|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
57-531 |
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: 970.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 57 GVYNGSWGGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLV 136
Cdd:cd07130 1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 137 SLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICG 216
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 217 NVCLWKGAPTTSLTSVAVTKIIAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGR 296
Cdd:cd07130 161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 297 CLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPL 376
Cdd:cd07130 241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 377 HTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIViELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVK 456
Cdd:cd07130 321 HTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVP 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841878009 457 QGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGRESGSDSWKQYMRRSTCTINYS 531
Cdd:cd07130 400 QGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
57-531 |
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: 901.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 57 GVYNGSWGGRG-EIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNL 135
Cdd:cd07086 1 GVIGGEWVGSGgETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 136 VSLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALIC 215
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 216 GNVCLWKGAPTTSLTSVAVTKIIAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFG 295
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 296 RCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGP 375
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 376 LHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIER--PGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNN 453
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841878009 454 GVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGRESGSDSWKQYMRRSTCTINYS 531
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
42-543 |
0e+00 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 741.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 42 QYAWLKELGLREENEGVY-NGSWGGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQ 120
Cdd:PLN02315 7 EYEFLSEIGLSSRNLGCYvGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 121 IGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNF 200
Cdd:PLN02315 87 IGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 201 PVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAVTKIIAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGST 280
Cdd:PLN02315 167 PCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 281 NVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQ 360
Cdd:PLN02315 247 KVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 361 VRIGDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIViELPHNSSIVHTETFAPILYVL 440
Cdd:PLN02315 327 VKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 441 KFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGRESGSDSWKQY 520
Cdd:PLN02315 406 KFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQY 485
|
490 500
....*....|....*....|...
gi 1841878009 521 MRRSTCTINYSKDLPLAQGIKFN 543
Cdd:PLN02315 486 MRRSTCTINYGNELPLAQGINFG 508
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
93-528 |
2.63e-167 |
|
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: 480.94 E-value: 2.63e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 93 EETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPM 172
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 173 LPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAVTKIIAQVLeknkLPGAIC 252
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAG----LPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 253 SLACGGAD-IGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAG 331
Cdd:cd07078 157 NVVTGDGDeVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 332 QRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIER-PG 410
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 411 NYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIP 490
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVA--ERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 1841878009 491 TSGAEIGGAFGGNKHTGGGRESGSDSWKQYMRRSTCTI 528
Cdd:cd07078 395 SVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
65-525 |
4.87e-163 |
|
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: 471.25 E-value: 4.87e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 65 GRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIF 144
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 145 VEGVGEVQEYVDICDYAVGLSRMFGGPMLPSeRPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGA 224
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 225 PTTSLTSVAVTKIIAQVleknKLP-GAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGG 303
Cdd:pfam00171 163 ELTPLTALLLAELFEEA----GLPaGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 304 NNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVK 383
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 384 MFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSI 463
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841878009 464 FTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGRESGSDSWKQYMRRST 525
Cdd:pfam00171 399 FTSDLERALRVA--RRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
60-530 |
1.96e-162 |
|
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: 470.38 E-value: 1.96e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVS 137
Cdd:COG1012 11 GGEWvaAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 138 LEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGN 217
Cdd:COG1012 91 LETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 218 VCLWKGAPTTSLTSVAVTKIIAQVleknKLP-GAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGR 296
Cdd:COG1012 171 TVVLKPAEQTPLSALLLAELLEEA----GLPaGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 297 CLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPL 376
Cdd:COG1012 247 VTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 377 HTKQAVKMFLDAVEVAKQQGGSVVCGGKVIER-PGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGV 455
Cdd:COG1012 327 ISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDT 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841878009 456 KQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGRESGSDSWKQYMRRSTCTINY 530
Cdd:COG1012 407 EYGLAASVFTRDLARARRVA--RRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
60-531 |
1.14e-130 |
|
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: 389.40 E-value: 1.14e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSWGGR--GEIVTTYCPAN-NQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLV 136
Cdd:cd07131 4 GGEWVDSasGETFDSRNPADlEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 137 SLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICG 216
Cdd:cd07131 84 TREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 217 NVCLWKGAPTTSltsvAVTKIIAQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFG 295
Cdd:cd07131 164 NTVVFKPAEDTP----ACALKLVELFAEAGLPPGVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 296 RCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGP 375
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 376 LHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIER----PGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGW 451
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 452 NNGVKQGLSSSIFTKDLGRIFRWLGpkgsDC--GIVNVNIPTSGAEIGGAFGGNKHTGGG-RESGSDSWKQYMRRSTCTI 528
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARR----DLeaGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
...
gi 1841878009 529 NYS 531
Cdd:cd07131 476 DYS 478
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
97-528 |
1.57e-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: 371.95 E-value: 1.57e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 97 KKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSE 176
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 177 RPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAVTKIIAQVLeknkLPGAICSLAC 256
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG----LPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 257 GGAD-IGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCT 335
Cdd:cd06534 157 GGGDeVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 336 TSRRLFLHESIHDEVVEKLMkayaqvrigdpwdantlygplhtkqavkmfldavevakqqggsvvcggkvierpgnyvep 415
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV------------------------------------------------------------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 416 TIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAE 495
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVA--ERLRAGTVYINDSSIGVG 334
|
410 420 430
....*....|....*....|....*....|...
gi 1841878009 496 IGGAFGGNKHTGGGRESGSDSWKQYMRRSTCTI 528
Cdd:cd06534 335 PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
56-515 |
5.80e-116 |
|
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: 351.55 E-value: 5.80e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 56 EGVYNGSWGGRGEIVTTYCPAN-NQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGN 134
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 135 LVSLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALI 214
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 215 CGNVCLWKGAPTTSLTSVAVTKIIAQVleknKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQER 293
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEA----GLPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 294 FGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLY 373
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 374 GPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERP--GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGW 451
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841878009 452 NNGVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGNKHTG-GGRESGSD 515
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFK--RRVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEA 460
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
75-521 |
4.84e-106 |
|
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: 325.16 E-value: 4.84e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVqey 154
Cdd:cd07103 4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 155 vdicDYAVGLSRMFG-------GPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTT 227
Cdd:cd07103 81 ----DYAASFLEWFAeearriyGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 228 SLTSVAvtkiIAQVLEKNKLP-GAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQV----ALTVQerfgRCLLELG 302
Cdd:cd07103 157 PLSALA----LAELAEEAGLPaGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLmaqaADTVK----RVSLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 303 GNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAV 382
Cdd:cd07103 229 GNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 383 KMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSS 462
Cdd:cd07103 309 EKVEALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAY 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 463 IFTKDLGRIFRwLGpKGSDCGIVNVNIPT-SGAEIggAFGGNKHTGGGRESGSDSWKQYM 521
Cdd:cd07103 389 VFTRDLARAWR-VA-EALEAGMVGINTGLiSDAEA--PFGGVKESGLGREGGKEGLEEYL 444
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
67-473 |
7.58e-101 |
|
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: 312.28 E-value: 7.58e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 67 GEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVE 146
Cdd:cd07088 12 GETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 147 GVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPT 226
Cdd:cd07088 92 ARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 227 TSLTSVAvtkiIAQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNN 305
Cdd:cd07088 172 TPLNALE----FAELVDEAGLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 306 AIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMF 385
Cdd:cd07088 248 PAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 386 LDAVEVAKQQGGSVVCGGKVIE-RPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIF 464
Cdd:cd07088 328 EEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIY 407
|
....*....
gi 1841878009 465 TKDLGRIFR 473
Cdd:cd07088 408 TENLNTAMR 416
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
75-522 |
7.99e-99 |
|
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: 306.78 E-value: 7.99e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAW--QIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQ 152
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 153 EYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSV 232
Cdd:cd07114 84 YLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 233 AVTKIIAQ------VLekNKLPGaicslacGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNA 306
Cdd:cd07114 164 ELAKLAEEagfppgVV--NVVTG-------FGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 307 IIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFL 386
Cdd:cd07114 235 NIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 387 DAVEVAKQQGGSVVCGGKVIERP----GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSS 462
Cdd:cd07114 315 RYVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841878009 463 IFTKDLGRIFRWlgPKGSDCGIVNVNI-----PTSgaeiggAFGGNKHTGGGRESGSDSWKQYMR 522
Cdd:cd07114 395 IWTRDLARAHRV--ARAIEAGTVWVNTyralsPSS------PFGGFKDSGIGRENGIEAIREYTQ 451
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
75-520 |
2.95e-96 |
|
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: 300.12 E-value: 2.95e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVG-EVQE 153
Cdd:cd07115 4 PATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 154 YVDICDYAVGLSRMFGGPMLPSeRPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVA 233
Cdd:cd07115 84 AADTFRYYAGWADKIEGEVIPV-RGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 234 VTKIIAQVleknKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFED 312
Cdd:cd07115 163 IAELMAEA----GFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 313 ADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVEVA 392
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 393 KQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIF 472
Cdd:cd07115 319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1841878009 473 RWlgPKGSDCGIVNVNipTSGA-EIGGAFGGNKHTGGGRESGSDSWKQY 520
Cdd:cd07115 399 RV--AAALKAGTVWIN--TYNRfDPGSPFGGYKQSGFGREMGREALDEY 443
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
75-525 |
2.03e-94 |
|
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: 294.82 E-value: 2.03e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEY 154
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 155 VDICDYAVGLSrmfggpmLPSER----PGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLT 230
Cdd:cd07106 84 VAWLRYTASLD-------LPDEVieddDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 231 SVAVTKIIAQVLeknklPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVF 310
Cdd:cd07106 157 TLKLGELAQEVL-----PPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 311 EDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQ---AVKMFLD 387
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMqydKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 388 AvevAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKD 467
Cdd:cd07106 312 D---AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSD 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 468 LGRIFRwLGPKgSDCGIVNVNiptSGAEIGGA--FGGNKHTGGGRESGSDSWKQYMRRST 525
Cdd:cd07106 389 LERAEA-VARR-LEAGTVWIN---THGALDPDapFGGHKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
91-520 |
6.43e-94 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 293.28 E-value: 6.43e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 91 DYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGG 170
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 171 PMLPSERPGhalieQWN-----PLGLVGIITAFNFPV-----AVygwnnAIALICGNVCLWKGAPTTsltsvAVTK--II 238
Cdd:cd07104 81 EILPSDVPG-----KESmvrrvPLGVVGVISPFNFPLilamrSV-----APALALGNAVVLKPDSRT-----PVTGglLI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 239 AQVLEKNKLP-GAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNL 317
Cdd:cd07104 146 AEIFEEAGLPkGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 318 VIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQGG 397
Cdd:cd07104 226 AVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 398 SVVCGGKvieRPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRwLGp 477
Cdd:cd07104 306 RLLTGGT---YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMA-FA- 380
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1841878009 478 KGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGRESGSDSWKQY 520
Cdd:cd07104 381 ERLETGMVHINDQTVNDEPHVPFGGVKASGGGRFGGPASLEEF 423
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
75-516 |
2.53e-91 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 287.30 E-value: 2.53e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEY 154
Cdd:cd07150 6 PADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 155 VDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVav 234
Cdd:cd07150 86 PELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 235 tkIIAQVLEKNKLP-GAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDA 313
Cdd:cd07150 164 --KIAEIMEEAGLPkGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 314 DLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVEVAK 393
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 394 QQGGSVVCGGKvieRPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFR 473
Cdd:cd07150 322 AKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFK 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1841878009 474 WlgPKGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGRESGSDS 516
Cdd:cd07150 399 L--AERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWS 439
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
72-516 |
9.66e-90 |
|
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: 283.30 E-value: 9.66e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 72 TYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGev 151
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 152 qeyVDI----------CDYAVGLsrmfGGPMLPSErPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLW 221
Cdd:cd07093 79 ---RDIpraaanfrffADYILQL----DGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 222 KGAPTTSLTSVavtkIIAQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLE 300
Cdd:cd07093 151 KPSEWTPLTAW----LLAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 301 LGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQ 380
Cdd:cd07093 227 LGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 381 AVKMFLDAVEVAKQQGGSVVCGGKVIERP----GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVK 456
Cdd:cd07093 307 HLEKVLGYVELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTP 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841878009 457 QGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN------IPTsgaeiggAFGGNKHTGGGRESGSDS 516
Cdd:cd07093 387 YGLAAYVWTRDLGRAHRV--ARRLEAGTVWVNcwlvrdLRT-------PFGGVKASGIGREGGDYS 443
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
75-522 |
1.56e-88 |
|
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: 279.98 E-value: 1.56e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGV-GEVQE 153
Cdd:cd07092 4 PATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 154 YVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVA 233
Cdd:cd07092 84 AVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 234 VTKIIAQVLEknklPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDA 313
Cdd:cd07092 164 LAELAAEVLP----PGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 314 DLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVEVAK 393
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 394 qQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFR 473
Cdd:cd07092 320 -AHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1841878009 474 WLGPKGSDCGIVNVNIPTSgAEIggAFGGNKHTGGGRESGSDSWKQYMR 522
Cdd:cd07092 399 LSARLDFGTVWVNTHIPLA-AEM--PHGGFKQSGYGKDLSIYALEDYTR 444
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
70-512 |
2.44e-87 |
|
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: 276.92 E-value: 2.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 70 VTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVG 149
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 150 EVQEYVDICDYAVGLSRMFGGPMLPSE----RPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAP 225
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 226 TTSLTSVAVTKIIaqvlEKNKLP-GAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGN 304
Cdd:cd07145 161 NTPLTAIELAKIL----EEAGLPpGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 305 NAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKM 384
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 385 FLDAVEVAKQQGGSVVCGGKVIErpGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIF 464
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1841878009 465 TKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGRES 512
Cdd:cd07145 395 TNDINRALKV--ARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREG 440
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
75-530 |
1.78e-86 |
|
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: 274.64 E-value: 1.78e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEY 154
Cdd:cd07107 4 PATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 155 VDICDYAVGLSRMFGGPMLPSErPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAV 234
Cdd:cd07107 84 AALLDYFAGLVTELKGETIPVG-GRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 235 TKIIAQVLEknklPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDAD 314
Cdd:cd07107 163 AELAREVLP----PGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 315 LNLVIPSALFAA-VGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVEVAK 393
Cdd:cd07107 239 PEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 394 QQGGSVVCGGKVIERP----GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLG 469
Cdd:cd07107 319 REGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841878009 470 RIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGNKHTGGGRESGSDSWKQYMRRSTCTINY 530
Cdd:cd07107 399 QAHR--TARRVEAGYVWIN-GSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
58-530 |
4.29e-86 |
|
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: 275.64 E-value: 4.29e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 58 VYNGSWGGRGEIVTTYCPAN-NQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLV 136
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 137 SLEMGKIFVEGVGEVQEYVDICD-YAVGLSRMFGGP--MLPSERPGHALIeqwnPLGLVGIITAFNFPVAVYGWNNAIAL 213
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEyYAREMLRLRGFPveMVPGEDNRYVYR----PLGVGAVISPWNFPLAILAGMTTAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 214 ICGNVCLWKGAPTTSLtsvaVTKIIAQVLEKNKLP-GAICSLACGGADIGTAMAKDERIDLLSFTGSTNVG---KQVALT 289
Cdd:cd07124 192 VTGNTVVLKPAEDTPV----IAAKLVEILEEAGLPpGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGlriYERAAK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 290 VQERFG---RCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDP 366
Cdd:cd07124 268 VQPGQKwlkRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 367 WDANTLYGPLHTKQAVKMFLDAVEVAKqQGGSVVCGGKVIERP--GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKT 444
Cdd:cd07124 348 EDPEVYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 445 EEEVFGWNNGVKQGLSSSIFTKDLGRI--FRwlgpKGSDCGIVNVNIPTSGAEIG-GAFGGNKHTG-GGRESGSDSWKQY 520
Cdd:cd07124 427 FDEALEIANDTEYGLTGGVFSRSPEHLerAR----REFEVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDYLLQF 502
|
490
....*....|
gi 1841878009 521 MRRSTCTINY 530
Cdd:cd07124 503 MQPKTVTENF 512
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
61-513 |
1.43e-85 |
|
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: 272.64 E-value: 1.43e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 61 GSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVR---QIGDALRDKIkvlGNL 135
Cdd:cd07151 1 GEWrdGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEkaaQILEERRDEI---VEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 136 VSLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALIC 215
Cdd:cd07151 78 LIRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 216 GNVCLWKGAPTTSLTSvavTKIIAQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERF 294
Cdd:cd07151 158 GNAVVLKPASDTPITG---GLLLAKIFEEAGLPKGVLNVVVGaGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 295 GRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYG 374
Cdd:cd07151 235 KKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 375 PLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVierPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNG 454
Cdd:cd07151 315 PLINESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1841878009 455 VKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGRESG 513
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQF--ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNG 448
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
73-521 |
3.58e-85 |
|
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: 271.42 E-value: 3.58e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 73 YCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWA-EIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGK-IFVEGVGE 150
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGApVMTARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 151 VQEYVDICDYAVGLSRMF------GGPMLPSErPGHALIEQwNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGA 224
Cdd:cd07089 82 VDGPIGHLRYFADLADSFpwefdlPVPALRGG-PGRRVVRR-EPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 225 PTTSLTSVAVTKIIAqvlEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGN 304
Cdd:cd07089 160 PDTPLSALLLGEIIA---ETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 305 NAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKM 384
Cdd:cd07089 237 SANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 385 FLDAVEVAKQQGGSVVCGGkviERP-----GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGL 459
Cdd:cd07089 317 VEGYIARGRDEGARLVTGG---GRPagldkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841878009 460 SSSIFTKDLGR---IFRWLgpkgsDCGIVNVNiPTSGAEIGGAFGGNKHTGGGRESGSDSWKQYM 521
Cdd:cd07089 394 SGGVWSADVDRayrVARRI-----RTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
60-521 |
6.12e-85 |
|
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: 271.49 E-value: 6.12e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQ--IWAEIPAPKRGEIVRQIGDALRDKIKVLGNL 135
Cdd:cd07119 3 DGEWveAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDsgEWPHLPAQERAALLFRIADKIREDAEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 136 VSLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQwNPLGLVGIITAFNFPVAVYGWNNAIALIC 215
Cdd:cd07119 83 ETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVR-EPVGVCGLITPWNYPLLQAAWKLAPALAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 216 GNVCLWKGAPTTSLTSVAVTKIIAQVleknKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERF 294
Cdd:cd07119 162 GNTVVIKPSEVTPLTTIALFELIEEA----GLPAGVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 295 GRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYG 374
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 375 PLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERP----GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFG 450
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841878009 451 WNNGVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN---IPTSGAEiggaFGGNKHTGGGRESGSDSWKQYM 521
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVA--RRLRAGTVWINdyhPYFAEAP----WGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
72-522 |
7.68e-85 |
|
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: 270.33 E-value: 7.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 72 TYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEV 151
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 152 QEYVDICDYAVGLSRMFGGPM--LPSERPGHALIEqwnPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSL 229
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHvpLPGGSFAYTRRE---PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 230 TSVavtkIIAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIV 309
Cdd:cd07090 158 TAL----LLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 310 FEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAV 389
Cdd:cd07090 234 FDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 390 EVAKQQGGSVVCGGKVIE-----RPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIF 464
Cdd:cd07090 314 ESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVF 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1841878009 465 TKDLGRIFRWLGP-KGSDCGIVNVNIptSGAEIggAFGGNKHTGGGRESGSDSWKQYMR 522
Cdd:cd07090 394 TRDLQRAHRVIAQlQAGTCWINTYNI--SPVEV--PFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
73-522 |
5.17e-84 |
|
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: 268.32 E-value: 5.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 73 YCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQ 152
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 153 EYVDICDYAVGL-------SRMFGGPMLPserpGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAP 225
Cdd:cd07099 81 LALEAIDWAARNaprvlapRKVPTGLLMP----NKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 226 TTSLTSVAVTKIIAQVLeknkLPGAICSLACGGADIGTAMAkDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNN 305
Cdd:cd07099 157 VTPLVGELLAEAWAAAG----PPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 306 AIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMF 385
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 386 LDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFT 465
Cdd:cd07099 312 RRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841878009 466 KDL---GRIFRWLgpkgsDCGIVNVNIPTSGAEIGGA-FGGNKHTGGGRESGSDSWKQYMR 522
Cdd:cd07099 392 RDLaraEAIARRL-----EAGAVSINDVLLTAGIPALpFGGVKDSGGGRRHGAEGLREFCR 447
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
93-511 |
3.15e-83 |
|
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: 265.48 E-value: 3.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 93 EETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEYVDICD-YAVGLSRMfggp 171
Cdd:cd07100 2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRyYAENAEAF---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 172 MLPSERP---GHALIeQWNPLGLVGIITAFNFP---VAVYGwnnAIALICGNVCLWKGAPTTSLTSVAvtkiIAQVLEKN 245
Cdd:cd07100 78 LADEPIEtdaGKAYV-RYEPLGVVLGIMPWNFPfwqVFRFA---APNLMAGNTVLLKHASNVPGCALA----IEELFREA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 246 KLP-GAICSLACGGADIGTAMAkDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALF 324
Cdd:cd07100 150 GFPeGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 325 AAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGK 404
Cdd:cd07100 229 GRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 405 VIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLG---RIFRWLgpkgsD 481
Cdd:cd07100 309 RPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLEraeRVARRL-----E 383
|
410 420 430
....*....|....*....|....*....|.
gi 1841878009 482 CGIVNVNIPT-SGAEIggAFGGNKHTGGGRE 511
Cdd:cd07100 384 AGMVFINGMVkSDPRL--PFGGVKRSGYGRE 412
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
60-528 |
5.02e-83 |
|
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: 266.38 E-value: 5.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQI--WAEIPAPKRGEIVRQIGDALRDKIKVLGNL 135
Cdd:cd07091 9 NNEFvdSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 136 VSLEMGKIFVEG-VGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQwNPLGLVGIITAFNFPVAVYGWNNAIALI 214
Cdd:cd07091 89 ESLDNGKPLEESaKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRR-EPIGVCGQIIPWNFPLLMLAWKLAPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 215 CGNVCLWKGAPTTSLTSVAVtkiiAQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVA-LTVQE 292
Cdd:cd07091 168 AGNTVVLKPAEQTPLSALYL----AELIKEAGFPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIMeAAAKS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 293 RFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTL 372
Cdd:cd07091 244 NLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 373 YGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWN 452
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 453 NGVKQGLSSSIFTKDLGRIFR----------WLgpkgsDC-GIVNVNIPtsgaeiggaFGGNKHTGGGRESGSDSWKQYM 521
Cdd:cd07091 404 NDTEYGLAAGVFTKDINKALRvsralkagtvWV-----NTyNVFDAAVP---------FGGFKQSGFGRELGEEGLEEYT 469
|
....*..
gi 1841878009 522 RRSTCTI 528
Cdd:cd07091 470 QVKAVTI 476
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
75-528 |
1.23e-82 |
|
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: 264.48 E-value: 1.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWA-EIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQE 153
Cdd:cd07109 4 PSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 154 YVDICDYAVGLSRMFGGPMLPSErPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVA 233
Cdd:cd07109 84 AARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 234 vtkiIAQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFED 312
Cdd:cd07109 163 ----LAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 313 ADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGdPWDANTLYGPLHTKQAVKMFLDAVEVA 392
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 393 KQQGGSVVCGGKVIERP---GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLG 469
Cdd:cd07109 318 RARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1841878009 470 RIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGRESGSDSWKQYMRRSTCTI 528
Cdd:cd07109 398 RALRV--ARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
39-521 |
3.48e-82 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 265.02 E-value: 3.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 39 NQAQYAWLKELGLREeNEGVYNGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGE 116
Cdd:PLN02278 10 AQSALVKLRNAGLLR-TQGLIGGKWtdAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 117 IVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIIT 196
Cdd:PLN02278 89 ILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAIT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 197 AFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAVtkiiAQVLEKNKLPGAICSLACGGA-DIGTAMAKDERIDLLS 275
Cdd:PLN02278 169 PWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAA----AELALQAGIPPGVLNVVMGDApEIGDALLASPKVRKIT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 276 FTGSTNVGK----QVALTVQerfgRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVV 351
Cdd:PLN02278 245 FTGSTAVGKklmaGAAATVK----RVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 352 EKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTE 431
Cdd:PLN02278 321 EAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 432 TFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN---IPTSGAeiggAFGGNKHTGG 508
Cdd:PLN02278 401 VFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRV--SEALEYGIVGVNeglISTEVA----PFGGVKQSGL 474
|
490
....*....|...
gi 1841878009 509 GRESGSDSWKQYM 521
Cdd:PLN02278 475 GREGSKYGIDEYL 487
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
73-511 |
3.23e-81 |
|
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: 261.03 E-value: 3.23e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 73 YCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQ 152
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 153 EYVDICDYAVGLSRMFGGPMLP---SER-PGH-ALIEQWnPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTT 227
Cdd:cd07147 84 RAIDTFRIAAEEATRIYGEVLPldiSARgEGRqGLVRRF-PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 228 SLTSVavtkIIAQVLEKNKLP-GAICSLACGgADIGTAMAKDERIDLLSFTGSTNVGkqvaLTVQERFGR--CLLELGGN 304
Cdd:cd07147 163 PLSAL----ILGEVLAETGLPkGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVG----WDLKARAGKkkVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 305 NAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKM 384
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 385 FLDAVEVAKQQGGSVVCGGKvieRPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIF 464
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1841878009 465 TKDLGRIFR-WlgpKGSDCGIVNVN-IPTSGAEiGGAFGGNKHTGGGRE 511
Cdd:cd07147 391 TRDLEKALRaW---DELEVGGVVINdVPTFRVD-HMPYGGVKDSGIGRE 435
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
75-511 |
7.60e-81 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 259.99 E-value: 7.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGK-IFVEGVGEVQE 153
Cdd:cd07108 4 PATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNaLRTQARPEAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 154 YVDICDYAVGLSRMFGGPMLPSeRPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVA 233
Cdd:cd07108 84 LADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 234 VTKIIAQVLeknklPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFED 312
Cdd:cd07108 163 LAEILAQVL-----PAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 313 ADLNLVIPSALFAAVGT-AGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVEV 391
Cdd:cd07108 238 ADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 392 AKQ-QGGSVVCGGK----VIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTK 466
Cdd:cd07108 318 GLStSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1841878009 467 DLGRIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGNKHTGGGRE 511
Cdd:cd07108 398 DLGRALR--AAHALEAGWVQVN-QGGGQQPGQSYGGFKQSGLGRE 439
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
73-511 |
1.40e-80 |
|
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: 259.45 E-value: 1.40e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 73 YCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQ 152
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 153 EYVDICDYAVGLSRMFGGPMLPSE-------RPGHALIEqwnPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAP 225
Cdd:cd07149 84 RAIETLRLSAEEAKRLAGETIPFDaspggegRIGFTIRE---PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 226 TTSLTSVAvtkiIAQVLEKNKLPGAICSLACGGAD-IGTAMAKDERIDLLSFTGSTNVGKQVALTVQERfgRCLLELGGN 304
Cdd:cd07149 161 QTPLSALK----LAELLLEAGLPKGALNVVTGSGEtVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--KVTLELGSN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 305 NAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKM 384
Cdd:cd07149 235 AAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 385 FLDAVEVAKQQGGSVVCGGKvieRPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIF 464
Cdd:cd07149 315 IEEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1841878009 465 TKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEiGGAFGGNKHTGGGRE 511
Cdd:cd07149 392 TNDLQKALKAA--RELEVGGVMINdSSTFRVD-HMPYGGVKESGTGRE 436
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
60-512 |
1.06e-79 |
|
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: 257.77 E-value: 1.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVS 137
Cdd:cd07117 6 NGEWvkGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 138 LEMGKIFVEGVGevqeyVDIcDYAVGLSRMFGGPMLPSERPGHALIEQW------NPLGLVGIITAFNFPVAVYGWNNAI 211
Cdd:cd07117 86 LDNGKPIRETRA-----VDI-PLAADHFRYFAGVIRAEEGSANMIDEDTlsivlrEPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 212 ALICGNVCLWKGAPTTSLTSVAVTKIIAQVLEKnklpGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQ 291
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPK----GVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 292 ERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANT 371
Cdd:cd07117 236 KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 372 LYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGG-KVIERP---GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEE 447
Cdd:cd07117 316 QMGAQVNKDQLDKILSYVDIAKEEGAKILTGGhRLTENGldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDE 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841878009 448 VFGWNNGVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGNKHTGGGRES 512
Cdd:cd07117 396 VIDMANDSEYGLGGGVFTKDINRALRV--ARAVETGRVWVNtynqIPA-----GAPFGGYKKSGIGRET 457
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
75-528 |
1.16e-79 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 256.88 E-value: 1.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQI--WAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQ 152
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 153 EYVDICDYAVGLSRMFGGPM---LPSERPGHALIEqwnPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSL 229
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSynnLGDDMLGLVLRE---PIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 230 TSVavtkIIAQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAII 308
Cdd:cd07118 161 TTL----MLAELLIEAGLPAGVVNIVTGyGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 309 VFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDA 388
Cdd:cd07118 237 VFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 389 VEVAKQQGGSVVCGGKVIE-RPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKD 467
Cdd:cd07118 317 VDAGRAEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841878009 468 LGRIFrwLGPKGSDCGIVNVN-IPTSGAEIggAFGGNKHTGGGRESGSDSWKQYMRRSTCTI 528
Cdd:cd07118 397 IDTAL--TVARRIRAGTVWVNtFLDGSPEL--PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
60-522 |
1.31e-79 |
|
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: 257.42 E-value: 1.31e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQI--WAEIPAPKRGEIVRQIGDALRDKIKVLGNL 135
Cdd:cd07142 9 NGQFvdAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 136 VSLEMGKIFVEG-VGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHA--LIEqwnPLGLVGIITAFNFPVAVYGWNNAIA 212
Cdd:cd07142 89 ETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVytLHE---PIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 213 LICGNVCLWKGAPTTSLTSVAVTKIIAQVleknKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVA-LTV 290
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEA----GLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMqLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 291 QERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDAN 370
Cdd:cd07142 242 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 371 TLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFG 450
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841878009 451 WNNGVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIpTSGAEIGGAFGGNKHTGGGRESGSDSWKQYMR 522
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLS--RALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
75-511 |
1.30e-77 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 251.58 E-value: 1.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEY 154
Cdd:cd07094 6 PYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 155 VDICDYAVGLSRMFGGPMLPSE----RPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLT 230
Cdd:cd07094 86 IDTLRLAAEEAERIRGEEIPLDatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 231 SVAVTKIIaqvLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKqvALTVQERFGRCLLELGGNNAIIVF 310
Cdd:cd07094 166 ALELAKIL---VEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGE--ALRANAGGKRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 311 EDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVE 390
Cdd:cd07094 241 RDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 391 VAKQQGGSVVCGGkviERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGR 470
Cdd:cd07094 321 EAVEAGARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNV 397
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1841878009 471 IFRwlGPKGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGRE 511
Cdd:cd07094 398 AFK--AAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGRE 436
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
60-511 |
3.78e-77 |
|
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: 251.11 E-value: 3.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVS 137
Cdd:cd07559 6 NGEWvaPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 138 LEMGKIFVEGVGevqeyVDIcDYAVGLSRMFGGPMLPSERPGHALIEQ------WNPLGLVGIITAFNFPVAVYGWNNAI 211
Cdd:cd07559 86 LDNGKPIRETLA-----ADI-PLAIDHFRYFAGVIRAQEGSLSEIDEDtlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 212 ALICGNVCLWKGAPTTSLTSVAVTKIIAQVLEK---NKLPGAicslacgGADIGTAMAKDERIDLLSFTGSTNVGKQVAL 288
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDLLPKgvvNVVTGF-------GSEAGKPLASHPRIAKLAFTGSTTVGRLIMQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 289 TVQERFGRCLLELGGNNAIIVFEDA---DLNLVIpSALFAAVGTA---GQRCTTSRRLFLHESIHDEVVEKLMKAYAQVR 362
Cdd:cd07559 233 YAAENLIPVTLELGGKSPNIFFDDAmdaDDDFDD-KAEEGQLGFAfnqGEVCTCPSRALVQESIYDEFIERAVERFEAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 363 IGDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERP----GNYVEPTIVIELPHNSSIVHTETFAPILY 438
Cdd:cd07559 312 VGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841878009 439 VLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGNKHTGGGRE 511
Cdd:cd07559 392 VITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRV--ARGIQTGRVWVNcyhqYPA-----HAPFGGYKKSGIGRE 461
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
60-473 |
2.33e-76 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 249.06 E-value: 2.33e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW-GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSL 138
Cdd:PRK13473 8 NGELvAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 139 EMGK-IFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGN 217
Cdd:PRK13473 88 NCGKpLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 218 VCLWKGAPTTSLTSVAVTKIIAQVLEknklPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRC 297
Cdd:PRK13473 168 TVVLKPSEITPLTALKLAELAADILP----PGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 298 LLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLH 377
Cdd:PRK13473 244 HLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 378 TKQAVKMFLDAVEVAKQQG-GSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVK 456
Cdd:PRK13473 324 SAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSD 403
|
410
....*....|....*..
gi 1841878009 457 QGLSSSIFTKDLGRIFR 473
Cdd:PRK13473 404 YGLASSVWTRDVGRAHR 420
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
75-513 |
1.04e-75 |
|
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: 246.49 E-value: 1.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEY 154
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 155 VDICDYAVGLS---RMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTS 231
Cdd:cd07110 84 AGCFEYYADLAeqlDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 232 VAVTKIIAQVleknKLP-GAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVF 310
Cdd:cd07110 164 LELAEIAAEA----GLPpGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 311 EDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVE 390
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 391 VAKQQGGSVVCGGKVIE--RPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDL 468
Cdd:cd07110 320 RGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1841878009 469 GRIFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGNKHTGGGRESG 513
Cdd:cd07110 400 ERCDRV--AEALEAGIVWINCSQP-CFPQAPWGGYKRSGIGRELG 441
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
67-522 |
3.17e-75 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 246.33 E-value: 3.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 67 GEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVE 146
Cdd:PRK13252 21 GETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 147 G-VGEVQEYVDICDYAVGLSRMFGGPMLPSeRPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAP 225
Cdd:PRK13252 101 TsVVDIVTGADVLEYYAGLAPALEGEQIPL-RGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 226 TTSLTSVAVTKIIAQVleknKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNN 305
Cdd:PRK13252 180 VTPLTALKLAEIYTEA----GLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 306 AIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMF 385
Cdd:PRK13252 256 PLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 386 LDAVEVAKQQGGSVVCGGKVIER----PGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSS 461
Cdd:PRK13252 336 LGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAA 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841878009 462 SIFTKDLGRIFRWLGpkGSDCGIVNVNipTSG---AEIggAFGGNKHTGGGRESGSDSWKQYMR 522
Cdd:PRK13252 416 GVFTADLSRAHRVIH--QLEAGICWIN--TWGespAEM--PVGGYKQSGIGRENGIATLEHYTQ 473
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
60-513 |
3.21e-75 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 245.95 E-value: 3.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQ--IWAEIPAPKRGEIVRQIGDALRDKIKVLGNL 135
Cdd:cd07139 4 GGRWvaPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDngPWPRLSPAERAAVLRRLADALEARADELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 136 VSLEMGK-IFVEGVGEVQEYVDICDYAVGLSRMFGgpmLPSERP----GHALIEQwNPLGLVGIITAFNFPVAVYGWNNA 210
Cdd:cd07139 84 WTAENGMpISWSRRAQGPGPAALLRYYAALARDFP---FEERRPgsggGHVLVRR-EPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 211 IALICGNVCLWKGAPTTSLTSVavtkIIAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTV 290
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAY----LLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 291 QERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDAN 370
Cdd:cd07139 236 GERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 371 TLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKvieRP-----GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTE 445
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGG---RPagldrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841878009 446 EEVFGWNNGVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVNIPTSgaEIGGAFGGNKHTGGGRESG 513
Cdd:cd07139 393 DDAVRIANDSDYGLSGSVWTADVERglaVARRI-----RTGTVGVNGFRL--DFGAPFGGFKQSGIGREGG 456
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
75-530 |
1.66e-74 |
|
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: 244.27 E-value: 1.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQI-WAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGK-IFVEGVGEVQ 152
Cdd:cd07113 22 PATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKsIHLSRAFEVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 153 EYVDICDYAVGLSRMFGG----PMLPS---ERpgHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAP 225
Cdd:cd07113 102 QSANFLRYFAGWATKINGetlaPSIPSmqgER--YTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 226 TTSLTSVAvtkiIAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNN 305
Cdd:cd07113 180 FTPLTLLR----VAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 306 AIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMF 385
Cdd:cd07113 256 AAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 386 LDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFT 465
Cdd:cd07113 336 CSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWT 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841878009 466 KDLGRIFRWLgPKgSDCGIVNVNIPTSgAEIGGAFGGNKHTGGGRESGSDSWKQYMRRSTCTINY 530
Cdd:cd07113 416 NNLSKALRYI-PR-IEAGTVWVNMHTF-LDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY 477
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
72-521 |
4.53e-73 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 239.55 E-value: 4.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 72 TYCPANNQPIAKVRQANLEDYEETIKKAKEAWQ--IWAEIPApKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVG 149
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 150 EVQEYVDICDYAVGLSRMFGGPMLPSErPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSL 229
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPE-PGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 230 TSVAVTKIIAQVLEknkLP-GAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAII 308
Cdd:cd07120 159 INAAIIRILAEIPS---LPaGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 309 VFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDA 388
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 389 VEVAKQQGGSVVC-GGKVIER--PGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFT 465
Cdd:cd07120 316 VERAIAAGAEVVLrGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1841878009 466 KDLGRIFRWlgPKGSDCGIVNVNipTSGAEIGGA-FGGNKHTGGGRESGSDSWKQYM 521
Cdd:cd07120 396 RDLARAMRV--ARAIRAGTVWIN--DWNKLFAEAeEGGYRQSGLGRLHGVAALEDFI 448
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
60-511 |
5.61e-73 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 240.19 E-value: 5.61e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVS 137
Cdd:PRK11241 16 NGEWldANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 138 LEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGN 217
Cdd:PRK11241 96 LEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 218 VCLWKGAPTTSLTSVAvtkiIAQVLEKNKLPGAICSLACGGA-DIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGR 296
Cdd:PRK11241 176 TMVLKPASQTPFSALA----LAELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 297 CLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPL 376
Cdd:PRK11241 252 VSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 377 HTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVK 456
Cdd:PRK11241 332 IDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTE 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1841878009 457 QGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIgGAFGGNKHTGGGRE 511
Cdd:PRK11241 412 FGLAAYFYARDLSRVFRV--GEALEYGIVGINTGIISNEV-APFGGIKASGLGRE 463
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
67-528 |
9.62e-73 |
|
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: 239.56 E-value: 9.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 67 GEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQI---WAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKI 143
Cdd:cd07141 21 GKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 144 FVEG-VGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQwNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWK 222
Cdd:cd07141 101 FSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRH-EPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 223 GAPTTSLTSVAVTKIIAqvlEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTV-QERFGRCLLEL 301
Cdd:cd07141 180 PAEQTPLTALYLASLIK---EAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAgKSNLKRVTLEL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 302 GGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQA 381
Cdd:cd07141 257 GGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 382 VKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSS 461
Cdd:cd07141 337 FKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAA 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841878009 462 SIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAeIGGAFGGNKHTGGGRESGSDSWKQYMRRSTCTI 528
Cdd:cd07141 417 AVFTKDIDKAITF--SNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
67-530 |
1.34e-72 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 239.32 E-value: 1.34e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 67 GEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQI--WAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIF 144
Cdd:cd07140 20 GKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 145 VEGVG-EVQEYVDICDYAVGLSRMFGGPMLP--SERPGHAL-IEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCL 220
Cdd:cd07140 100 TLALKtHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 221 WKGAPTTSLTSVAvtkiIAQVLEKNKLP-GAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQE-RFGRCL 298
Cdd:cd07140 180 LKPAQVTPLTALK----FAELTVKAGFPkGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVsNLKKVS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 299 LELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHT 378
Cdd:cd07140 256 LELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNH 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 379 KQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTE--EEVFGWNNGVK 456
Cdd:cd07140 336 KAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841878009 457 QGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIpTSGAEIGGAFGGNKHTGGGRESGSDSWKQYMRRSTCTINY 530
Cdd:cd07140 416 YGLASGVFTKDINKALYV--SDKLEAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIEY 486
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
75-528 |
2.19e-72 |
|
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: 237.64 E-value: 2.19e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDyeetikkAKEAWQIWAEIPAP----KRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGE 150
Cdd:cd07146 6 PYTGEVVGTVPAGTEEA-------LREALALAASYRSTltryQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 151 VQEYVDICDYAVGLSRMFGGPMLPSERPGHA----LIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPT 226
Cdd:cd07146 79 VGRAADVLRFAAAEALRDDGESFSCDLTANGkarkIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 227 TSLTSVAvtkiIAQVLEKNKLPGAICSLACGG-ADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERfgRCLLELGGNN 305
Cdd:cd07146 159 TPLSAIY----LADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--RQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 306 AIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMF 385
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 386 LDAVEVAKQQGGSVVCGGkviERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFT 465
Cdd:cd07146 313 ENRVEEAIAQGARVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 466 KDLGRIFRWLgpKGSDCGIVNVN------IPTSgaeiggAFGGNKHTG-GGRESGSDSWKQYMRRSTCTI 528
Cdd:cd07146 390 NDLDTIKRLV--ERLDVGTVNVNevpgfrSELS------PFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
67-529 |
3.08e-72 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 238.46 E-value: 3.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 67 GEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQ-IWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIF- 144
Cdd:cd07144 22 GETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFEsWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYh 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 145 VEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQwNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGA 224
Cdd:cd07144 102 SNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLH-EPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 225 PTTSLTSVavtkIIAQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGG 303
Cdd:cd07144 181 ENTPLSLL----YFANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 304 NNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQV-RIGDPWDANTLYGPLHTKQAV 382
Cdd:cd07144 257 KSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDTVVGPQVSKTQY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 383 KMFLDAVEVAKQQGGSVVCGGKVIERP---GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGL 459
Cdd:cd07144 337 DRVLSYIEKGKKEGAKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGL 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 460 SSSIFTKDLGRIFRWLgpKGSDCGIVNVNiPTSGAEIGGAFGGNKHTGGGRESGSDSWKQYMRRSTCTIN 529
Cdd:cd07144 417 AAAVFTKDIRRAHRVA--RELEAGMVWIN-SSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHIN 483
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
81-521 |
3.53e-72 |
|
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: 237.19 E-value: 3.53e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 81 IAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEYVDICDY 160
Cdd:cd07152 4 LGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 161 AVGLSRMFGGPMLPSErPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAVtkiIAQ 240
Cdd:cd07152 84 AAGLPTQPQGEILPSA-PGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVV---IAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 241 VLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVAltvqERFGRCL----LELGGNNAIIVFEDADLN 316
Cdd:cd07152 160 LFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVG----EAAGRHLkkvsLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 317 LVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPL-HTKQAVKMfLDAVEVAKQQ 395
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLiNARQLDRV-HAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 396 GGSVVCGGkviERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRwL 475
Cdd:cd07152 315 GARLEAGG---TYDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA-L 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1841878009 476 GPKgSDCGIVNVNIPTSGAEIGGAFGGNKHTG-GGRESGSDSWKQYM 521
Cdd:cd07152 391 ADR-LRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFT 436
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
60-490 |
1.01e-70 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 234.33 E-value: 1.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVS 137
Cdd:cd07085 6 NGEWveSKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLIT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 138 LEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGN 217
Cdd:cd07085 86 LEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 218 VCLWKGAPTTSLTSVavtkIIAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRC 297
Cdd:cd07085 166 TFVLKPSERVPGAAM----RLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 298 LLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLH 377
Cdd:cd07085 242 QALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 378 TKQAVKMFLDAVEVAKQQGGSVVCGGKVIERP----GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNN 453
Cdd:cd07085 322 SPAAKERIEGLIESGVEEGAKLVLDGRGVKVPgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIIN 401
|
410 420 430
....*....|....*....|....*....|....*....
gi 1841878009 454 GVKQGLSSSIFTKD--LGRIFRwlgpKGSDCGIVNVNIP 490
Cdd:cd07085 402 ANPYGNGAAIFTRSgaAARKFQ----REVDAGMVGINVP 436
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
67-521 |
3.81e-70 |
|
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: 232.11 E-value: 3.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 67 GEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQ--IWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIF 144
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 145 VEGVGevqeyVDICD-------YAVGLSRMFGgPMLPSERPGHALIEQwNPLGLVGIITAFNFPVAVYGWNNAIALICGN 217
Cdd:cd07112 81 SDALA-----VDVPSaantfrwYAEAIDKVYG-EVAPTGPDALALITR-EPLGVVGAVVPWNFPLLMAAWKIAPALAAGN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 218 VCLWKGAPTTSLTSVAVTKIIAQ------VLekNKLPGAicslacgGADIGTAMAKDERIDLLSFTGSTNVGKQ-VALTV 290
Cdd:cd07112 154 SVVLKPAEQSPLTALRLAELALEaglpagVL--NVVPGF-------GHTAGEALGLHMDVDALAFTGSTEVGRRfLEYSG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 291 QERFGRCLLELGGNNAIIVFEDA-DLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDA 369
Cdd:cd07112 225 QSNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 370 NTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKV--IERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEE 447
Cdd:cd07112 305 ATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEE 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841878009 448 VFGWNNGVKQGLSSSIFTKDLGRIFRwlGPKGSDCGIVNVNIpTSGAEIGGAFGGNKHTGGGRESGSDSWKQYM 521
Cdd:cd07112 385 AVALANDSVYGLAASVWTSDLSRAHR--VARRLRAGTVWVNC-FDEGDITTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
60-521 |
1.09e-69 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 232.32 E-value: 1.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW-----GGRGEIVTtycPANNQPIAKVRQANLEDYEETIKKAKEAW-----QIWAEIPAPKRGEIVRQIGDALRDKI 129
Cdd:PLN02467 13 GGEWrepvlGKRIPVVN---PATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 130 KVLGNLVSLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGG--------PMlpSERPGHALieqWNPLGLVGIITAFNFP 201
Cdd:PLN02467 90 SELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkqkapvslPM--ETFKGYVL---KEPLGVVGLITPWNYP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 202 VAVYGWNNAIALICGNVCLWKGAPTTSLTSVAVTKIIAQVleknKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGST 280
Cdd:PLN02467 165 LLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREV----GLPPGVLNVVTGlGTEAGAPLASHPGVDKIAFTGST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 281 NVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQ 360
Cdd:PLN02467 241 ATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 361 VRIGDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKvieRP-----GNYVEPTIVIELPHNSSIVHTETFAP 435
Cdd:PLN02467 321 IKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGK---RPehlkkGFFIEPTIITDVTTSMQIWREEVFGP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 436 ILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN--------IPtsgaeiggaFGGNKHTG 507
Cdd:PLN02467 398 VLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERV--SEAFQAGIVWINcsqpcfcqAP---------WGGIKRSG 466
|
490
....*....|....
gi 1841878009 508 GGRESGSDSWKQYM 521
Cdd:PLN02467 467 FGRELGEWGLENYL 480
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
60-529 |
9.28e-69 |
|
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: 228.99 E-value: 9.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW-GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEI-PAPKRGEIVRQIGDALRDKIKVLGNLVS 137
Cdd:cd07082 7 NGEWkESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 138 LEMGKIFVEGVGEVQEYVDICDYAV-GLSRMFGGPMLPSERPGH----ALIEQwNPLGLVGIITAFNFPVavygwNNAI- 211
Cdd:cd07082 87 WEIGKTLKDALKEVDRTIDYIRDTIeELKRLDGDSLPGDWFPGTkgkiAQVRR-EPLGVVLAIGPFNYPL-----NLTVs 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 212 ----ALICGNVCLWKGAPTTSLTSVavtkIIAQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQV 286
Cdd:cd07082 161 klipALIMGNTVVFKPATQGVLLGI----PLAEAFHDAGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGNRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 287 AltVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDP 366
Cdd:cd07082 237 K--KQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 367 WDANTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKviERPGNYVEPTIvieLPHNSS---IVHTETFAPILYVLKFK 443
Cdd:cd07082 315 WDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG--REGGNLIYPTL---LDPVTPdmrLAWEEPFGPVLPIIRVN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 444 TEEEVFGWNNGVKQGLSSSIFTKDLGRIF---RWLgpkgsDCGIVNVNIPTS-GAEIgGAFGGNKHTGGGRESGSDSWKQ 519
Cdd:cd07082 390 DIEEAIELANKSNYGLQASIFTKDINKARklaDAL-----EVGTVNINSKCQrGPDH-FPFLGRKDSGIGTQGIGDALRS 463
|
490
....*....|
gi 1841878009 520 YMRRSTCTIN 529
Cdd:cd07082 464 MTRRKGIVIN 473
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
74-521 |
8.05e-68 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 226.04 E-value: 8.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 74 CPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKifvegvGEVQE 153
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGK------ARRHA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 154 YVDICDYAVGlSRMFG---GPMLPSERPGHAL------IEQWNPLGLVGIITAFNFPVAVyGWNNAI-ALICGNVCLWKG 223
Cdd:cd07101 76 FEEVLDVAIV-ARYYArraERLLKPRRRRGAIpvltrtTVNRRPKGVVGVISPWNYPLTL-AVSDAIpALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 224 APTTSLTSVAVtkiiAQVLEKNKLPGAICSLACG-GADIGTAMAkdERIDLLSFTGSTNVGKQVALTVQERFGRCLLELG 302
Cdd:cd07101 154 DSQTALTALWA----VELLIEAGLPRDLWQVVTGpGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLIGCSLELG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 303 GNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAV 382
Cdd:cd07101 228 GKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 383 KMFLDAVEVAKQQGGSVVCGGKviERP--GNYV-EPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGL 459
Cdd:cd07101 308 DRVTAHVDDAVAKGATVLAGGR--ARPdlGPYFyEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841878009 460 SSSIFTKDLGRIfRWLGPKgSDCGIVNVN--IPTSGAEIGGAFGGNKHTGGGRESGSDSWKQYM 521
Cdd:cd07101 386 NASVWTRDGARG-RRIAAR-LRAGTVNVNegYAAAWASIDAPMGGMKDSGLGRRHGAEGLLKYT 447
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
119-473 |
1.34e-66 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 221.53 E-value: 1.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 119 RQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAF 198
Cdd:PRK10090 2 RKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 199 NFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAVTKIIAQVleknKLPGAICSLACG-GADIGTAMAKDERIDLLSFT 277
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI----GLPKGVFNLVLGrGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 278 GSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKA 357
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 358 YAQVRIGDPWDANTL-YGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPI 436
Cdd:PRK10090 238 MQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 1841878009 437 LYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFR 473
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMK 354
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
53-529 |
1.24e-65 |
|
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: 220.86 E-value: 1.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 53 EENEGVY-NGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQI-WA-EIPAPKRGEIVRQIGDALRD 127
Cdd:cd07143 4 EQPTGLFiNGEFvdSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGlKVSGSKRGRCLSKLADLMER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 128 KIKVLGNLVSLEMGKIFVEGVG-EVQEYVDICDYAVGLSRMFGGPMLP--SERPGHALIEqwnPLGLVGIITAFNFPVAV 204
Cdd:cd07143 84 NLDYLASIEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVIEtdIKKLTYTRHE---PIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 205 YGWNNAIALICGNVCLWKGAPTTSLTSVAVTKIIAqvlEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGK 284
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIP---EAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 285 QV-ALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRI 363
Cdd:cd07143 238 KVmEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 364 GDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFK 443
Cdd:cd07143 318 GDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 444 TEEEVFGWNNGVKQGLSSSIFTKDLGRIFRWLGP-KGSDCGIVNVNIPTSGAeiggAFGGNKHTGGGRESGSDSWKQYMR 522
Cdd:cd07143 398 TEEEAIKRANDSTYGLAAAVFTNNINNAIRVANAlKAGTVWVNCYNLLHHQV----PFGGYKQSGIGRELGEYALENYTQ 473
|
....*..
gi 1841878009 523 RSTCTIN 529
Cdd:cd07143 474 IKAVHIN 480
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
60-524 |
2.33e-65 |
|
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: 219.96 E-value: 2.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVS 137
Cdd:cd07111 27 NGKWvkPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLES 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 138 LEMGKifvegvgEVQEYVDiCDYAVGLSRMF----GGPMLPSERPGhalieqWNPLGLVGIITAFNFPVAVYGWNNAIAL 213
Cdd:cd07111 107 LDNGK-------PIRESRD-CDIPLVARHFYhhagWAQLLDTELAG------WKPVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 214 ICGNVCLWKGAPTTSLTSVAVTKIIAQVleknKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQER 293
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEA----GLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 294 FGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLY 373
Cdd:cd07111 249 GKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 374 GPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNN 453
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALAN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841878009 454 GVKQGLSSSIFTKDLGRIFRwLGPkGSDCGIVNVNI-----PTSGaeiggaFGGNKHTGGGRESGSDSWKQYMRRS 524
Cdd:cd07111 409 NTPYGLAASVWSENLSLALE-VAL-SLKAGVVWINGhnlfdAAAG------FGGYRESGFGREGGKEGLYEYLRPS 476
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
77-529 |
5.40e-63 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 214.75 E-value: 5.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 77 NNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEYVD 156
Cdd:cd07125 56 HERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAID 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 157 ICD-YAVGLSRMFGGPMLPS---ERPGHalieQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSV 232
Cdd:cd07125 136 FCRyYAAQARELFSDPELPGptgELNGL----ELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 233 AVTKIiaqvLEKNKLPGAICSLA-CGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGR--CLL-ELGGNNAII 308
Cdd:cd07125 212 RAVEL----LHEAGVPRDVLQLVpGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPilPLIaETGGKNAMI 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 309 VFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMfLDA 388
Cdd:cd07125 288 VDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKL-LRA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 389 VEVAKQQGGSVVCGGKVIERPGNYVEPTIvIELpHNSSIVHTETFAPILYVLKFKTE--EEVFGWNNGVKQGLSSSIFTK 466
Cdd:cd07125 367 HTELMRGEAWLIAPAPLDDGNGYFVAPGI-IEI-VGIFDLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSR 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841878009 467 DLGRIFRWLgpKGSDCGIVNVNIPTSGAeIGGA--FGGNKHTGGGRESGSDSW-KQYMRRSTCTIN 529
Cdd:cd07125 445 DEREIEYWR--ERVEAGNLYINRNITGA-IVGRqpFGGWGLSGTGPKAGGPNYlLRFGNEKTVSLN 507
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
67-522 |
6.20e-63 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 214.30 E-value: 6.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 67 GEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQ--IWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIF 144
Cdd:PLN02766 35 GKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 145 VEGvgevqEYVDICDyAVGLSRMFGGP-------MLPSERP--GHALIEqwnPLGLVGIITAFNFPVAVYGWNNAIALIC 215
Cdd:PLN02766 115 ALG-----KAVDIPA-AAGLLRYYAGAadkihgeTLKMSRQlqGYTLKE---PIGVVGHIIPWNFPSTMFFMKVAPALAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 216 GNVCLWKGAPTTSLTSVavtkIIAQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQE-R 293
Cdd:PLN02766 186 GCTMVVKPAEQTPLSAL----FYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 294 FGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLY 373
Cdd:PLN02766 262 LKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 374 GPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNN 453
Cdd:PLN02766 342 GPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKAN 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841878009 454 GVKQGLSSSIFTKDL---GRIFRWLgpkgsDCGIVNVNIpTSGAEIGGAFGGNKHTGGGRESGSDSWKQYMR 522
Cdd:PLN02766 422 NTKYGLAAGIVTKDLdvaNTVSRSI-----RAGTIWVNC-YFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
58-523 |
7.98e-62 |
|
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: 211.28 E-value: 7.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 58 VYNGSWGGRGEIVTTYCPAN-NQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLV 136
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 137 SLEMGKIFVEGVGEVQEYVDICDY-AVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALIC 215
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYyARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 216 GNVCLWKGAPTTSLTSVAVTKIIAqvlEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQER-- 293
Cdd:cd07083 182 GNTVIAKPAEDAVVVGYKVFEIFH---EAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLap 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 294 ----FGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDA 369
Cdd:cd07083 259 gqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 370 NTLYGPLHTKQAVKMFLDAVEVAKQQgGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEE--E 447
Cdd:cd07083 339 GTDLGPVIDAEQEAKVLSYIEHGKNE-GQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaE 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841878009 448 VFGWNNGVKQGLSSSIFTKDLGRIfRWLGPKgSDCGIVNVNIPTSGAEIG-GAFGGNKHTGGGRESGSdswKQYMRR 523
Cdd:cd07083 418 ALEVANSTPYGLTGGVYSRKREHL-EEARRE-FHVGNLYINRKITGALVGvQPFGGFKLSGTNAKTGG---PHYLRR 489
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
60-513 |
3.08e-61 |
|
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: 208.90 E-value: 3.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW-----GGRGEIVttyCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGN 134
Cdd:cd07138 4 DGAWvapagTETIDVI---NPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 135 LVSLEMGK-IFVEGVGEVQEYVDICDYAVGLSRMFggPMlpSERPGHALIeQWNPLGLVGIITAFNFPVavygwnNAI-- 211
Cdd:cd07138 81 AITLEMGApITLARAAQVGLGIGHLRAAADALKDF--EF--EERRGNSLV-VREPIGVCGLITPWNWPL------NQIvl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 212 ----ALICGNVCLWKGAPTTSLTSVavtkIIAQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQV 286
Cdd:cd07138 150 kvapALAAGCTVVLKPSEVAPLSAI----ILAEILDEAGLPAGVFNLVNGdGPVVGEALSAHPDVDMVSFTGSTRAGKRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 287 ALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDP 366
Cdd:cd07138 226 AEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 367 WDANTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGkvIERP-----GNYVEPTIVIELPHNSSIVHTETFAPILYVLK 441
Cdd:cd07138 306 RDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG--PGRPeglerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIP 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841878009 442 FKTEEEVFGWNNGVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVNipTSGAEIGGAFGGNKHTGGGRESG 513
Cdd:cd07138 384 YDDEDEAIAIANDTPYGLAGYVWSADPERaraVARRL-----RAGQVHIN--GAAFNPGAPFGGYKQSGNGREWG 451
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
64-515 |
9.11e-61 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 208.96 E-value: 9.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 64 GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKI 143
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 144 FVEGVGEVQEYVDICDY----AVGLSRmfggpmlPSERPGhAL------IEQWNPLGLVGIITAFNFPVAVyGWNNAI-A 212
Cdd:PRK09407 108 RRHAFEEVLDVALTARYyarrAPKLLA-------PRRRAG-ALpvltktTELRQPKGVVGVISPWNYPLTL-AVSDAIpA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 213 LICGNVCLWKGAPTTSLTSVAVtkiiAQVLEKNKLPGAICSLACG-GADIGTAMAkdERIDLLSFTGSTNVGKQVALTVQ 291
Cdd:PRK09407 179 LLAGNAVVLKPDSQTPLTALAA----VELLYEAGLPRDLWQVVTGpGPVVGTALV--DNADYLMFTGSTATGRVLAEQAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 292 ERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANT 371
Cdd:PRK09407 253 RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 372 LYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVieRP--GNYV-EPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEV 448
Cdd:PRK09407 333 DMGSLISEAQLETVSAHVDDAVAKGATVLAGGKA--RPdlGPLFyEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEA 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841878009 449 FGWNNGVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVN---IPTSGAeIGGAFGGNKHTGGGRESGSD 515
Cdd:PRK09407 411 VERANDTPYGLNASVWTGDTARgraIAARI-----RAGTVNVNegyAAAWGS-VDAPMGGMKDSGLGRRHGAE 477
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
75-470 |
2.34e-60 |
|
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: 205.94 E-value: 2.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEY 154
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 155 VDICDYAVGLSRmfgGPMLPSERPGHALIEQW---NPLGLVGIITAFNFP--VAVygwnNAI--ALICGNVCLWKGAPTT 227
Cdd:cd07102 83 LERARYMISIAE---EALADIRVPEKDGFERYirrEPLGVVLIIAPWNYPylTAV----NAVipALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 228 SLTSVAvtkiIAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAI 307
Cdd:cd07102 156 PLCGER----FAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 308 IVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLD 387
Cdd:cd07102 232 YVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 388 AVEVAKQQGGSVVCGGK---VIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIF 464
Cdd:cd07102 312 QIADAIAKGARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVW 391
|
....*.
gi 1841878009 465 TKDLGR 470
Cdd:cd07102 392 TKDIAR 397
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
67-522 |
4.93e-60 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 207.35 E-value: 4.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 67 GEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQ--IWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIF 144
Cdd:PLN02466 72 GKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 145 VEGVG-EVQEYVDICDYAVGLSRMFGGPMLPSERPGHALIEQwNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKG 223
Cdd:PLN02466 152 EQSAKaELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLH-EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 224 APTTSLTSVAVTKIiaqvLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQV-ALTVQERFGRCLLEL 301
Cdd:PLN02466 231 AEQTPLSALYAAKL----LHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVlELAAKSNLKPVTLEL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 302 GGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKlMKAYAQVR-IGDPWDANTLYGPLHTKQ 380
Cdd:PLN02466 307 GGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK-AKARALKRvVGDPFKKGVEQGPQIDSE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 381 AVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLS 460
Cdd:PLN02466 386 QFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLA 465
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841878009 461 SSIFTKDL---GRIFRWLgpkgsDCGIVNVN--------IPtsgaeiggaFGGNKHTGGGRESGSDSWKQYMR 522
Cdd:PLN02466 466 AGVFTQNLdtaNTLSRAL-----RVGTVWVNcfdvfdaaIP---------FGGYKMSGIGREKGIYSLNNYLQ 524
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
99-513 |
1.32e-58 |
|
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: 200.96 E-value: 1.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 99 AKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMlPSERP 178
Cdd:cd07095 9 ARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTGER-ATPMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 179 GHALIEQWNPLGLVGIITAFNFPVAVYgwNNAI--ALICGNVCLWKGAPTTSltsvAVTKIIAQVLEKNKLPGAICSLAC 256
Cdd:cd07095 88 QGRAVLRHRPHGVMAVFGPFNFPGHLP--NGHIvpALLAGNTVVFKPSELTP----AVAELMVELWEEAGLPPGVLNLVQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 257 GGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCL-LELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCT 335
Cdd:cd07095 162 GGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 336 TSRRLFLHES-IHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVE 414
Cdd:cd07095 242 CARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 415 PTIvIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDlGRIFRWLGPKgSDCGIVNVNIPTSGA 494
Cdd:cd07095 322 PGI-IDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDD-EALFERFLAR-IRAGIVNWNRPTTGA 398
|
410
....*....|....*....
gi 1841878009 495 EIGGAFGGNKHTGGGRESG 513
Cdd:cd07095 399 SSTAPFGGVGLSGNHRPSA 417
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
67-473 |
6.44e-57 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 198.62 E-value: 6.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 67 GEIVTT------YCPAN-NQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLE 139
Cdd:PRK03137 43 GERITTedkivsINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 140 MGKIFVEGVGEVQEYVDICDY----AVGLSrmFGGPMLPseRPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALIC 215
Cdd:PRK03137 123 AGKPWAEADADTAEAIDFLEYyarqMLKLA--DGKPVES--RPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 216 GNVCLWKGAPTTSLTSVAVtkiiAQVLEKNKLP-GAICSLACGGADIGTAMAKDERIDLLSFTGSTNVG---KQVALTVQ 291
Cdd:PRK03137 199 GNTVLLKPASDTPVIAAKF----VEVLEEAGLPaGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlriYERAAKVQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 292 E---RFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWD 368
Cdd:PRK03137 275 PgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPED 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 369 aNTLYGPLHTKQAVKMFLDAVEVAKQQgGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEV 448
Cdd:PRK03137 355 -NAYMGPVINQASFDKIMSYIEIGKEE-GRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHA 432
|
410 420
....*....|....*....|....*
gi 1841878009 449 FGWNNGVKQGLSSSIFTKDLGRIFR 473
Cdd:PRK03137 433 LEIANNTEYGLTGAVISNNREHLEK 457
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
91-510 |
2.29e-56 |
|
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: 194.72 E-value: 2.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 91 DYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMG------KIFVEGVGEVqeyvdICDYAVGL 164
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGataawaGFNVDLAAGM-----LREAASLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 165 SRMFGGPMlPSERPGH-ALIEQwNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAvtkiIAQVLE 243
Cdd:cd07105 76 TQIIGGSI-PSDKPGTlAMVVK-EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWL----IGRVFH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 244 KNKLP-GAICSLACGGAD---IGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVI 319
Cdd:cd07105 150 EAGLPkGVLNVVTHSPEDapeVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 320 PSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRiGDPWDANTLYGPLHTKQAVKMFLDAVEvakqQGGSV 399
Cdd:cd07105 230 NAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLF-AGPVVLGSLVSAAAADRVKELVDDALS----KGAKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 400 VCGGKVIERP-GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRwLGpK 478
Cdd:cd07105 305 VVGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALA-VA-K 382
|
410 420 430
....*....|....*....|....*....|..
gi 1841878009 479 GSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGR 510
Cdd:cd07105 383 RIESGAVHINGMTVHDEPTLPHGGVKSSGYGR 414
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
75-511 |
6.78e-54 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 188.92 E-value: 6.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEY 154
Cdd:PRK13968 14 PATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 155 VDICD-YAvglsrMFGGPMLPSE----RPGHALIEqWNPLGLVGIITAFNFPVavygWN---NAIA-LICGNVCLWKGAP 225
Cdd:PRK13968 94 ANLCDwYA-----EHGPAMLKAEptlvENQQAVIE-YRPLGTILAIMPWNFPL----WQvmrGAVPiLLAGNGYLLKHAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 226 TTsltsVAVTKIIAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNN 305
Cdd:PRK13968 164 NV----MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 306 AIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMF 385
Cdd:PRK13968 240 PFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 386 LDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFT 465
Cdd:PRK13968 320 HHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFT 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1841878009 466 KDLGRIFRWlgPKGSDCGIVNVN-IPTSGAEIggAFGGNKHTGGGRE 511
Cdd:PRK13968 400 TDETQARQM--AARLECGGVFINgYCASDARV--AFGGVKKSGFGRE 442
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
73-513 |
1.76e-52 |
|
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: 185.20 E-value: 1.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 73 YCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGV-GEV 151
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 152 qeyVDICDYAVGLSRMFGGPMLPSERPGHALIE------QWNPLGLVGIITAFNFPvavygWNNAI-----ALICGNVCL 220
Cdd:cd07098 81 ---LVTCEKIRWTLKHGEKALRPESRPGGLLMFykrarvEYEPLGVVGAIVSWNYP-----FHNLLgpiiaALFAGNAIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 221 WKGAPTTSLTSVAVTKIIAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLE 300
Cdd:cd07098 153 VKVSEQVAWSSGFFLSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 301 LGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYG----PL 376
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGamisPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 377 HTKQAVKMFLDAVEvakqQGGSVVCGGKVIERP----GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWN 452
Cdd:cd07098 313 RFDRLEELVADAVE----KGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841878009 453 NGVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNiptsgaEIGGA-------FGGNKHTGGGRESG 513
Cdd:cd07098 389 NSTEYGLGASVFGKDIKRARRIA--SQLETGMVAIN------DFGVNyyvqqlpFGGVKGSGFGRFAG 448
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
75-490 |
2.57e-49 |
|
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: 177.00 E-value: 2.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEY 154
Cdd:TIGR01722 23 PATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVARG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 155 VDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAV 234
Cdd:TIGR01722 103 LEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 235 tkiiAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDAD 314
Cdd:TIGR01722 183 ----AELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 315 LNLVIPSALFAAVGTAGQRCTTSRRLFLHESIhDEVVEKLMKAYAQVRIGdPW-DANTLYGPLHTKQAVKMFLDAVEVAK 393
Cdd:TIGR01722 259 KDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIG-PGdDPGAEMGPLITPQAKDRVASLIAGGA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 394 QQGGSVVCGGKVIE----RPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLG 469
Cdd:TIGR01722 337 AEGAEVLLDGRGYKvdgyEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGA 416
|
410 420
....*....|....*....|...
gi 1841878009 470 --RIFRWLgpkgSDCGIVNVNIP 490
Cdd:TIGR01722 417 aaRRFQHE----IEVGQVGVNVP 435
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
60-512 |
3.39e-49 |
|
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: 176.87 E-value: 3.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSWGG--RGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVS 137
Cdd:cd07116 6 GGEWVApvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 138 LEMGKIFVEGVG-EVQEYVDICDYAVGLSRMFGGPM--LPSERPGHALIEqwnPLGLVGIITAFNFPVAVYGWNNAIALI 214
Cdd:cd07116 86 WDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSIseIDENTVAYHFHE---PLGVVGQIIPWNFPLLMATWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 215 CGNVCLWKGAPTTSLTSVAVTKIIAQVLEknklPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERF 294
Cdd:cd07116 163 AGNCVVLKPAEQTPASILVLMELIGDLLP----PGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 295 GRCLLELGGNNAIIVFE------DADLNLVIPS-ALFAAvgTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPW 367
Cdd:cd07116 239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEGfVMFAL--NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 368 DANTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGN----YVEPTiVIELPHNSSIVHTETFAPILYVLKFK 443
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPT-TFKGGNKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841878009 444 TEEEVFGWNNGVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGNKHTGGGRES 512
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRM--GRGIQAGRVWTNcyhlYPA-----HAAFGGYKQSGIGREN 461
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
64-446 |
4.12e-47 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 177.05 E-value: 4.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 64 GGRGEIVTtyCPAN-NQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGK 142
Cdd:COG4230 568 SGEARPVR--NPADhSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGK 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 143 IFVEGVGEVQEYVDICD-YAVGLSRMFGGPMlpserpghalieQWNPLGLVGIITAFNFPVA-----VygwnnAIALICG 216
Cdd:COG4230 646 TLPDAIAEVREAVDFCRyYAAQARRLFAAPT------------VLRGRGVFVCISPWNFPLAiftgqV-----AAALAAG 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 217 NVCLWKGAPTTSLT-SVAVtkiiaQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERF 294
Cdd:COG4230 709 NTVLAKPAEQTPLIaARAV-----RLLHEAGVPADVLQLLPGdGETVGAALVADPRIAGVAFTGSTETARLINRTLAARD 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 295 GRCLL---ELGGNNAIIVfeD---------ADlnlVIPSAlFaavGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVR 362
Cdd:COG4230 784 GPIVPliaETGGQNAMIV--DssalpeqvvDD---VLASA-F---DSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELR 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 363 IGDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQggsvvcgGKVIERP--------GNYVEPTIvIELPHNSSIvHTETFA 434
Cdd:COG4230 855 VGDPADLSTDVGPVIDAEARANLEAHIERMRAE-------GRLVHQLplpeecanGTFVAPTL-IEIDSISDL-EREVFG 925
|
410
....*....|..
gi 1841878009 435 PILYVLKFKTEE 446
Cdd:COG4230 926 PVLHVVRYKADE 937
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
60-524 |
1.03e-46 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 170.48 E-value: 1.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSWGGRGEIVTTYCPANNQPI-AKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSL 138
Cdd:TIGR01238 43 GHSYKADGEAQPVTNPADRRDIvGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 139 EMGKIFVEGVGEVQEYVDICDYAVGLSRmfggPMLPSERPghalieqwNPLGLVGIITAFNFPVAVYGWNNAIALICGNV 218
Cdd:TIGR01238 123 EAGKTIHNAIAEVREAVDFCRYYAKQVR----DVLGEFSV--------ESRGVFVCISPWNFPLAIFTGQISAALAAGNT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 219 CLWKGAPTTSLTSvavTKIIAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERF---G 295
Cdd:TIGR01238 191 VIAKPAEQTSLIA---YRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdapV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 296 RCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGP 375
Cdd:TIGR01238 268 PLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 376 LHTKQAVKMFLDAVEVAKQQGGSV---VCGGKVIERPGNYVEPTIvIELpHNSSIVHTETFAPILYVLKFKTEE--EVFG 450
Cdd:TIGR01238 348 VIDAEAKQNLLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTL-FEL-DDIAELSEEVFGPVLHVVRYKAREldQIVD 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841878009 451 WNNGVKQGLSSSIFTKDLGRIfRWLgPKGSDCGIVNVNIPTSGAEIG-GAFGGNKHTGGGRESGSDSWKQYMRRS 524
Cdd:TIGR01238 426 QINQTGYGLTMGVHSRIETTY-RWI-EKHARVGNCYVNRNQVGAVVGvQPFGGQGLSGTGPKAGGPHYLYRLTQV 498
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
64-446 |
1.33e-46 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 175.39 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 64 GGRGEIVTTYCPANN-QPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGK 142
Cdd:PRK11904 558 NGEGEARPVVSPADRrRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGK 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 143 IFVEGVGEVQEYVDICD-YAVGLSRMFGGP-MLPS---ERpghalieqwNPLGLVG-----IITAFNFPVAVYGWNNAIA 212
Cdd:PRK11904 638 TLQDAIAEVREAVDFCRyYAAQARRLFGAPeKLPGptgES---------NELRLHGrgvfvCISPWNFPLAIFLGQVAAA 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 213 LICGNVCLWKGAPTTSLTSVAVTKIiaqvLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQ 291
Cdd:PRK11904 709 LAAGNTVIAKPAEQTPLIAAEAVKL----LHEAGIPKDVLQLLPGdGATVGAALTADPRIAGVAFTGSTETARIINRTLA 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 292 ERFGR--CLL-ELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWD 368
Cdd:PRK11904 785 ARDGPivPLIaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRL 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 369 ANTLYGPLHTKQAVKMFLDAVEVAKQQgGSVVCGGKVIE--RPGNYVEPTIvIELPhNSSIVHTETFAPILYVLKFKTEE 446
Cdd:PRK11904 865 LSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPAgtENGHFVAPTA-FEID-SISQLEREVFGPILHVIRYKASD 941
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
75-446 |
1.54e-46 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 175.05 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PAN-NQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQE 153
Cdd:PRK11905 574 PADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVRE 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 154 YVDICD-YAVGLSRMFGGPMLPserpghalieqwnPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLT-S 231
Cdd:PRK11905 654 AVDFLRyYAAQARRLLNGPGHK-------------PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIaA 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 232 VAVtkiiaQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGR--CLL-ELGGNNAI 307
Cdd:PRK11905 721 RAV-----RLLHEAGVPKDALQLLPGdGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpvPLIaETGGQNAM 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 308 IVfeD---------ADlnlVIPSAlFAavgTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHT 378
Cdd:PRK11905 796 IV--DssalpeqvvAD---VIASA-FD---SAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVID 866
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841878009 379 KQAVKMFLDAVEVAKQQGGSVvcggKVIERP-----GNYVEPTIvIELPHNSSIVHtETFAPILYVLKFKTEE 446
Cdd:PRK11905 867 AEAQANIEAHIEAMRAAGRLV----HQLPLPaetekGTFVAPTL-IEIDSISDLER-EVFGPVLHVVRFKADE 933
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
67-511 |
2.07e-46 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 168.76 E-value: 2.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 67 GEIVTTYCPANNQPIakvrqanledyEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVE 146
Cdd:PRK09406 11 GETVKTFTALTDDEV-----------DAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 147 GVGEVQEYVDICDY-----------------AVGLSRMFGgpmlpserpghalieQWNPLGLVGIITAFNFPVavygWN- 208
Cdd:PRK09406 80 AKAEALKCAKGFRYyaehaealladepadaaAVGASRAYV---------------RYQPLGVVLAVMPWNFPL----WQv 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 209 ---NAIALICGNVCLWKGA---PTTSLtsvavtkIIAQVLEKNKLP-GAICSLACGgADIGTAMAKDERIDLLSFTGSTN 281
Cdd:PRK09406 141 vrfAAPALMAGNVGLLKHAsnvPQTAL-------YLADLFRRAGFPdGCFQTLLVG-SGAVEAILRDPRVAAATLTGSEP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 282 VGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQV 361
Cdd:PRK09406 213 AGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 362 RIGDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLK 441
Cdd:PRK09406 293 RVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYR 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841878009 442 FKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEIGgaFGGNKHTGGGRE 511
Cdd:PRK09406 373 VADIDEAIEIANATTFGLGSNAWTRDEAEQERFI--DDLEAGQVFINgMTVSYPELP--FGGVKRSGYGRE 439
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
75-509 |
4.67e-46 |
|
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: 167.60 E-value: 4.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVrqaNLEDYEETIKKAKEAWQIWAE----IPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGE 150
Cdd:cd07148 6 PFDLKPIGEV---PTVDWAAIDKALDTAHALFLDrnnwLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 151 VQEYVDICDYAVGLSRMFGG---PM-LPSERPGHALIEQWNPLGLVGIITAFNFPV--AVYGWNNAIALICGnvCLWKGA 224
Cdd:cd07148 83 VTRAIDGVELAADELGQLGGreiPMgLTPASAGRIAFTTREPIGVVVAISAFNHPLnlIVHQVAPAIAAGCP--VIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 225 PTTSLTSVAVTKIiaqvLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVG-----KQVALTvqerfgRCLL 299
Cdd:cd07148 161 LATPLSCLAFVDL----LHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGwmlrsKLAPGT------RCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 300 ELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTK 379
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 380 QAVKMFLDAVEVAKQQGGSVVCGGKVIERpgNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGL 459
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARLLCGGKRLSD--TTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAF 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1841878009 460 SSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGG 509
Cdd:cd07148 389 QAAVFTKDLDVALKAV--RRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
42-511 |
7.14e-45 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 165.45 E-value: 7.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 42 QYAWLKELGLREENEGVYNGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQ--IWAEIPAPKRGEI 117
Cdd:PRK09847 7 AYWQDKALSLAIENRLFINGEYtaAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 118 VRQIGDALRDKIKVLGNLVSLEMGKIF-------VEGVGEVQEYvdicdYAVGLSRMFGgPMLPSERPGHALIEQwNPLG 190
Cdd:PRK09847 87 LNKLADLMEAHAEELALLETLDTGKPIrhslrddIPGAARAIRW-----YAEAIDKVYG-EVATTSSHELAMIVR-EPVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 191 LVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAvtkiIAQVLEKNKLPGAICSLACG-GADIGTAMAKDE 269
Cdd:PRK09847 160 VIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIR----LAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 270 RIDLLSFTGSTNVGKQVALTV-QERFGRCLLELGGNNAIIVFEDA-DLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIH 347
Cdd:PRK09847 236 DIDAIAFTGSTRTGKQLLKDAgDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 348 DEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQGgSVVCGGKVIERPGnYVEPTIVIELPHNSSI 427
Cdd:PRK09847 316 DEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 428 VHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGaEIGGAFGGNKHTG 507
Cdd:PRK09847 394 SREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRM--SRRLKAGSVFVNNYNDG-DMTVPFGGYKQSG 470
|
....
gi 1841878009 508 GGRE 511
Cdd:PRK09847 471 NGRD 474
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
60-512 |
2.76e-43 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 160.89 E-value: 2.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW-GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSL 138
Cdd:PRK09457 6 NGDWiAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 139 EMGKIFVEGVGEVQEYVDICDYAVGLSRMFGGPMlPSERPGHALIEQWNPLGLVGIITAFNFPvavyGW--NNAI--ALI 214
Cdd:PRK09457 86 ETGKPLWEAATEVTAMINKIAISIQAYHERTGEK-RSEMADGAAVLRHRPHGVVAVFGPYNFP----GHlpNGHIvpALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 215 CGNVCLWKGAPTTSltsvAVTKIIAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVG----KQVAltv 290
Cdd:PRK09457 161 AGNTVVFKPSELTP----WVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGyllhRQFA--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 291 qERFGRCL-LELGGNNAIIVFEDADL----NLVIPSALFaavgTAGQRCTTSRRLFLHESIH-DEVVEKLMKAYAQVRIG 364
Cdd:PRK09457 234 -GQPEKILaLEMGGNNPLVIDEVADIdaavHLIIQSAFI----SAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 365 dPWDANT--LYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIERPGNYVEPTI-----VIELPHNssivhtETFAPIL 437
Cdd:PRK09457 309 -RWDAEPqpFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIidvtgVAELPDE------EYFGPLL 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841878009 438 YVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGRES 512
Cdd:PRK09457 382 QVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFL--LEIRAGIVNWNKPLTGASSAAPFGGVGASGNHRPS 454
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
75-535 |
6.88e-40 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 153.36 E-value: 6.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 75 PANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEY 154
Cdd:PLN02419 136 PATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 155 VDICDYAVGLSRMFGGPMLPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVav 234
Cdd:PLN02419 216 LEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASV-- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 235 tkIIAQVLEKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDAD 314
Cdd:PLN02419 294 --ILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDAN 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 315 LNLVIPSALFAAVGTAGQRCTT-SRRLFLHE--SIHDEVVEKlMKAYaQVRIGDPWDANtlYGPLHTKQAVKMFLDAVEV 391
Cdd:PLN02419 372 IDATLNALLAAGFGAAGQRCMAlSTVVFVGDakSWEDKLVER-AKAL-KVTCGSEPDAD--LGPVISKQAKERICRLIQS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 392 AKQQGGSVVCGGKVIERP----GNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKD 467
Cdd:PLN02419 448 GVDDGAKLLLDGRDIVVPgyekGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSS 527
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841878009 468 --LGRIFRwlgpKGSDCGIVNVNIPTSGAEIGGAFGGNKHTGGGR-----ESGSDSWKQYmrrSTCTINYsKDLP 535
Cdd:PLN02419 528 gaAARKFQ----MDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDlnfygKAGVDFFTQI---KLVTQKQ-KDIH 594
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
60-532 |
3.76e-39 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 149.52 E-value: 3.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSW--GGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVS 137
Cdd:PLN00412 21 DGEWrtSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 138 LEMGKIFVEGVGEVQEYVDICDYAV--GLSRMFGGPMLPS------ERPGHALIEQWnPLGLVGIITAFNFPVAVYGWNN 209
Cdd:PLN00412 101 KEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFLVSdsfpgnERNKYCLTSKI-PLGVVLAIPPFNYPVNLAVSKI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 210 AIALICGNVCLWKgAPTTSLTSVAVTkiiAQVLEKNKLPGAICSLACG-GADIGTAMAKDERIDLLSFTGStNVGkqVAL 288
Cdd:PLN00412 180 APALIAGNAVVLK-PPTQGAVAALHM---VHCFHLAGFPKGLISCVTGkGSEIGDFLTMHPGVNCISFTGG-DTG--IAI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 289 TVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWD 368
Cdd:PLN00412 253 SKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 369 ANTLyGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKvieRPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEV 448
Cdd:PLN00412 333 DCDI-TPVVSESSANFIEGLVMDAKEKGATFCQEWK---REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 449 FGWNNGVKQGLSSSIFTKDLGRIFRWlgpkgSDC---GIVNVNIPTSGAEIGGAFGGNKHTGGGRESGSDSWKQYMRRST 525
Cdd:PLN00412 409 IHHCNASNFGLQGCVFTRDINKAILI-----SDAmetGTVQINSAPARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKS 483
|
....*..
gi 1841878009 526 CTINYSK 532
Cdd:PLN00412 484 TVINLPK 490
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
84-446 |
7.39e-35 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 140.11 E-value: 7.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 84 VRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGVGEVQEYVDICDY-AV 162
Cdd:PRK11809 676 VREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYyAG 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 163 GLSRMFGGpmlpserpghaliEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAVTKIIaqvL 242
Cdd:PRK11809 756 QVRDDFDN-------------DTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRIL---L 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 243 EKNKLPGAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQVALTVQERF---GRC---LLELGGNNAIIVFEDADLN 316
Cdd:PRK11809 820 EAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqGRPiplIAETGGQNAMIVDSSALTE 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 317 LVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQG 396
Cdd:PRK11809 900 QVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKG 979
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1841878009 397 GSV---VCGGKVIERPGNYVEPTIvIELPHNSSIvHTETFAPILYVLKFKTEE 446
Cdd:PRK11809 980 RPVfqaARENSEDWQSGTFVPPTL-IELDSFDEL-KREVFGPVLHVVRYNRNQ 1030
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
177-467 |
2.88e-34 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 134.19 E-value: 2.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 177 RPGHALIEQwNPLGLVGIITAFNFPV------AVygwnNAIAliCGNVCLWKG---APTTSltsvavtKIIAQVLEKnKL 247
Cdd:cd07087 90 QPAKAYVIP-EPLGVVLIIGPWNYPLqlalapLI----GAIA--AGNTVVLKPselAPATS-------ALLAKLIPK-YF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 248 PGAICSLACGGADIGTAMAKdERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAV 327
Cdd:cd07087 155 DPEAVAVVEGGVEVATALLA-EPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 328 GTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVrIGDPWDANTLYGPL----HTKQAVKMFldavevakqQGGSVVCGG 403
Cdd:cd07087 234 LNAGQTCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIinerHFDRLASLL---------DDGKVVIGG 303
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841878009 404 KViERPGNYVEPTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKD 467
Cdd:cd07087 304 QV-DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSED 366
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
177-528 |
1.17e-33 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 133.62 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 177 RPGHALIeQWNPLGLVGIITAFNFPV--AVYGWNNAIAliCGNVCLWKgaptTSLTSVAVTKIIAQVLEKnKLPGAICSL 254
Cdd:PTZ00381 99 GPGKSYI-IPEPLGVVLVIGAWNYPLnlTLIPLAGAIA--AGNTVVLK----PSELSPHTSKLMAKLLTK-YLDPSYVRV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 255 ACGGADIGTAMAKdERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRC 334
Cdd:PTZ00381 171 IEGGVEVTTELLK-EPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTC 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 335 TTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTlYGPLHTKQAVKMFldaVEVAKQQGGSVVCGGKVIERpGNYVE 414
Cdd:PTZ00381 250 VAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSED-YSRIVNEFHTKRL---AELIKDHGGKVVYGGEVDIE-NKYVA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 415 PTIVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDlGRIFRWLGPKGSDCGIV--------- 485
Cdd:PTZ00381 325 PTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGED-KRHKELVLENTSSGAVVindcvfhll 403
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1841878009 486 NVNIPtsgaeiggaFGGNKHTGGGRESGSDSWKQY------MRRSTCTI 528
Cdd:PTZ00381 404 NPNLP---------FGGVGNSGMGAYHGKYGFDTFshpkpvLNKSTGNS 443
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
188-467 |
7.21e-31 |
|
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: 124.64 E-value: 7.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 188 PLGLVGIITAFNFPV-----AVYGwnnAIAliCGNVCLWKGAPTTSLTSVAVTKIIAQVLEknklPGAIcSLACGGADIG 262
Cdd:cd07135 108 PLGVVLIIGPWNYPVllalsPLVG---AIA--AGCTVVLKPSELTPHTAALLAELVPKYLD----PDAF-QVVQGGVPET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 263 TAMAkDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFL 342
Cdd:cd07135 178 TALL-EQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 343 HESIHDEVVEKLMKAYAQVRIGDPwDANTLYGPLHTKQAvkmFLDAVEVAKQQGGSVVCGGKViERPGNYVEPTIVIELP 422
Cdd:cd07135 257 DPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRH---FNRLKSLLDTTKGKVVIGGEM-DEATRFIPPTIVSDVS 331
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1841878009 423 HNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKD 467
Cdd:cd07135 332 WDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDD 376
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
67-467 |
1.97e-30 |
|
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: 124.62 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 67 GEIVTTYCPAN-NQPIAKVRQANLEDYEETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKvlGNLVSLEM---GK 142
Cdd:cd07123 45 GNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYR--YELNAATMlgqGK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 143 IFVEGvgEVQEYVDICDYAvglsRM---FGGPMLPSERPGHALIEqWN-----PL-GLVGIITAFNFpvavygwnNAIAL 213
Cdd:cd07123 123 NVWQA--EIDAACELIDFL----RFnvkYAEELYAQQPLSSPAGV-WNrleyrPLeGFVYAVSPFNF--------TAIGG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 214 -------ICGNVCLWKGAPTTSLTSVAVTKIiaqvLEKNKLP-GAICSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQ 285
Cdd:cd07123 188 nlagapaLMGNVVLWKPSDTAVLSNYLVYKI----LEEAGLPpGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 286 VALTVQER------FGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYA 359
Cdd:cd07123 264 LWKQIGENldryrtYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 360 QVRIGDPWDANTLYGPLHTKQAVKMFLDAVEVAKQQGG-SVVCGGKVIERPGNYVEPTIVIELPHNSSIVHTETFAPIL- 437
Cdd:cd07123 344 EIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEaEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLt 423
|
410 420 430
....*....|....*....|....*....|..
gi 1841878009 438 -YVLKFKTEEEVFGW-NNGVKQGLSSSIFTKD 467
Cdd:cd07123 424 vYVYPDSDFEETLELvDTTSPYALTGAIFAQD 455
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
188-467 |
7.50e-29 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 119.15 E-value: 7.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 188 PLGLVGIITAFNFP-----VAVYGwnnAIAliCGNVCLWKGAPTTSLTSVAVTKIIAQVLEKNklpgaicSLAC--GGAD 260
Cdd:cd07136 100 PYGVVLIIAPWNYPfqlalAPLIG---AIA--AGNTAVLKPSELTPNTSKVIAKIIEETFDEE-------YVAVveGGVE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 261 IGTAMAkDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRL 340
Cdd:cd07136 168 ENQELL-DQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 341 FLHESIHDEVVeKLMKAYAQVRIGDPWDANTLYGPL----HTKQAVKMFldavevakqQGGSVVCGGKvIERPGNYVEPT 416
Cdd:cd07136 247 LVHESVKEKFI-KELKEEIKKFYGEDPLESPDYGRIinekHFDRLAGLL---------DNGKIVFGGN-TDRETLYIEPT 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1841878009 417 IVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKD 467
Cdd:cd07136 316 ILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSED 366
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
188-513 |
1.24e-26 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 112.32 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 188 PLGLVGIITAFNFPVavygwNNAI-----ALICGNVCLWKGAPTTSLTSVAVTKIIAQVLEKNKLpgAICSlacGGADIG 262
Cdd:cd07134 100 PKGVCLIISPWNYPF-----NLAFgplvsAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV--AVFE---GDAEVA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 263 TAMAkDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRRLFL 342
Cdd:cd07134 170 QALL-ELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 343 HESIHDEVVEKLMKAYAQVRIGDPWDANT-----LYGPLHTKQAVKMFLDAVEvakqQGGSVVCGGKViERPGNYVEPTI 417
Cdd:cd07134 249 HESVKDAFVEHLKAEIEKFYGKDAARKASpdlarIVNDRHFDRLKGLLDDAVA----KGAKVEFGGQF-DAAQRYIAPTV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 418 VIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRWLGPKGS-DCGI-------VNVNI 489
Cdd:cd07134 324 LTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSgGVVVndvvlhfLNPNL 403
|
330 340
....*....|....*....|....
gi 1841878009 490 PtsgaeiggaFGGNKHTGGGRESG 513
Cdd:cd07134 404 P---------FGGVNNSGIGSYHG 418
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
184-524 |
2.84e-25 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 108.48 E-value: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 184 EQWnPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAVTKIIAQVLeknKLPGAICSLACGGADIGT 263
Cdd:cd07084 97 YRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAG---LLPPEDVTLINGDGKTMQ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 264 AMAKDERIDLLSFTGSTNVGKqvALTVQERFGRCLLELGGNNAIIVFEDAD-LNLVIPSALFAAVGTAGQRCTTSRRLFL 342
Cdd:cd07084 173 ALLLHPNPKMVLFTGSSRVAE--KLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 343 HESIHDE-VVEKLMKAYAQVRIGDpwdanTLYGPLHTKQAVKMfldaVEVAKQQGGSVVCGG----KVIERPGNY--VEP 415
Cdd:cd07084 251 PENWSKTpLVEKLKALLARRKLED-----LLLGPVQTFTTLAM----IAHMENLLGSVLLFSgkelKNHSIPSIYgaCVA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 416 T---IVIELPHNSSIVHT-ETFAPILYVLKFKTEEEVFGWNNGVK-QG-LSSSIFTKDLGRIFRWLGPKGSDCGIVNVNI 489
Cdd:cd07084 322 SalfVPIDEILKTYELVTeEIFGPFAIVVEYKKDQLALVLELLERmHGsLTAAIYSNDPIFLQELIGNLWVAGRTYAILR 401
|
330 340 350
....*....|....*....|....*....|....*..
gi 1841878009 490 PTSGAEIGG--AFGGNKHTGGGRESGSDSWKQYMRRS 524
Cdd:cd07084 402 GRTGVAPNQnhGGGPAADPRGAGIGGPEAIKLVWRCH 438
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
186-524 |
1.79e-22 |
|
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: 100.81 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 186 WNPLGLVGI-ITAFNFPVavygW----NNAIALICGNVCLWKGAPTTSLTSVAVTKIIaqvLEKNKLP-GAIcSLACGGA 259
Cdd:cd07128 141 LTPRRGVAVhINAFNFPV----WgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDI---VESGLLPeGAL-QLICGSV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 260 diGTAMAKDERIDLLSFTGSTNVGKQVAL--TVQERFGRCLLELGGNNAIIVFEDA-----DLNLVIPSALFAAVGTAGQ 332
Cdd:cd07128 213 --GDLLDHLGEQDVVAFTGSAATAAKLRAhpNIVARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 333 RCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLDAVEvAKQQGGSVVCGGKVIERP--- 409
Cdd:cd07128 291 KCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVA-TLLAEAEVVFGGPDRFEVvga 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 410 ----GNYVEPTI-VIELPHNSSIVH-TETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKD---LGRIFRWLGPKGs 480
Cdd:cd07128 370 daekGAFFPPTLlLCDDPDAATAVHdVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDpafARELVLGAAPYH- 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1841878009 481 dcGIVNVNIPTSGAEIGG--------AFGGNKHTGGGRE-SGSDSWKQYMRRS 524
Cdd:cd07128 449 --GRLLVLNRDSAKESTGhgsplpqlVHGGPGRAGGGEElGGLRGVKHYMQRT 499
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
172-448 |
4.14e-22 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 99.10 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 172 MLPSER-------PGHALIeQWNPLGLVGIITAFNFPVAVygwnnAIA-LIC----GNVCLWKGAPTTSLTSVAVTKIIA 239
Cdd:cd07133 79 MKPSRRhvgllflPAKAEV-EYQPLGVVGIIVPWNYPLYL-----ALGpLIAalaaGNRVMIKPSEFTPRTSALLAELLA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 240 QVLEKNKLpgaicSLACGGADIGTAMAKdERIDLLSFTGSTNVGKQVA------LT-VQerfgrclLELGGNNAIIVFED 312
Cdd:cd07133 153 EYFDEDEV-----AVVTGGADVAAAFSS-LPFDHLLFTGSTAVGRHVMraaaenLTpVT-------LELGGKSPAIIAPD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 313 ADLNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQvRIGDpWDANTLYGPLHTKQAVKMFLDAVEVA 392
Cdd:cd07133 220 ADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAK-MYPT-LADNPDYTSIINERHYARLQGLLEDA 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841878009 393 KQQGGSVVcggKVIERPGNYVE-----PTIVIELPHNSSIVHTETFAPILYVLKFKTEEEV 448
Cdd:cd07133 298 RAKGARVI---ELNPAGEDFAAtrklpPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEA 355
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
185-467 |
1.29e-21 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 97.68 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 185 QWNPLGLVGIITAFNFPVA-----VYGwnnAIAliCGNVCLWKGAPTTSLTSVAVTKIIAQVLEKNKLPgaicsLACGGA 259
Cdd:cd07132 97 YKEPLGVVLIIGAWNYPLQltlvpLVG---AIA--AGNCVVIKPSEVSPATAKLLAELIPKYLDKECYP-----VVLGGV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 260 DIGTAMAKdERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGTAGQRCTTSRR 339
Cdd:cd07132 167 EETTELLK-QRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 340 LFLHESIHDEVVEKLMKAYAQVRIGDPWDANTlYGPLHTK---QAVKMFLDavevakqqGGSVVCGGKVIERPgNYVEPT 416
Cdd:cd07132 246 VLCTPEVQEKFVEALKKTLKEFYGEDPKESPD-YGRIINDrhfQRLKKLLS--------GGKVAIGGQTDEKE-RYIAPT 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1841878009 417 IVIELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKD 467
Cdd:cd07132 316 VLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
188-517 |
2.36e-18 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 87.47 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 188 PLGLVGIITAFNFPVA-----VYGwnnAIAliCGNVCLWKGAPTTSLTSVAVTKIIAQVLEKNklpgAIcSLACGGADIG 262
Cdd:cd07137 101 PLGVVLVISAWNFPFLlslepVIG---AIA--AGNAVVLKPSELAPATSALLAKLIPEYLDTK----AI-KVIEGGVPET 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 263 TAMAkDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVGT-AGQRCTTSRRLF 341
Cdd:cd07137 171 TALL-EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 342 LHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTK--QAVKMFLDAVEVAKqqggSVVCGGKvIERPGNYVEPTIVI 419
Cdd:cd07137 250 VEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHhfQRLSRLLDDPSVAD----KIVHGGE-RDEKNLYIEPTILL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 420 ELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFT--KDLGRIFRWLGPKGS----DCgIVNVNIPTSg 493
Cdd:cd07137 325 DPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTknKELKRRIVAETSSGGvtfnDT-VVQYAIDTL- 402
|
330 340
....*....|....*....|....
gi 1841878009 494 aeiggAFGGNKHTGGGRESGSDSW 517
Cdd:cd07137 403 -----PFGGVGESGFGAYHGKFSF 421
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
188-523 |
4.35e-16 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 80.86 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 188 PLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAVTKIIAQVLEknklPGAICSLAcgGADIGTAMAK 267
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLD----SSAVRVVE--GAVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 268 DERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIVFEDADLNLVIPSALFAAVG-TAGQRCTTSRRLFLHESI 346
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEY 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 347 HDEVVEKLMKAYAQVRIGDPW---DANTLYGPLHTKQAVKMfLDAVEVAKQqggsVVCGGKViERPGNYVEPTIVIELPH 423
Cdd:PLN02174 266 APKVIDAMKKELETFYGKNPMeskDMSRIVNSTHFDRLSKL-LDEKEVSDK----IVYGGEK-DRENLKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 424 NSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDlGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGN 503
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHN-KKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGV 418
|
330 340
....*....|....*....|
gi 1841878009 504 KHTGGGRESGSDSWKQYMRR 523
Cdd:PLN02174 419 GESGMGAYHGKFSFDAFSHK 438
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
81-524 |
6.85e-16 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 80.52 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 81 IAKVRQANLEDYEETikkakeawqiwaeipAPKRGEIVRqiGDAlrdKIKVLGNLVSL----EMGKifveGVGEVQEYVD 156
Cdd:PRK11903 72 IVKVLQANRDAYYDI---------------ATANSGTTR--NDS---AVDIDGGIFTLgyyaKLGA----ALGDARLLRD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 157 ICDYAVGLSRMFGGPMLPSERPGHALIeqwnplglvgiITAFNFPVavYG-WNNA-IALICGNVCLWKGAPTTSLTSvav 234
Cdd:PRK11903 128 GEAVQLGKDPAFQGQHVLVPTRGVALF-----------INAFNFPA--WGlWEKAaPALLAGVPVIVKPATATAWLT--- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 235 TKIIAQVLEKNKLPGAICSLACGGAdiGTAMAKDERIDLLSFTGSTNVGKQVAL--TVQERFGRCLLELGGNNAIIVFED 312
Cdd:PRK11903 192 QRMVKDVVAAGILPAGALSVVCGSS--AGLLDHLQPFDVVSFTGSAETAAVLRShpAVVQRSVRVNVEADSLNSALLGPD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 313 AD-----LNLVIPSALFAAVGTAGQRCTTSRRLFLHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTKQAVKMFLD 387
Cdd:PRK11903 270 AApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 388 AVEVAKQQGGSVVCGGKV--IERP---GNYVEPTI-VIELPHNSSIVH-TETFAPILYVLKFKTEEEVFGWNNGVKQGLS 460
Cdd:PRK11903 350 GLAALRAQAEVLFDGGGFalVDADpavAACVGPTLlGASDPDAATAVHdVEVFGPVATLLPYRDAAHALALARRGQGSLV 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841878009 461 SSIFTKD---LGRIFRWLGPKGsdcGIVNVNIPTSGAEIGG--------AFGGNKHTGGGRE-SGSDSWKQYMRRS 524
Cdd:PRK11903 430 ASVYSDDaafLAAAALELADSH---GRVHVISPDVAALHTGhgnvmpqsLHGGPGRAGGGEElGGLRALAFYHRRS 502
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
188-524 |
9.35e-14 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 73.61 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 188 PLGLVGIITAFNFPV--AVYGWNNAIAliCGNVCLWKGAPTTSLTSVAVTKIIAQVLEKNKLpgaicSLACGGADIGTAM 265
Cdd:PLN02203 108 PLGVVLIFSSWNFPIglSLEPLIGAIA--AGNAVVLKPSELAPATSAFLAANIPKYLDSKAV-----KVIEGGPAVGEQL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 266 AkDERIDLLSFTGSTNVGKQVALTVQERFGRCLLELGGNNAIIV---FEDADLNLVIPSALFAAVGT-AGQRCTTSRRLF 341
Cdd:PLN02203 181 L-QHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 342 LHESIHDEVVEKLMKAYAQVRIGDPWDANTLYGPLHTK--QAVKMFLDAVEVAkqqgGSVVCGGKVIERpGNYVEPTIVI 419
Cdd:PLN02203 260 VEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKhfQRLSNLLKDPRVA----ASIVHGGSIDEK-KLFIEPTILL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 420 ELPHNSSIVHTETFAPILYVLKFKTEEEVFGWNNGVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEiGGA 499
Cdd:PLN02203 335 NPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACD-SLP 413
|
330 340 350
....*....|....*....|....*....|.
gi 1841878009 500 FGGNKHTGGGRESGSDSW------KQYMRRS 524
Cdd:PLN02203 414 FGGVGESGFGRYHGKYSFdtfsheKAVLRRS 444
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
60-447 |
6.16e-13 |
|
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: 70.99 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 60 NGSWGGRGEIVTTYCPANNQPIAKVRQANLEDYEETIKKAKEAWQ--IWAEIPAPKR----GEIVRQIGDALRdKIKV-- 131
Cdd:cd07126 4 AGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKsgLHNPLKNPERyllyGDVSHRVAHELR-KPEVed 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 132 -LGNLVSLEMGKIFVEGVGEV---QEYV-----DICDYavgLSRMFGGPMLPSERPGHALieQWnPLGLVGIITAFNFPV 202
Cdd:cd07126 83 fFARLIQRVAPKSDAQALGEVvvtRKFLenfagDQVRF---LARSFNVPGDHQGQQSSGY--RW-PYGPVAIITPFNFPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 203 AVYGWNNAIALICGNVCLWKGAPTTSLtsvaVTKIIAQVLEKNKLPGAICSLA-CGGADIGTAMaKDERIDLLSFTGSTN 281
Cdd:cd07126 157 EIPALQLMGALFMGNKPLLKVDSKVSV----VMEQFLRLLHLCGMPATDVDLIhSDGPTMNKIL-LEANPRMTLFTGSSK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 282 VGKQVALTVQerfGRCLLELGGNNAIIVFED-ADLNLVIPSALFAAVGTAGQRCTTSRRLFLHES-IHDEVVEKLMKAYA 359
Cdd:cd07126 232 VAERLALELH---GKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 360 QVRIGDpwdanTLYGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKVIE---RPGNY--VEPTIV------IELPHNSSIV 428
Cdd:cd07126 309 QRKLED-----LTIGPVLTWTTERILDHVDKLLAIPGAKVLFGGKPLTnhsIPSIYgaYEPTAVfvpleeIAIEENFELV 383
|
410
....*....|....*....
gi 1841878009 429 HTETFAPILYVLKFKTEEE 447
Cdd:cd07126 384 TTEVFGPFQVVTEYKDEQL 402
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
188-448 |
1.45e-11 |
|
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: 66.41 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 188 PLGLVGIITAFNFPVA--VYGWNNAIALICGNVCLWKGAPTTSLTSVAVTKIIAQVLEKNKLPGAICSL-ACGGADIGTA 264
Cdd:cd07129 105 PLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAALRATGLPAGVFSLlQGGGREVGVA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 265 MAKDERIDLLSFTGSTNVGKQVALTVQER------FGrcllELGGNNAIIVFedadlnlviPSAL----------FAA-- 326
Cdd:cd07129 185 LVKHPAIKAVGFTGSRRGGRALFDAAAARpepipfYA----ELGSVNPVFIL---------PGALaergeaiaqgFVGsl 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 327 VGTAGQRCTTSRRLFLHESIH-DEVVEKLMKAYAQVrigDPwdantlyGPLHTKQAVKMFLDAVEVAKQQGGSVVCGGKV 405
Cdd:cd07129 252 TLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAA---PA-------QTMLTPGIAEAYRQGVEALAAAPGVRVLAGGA 321
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1841878009 406 IERPGNYVEPTIV---IELPHNSSIVHTETFAPILYVLKFKTEEEV 448
Cdd:cd07129 322 AAEGGNQAAPTLFkvdAAAFLADPALQEEVFGPASLVVRYDDAAEL 367
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
188-441 |
1.15e-07 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 54.41 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 188 PLGLVGIITAFNFPVavygWNNA----IALICGNVCLWKGAPTTSLTSVAVTKIIAQVLEKNKLPGAICSLACG--GADI 261
Cdd:cd07127 193 PRGVALVIGCSTFPT----WNGYpglfASLATGNPVIVKPHPAAILPLAITVQVAREVLAEAGFDPNLVTLAADtpEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 262 GTAMAKDERIDLLSFTGSTNVGKQVALTVqeRFGRCLLELGGNNAIIVFEDADL-----NLVIPSALFaavgtAGQRCTT 336
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSNAFGDWLEANA--RQAQVYTEKAGVNTVVVDSTDDLkamlrNLAFSLSLY-----SGQMCTT 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 337 SRRLFL----------HESiHDEVVEKLMKAYAQVrIGDPWDANTLYGPLHTKQAVKMFLDAvevakQQGGSVVCGGKVI 406
Cdd:cd07127 342 PQNIYVprdgiqtddgRKS-FDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIAEA-----RQLGEVLLASEAV 414
|
250 260 270
....*....|....*....|....*....|....*....
gi 1841878009 407 ERP---GNYVEPTIVIELPHNSSIVHT-ETFAPILYVLK 441
Cdd:cd07127 415 AHPefpDARVRTPLLLKLDASDEAAYAeERFGPIAFVVA 453
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
93-354 |
1.55e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 47.65 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 93 EETIKKAKEAWQIWAEIPAPKRGEIVRQIGDALRDKIKVLGNLVSLEMGKIFVEGvgEVQEYVDICDYAVGLSRMFGGPM 172
Cdd:cd07081 2 DDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVED--KVIKNHFAAEYIYNVYKDEKTCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 173 LPSERPGHALIEQWNPLGLVGIITAFNFPVAVYGWNNAIALICGNVCLWKGAPTTSLTSVAVTKIIAQVLEKNKLP-GAI 251
Cdd:cd07081 80 VLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPeNLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841878009 252 CSLACGGADIGTAMAKDERIDLLSFTGSTNVGKQValtvqERFGRCLLELG-GNNAIIVFEDADLNLVIPSALFAAVGTA 330
Cdd:cd07081 160 GWIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAA-----YSSGKPAIGVGaGNTPVVIDETADIKRAVQSIVKSKTFDN 234
|
250 260
....*....|....*....|....
gi 1841878009 331 GQRCTTSRRLFLHESIHDEVVEKL 354
Cdd:cd07081 235 GVICASEQSVIVVDSVYDEVMRLF 258
|
|
| |
