146 EVQEYVDICDY-----------------AVGLSRmiggpilpsersghALIeQWNPVGLVGIITAFNFPVavygWN---- 204
Cdd:PRK09406 83 EALKCAKGFRYyaehaealladepadaaAVGASR--------------AYV-RYQPLGVVLAVMPWNFPL----WQvvrf 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 205 NAIAMICGNVCLWKGA---PTTSLIsvavtkiIAKVLEDNKLP-GAICSLTCGgADIGTAMAKDERVNLLSFTGSTQVGK 280
Cdd:PRK09406 144 AAPALMAGNVGLLKHAsnvPQTALY-------LADLFRRAGFPdGCFQTLLVG-SGAVEAILRDPRVAAATLTGSEPAGR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 281 QVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLVM---------------------- 338
Cdd:PRK09406 216 AVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVhadvydafaekfvarmaalrvg 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 339 ------------------------------------------DRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKN 376
Cdd:PRK09406 296 dptdpdtdvgplateqgrdevekqvddavaagatilcggkrpDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 982742419 377 EEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEIGgaFGGEKHTGGGRE 443
Cdd:PRK09406 376 IDEAIEIANATTFGLGSNAWTRDEAEQERFI--DDLEAGQVFINgMTVSYPELP--FGGVKRSGYGRE 439
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
71-441 |
1.75e-21 |
|
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: 96.72 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 71 PANNEPIARVRQASVADYEETVKKAREAWKIWAD-IPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQE 149
Cdd:cd07148 6 PFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNwLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 150 YVDICDYAVGLSRMIGGPILP----SERSGHALIEQWNPVGLVGIITAFNFPV--AVYGWNNAIAMICGnvCLWKGAPTT 223
Cdd:cd07148 86 AIDGVELAADELGQLGGREIPmgltPASAGRIAFTTREPIGVVVAISAFNHPLnlIVHQVAPAIAAGCP--VIVKPALAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 224 SLISVAVTKIiakvLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGkqvgLMVQERFG---RSLLELGGN 300
Cdd:cd07148 164 PLSCLAFVDL----LHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVG----WMLRSKLApgtRCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 301 NAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLV----------------------------------------MDR 340
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFvpaeiaddfaqrlaaaaeklvvgdptdpdtevgplirpreVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 341 PGNYVE----------------------PTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTK 398
Cdd:cd07148 316 VEEWVNeavaagarllcggkrlsdttyaPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTK 395
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 982742419 399 DLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGG 441
Cdd:cd07148 396 DLDVALKAV--RRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
184-399 |
7.45e-17 |
|
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: 82.57 E-value: 7.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 184 PVGLVGIITAFNFPV------AVygwnNAIAmiCGNVCLWKG---APTTSlisvavtKIIAKVLEDnKLPGAICSLTCGG 254
Cdd:cd07087 100 PLGVVLIIGPWNYPLqlalapLI----GAIA--AGNTVVLKPselAPATS-------ALLAKLIPK-YFDPEAVAVVEGG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 255 ADIGTAMAKdERVNLLSFTGSTQVGKQVglMvqERFGRSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRC 330
Cdd:cd07087 166 VEVATALLA-EPFDHIFFTGSPAVGKIV--M--EAAAKHLtpvtLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 331 --------------------------------------------TTARRLV-------------MDRPGNYVEPTIVTGL 353
Cdd:cd07087 241 iapdyvlvhesikdelieelkkaikefygedpkespdygriineRHFDRLAsllddgkvviggqVDKEERYIAPTILDDV 320
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 982742419 354 GHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 399
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSED 366
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
95-336 |
2.55e-16 |
|
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: 80.74 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 95 AREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGK--ILVEGVGEVQEYVDICDYAVGLSRMIGGPI--LP 170
Cdd:cd07084 8 ADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKgwMFAENICGDQVQLRARAFVIYSYRIPHEPGnhLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 171 SERSGHALIEQWnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLednKLPGAICSL 250
Cdd:cd07084 88 QGLKQQSHGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAG---LLPPEDVTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 251 TCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQERFGRSLLELGGNNAIIAFEDAD-LSLVVPSALFAAVGTAGQR 329
Cdd:cd07084 164 INGDGKTMQALLLHPNPKMVLFTGSSRVAEK--LALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQK 241
|
....*..
gi 982742419 330 CTTARRL 336
Cdd:cd07084 242 CTAQSML 248
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
184-441 |
4.49e-16 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 80.46 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 184 PVGLVGIITAFNFPV--AVYGWNNAIAmiCGNVCLWKgaptTSLISVAVTKIIAKVLeDNKLPGAICSLTCGGADIGTAM 261
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLnlTLIPLAGAIA--AGNTVVLK----PSELSPHTSKLMAKLL-TKYLDPSYVRVIEGGVEVTTEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 262 AKdERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRC----------- 330
Cdd:PTZ00381 182 LK-EPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCvapdyvlvhrs 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 331 ---------------------------------TTARRLV---------------MDRPGNYVEPTIVTGLGHDASIAHT 362
Cdd:PTZ00381 261 ikdkfiealkeaikeffgedpkksedysrivneFHTKRLAelikdhggkvvyggeVDIENKYVAPTIIVNPDLDSPLMQE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 363 ETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDlGRIFRWLGPKGSDCGIV---------NVNIPtsgaeiggaFG 433
Cdd:PTZ00381 341 EIFGPILPILTYENIDEVLEFINSRPKPLALYYFGED-KRHKELVLENTSSGAVVindcvfhllNPNLP---------FG 410
|
....*...
gi 982742419 434 GEKHTGGG 441
Cdd:PTZ00381 411 GVGNSGMG 418
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
184-399 |
2.95e-15 |
|
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: 77.54 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 184 PVGLVGIITAFNFP-----VAVYGwnnAIAmiCGNVCLWKgaPttSLISVAVTKIIAKVLEDNKLPGAICSLTcGGADIG 258
Cdd:cd07136 100 PYGVVLIIAPWNYPfqlalAPLIG---AIA--AGNTAVLK--P--SELTPNTSKVIAKIIEETFDEEYVAVVE-GGVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 259 TAMAkDERVNLLSFTGSTQVGKqvglMVQERFGRSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTA- 333
Cdd:cd07136 170 QELL-DQKFDYIFFTGSVRVGK----IVMEAAAKHLtpvtLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPd 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 334 -------------------------------------------RRLV-------------MDRPGNYVEPTIVTGLGHDA 357
Cdd:cd07136 245 yvlvhesvkekfikelkeeikkfygedplespdygriinekhfDRLAglldngkivfggnTDRETLYIEPTILDNVTWDD 324
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 982742419 358 SIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 399
Cdd:cd07136 325 PVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSED 366
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
184-399 |
5.32e-14 |
|
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: 73.79 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 184 PVGLVGIITAFNFPV-----AVYGwnnAIAmiCGNVCLWKG---APTTSLIsvaVTKIIAKVLEdnklPGAICSLTCGGA 255
Cdd:cd07135 108 PLGVVLIIGPWNYPVllalsPLVG---AIA--AGCTVVLKPselTPHTAAL---LAELVPKYLD----PDAFQVVQGGVP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 256 DIGTAMakDERVNLLSFTGSTQVGKqvglMVQERFGRSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRC- 330
Cdd:cd07135 176 ETTALL--EQKFDKIFYTGSGRVGR----IIAEAAAKHLtpvtLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICv 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 331 ------------------------------------------------------TTARRLV----MDRPGNYVEPTIVTG 352
Cdd:cd07135 250 apdyvlvdpsvydefveelkkvldefypgganaspdytrivnprhfnrlkslldTTKGKVViggeMDEATRFIPPTIVSD 329
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 982742419 353 LGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 399
Cdd:cd07135 330 VSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDD 376
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
63-399 |
1.48e-12 |
|
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: 69.54 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 63 GEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKI-QVLGSLVSLEMGKIL 140
Cdd:cd07123 45 GNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLGQGKNV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 141 VEGvgEVQEYVDICD-------YAVGLSRMigGPILPSERSGHALieQWNPV-GLVGIITAFNFpVAVYGwNNAIA-MIC 211
Cdd:cd07123 125 WQA--EIDAACELIDflrfnvkYAEELYAQ--QPLSSPAGVWNRL--EYRPLeGFVYAVSPFNF-TAIGG-NLAGApALM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 212 GNVCLWKGAPTTSLISVAVTKIiakvLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQER- 289
Cdd:cd07123 197 GNVVLWKPSDTAVLSNYLVYKI----LEEAGLPpGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENl 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 290 -----FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL---------------------------- 336
Cdd:cd07123 273 dryrtYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAyvpeslwpevkerlleelkeikmgdpdd 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 337 -------VMDRP------------------------------GNYVEPTIVTGLGHDASIAHTETFAPIL--YVFKFKNE 377
Cdd:cd07123 353 fsnfmgaVIDEKafdrikgyidhaksdpeaeiiaggkcddsvGYFVEPTVIETTDPKHKLMTEEIFGPVLtvYVYPDSDF 432
|
410 420
....*....|....*....|...
gi 982742419 378 EEVFAWNNEV-KQGLSSSIFTKD 399
Cdd:cd07123 433 EETLELVDTTsPYALTGAIFAQD 455
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
184-330 |
7.40e-11 |
|
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: 64.04 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 184 PVGLVGIITAFNFPVAVygwnnAIA-MIC----GNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLpgaicSLTCGGADIG 258
Cdd:cd07133 101 PLGVVGIIVPWNYPLYL-----ALGpLIAalaaGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-----AVVTGGADVA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 259 TAMAK---DervNLLsFTGSTQVGKQVglM---------VQerfgrslLELGGNN-AIIAfEDADLSLVVPSALFAAVGT 325
Cdd:cd07133 171 AAFSSlpfD---HLL-FTGSTAVGRHV--MraaaenltpVT-------LELGGKSpAIIA-PDADLAKAAERIAFGKLLN 236
|
....*
gi 982742419 326 AGQRC 330
Cdd:cd07133 237 AGQTC 241
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
181-399 |
2.07e-10 |
|
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: 62.62 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 181 QWNPVGLVGIITAFNFPVA-----VYGwnnAIAmiCGNVCLWKgaPttSLISVAVTKIIAKVLE---DNKLPGAIcsltC 252
Cdd:cd07132 97 YKEPLGVVLIIGAWNYPLQltlvpLVG---AIA--AGNCVVIK--P--SEVSPATAKLLAELIPkylDKECYPVV----L 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 253 GGADIGTAMAKdERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTT 332
Cdd:cd07132 164 GGVEETTELLK-QRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 333 A--------------------------------------------RRLV-------------MDRPGNYVEPTIVTGLGH 355
Cdd:cd07132 243 PdyvlctpevqekfvealkktlkefygedpkespdygriindrhfQRLKkllsggkvaiggqTDEKERYIAPTVLTDVKP 322
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 982742419 356 DASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 399
Cdd:cd07132 323 SDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
184-445 |
2.25e-10 |
|
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: 62.24 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 184 PVGLVGIITAFNFPVA------VYgwnnAIAmiCGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLpgAICSltcGGADI 257
Cdd:cd07134 100 PKGVCLIISPWNYPFNlafgplVS----AIA--AGNTAILKPSELTPHTSAVIAKIIREAFDEDEV--AVFE---GDAEV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 258 GTAmakdervnLLS-------FTGSTQVGKqvglMVQERFGRSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTA 326
Cdd:cd07134 169 AQA--------LLElpfdhifFTGSPAVGK----IVMAAAAKHLasvtLELGGKSPTIVDETADLKKAAKKIAWGKFLNA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 327 GQRC------------------------------TTAR-------RLVMDR---------------------------PG 342
Cdd:cd07134 237 GQTCiapdyvfvhesvkdafvehlkaeiekfygkDAARkaspdlaRIVNDRhfdrlkgllddavakgakvefggqfdaAQ 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 343 NYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGS-DCGI----- 416
Cdd:cd07134 317 RYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSgGVVVndvvl 396
|
330 340 350
....*....|....*....|....*....|.
gi 982742419 417 --VNVNIPtsgaeiggaFGGEKHTGGGRESG 445
Cdd:cd07134 397 hfLNPNLP---------FGGVNNSGIGSYHG 418
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
56-349 |
1.28e-08 |
|
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: 57.28 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSW-GGRGEVITTYCPANNEPIARVRQASVaDYEETVKKAREawkiwadIPAPK--------RGEIVRQIGDALREK-- 124
Cdd:cd07128 6 AGQWhAGTGDGRTLHDAVTGEVVARVSSEGL-DFAAAVAYARE-------KGGPAlraltfheRAAMLKALAKYLMERke 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 125 -----------------------IQVL---GSLVSLEM--GKILVEGVGEVqeyvdicdyavgLSR---MIGGPILpSER 173
Cdd:cd07128 78 dlyalsaatgatrrdswididggIGTLfayASLGRRELpnAHFLVEGDVEP------------LSKdgtFVGQHIL-TPR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 174 SGHALIeqwnpvglvgiITAFNFPVavygW----NNAIAMICGNVCLWKGAPTTSLISVAVTKIIakvLEDNKLP-GAIc 248
Cdd:cd07128 145 RGVAVH-----------INAFNFPV----WgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDI---VESGLLPeGAL- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 249 SLTCGGAdiGTAMAKDERVNLLSFTGSTQVGKQVGLM--VQERFGRSLLELGGNNAIIAFEDA-----DLSLVVPSALFA 321
Cdd:cd07128 206 QLICGSV--GDLLDHLGEQDVVAFTGSAATAAKLRAHpnIVARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVARE 283
|
330 340
....*....|....*....|....*...
gi 982742419 322 AVGTAGQRCTTARRLVMdrPGNYVEPTI 349
Cdd:cd07128 284 MTVKAGQKCTAIRRAFV--PEARVDAVI 309
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
184-445 |
2.08e-07 |
|
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: 53.18 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 184 PVGLVGIITAFNFPVA-----VYGwnnAIAmiCGNVCLWKgaptTSLISVAVTKIIAKVLEDNKLPGAIcSLTCGGADIG 258
Cdd:cd07137 101 PLGVVLVISAWNFPFLlslepVIG---AIA--AGNAVVLK----PSELAPATSALLAKLIPEYLDTKAI-KVIEGGVPET 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 259 TAMAkDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGT-AGQRCTT----- 332
Cdd:cd07137 171 TALL-EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIApdyvl 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 333 ------------------------------ARRLV--------------------------MDRPGNYVEPTIVTGLGHD 356
Cdd:cd07137 250 veesfaptlidalkntlekffgenpkeskdLSRIVnshhfqrlsrllddpsvadkivhggeRDEKNLYIEPTILLDPPLD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 357 ASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT--KDLGRIFRWLGPKGS----DCgIVNVNIPTSgaeigg 430
Cdd:cd07137 330 SSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTknKELKRRIVAETSSGGvtfnDT-VVQYAIDTL------ 402
|
330
....*....|....*
gi 982742419 431 AFGGEKHTGGGRESG 445
Cdd:cd07137 403 PFGGVGESGFGAYHG 417
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
184-332 |
5.37e-06 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 48.89 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 184 PVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKgaptTSLISVAVTKIIAKVLEDNKLPGAICSLTcgGADIGTAMAK 263
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLK----PSELAPASSALLAKLLEQYLDSSAVRVVE--GAVTETTALL 185
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 264 DERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVG-TAGQRCTT 332
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACIS 255
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
56-369 |
9.30e-06 |
|
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: 47.88 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 56 NGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWK--IWADIPAPKR----GEIVRQIGDALReKIQV-- 127
Cdd:cd07126 4 AGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKsgLHNPLKNPERyllyGDVSHRVAHELR-KPEVed 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 128 -LGSLVSLEMGKILVEGVGEV---QEYV-----DICDYavgLSR--MIGGPILPSERSGHalieQWnPVGLVGIITAFNF 196
Cdd:cd07126 83 fFARLIQRVAPKSDAQALGEVvvtRKFLenfagDQVRF---LARsfNVPGDHQGQQSSGY----RW-PYGPVAIITPFNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 197 PVAVYGWNNAIAMICGNVCLWKGaptTSLISVAVTKIIaKVLEDNKLPGAICSLT-CGGADIGTAMaKDERVNLLSFTGS 275
Cdd:cd07126 155 PLEIPALQLMGALFMGNKPLLKV---DSKVSVVMEQFL-RLLHLCGMPATDVDLIhSDGPTMNKIL-LEANPRMTLFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 276 TQVGKQVGLMVQerfGRSLLELGGNNAIIAFED-ADLSLVVPSALFAAVGTAGQRCTTARRLVMDRpgNYVEPTIVTGLG 354
Cdd:cd07126 230 SKVAERLALELH---GKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHE--NWVQAGILDKLK 304
|
330
....*....|....*..
gi 982742419 355 HDASIAHTE--TFAPIL 369
Cdd:cd07126 305 ALAEQRKLEdlTIGPVL 321
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
184-331 |
1.42e-05 |
|
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: 47.15 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 184 PVGLVGIITAFNFPVA--VYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSL-TCGGADIGTA 260
Cdd:cd07129 105 PLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAALRATGLPAGVFSLlQGGGREVGVA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 261 MAKDERVNLLSFTGSTQVGKQVGLMVQER------FGrsllELGGNNAIIafedadlslVVPSAL----------FAA-- 322
Cdd:cd07129 185 LVKHPAIKAVGFTGSRRGGRALFDAAAARpepipfYA----ELGSVNPVF---------ILPGALaergeaiaqgFVGsl 251
|
....*....
gi 982742419 323 VGTAGQRCT 331
Cdd:cd07129 252 TLGAGQFCT 260
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
191-335 |
1.31e-03 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 41.23 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742419 191 ITAFNFPVavYG-WNNA-IAMICGNVCLWKGAPTTSLISvavTKIIAKVLEDNKLPGAICSLTCGGAdiGTAMAKDERVN 268
Cdd:PRK11903 155 INAFNFPA--WGlWEKAaPALLAGVPVIVKPATATAWLT---QRMVKDVVAAGILPAGALSVVCGSS--AGLLDHLQPFD 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 982742419 269 LLSFTGSTQVGKQVGLM--VQERFGRSLLELGGNNAIIAFEDADLSlvvpSALFAAVG---------TAGQRCTTARR 335
Cdd:PRK11903 228 VVSFTGSAETAAVLRSHpaVVQRSVRVNVEADSLNSALLGPDAAPG----SEAFDLFVkevvremtvKSGQKCTAIRR 301
|
|
| |
