|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
22-484 |
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: 824.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGE 101
Cdd:cd07130 15 TSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLT 181
Cdd:cd07130 95 VQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 182 ALACQALFERVLKnFKDAPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMIL 261
Cdd:cd07130 175 AIAVTKIVARVLE-KNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 262 GPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDKHGFDAMQDAL 340
Cdd:cd07130 254 MEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDdGTLVGPLHTKAAVDNYLAAI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 341 EQALSEGGKV-FGGKRQLEDkfpnAYYVSPAIVEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTT 419
Cdd:cd07130 334 EEAKSQGGTVlFGGKVIDGP----GNYVEPTIVEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTT 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224333486 420 DVREAEQFMSAVGSDCGIANVNIGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQTNTVNYS 484
Cdd:cd07130 410 DLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
23-484 |
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: 771.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEV 102
Cdd:cd07086 17 SRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 103 QEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTA 182
Cdd:cd07086 97 QEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 183 LACQALFERVLKnFKDAPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILG 262
Cdd:cd07086 177 IAVTKILAEVLE-KNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVM 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 263 PSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQDALE 341
Cdd:cd07086 256 DDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLdEGTLVGPLINQAAVEKYLNAIE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 342 QALSEGGKV-FGGKRQleDKFPNAYYVSPAIVEMPEQSD-VVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTT 419
Cdd:cd07086 336 IAKSQGGTVlTGGKRI--DGGEPGNYVEPTIVTGVTDDArIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTE 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224333486 420 DVREAEQFMSAVGSDCGIANVNIGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQTNTVNYS 484
Cdd:cd07086 414 DLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
25-495 |
8.02e-176 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 503.98 E-value: 8.02e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 25 SPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQE 104
Cdd:PLN02315 40 NPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 105 MIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTALA 184
Cdd:PLN02315 120 IIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 185 CQALFERVLKNfKDAPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPS 264
Cdd:PLN02315 200 MTKLVAEVLEK-NNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 265 ADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDKHGFDAMQDALEQA 343
Cdd:PLN02315 279 ADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEkGTLLGPLHTPESKKNFEKGIEII 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 344 LSEGGKVFGGKRQLEdkfPNAYYVSPAIVEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVRE 423
Cdd:PLN02315 359 KSQGGKILTGGSAIE---SEGNFVQPTIVEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPET 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224333486 424 AEQFMSAVGSDCGIANVNIGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQTNTVNYSLELPLAQGITF 495
Cdd:PLN02315 436 IFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINYGNELPLAQGINF 507
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
22-483 |
2.03e-171 |
|
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: 491.56 E-value: 2.03e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGE 101
Cdd:COG1012 24 DVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLT 181
Cdd:COG1012 104 VDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 182 ALACQALFERVlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMI 260
Cdd:COG1012 184 ALLLAELLEEA-----GLPAGVLNVVTGdGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 261 LGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQDA 339
Cdd:COG1012 259 VLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLdPGTDMGPLISEAQLERVLAY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 340 LEQALSEGGK-VFGGKRqleDKFPNAYYVSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIF 417
Cdd:COG1012 339 IEDAVAEGAElLTGGRR---PDGEGGYFVEPTVLAdVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVF 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224333486 418 TTDVREAEQFMSAVgsDCGIANVNIGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQTNTVNY 483
Cdd:COG1012 416 TRDLARARRVARRL--EAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
17-478 |
9.18e-155 |
|
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: 448.52 E-value: 9.18e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 17 QAGKQPVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQ 96
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 97 EGLGEVQEMIDICDFAVGLSRQLYGLTIASeRPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSE 176
Cdd:pfam00171 85 EARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 177 KTPLTALACQALFERVlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGG 255
Cdd:pfam00171 164 LTPLTALLLAELFEEA-----GLPAGVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 256 NNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFD 334
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLdPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 335 AMQDALEQALSEGGKVF-GGKRQLEdkfpNAYYVSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGL 412
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLtGGEAGLD----NGYFVEPTVLAnVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224333486 413 SSCIFTTDVREAEQFMSAVgsDCGIANVNIGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQT 478
Cdd:pfam00171 395 AAGVFTSDLERALRVARRL--EAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
44-478 |
3.60e-141 |
|
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: 412.76 E-value: 3.60e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 44 EQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQEMIDICDFAVGLSRQLYGLT 123
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 124 IASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTALACQALFERVLKnfkdaPQYL 203
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGL-----PPGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 204 SQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVGTA 282
Cdd:cd07078 156 LNVVTGdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 283 GQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQDALEQALSEGGKV-FGGKRqleDK 360
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLdPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLlCGGKR---LE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 361 FPNAYYVSPAIVEMPEQSDVVCT-ETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVgsDCGIAN 439
Cdd:cd07078 313 GGKGYFVPPTVLTDVDPDMPIAQeEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERL--EAGTVW 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 1224333486 440 VNIGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQT 478
Cdd:cd07078 391 INDYSVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKT 429
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
39-484 |
1.79e-119 |
|
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: 358.97 E-value: 1.79e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 39 GAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQEMIDICDFAVGLSRQ 118
Cdd:cd07131 35 TASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 119 LYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTALA-CQALFERVLknfk 197
Cdd:cd07131 115 LFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKlVELFAEAGL---- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 198 daPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILF 276
Cdd:cd07131 191 --PPGVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALW 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 277 SAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQDALEQALSEGGKVF-GGK 354
Cdd:cd07131 269 SAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLdEETDMGPLINEAQLEKVLNYNEIGKEEGATLLlGGE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 355 RQLEDKFPNAYYVSPAIVEM-PEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVgs 433
Cdd:cd07131 349 RLTGGGYEKGYFVEPTVFTDvTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDL-- 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1224333486 434 DCGIANVNIGPSGAEIGGAFGGEKETGGG-RESGSDAWRGYMRRQTNTVNYS 484
Cdd:cd07131 427 EAGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYVDYS 478
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
32-469 |
9.32e-111 |
|
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: 336.53 E-value: 9.32e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 32 IGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQEMIDICDF 111
Cdd:cd07097 28 VGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 112 AVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTALACQALFER 191
Cdd:cd07097 108 YAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 192 VlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMA 270
Cdd:cd07097 188 A-----GLPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 271 VRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNL-IGPLIDKHGFDAMQDALEQALSEGGK 349
Cdd:cd07097 263 VECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVdIGPVVSERQLEKDLRYIEIARSEGAK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 350 -VFGGKR-QLEDKfpnAYYVSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQ 426
Cdd:cd07097 343 lVYGGERlKRPDE---GYYLAPALFAgVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATH 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1224333486 427 FMSavGSDCGIANVNIGPSGAEIGGAFGGEKETG-GGRESGSDA 469
Cdd:cd07097 420 FKR--RVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEAA 461
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
49-478 |
1.39e-107 |
|
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: 324.57 E-value: 1.39e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 49 RAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQEMIDICDFAVGLSRQLYGLTIASER 128
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 129 PGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTALACQALFERVLknfkdAPQYLSQVII 208
Cdd:cd06534 82 PGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG-----LPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 209 GGRD-AGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCT 287
Cdd:cd06534 157 GGGDeVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 288 TLRRLIAHESVKEEIVTRLKAAYSKVRighplegnligplidkHGFDAMQdaleqalseggkvfggkrqledkfpnayyv 367
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLVTVLVDVD----------------PDMPIAQ------------------------------ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 368 spaivempeqsdvvcTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVgsDCGIANVNIGPSGA 447
Cdd:cd06534 271 ---------------EEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERL--RAGTVYINDSSIGV 333
|
410 420 430
....*....|....*....|....*....|.
gi 1224333486 448 EIGGAFGGEKETGGGRESGSDAWRGYMRRQT 478
Cdd:cd06534 334 GPEAPFGGVKNSGIGREGGPYGLEEYTRTKT 364
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
23-474 |
1.43e-100 |
|
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: 309.36 E-value: 1.43e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEV 102
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 103 QEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAvwawNTTL----ALVCGNAVIWKPSEKT 178
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAA----MITRkiapALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 179 PLTALACQALFER------VLknfkdapqylsQVIIGGRDA-GAALVDDPRVALISATGSTRMGREVAPKVAARFARSIL 251
Cdd:cd07103 157 PLSALALAELAEEaglpagVL-----------NVVTGSPAEiGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 252 ELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDK 330
Cdd:cd07103 226 ELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLdEGTDMGPLINE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 331 HGFDAMQDALEQALSEGGKV-FGGKRQLEDkfpnAYYVSPAIV-EMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAV 408
Cdd:cd07103 306 RAVEKVEALVEDAVAKGAKVlTGGKRLGLG----GYFYEPTVLtDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDT 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1224333486 409 PQGLSSCIFTTDVREAEQFMSAVgsDCGIANVNIG-PSGAEIggAFGGEKETGGGRESGSDAWRGYM 474
Cdd:cd07103 382 PYGLAAYVFTRDLARAWRVAEAL--EAGMVGINTGlISDAEA--PFGGVKESGLGREGGKEGLEEYL 444
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
23-481 |
8.62e-94 |
|
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: 292.15 E-value: 8.62e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFE--AWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLG 100
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 101 EVQEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPL 180
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 181 TALACQALFERVlkNFkdaPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAM 259
Cdd:cd07114 161 STLELAKLAEEA--GF---PPGVVNVVTGfGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 260 ILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQD 338
Cdd:cd07114 236 IVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLdPETQMGPLATERQLEKVER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 339 ALEQALSEGGKV-FGGKRQLEDKFPNAYYVSPAIVEMPEQSDVVC-TETFAPILYVVGYKDFAEALRLNNAVPQGLSSCI 416
Cdd:cd07114 316 YVARAREEGARVlTGGERPSGADLGAGYFFEPTILADVTNDMRIAqEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224333486 417 FTTDVREAEQFMSAVgsDCGIANVN----IGPSgaeigGAFGGEKETGGGRESGSDAWRGYMrrQTNTV 481
Cdd:cd07114 396 WTRDLARAHRVARAI--EAGTVWVNtyraLSPS-----SPFGGFKDSGIGRENGIEAIREYT--QTKSV 455
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
19-483 |
6.73e-92 |
|
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: 289.12 E-value: 6.73e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 19 GKQPVHSPIDGSRI-GSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQE 97
Cdd:cd07124 46 EKIESRNPADPSEVlGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 98 GLGEVQEMIDICDFAVGLSRQLYGLTiASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEK 177
Cdd:cd07124 126 ADADVAEAIDFLEYYAREMLRLRGFP-VEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAED 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 178 TPLTAlacqALFERVLKnfkDA--PQYLSQVIIG-GRDAGAALVDDPRVALISATGStrmgREVAPKVAARFA------- 247
Cdd:cd07124 205 TPVIA----AKLVEILE---EAglPPGVVNFLPGpGEEVGDYLVEHPDVRFIAFTGS----REVGLRIYERAAkvqpgqk 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 248 ---RSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNL 323
Cdd:cd07124 274 wlkRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDpEVY 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 324 IGPLIDKHGFDAMQDALEQALSEGGKVFGGKRqlEDKFPNAYYVSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEAL 402
Cdd:cd07124 354 MGPVIDKGARDRIRRYIEIGKSEGRLLLGGEV--LELAAEGYFVQPTIFAdVPPDHRLAQEEIFGPVLAVIKAKDFDEAL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 403 RLNNAVPQGLSSCIFTTDVREAEQFMSAVgsDCGIANVNIGPSGAEIG-GAFGGEKETG-GGRESGSDAWRGYMRRQTNT 480
Cdd:cd07124 432 EIANDTEYGLTGGVFSRSPEHLERARREF--EVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDYLLQFMQPKTVT 509
|
...
gi 1224333486 481 VNY 483
Cdd:cd07124 510 ENF 512
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
42-481 |
9.13e-92 |
|
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: 285.96 E-value: 9.13e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 42 EVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQEMIDICDFAVGLSRQLYG 121
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 122 LTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTAlacQALFERVlknFKDA-- 199
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTG---GLLIAEI---FEEAgl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 200 PQYLSQVIIGGRD-AGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSA 278
Cdd:cd07104 155 PKGVLNVVPGGGSeIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 279 VGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGN-LIGPLIDKHGFDAMQDALEQALSEGGKVF-GGKRQ 356
Cdd:cd07104 235 FLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDtVIGPLINERQVDRVHAIVEDAVAAGARLLtGGTYE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 357 ledkfpNAYYVSPAIVEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFmsAVGSDCG 436
Cdd:cd07104 315 ------GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAF--AERLETG 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1224333486 437 IANVNIGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQTNTV 481
Cdd:cd07104 387 MVHINDQTVNDEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
21-478 |
5.93e-91 |
|
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: 285.31 E-value: 5.93e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 21 QPVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLG 100
Cdd:cd07088 15 IDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 101 EVQEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPL 180
Cdd:cd07088 95 EVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 181 TALACQALFERVlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAM 259
Cdd:cd07088 175 NALEFAELVDEA-----GLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 260 ILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNL-IGPLIDKHGFDAMQD 338
Cdd:cd07088 250 IVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATdMGPLVNEAALDKVEE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 339 ALEQALSEGGKV-FGGKRqleDKFPNAYYVSPAIVEMPEQ-SDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCI 416
Cdd:cd07088 330 MVERAVEAGATLlTGGKR---PEGEKGYFYEPTVLTNVRQdMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYI 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224333486 417 FTTDVREAEQFMSAVgsDCGIANVNIGPsGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQT 478
Cdd:cd07088 407 YTENLNTAMRATNEL--EFGETYINREN-FEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKV 465
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
21-464 |
5.42e-88 |
|
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: 277.17 E-value: 5.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 21 QPVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLG 100
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 101 EVQEMIDICDFAVGLSRQLYGLTI---ASE----RPGHHMREtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWK 173
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIpfdASPggegRIGFTIRE---PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 174 PSEKTPLTALA-CQALFERVLknfkdaPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARfaRSIL 251
Cdd:cd07149 158 PASQTPLSALKlAELLLEAGL------PKGALNVVTGsGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--KVTL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 252 ELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDK 330
Cdd:cd07149 230 ELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLdEDTDVGPMISE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 331 HGFDAMQDALEQALSEGGKVF-GGKRQledkfpNAYYvSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAV 408
Cdd:cd07149 310 AEAERIEEWVEEAVEGGARLLtGGKRD------GAIL-EPTVLTdVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDS 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1224333486 409 PQGLSSCIFTTDVREAeqfMSAV-GSDCGIANVNIGPSGAEIGGAFGGEKETGGGRE 464
Cdd:cd07149 383 PYGLQAGVFTNDLQKA---LKAArELEVGGVMINDSSTFRVDHMPYGGVKESGTGRE 436
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
22-474 |
2.61e-87 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 276.57 E-value: 2.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGE 101
Cdd:PLN02278 43 PVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLT 181
Cdd:PLN02278 123 VAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 182 ALACQALFERVlknfkDAPQYLSQVIIGGRDA-GAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMI 260
Cdd:PLN02278 203 ALAAAELALQA-----GIPPGVLNVVMGDAPEiGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 261 LGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQDA 339
Cdd:PLN02278 278 VFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFeEGVTQGPLINEAAVQKVESH 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 340 LEQALSEGGKVF-GGKRQledKFPNAYYVSPAIVEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFT 418
Cdd:PLN02278 358 VQDAVSKGAKVLlGGKRH---SLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFT 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1224333486 419 TDVREAEQFMSAVgsDCGIANVNIGPSGAEIgGAFGGEKETGGGRESGSDAWRGYM 474
Cdd:PLN02278 435 RDLQRAWRVSEAL--EYGIVGVNEGLISTEV-APFGGVKQSGLGREGSKYGIDEYL 487
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
22-467 |
3.42e-87 |
|
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: 274.98 E-value: 3.42e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGE 101
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLT 181
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 182 ALACQALFERVlknfkDAPQYLSQVIIGGRDA-GAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMI 260
Cdd:cd07150 162 GLKIAEIMEEA-----GLPKGVFNVVTGGGAEvGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 261 LGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDKHGFDAMQDA 339
Cdd:cd07150 237 VLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDpDTVIGPLISPRQVERIKRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 340 LEQALSEGGKVFGGkrqleDKFPNAYYVSPAIVEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTT 419
Cdd:cd07150 317 VEDAVAKGAKLLTG-----GKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1224333486 420 DVREAEQFmsAVGSDCGIANVNIGPSGAEIGGAFGGEKETGGGRESGS 467
Cdd:cd07150 392 DLQRAFKL--AERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGE 437
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
24-477 |
8.71e-87 |
|
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: 274.10 E-value: 8.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 24 HSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQ 103
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 104 EMIDICDFAVGLSRQLYGltiASERPGHHM------RETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEK 177
Cdd:cd07099 81 LALEAIDWAARNAPRVLA---PRKVPTGLLmpnkkaTVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 178 TPLTALACQALFERVlknfkDAPQYLSQVIIGGRDAGAALVDDpRVALISATGSTRMGREVAPKVAARFARSILELGGNN 257
Cdd:cd07099 158 TPLVGELLAEAWAAA-----GPPQGVLQVVTGDGATGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 258 AMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNL-IGPLIDKHGFDAM 336
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDAdIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 337 QDALEQALSEGGKVFGGKRQLEDKfpnAYYVSPAI-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSC 415
Cdd:cd07099 312 RRHVDDAVAKGAKALTGGARSNGG---GPFYEPTVlTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSAS 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1224333486 416 IFTTDVREAEQFMSAVgsDCGIANVNIGPSGAEIGGA-FGGEKETGGGRESGSDAWRGYMRRQ 477
Cdd:cd07099 389 VFSRDLARAEAIARRL--EAGAVSINDVLLTAGIPALpFGGVKDSGGGRRHGAEGLREFCRPK 449
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
23-481 |
1.34e-86 |
|
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: 273.67 E-value: 1.34e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGK-ITQEGLGE 101
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKpITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYGLTIASErPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLT 181
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 182 AlacqALFERVlknFKDA--PQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNA 258
Cdd:cd07093 160 A----WLLAEL---ANEAglPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 259 MILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQ 337
Cdd:cd07093 233 NIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLdPDTEVGPLISKEHLEKVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 338 DALEQALSEGGKVF-GGKRQLEDKFPNAYYVSPAIVEMPEQSDVVCT-ETFAPILYVVGYKDFAEALRLNNAVPQGLSSC 415
Cdd:cd07093 313 GYVELARAEGATILtGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQeEIFGPVVTVIPFDDEEEAIELANDTPYGLAAY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224333486 416 IFTTDVREAEQFMSAVgsDCGIANVNiGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQTNTV 481
Cdd:cd07093 393 VWTRDLGRAHRVARRL--EAGTVWVN-CWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
23-478 |
1.62e-85 |
|
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: 270.55 E-value: 1.62e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEV 102
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 103 qemidicDFAVGLSRQLYGLTIASER----PGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKT 178
Cdd:cd07106 81 -------GGAVAWLRYTASLDLPDEVieddDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 179 PLTALACQALFERVLknfkdaPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNA 258
Cdd:cd07106 154 PLCTLKLGELAQEVL------PPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 259 MILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQ 337
Cdd:cd07106 228 AIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLdPGTTLGPVQNKMQYDKVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 338 DALEQALSEGGKVFGGKRQLEDKfpnAYYVSPAIV-EMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCI 416
Cdd:cd07106 308 ELVEDAKAKGAKVLAGGEPLDGP---GYFIPPTIVdDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASV 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224333486 417 FTTDVREAEqfmsAVGS--DCGIANVN----IGPSgaeigGAFGGEKETGGGRESGSDAWRGYMRRQT 478
Cdd:cd07106 385 WSSDLERAE----AVARrlEAGTVWINthgaLDPD-----APFGGHKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-443 |
2.61e-85 |
|
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: 270.93 E-value: 2.61e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 21 QPVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLG 100
Cdd:cd07085 18 LDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 101 EVQEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPL 180
Cdd:cd07085 98 DVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 181 TALacqalfeRVLKNFKDA--PQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNA 258
Cdd:cd07085 178 AAM-------RLAELLQEAglPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 259 MILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQ 337
Cdd:cd07085 251 AVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDdPGADMGPVISPAAKERIE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 338 DALEQALSEGGK-VFGGKRQLEDKFPNAYYVSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSC 415
Cdd:cd07085 331 GLIESGVEEGAKlVLDGRGVKVPGYENGNFVGPTILDnVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAA 410
|
410 420
....*....|....*....|....*...
gi 1224333486 416 IFTTDVREAEQFMSAVgsDCGIANVNIG 443
Cdd:cd07085 411 IFTRSGAAARKFQREV--DAGMVGINVP 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
21-466 |
7.40e-85 |
|
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: 270.99 E-value: 7.40e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 21 QPVHSPIDGSR-IGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGL 99
Cdd:cd07125 48 APVIDPADHERtIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 100 GEVQEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTP 179
Cdd:cd07125 128 AEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 180 LTA-LACQALFErvlknfKDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARS---ILELG 254
Cdd:cd07125 208 LIAaRAVELLHE------AGVPRDVLQLVPGdGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPIlplIAETG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 255 GNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDKHGf 333
Cdd:cd07125 282 GKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDlSTDVGPLIDKPA- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 334 DAMQDALEQALSEGGKVFgGKRQLEDKFPnaYYVSPAIVEMPEqSDVVCTETFAPILYVVGYK--DFAEALRLNNAVPQG 411
Cdd:cd07125 361 GKLLRAHTELMRGEAWLI-APAPLDDGNG--YFVAPGIIEIVG-IFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYG 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1224333486 412 LSSCIFTTDVREAEQFMSAVGSdcGIANVNIGPSGAEIG-GAFGGEKETGGGRESG 466
Cdd:cd07125 437 LTLGIHSRDEREIEYWRERVEA--GNLYINRNITGAIVGrQPFGGWGLSGTGPKAG 490
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
22-465 |
7.31e-84 |
|
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: 266.52 E-value: 7.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGE 101
Cdd:cd07145 2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYGLTIASERPGHHMR----ETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEK 177
Cdd:cd07145 82 VERTIRLFKLAAEEAKVLRGETIPVDAYEYNERriafTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 178 TPLTALACQALFERVlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGN 256
Cdd:cd07145 162 TPLTAIELAKILEEA-----GLPPGVINVVTGyGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 257 NAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDA 335
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLdESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 336 MQDALEQALSEGGKV-FGGKRQledkfPNAYYvSPAIVEMPEQSDVVC-TETFAPILYVVGYKDFAEALRLNNAVPQGLS 413
Cdd:cd07145 317 MENLVNDAVEKGGKIlYGGKRD-----EGSFF-PPTVLENDTPDMIVMkEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQ 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1224333486 414 SCIFTTDVREAEQFMSAVgsDCGIANVNIGPSGAEIGGAFGGEKETGGGRES 465
Cdd:cd07145 391 ASVFTNDINRALKVAREL--EAGGVVINDSTRFRWDNLPFGGFKKSGIGREG 440
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
21-481 |
1.28e-82 |
|
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: 263.66 E-value: 1.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 21 QPVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAW-RNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGL 99
Cdd:cd07082 18 IEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWwPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 100 GEVQEMIDICDFAVGLSRQLYGLTI-------ASERPGHHMREtwhPLGVVGVISAFNFPVavwawNTTL-----ALVCG 167
Cdd:cd07082 98 KEVDRTIDYIRDTIEELKRLDGDSLpgdwfpgTKGKIAQVRRE---PLGVVLAIGPFNYPL-----NLTVsklipALIMG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 168 NAVIWKPSEKTPLTALacqalfeRVLKNFKDA--PQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVApKVAA 244
Cdd:cd07082 170 NTVVFKPATQGVLLGI-------PLAEAFHDAgfPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGNRLK-KQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 245 RFaRSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNL- 323
Cdd:cd07082 242 MK-RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVd 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 324 IGPLIDKHGFDAMQDALEQALSEGGK-VFGGKRQLEDkfpnayYVSPAIVEMP-EQSDVVCTETFAPILYVVGYKDFAEA 401
Cdd:cd07082 321 ITPLIDPKSADFVEGLIDDAVAKGATvLNGGGREGGN------LIYPTLLDPVtPDMRLAWEEPFGPVLPIIRVNDIEEA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 402 LRLNNAVPQGLSSCIFTTDVREAEQFMSAVgsDCGIANVNIGPS-GAEIgGAFGGEKETGGGRESGSDAWRgYMRRQTNT 480
Cdd:cd07082 395 IELANKSNYGLQASIFTKDINKARKLADAL--EVGTVNINSKCQrGPDH-FPFLGRKDSGIGTQGIGDALR-SMTRRKGI 470
|
.
gi 1224333486 481 V 481
Cdd:cd07082 471 V 471
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
23-483 |
6.22e-82 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 261.54 E-value: 6.22e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEV 102
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 103 QEMIDICDFAVGLSRQLYGLTIASERPGHHM--REtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPL 180
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLHYtlRE---PYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 181 TALACQALFERVLknfkdaPQYLSQVIIGGRD-AGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAM 259
Cdd:cd07107 158 SALRLAELAREVL------PPGVFNILPGDGAtAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 260 ILGPSADLDMAVRAILFSA-VGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQ 337
Cdd:cd07107 232 IVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTdPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 338 DALEQALSEGGK-VFGGKRQLEDKFPNAYYVSPAIV-EMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSC 415
Cdd:cd07107 312 HYIDSAKREGARlVTGGGRPEGPALEGGFYVEPTVFaDVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224333486 416 IFTTDVREAEQFMSAVgsDCGIANVNiGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQTNTVNY 483
Cdd:cd07107 392 IWTNDISQAHRTARRV--EAGYVWIN-GSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
23-464 |
1.27e-80 |
|
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: 258.06 E-value: 1.27e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGK-ITQEGLGE 101
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNaLRTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYGLTIASeRPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLT 181
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 182 ALACQALFERVLknfkdaPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMI 260
Cdd:cd07108 160 VLLLAEILAQVL------PAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 261 LGPSADLDMAVRAILFSAVGT-AGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQD 338
Cdd:cd07108 234 VFPDADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLdEATDIGAIISEKQFAKVCG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 339 ALEQALSE-GGKVF-GGKRQLEDKFPNAYYVSPAIV-EMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSC 415
Cdd:cd07108 314 YIDLGLSTsGATVLrGGPLPGEGPLADGFFVQPTIFsGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAY 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1224333486 416 IFTTDVREAEQFMSAVgsDCGIANVNIGpSGAEIGGAFGGEKETGGGRE 464
Cdd:cd07108 394 VWTRDLGRALRAAHAL--EAGWVQVNQG-GGQQPGQSYGGFKQSGLGRE 439
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
23-481 |
1.17e-79 |
|
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: 255.62 E-value: 1.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEA-WRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGE 101
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYGLTIASErPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLT 181
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 182 ALACQALFERVlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMI 260
Cdd:cd07109 160 ALRLAELAEEA-----GLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 261 LGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNLIGPLIDKHGFDAMQDAL 340
Cdd:cd07109 235 VFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 341 EQALSEGGKVFGGKRQLEDKFPNAYYVSPAIV-EMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTT 419
Cdd:cd07109 315 ARARARGARIVAGGRIAEGAPAGGYFVAPTLLdDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224333486 420 DVREAEQFMSAVgsDCGIANVNIGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQTNTV 481
Cdd:cd07109 395 DGDRALRVARRL--RAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
43-464 |
4.91e-79 |
|
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: 253.15 E-value: 4.91e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 43 VEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQEMIDICDF-AVGLSRQLYG 121
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 122 LTIASERPGHHMRetWHPLGVVGVISAFNFP---VAVWAwntTLALVCGNAVIWKPSEKTPLTALACQALFERVlknfkD 198
Cdd:cd07100 81 EPIETDAGKAYVR--YEPLGVVLGIMPWNFPfwqVFRFA---APNLMAGNTVLLKHASNVPGCALAIEELFREA-----G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 199 APQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSA 278
Cdd:cd07100 151 FPEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 279 VGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQDALEQALSEGGKV-FGGKRq 356
Cdd:cd07100 231 LQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMdEDTDLGPLARKDLRDELHEQVEEAVAAGATLlLGGKR- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 357 leDKFPNAYYvSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVgsDC 435
Cdd:cd07100 310 --PDGPGAFY-PPTVLTdVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRL--EA 384
|
410 420 430
....*....|....*....|....*....|
gi 1224333486 436 GIANVN-IGPSGAEIggAFGGEKETGGGRE 464
Cdd:cd07100 385 GMVFINgMVKSDPRL--PFGGVKRSGYGRE 412
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
23-485 |
1.66e-78 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 252.28 E-value: 1.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVhwegAAEVEQQVSRAehaFEAWRNVPAP----RRGELVRQFGDVLRQYKADLGELVSWEAGKITQEG 98
Cdd:cd07146 3 VRNPYTGEVVGTV----PAGTEEALREA---LALAASYRSTltryQRSAILNKAAALLEARREEFARLITLESGLCLKDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 99 LGEVQEMIDICDFAVGLSRQLYGLTIAS-------ERPGHHMREtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVI 171
Cdd:cd07146 76 RYEVGRAADVLRFAAAEALRDDGESFSCdltangkARKIFTLRE---PLGVVLAITPFNHPLNQVAHKIAPAIAANNRIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 172 WKPSEKTPLTALA-CQALFERVLknfkdAPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARfaRSI 250
Cdd:cd07146 153 LKPSEKTPLSAIYlADLLYEAGL-----PPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--RQL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 251 LELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLID 329
Cdd:cd07146 226 LELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMdPATDMGTVID 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 330 KHGFDAMQDALEQALSEGGKV-FGGKRQledkfpNAYYvSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNA 407
Cdd:cd07146 306 EEAAIQIENRVEEAIAQGARVlLGNQRQ------GALY-APTVLDhVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNS 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224333486 408 VPQGLSSCIFTTDVREAEQFMSAVgsDCGIANVNIGPSGAEIGGAFGGEKETG-GGRESGSDAwrgyMRRQTNTVNYSL 485
Cdd:cd07146 379 TAYGLSSGVCTNDLDTIKRLVERL--DVGTVNVNEVPGFRSELSPFGGVKDSGlGGKEGVREA----MKEMTNVKTYSL 451
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
25-473 |
3.18e-78 |
|
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: 251.59 E-value: 3.18e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 25 SPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGK-ITQEGLGEVQ 103
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKpIRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 104 EMIDICDFAVGLSRQLYGLTIASERP--GHHMREtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLT 181
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRGPflNYTVRE---PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 182 ALACQALFERVlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMI 260
Cdd:cd07115 160 ALRIAELMAEA-----GFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 261 LGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNL-IGPLIDKHGFDAMQDA 339
Cdd:cd07115 235 VFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTqMGPLVSQAQFDRVLDY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 340 LEQALSEGGKVF-GGKRQLEdkfpNAYYVSPAIVEMPEQSDVVCT-ETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIF 417
Cdd:cd07115 315 VDVGREEGARLLtGGKRPGA----RGFFVEPTIFAAVPPEMRIAQeEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVW 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1224333486 418 TTDVREAEQFMSAVGSdcgiANVNIGPSGA-EIGGAFGGEKETGGGRESGSDAWRGY 473
Cdd:cd07115 391 TRDLGRAHRVAAALKA----GTVWINTYNRfDPGSPFGGYKQSGFGREMGREALDEY 443
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
42-469 |
1.16e-76 |
|
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: 246.80 E-value: 1.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 42 EVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQEMIDICDFAVGLSRQLYG 121
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 122 LTiASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTAlacqalfERVLKNFKDA-- 199
Cdd:cd07095 81 ER-ATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVA-------ELMVELWEEAgl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 200 PQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSI-LELGGNNAMILGPSADLDMAVRAILFSA 278
Cdd:cd07095 153 PPGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLIVQSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 279 VGTAGQRCTTLRRLIAHESVK-EEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQDALEQALSEGGKVFGGKRQ 356
Cdd:cd07095 233 FLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDaEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 357 LEDKfpnAYYVSPAIVEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSavGSDCG 436
Cdd:cd07095 313 LVAG---TAFLSPGIIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLA--RIRAG 387
|
410 420 430
....*....|....*....|....*....|...
gi 1224333486 437 IANVNIGPSGAEIGGAFGGEKETGGGRESGSDA 469
Cdd:cd07095 388 IVNWNRPTTGASSTAPFGGVGLSGNHRPSAYYA 420
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
23-475 |
2.89e-76 |
|
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: 246.47 E-value: 2.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGL-GE 101
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYGLTIASERPGHH---MREtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKT 178
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTsmiRRE---PIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 179 PLTALACQALFERVLknfkdaPQYLSQVIIGGRD-AGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNN 257
Cdd:cd07092 158 PLTTLLLAELAAEVL------PPGVVNVVCGGGAsAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 258 AMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAM 336
Cdd:cd07092 232 PVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDdEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 337 QDALEQAlSEGGKVFGGKRQLEDkfpNAYYVSPAIVEMPEQSD-VVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSC 415
Cdd:cd07092 312 AGFVERA-PAHARVLTGGRRAEG---PGYFYEPTVVAGVAQDDeIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224333486 416 IFTTDVREAEQFMSAVgsDCGIANVNI-GPSGAEIggAFGGEKETGGGRESGSDAWRGYMR 475
Cdd:cd07092 388 VWTRDVGRAMRLSARL--DFGTVWVNThIPLAAEM--PHGGFKQSGYGKDLSIYALEDYTR 444
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
23-464 |
1.56e-75 |
|
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: 244.65 E-value: 1.56e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEV 102
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 103 QEMIDICDFAVGLSRQLYGLTIASE-RPGHHMRETW---HPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKT 178
Cdd:cd07094 83 DRAIDTLRLAAEEAERIRGEEIPLDaTQGSDNRLAWtirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 179 PLTALAcqalFERVLKNFKDAPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKvaARFARSILELGGNNA 258
Cdd:cd07094 163 PLSALE----LAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRAN--AGGKRIALELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 259 MILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQ 337
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLdEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 338 DALEQALSEGGKVFGGKRqledkfPNAYYVSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCI 416
Cdd:cd07094 317 RWVEEAVEAGARLLCGGE------RDGALFKPTVLEdVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGI 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1224333486 417 FTTDVREAeqFMSAVGSDCGIANVNIGPSGAEIGGAFGGEKETGGGRE 464
Cdd:cd07094 391 FTRDLNVA--FKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGRE 436
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
23-482 |
1.22e-74 |
|
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: 242.59 E-value: 1.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEV 102
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 103 QEMIDICDFAVGLSRQLYGLTI--ASERPGHHMREtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPL 180
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVplPGGSFAYTRRE---PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 181 TALAcqaLFERvlknFKDA--PQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNA 258
Cdd:cd07090 158 TALL---LAEI----LTEAglPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 259 MILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQ 337
Cdd:cd07090 231 LIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLdEDTQMGALISEEHLEKVL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 338 DALEQALSEGGKVF-GGKR-QLEDKFPNAYYVSPAI-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSS 414
Cdd:cd07090 311 GYIESAKQEGAKVLcGGERvVPEDGLENGFYVSPCVlTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 415 CIFTTDVREAEQFMSAV--GSdCGIANVNIGPsgAEIggAFGGEKETGGGRESGSDAWRGYMRRQTNTVN 482
Cdd:cd07090 391 GVFTRDLQRAHRVIAQLqaGT-CWINTYNISP--VEV--PFGGYKQSGFGRENGTAALEHYTQLKTVYVE 455
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
22-483 |
1.34e-74 |
|
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: 242.89 E-value: 1.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEA--WRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGK-ITQEG 98
Cdd:cd07091 22 PTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKpLEESA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 99 LGEVQEMIDICDFAVGLSRQLYGLTIasERPGHHMRETWH-PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEK 177
Cdd:cd07091 102 KGDVALSIKCLRYYAGWADKIQGKTI--PIDGNFLAYTRRePIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 178 TPLTALacqalfeRVLKNFKDA--PQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVApKVAAR--FARSILE 252
Cdd:cd07091 180 TPLSAL-------YLAELIKEAgfPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIM-EAAAKsnLKKVTLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 253 LGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKH 331
Cdd:cd07091 252 LGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFdPDTFQGPQVSKA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 332 GFDAMQDALEQALSEGGKVFGGKRQLEDKfpnAYYVSPAI-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQ 410
Cdd:cd07091 332 QFDKILSYIESGKKEGATLLTGGERHGSK---GYFIQPTVfTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEY 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224333486 411 GLSSCIFTTDVREAEQFMSAVGSdcGIANVNigpSGAEIGGA--FGGEKETGGGRESGSDAWRGYMrrQTNTVNY 483
Cdd:cd07091 409 GLAAGVFTKDINKALRVSRALKA--GTVWVN---TYNVFDAAvpFGGFKQSGFGRELGEEGLEEYT--QVKAVTI 476
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
21-466 |
2.04e-74 |
|
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: 242.21 E-value: 2.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 21 QPVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLG 100
Cdd:cd07151 12 IDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 101 EVQEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPL 180
Cdd:cd07151 92 EWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 181 TAlacQALFERVlknFKDA--PQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNN 257
Cdd:cd07151 172 TG---GLLLAKI---FEEAglPKGVLNVVVGaGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 258 AMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDKHGFDAM 336
Cdd:cd07151 246 PFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDpDTVVGPLINESQVDGL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 337 QDALEQALSEGG-KVFGGKRQledkfpnAYYVSPAI-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSS 414
Cdd:cd07151 326 LDKIEQAVEEGAtLLVGGEAE-------GNVLEPTVlSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSG 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1224333486 415 CIFTTDVREAEQFmsAVGSDCGIANVNIGPSGAEIGGAFGGEKETGGGRESG 466
Cdd:cd07151 399 AVFTSDLERGVQF--ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNG 448
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
23-478 |
5.32e-74 |
|
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: 240.99 E-value: 5.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAW-RNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGK-ITQEGLG 100
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGApVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 101 EVQEMIDICDFAVGLSRQLYG---LTIASERPGHHMRETWH-PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSE 176
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWefdLPVPALRGGPGRRVVRRePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 177 KTPLTALACQALFERVlknfkDAPQ-YLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGG 255
Cdd:cd07089 161 DTPLSALLLGEIIAET-----DLPAgVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 256 NNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFD 334
Cdd:cd07089 236 KSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPAdPGTVMGPLISAAQRD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 335 AMQDALEQALSEGGK-VFGGKRqlEDKFPNAYYVSPAI-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGL 412
Cdd:cd07089 316 RVEGYIARGRDEGARlVTGGGR--PAGLDKGFYVEPTLfADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224333486 413 SSCIFTTDVREAeqfmSAVGS--DCGIANVNiGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQT 478
Cdd:cd07089 394 SGGVWSADVDRA----YRVARriRTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
29-481 |
1.62e-73 |
|
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: 239.12 E-value: 1.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 29 GSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQEMIDI 108
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 109 CDFAVGLSRQLYGLTIASERPghHMRETWH-PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTAlacQA 187
Cdd:cd07152 81 LHEAAGLPTQPQGEILPSAPG--RLSLARRvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSG---GV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 188 LFERVlknFKDA--PQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSA 265
Cdd:cd07152 156 VIARL---FEEAglPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 266 DLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNL-IGPLIDKHGFDAMQDALEQAL 344
Cdd:cd07152 233 DLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVaLGPLINARQLDRVHAIVDDSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 345 SEGGKVFGGKRQlEDKFPNAYYVSPAIVEMPEQSDvvctETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREA 424
Cdd:cd07152 313 AAGARLEAGGTY-DGLFYRPTVLSGVKPGMPAFDE----EIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 425 EqfmsAVGS--DCGIANVNIGPSGAEIGGAFGGEKETG-GGRESGSDAWRGYMRRQTNTV 481
Cdd:cd07152 388 M----ALADrlRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
25-473 |
4.80e-72 |
|
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: 235.70 E-value: 4.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 25 SPIDGSRIGSVHWEGAAEVEQQVSRAEHAFE--AWRNVPApRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEV 102
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 103 QEMIDICDFAVGLSRQLYGlTIASERPGHH---MREtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTP 179
Cdd:cd07120 82 SGAISELRYYAGLARTEAG-RMIEPEPGSFslvLRE---PMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 180 LTAlacqALFERVLKNFKDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNA 258
Cdd:cd07120 158 QIN----AAIIRILAEIPSLPAGVVNLFTEsGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 259 MILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDKHGFDAMQ 337
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDpASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 338 DALEQALSEGGKVF--GGKrqLEDKFPNAYYVSPAIVEMPE-QSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSS 414
Cdd:cd07120 314 RMVERAIAAGAEVVlrGGP--VTEGLAKGAFLRPTLLEVDDpDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAA 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1224333486 415 CIFTTDVREAeqFMSAVGSDCGIANVNigpsgaeIGGAFGGEKETGGGRESGSDAWRGY 473
Cdd:cd07120 392 SVWTRDLARA--MRVARAIRAGTVWIN-------DWNKLFAEAEEGGYRQSGLGRLHGV 441
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
3-478 |
1.35e-71 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 236.31 E-value: 1.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 3 AALLDRLGVNPALYQAGKQPVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKAD 82
Cdd:PRK09407 16 FERLRRLTARVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 83 LGELVSWEAGKITQEGLGEVQEMIDICDFavglsrqlYGLTIAS-----ERPG-----HHMRETWHPLGVVGVISAFNFP 152
Cdd:PRK09407 96 LLDLVQLETGKARRHAFEEVLDVALTARY--------YARRAPKllaprRRAGalpvlTKTTELRQPKGVVGVISPWNYP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 153 VAVWAWNTTLALVCGNAVIWKPSEKTPLTALACQALFERvlknfkdA--PQYLSQVIIG-GRDAGAALVDdpRVALISAT 229
Cdd:PRK09407 168 LTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYE-------AglPRDLWQVVTGpGPVVGTALVD--NADYLMFT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 230 GSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAA 309
Cdd:PRK09407 239 GSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 310 YSKVRIGHPLE-GNLIGPLIDKHGFDAMQDALEQALSEGGKVFGGKRQLEDKFPnaYYVSPAIVE-MPEQSDVVCTETFA 387
Cdd:PRK09407 319 VRAMRLGAGYDySADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGP--LFYEPTVLTgVTPDMELAREETFG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 388 PILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEqfmsAVGS--DCGIANVNIG--PSGAEIGGAFGGEKETGGGR 463
Cdd:PRK09407 397 PVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGR----AIAAriRAGTVNVNEGyaAAWGSVDAPMGGMKDSGLGR 472
|
490
....*....|....*
gi 1224333486 464 ESGSDAWRGYMRRQT 478
Cdd:PRK09407 473 RHGAEGLLKYTESQT 487
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
23-474 |
2.57e-70 |
|
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: 231.09 E-value: 2.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEV 102
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 103 QEMIDICDFAVGLSRQL---YGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTP 179
Cdd:cd07110 81 DDVAGCFEYYADLAEQLdakAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 180 LTalaCQALFErVLKNFKDAPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAM 259
Cdd:cd07110 161 LT---ELELAE-IAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 260 ILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQD 338
Cdd:cd07110 237 IVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLeEGVRLGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 339 ALEQALSEGGK-VFGGKRQleDKFPNAYYVSPAI-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCI 416
Cdd:cd07110 317 FIARGKEEGARlLCGGRRP--AHLEKGYFIAPTVfADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1224333486 417 FTTDVREAEQFMSAVgsDCGIANVNiGPSGAEIGGAFGGEKETGGGRESGSDAWRGYM 474
Cdd:cd07110 395 ISRDAERCDRVAEAL--EAGIVWIN-CSQPCFPQAPWGGYKRSGIGRELGEWGLDNYL 449
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
22-464 |
1.21e-69 |
|
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: 229.44 E-value: 1.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGE 101
Cdd:cd07147 2 EVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYG----LTI---ASERPGHHMRetwHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKP 174
Cdd:cd07147 82 VARAIDTFRIAAEEATRIYGevlpLDIsarGEGRQGLVRR---FPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 175 SEKTPLTALacqaLFERVLKNFKDAPQYLSqVIIGGRDAGAALVDDPRVALISATGSTRMG---REVAPKvaarfARSIL 251
Cdd:cd07147 159 ASRTPLSAL----ILGEVLAETGLPKGAFS-VLPCSRDDADLLVTDERIKLLSFTGSPAVGwdlKARAGK-----KKVVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 252 ELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDK 330
Cdd:cd07147 229 ELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKdDATDVGPMISE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 331 HGFDAMQDALEQALSEGGKVF-GGKRqledkfpNAYYVSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAV 408
Cdd:cd07147 309 SEAERVEGWVNEAVDAGAKLLtGGKR-------DGALLEPTILEdVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDS 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1224333486 409 PQGLSSCIFTTDVREAeqfMSAVGS-DCGIANVNIGPSGAEIGGAFGGEKETGGGRE 464
Cdd:cd07147 382 KFGLQAGVFTRDLEKA---LRAWDElEVGGVVINDVPTFRVDHMPYGGVKDSGIGRE 435
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
19-485 |
1.70e-69 |
|
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: 229.99 E-value: 1.70e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 19 GKQPVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEA-WRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGK-ITQ 96
Cdd:cd07144 23 ETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKpYHS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 97 EGLGEVQEMIDICDFAVGLSRQLYGLTIASERPGHhmRETWH-PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPS 175
Cdd:cd07144 103 NALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKL--AYTLHePYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 176 EKTPLTALACQALfervlknFKDA--PQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVApKVAARFARSI-L 251
Cdd:cd07144 181 ENTPLSLLYFANL-------VKEAgfPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATGRLVM-KAAAQNLKAVtL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 252 ELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKV-RIGHPLEGN-LIGPLID 329
Cdd:cd07144 253 ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDtVVGPQVS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 330 KHGFDAMQDALEQALSEGGKVFGGKRQLEDKFPNAYYVSPAI-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAV 408
Cdd:cd07144 333 KTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGKGYFIPPTIfTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDT 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224333486 409 PQGLSSCIFTTDVREAEQFMSAVGSdcgiANVNIGPSG-AEIGGAFGGEKETGGGRESGSDAWRGYMrrQTNTVNYSL 485
Cdd:cd07144 413 TYGLAAAVFTKDIRRAHRVARELEA----GMVWINSSNdSDVGVPFGGFKMSGIGRELGEYGLETYT--QTKAVHINL 484
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
22-474 |
5.41e-69 |
|
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: 228.35 E-value: 5.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEA--WRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGL 99
Cdd:cd07119 16 DIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 100 GEVQEMIDICDFAVGLSRQLYGLTIasERPGHHMRETWH-PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKT 178
Cdd:cd07119 96 IDIDDVANCFRYYAGLATKETGEVY--DVPPHVISRTVRePVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 179 PLTALACQALFERVlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNN 257
Cdd:cd07119 174 PLTTIALFELIEEA-----GLPAGVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 258 AMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNL-IGPLIDKHGFDAM 336
Cdd:cd07119 249 PNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTeMGPLVSAEHREKV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 337 QDALEQALSEGGK-VFGGKRQLEDKFPNAYYVSPAIVEMPEQS-DVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSS 414
Cdd:cd07119 329 LSYIQLGKEEGARlVCGGKRPTGDELAKGYFVEPTIFDDVDRTmRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAG 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224333486 415 CIFTTDVREAEQFMSAVGSdcGIANVN-IGPSGAEigGAFGGEKETGGGRESGSDAWRGYM 474
Cdd:cd07119 409 AVWTKDIARANRVARRLRA--GTVWINdYHPYFAE--APWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
24-478 |
1.10e-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: 226.81 E-value: 1.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 24 HSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVq 103
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 104 emidiCDFAVGlSRQlYGLT----IASERPGHHM------RETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWK 173
Cdd:cd07101 80 -----LDVAIV-ARY-YARRaerlLKPRRRRGAIpvltrtTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 174 PSEKTPLTALAC-QALFERVLknfkdaPQYLSQVIIG-GRDAGAALVDdpRVALISATGSTRMGREVAPKVAARFARSIL 251
Cdd:cd07101 153 PDSQTALTALWAvELLIEAGL------PRDLWQVVTGpGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRRLIGCSL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 252 ELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDK 330
Cdd:cd07101 225 ELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDyGPDMGSLISQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 331 HGFDAMQDALEQALSEGGKVFGGKRQLEDKFPnaYYVSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVP 409
Cdd:cd07101 305 AQLDRVTAHVDDAVAKGATVLAGGRARPDLGP--YFYEPTVLTgVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTD 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224333486 410 QGLSSCIFTTDVREAEQFmsAVGSDCGIANVNIG--PSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQT 478
Cdd:cd07101 383 YGLNASVWTRDGARGRRI--AARLRAGTVNVNEGyaAAWASIDAPMGGMKDSGLGRRHGAEGLLKYTETQT 451
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
25-488 |
1.87e-68 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 227.38 E-value: 1.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 25 SPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGK-ITQEGLGEVQ 103
Cdd:TIGR02299 22 SPATNEVLGSVARGGAADVDRAAKAAKEAFKRWAELKAAERKRYLHKIADLIEQHADEIAVLECLDCGQpLRQTRQQVIR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 104 EMIDICDFAVGLSRQLYGLTIASerPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTAl 183
Cdd:TIGR02299 102 AAENFRFFADKCEEAMDGRTYPV--DTHLNYTVRVPVGPVGLITPWNAPFMLSTWKIAPALAFGNTVVLKPAEWSPLTA- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 184 acqALFERVLKNFKDAPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGP 263
Cdd:TIGR02299 179 ---ARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNGADTLKRFSMELGGKSPVIVFD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 264 SADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDKHGFDAMQDALEQ 342
Cdd:TIGR02299 256 DADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDpETEVGPLIHPEHLAKVLGYVEA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 343 ALSEGGKVF-GGKRQLE--DKFPNA-YYVSPAI-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIF 417
Cdd:TIGR02299 336 AEKEGATILvGGERAPTfrGEDLGRgNYVLPTVfTGADNHMRIAQEEIFGPVLTVIPFKDEEEAIEKANDTRYGLAGYVW 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224333486 418 TTDVREAEQFMSAVgsDCGIANVNiGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMrrQTNTVNYSLELP 488
Cdd:TIGR02299 416 TNDVGRAHRVALAL--EAGMIWVN-SQNVRHLPTPFGGVKASGIGREGGTYSFDFYT--ETKNVALALGPH 481
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
32-420 |
5.49e-68 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 226.74 E-value: 5.49e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 32 IGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQEMIDICDF 111
Cdd:PRK03137 64 VGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 112 avgLSRQLYGLTIASE---RPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTAlacqAL 188
Cdd:PRK03137 144 ---YARQMLKLADGKPvesRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIA----AK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 189 FERVLKnfkDA--PQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMG---REVAPKVAA---RFARSILELGGNNAM 259
Cdd:PRK03137 217 FVEVLE---EAglPAGVVNFVPGsGSEVGDYLVDHPKTRFITFTGSREVGlriYERAAKVQPgqiWLKRVIAEMGGKDAI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 260 ILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNLIGPLIDKHGFDAMQDA 339
Cdd:PRK03137 294 VVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSY 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 340 LEQALSEGGKVFGGKRQLEDkfpnAYYVSPAIV-EMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFT 418
Cdd:PRK03137 374 IEIGKEEGRLVLGGEGDDSK----GYFIQPTIFaDVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVIS 449
|
..
gi 1224333486 419 TD 420
Cdd:PRK03137 450 NN 451
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
24-473 |
8.70e-68 |
|
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: 224.52 E-value: 8.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 24 HSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEA--WRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGE 101
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYGLT---IASERPGHHMREtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKT 178
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSynnLGDDMLGLVLRE---PIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 179 PLTALACQALFervlknfKDA--PQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGG 255
Cdd:cd07118 159 SGTTLMLAELL-------IEAglPAGVVNIVTGyGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 256 NNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFD 334
Cdd:cd07118 232 KNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLdPETKVGAIINEAQLA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 335 AMQDALEQALSEGGKVFGGKRQLEdkFPNAYYVSPAIV-EMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLS 413
Cdd:cd07118 312 KITDYVDAGRAEGATLLLGGERLA--SAAGLFYQPTIFtDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLS 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224333486 414 SCIFTTDVREAEQFMSAVGSdcGIANVNIGPSG-AEIggAFGGEKETGGGRESGSDAWRGY 473
Cdd:cd07118 390 AGVWSKDIDTALTVARRIRA--GTVWVNTFLDGsPEL--PFGGFKQSGIGRELGRYGVEEY 446
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
16-465 |
2.74e-67 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 224.07 E-value: 2.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 16 YQAGKQPV---HSPIDGSRIgsvhWEG----AAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVS 88
Cdd:PRK09457 9 WIAGQGEAfesRNPVSGEVL----WQGndatAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 89 WEAGKITQEGLGEVQEMIDicdfAVGLSRQLYgltiaSERPGHHMRET--------WHPLGVVGVISAFNFPVAVWAWNT 160
Cdd:PRK09457 85 RETGKPLWEAATEVTAMIN----KIAISIQAY-----HERTGEKRSEMadgaavlrHRPHGVVAVFGPYNFPGHLPNGHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 161 TLALVCGNAVIWKPSEKTPLTAlacqalfERVLKNFKDA--PQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREV 238
Cdd:PRK09457 156 VPALLAGNTVVFKPSELTPWVA-------ELTVKLWQQAglPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 239 APKVAARFARSI-LELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVK-EEIVTRLKAAYSKVRIG 316
Cdd:PRK09457 229 HRQFAGQPEKILaLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 317 HPLEGN--LIGPLIDKHGFDAMQDALEQALSEGGKVFGGKRQLEdkfPNAYYVSPAIVEMPEQSDVVCTETFAPILYVVG 394
Cdd:PRK09457 309 RWDAEPqpFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQ---AGTGLLTPGIIDVTGVAELPDEEYFGPLLQVVR 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224333486 395 YKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVGSdcGIANVNIGPSGAEIGGAFGGEKETGGGRES 465
Cdd:PRK09457 386 YDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRA--GIVNWNKPLTGASSAAPFGGVGASGNHRPS 454
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
23-483 |
2.99e-67 |
|
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: 223.86 E-value: 2.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFE-AWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGK-ITQEGLG 100
Cdd:cd07113 19 ITNPATEQVIASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKsIHLSRAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 101 EVQEMIDICDFAVGLSRQLYGLTIASERPGHH--------MREtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIW 172
Cdd:cd07113 99 EVGQSANFLRYFAGWATKINGETLAPSIPSMQgerytaftRRE---PVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 173 KPSEKTPLTALacqalfeRVLKNFKDA--PQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSI 250
Cdd:cd07113 176 KPSEFTPLTLL-------RVAELAKEAgiPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 251 LELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLID 329
Cdd:cd07113 249 LELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMdESVMFGPLAN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 330 KHGFDAMQDALEQALSEGGKVFGGKRQLEDKfpnAYYVSPAIVEMPEQSDVVCT-ETFAPILYVVGYKDFAEALRLNNAV 408
Cdd:cd07113 329 QPHFDKVCSYLDDARAEGDEIVRGGEALAGE---GYFVQPTLVLARSADSRLMReETFGPVVSFVPYEDEEELIQLINDT 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224333486 409 PQGLSSCIFTTDVREAEQFMSAVgsDCGIANVN----IGPSgaeigGAFGGEKETGGGRESGSDAWRGYMRRQTNTVNY 483
Cdd:cd07113 406 PFGLTASVWTNNLSKALRYIPRI--EAGTVWVNmhtfLDPA-----VPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY 477
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
22-474 |
7.16e-67 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 222.09 E-value: 7.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAW---RNVPAPRRGELVRqFGDVLRQYKADLGELVSWEAGK-ITQE 97
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESGvwsRLSPAERKAVLLR-LADLIEAHRDELALLETLDMGKpISDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 98 GLGEVQEMIDICDFAVGLSRQLYGlTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEK 177
Cdd:cd07112 84 LAVDVPSAANTFRWYAEAIDKVYG-EVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 178 TPLTA-----LACQA-LFERVLknfkdapqylsQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVApKVAAR--FAR 248
Cdd:cd07112 163 SPLTAlrlaeLALEAgLPAGVL-----------NVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFL-EYSGQsnLKR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 249 SILELGGNNAMILGPSA-DLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGP 326
Cdd:cd07112 231 VWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDpATRMGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 327 LIDKHGFDAMQDALEQALSEGGK-VFGGKRQLEDKfpNAYYVSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRL 404
Cdd:cd07112 311 LVSEAHFDKVLGYIESGKAEGARlVAGGKRVLTET--GGFFVEPTVFDgVTPDMRIAREEIFGPVLSVITFDSEEEAVAL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 405 NNAVPQGLSSCIFTTDVREAEQFMSAVgsDCGIANVNiGPSGAEIGGAFGGEKETGGGRESGSDAWRGYM 474
Cdd:cd07112 389 ANDSVYGLAASVWTSDLSRAHRVARRL--RAGTVWVN-CFDEGDITTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
23-478 |
1.42e-66 |
|
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: 221.68 E-value: 1.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEA--WRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGK-ITQEGL 99
Cdd:cd07139 18 VVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARLWTAENGMpISWSRR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 100 GEVQEMIDICDFAVGLSRqlyGLTIASERPGHHM------REtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWK 173
Cdd:cd07139 98 AQGPGPAALLRYYAALAR---DFPFEERRPGSGGghvlvrRE---PVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 174 PSEKTPLTALACQALFERVlknfkDAPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILEL 253
Cdd:cd07139 172 PSPETPLDAYLLAEAAEEA-----GLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLEL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 254 GGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDKHG 332
Cdd:cd07139 247 GGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDpATQIGPLASARQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 333 FDAMQDALEQALSEGGK-VFGGKRqlEDKFPNAYYVSPAIVEMPEQSDVVC-TETFAPILYVVGYKDFAEALRLNNAVPQ 410
Cdd:cd07139 327 RERVEGYIAKGRAEGARlVTGGGR--PAGLDRGWFVEPTLFADVDNDMRIAqEEIFGPVLSVIPYDDEDDAVRIANDSDY 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224333486 411 GLSSCIFTTDVREAeqfmSAVGSDCGIANVNIGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQT 478
Cdd:cd07139 405 GLSGSVWTADVERG----LAVARRIRTGTVGVNGFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKS 468
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
24-427 |
1.27e-65 |
|
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: 218.65 E-value: 1.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 24 HSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQ 103
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 104 EMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFP--VAVwawNTTL-ALVCGNAVIWKPSEKTPL 180
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPylTAV---NAVIpALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 181 TAlacqalfERVLKNFKDA--PQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNA 258
Cdd:cd07102 158 CG-------ERFAAAFAEAglPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 259 MILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDKHGFDAMQ 337
Cdd:cd07102 231 AYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDpSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 338 DALEQALSEGGKVFGGKRQLEDKFPNAYYVSPAI-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCI 416
Cdd:cd07102 311 AQIADAIAKGARALIDGALFPEDKAGGAYLAPTVlTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390
|
410
....*....|.
gi 1224333486 417 FTTDVREAEQF 427
Cdd:cd07102 391 WTKDIARAEAL 401
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
22-464 |
1.94e-64 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 216.31 E-value: 1.94e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGE 101
Cdd:PRK11241 29 DVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLT 181
Cdd:PRK11241 109 ISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 182 ALACQALFERVlknfkDAPQYLSQVIIGGR-DAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMI 260
Cdd:PRK11241 189 ALALAELAIRA-----GIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 261 LGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDKHGFDAMQDA 339
Cdd:PRK11241 264 VFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEkGVTIGPLIDEKAVAKVEEH 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 340 LEQALSEGGKVF-GGK-RQLEDKFpnayyVSPAI-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCI 416
Cdd:PRK11241 344 IADALEKGARVVcGGKaHELGGNF-----FQPTIlVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYF 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1224333486 417 FTTDVreAEQFMSAVGSDCGIANVNIGPSGAEIgGAFGGEKETGGGRE 464
Cdd:PRK11241 419 YARDL--SRVFRVGEALEYGIVGINTGIISNEV-APFGGIKASGLGRE 463
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
22-475 |
2.48e-63 |
|
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: 213.51 E-value: 2.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHwEGAAE-VEQQVSRAEHAFE--AWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEG 98
Cdd:cd07142 22 PTIDPRNGEVIAHVA-EGDAEdVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 99 -LGEVQEMIDICDFAVGLSRQLYGLTIASERPghHMRETWH-PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSE 176
Cdd:cd07142 101 rYAEVPLAARLFRYYAGWADKIHGMTLPADGP--HHVYTLHePIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 177 KTPLTALACQALFERVlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSI-LELG 254
Cdd:cd07142 179 QTPLSALLAAKLAAEA-----GLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSNLKPVtLELG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 255 GNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNL-IGPLIDKHGF 333
Cdd:cd07142 254 GKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVeQGPQVDKEQF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 334 DAMQDALEQALSEGGKVFGGKRQLEDKfpnAYYVSPAIVEMPEQSDVVCT-ETFAPILYVVGYKDFAEALRLNNAVPQGL 412
Cdd:cd07142 334 EKILSYIEHGKEEGATLITGGDRIGSK---GYYIQPTIFSDVKDDMKIARdEIFGPVQSILKFKTVDEVIKRANNSKYGL 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1224333486 413 SSCIFTTDVREAEQFMSAVGSdcGIANVNIGpSGAEIGGAFGGEKETGGGRESGSDAWRGYMR 475
Cdd:cd07142 411 AAGVFSKNIDTANTLSRALKA--GTVWVNCY-DVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
25-476 |
5.85e-63 |
|
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: 213.21 E-value: 5.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 25 SPID-GSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQ 103
Cdd:cd07083 38 SPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 104 EMIDICDF-AVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTA 182
Cdd:cd07083 118 EAIDFIRYyARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 183 LacqalfeRVLKNFKDA--PQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAAR------FARSILEL 253
Cdd:cd07083 198 Y-------KVFEIFHEAgfPPGVVQFLPGvGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLapgqtwFKRLYVET 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 254 GGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDKHG 332
Cdd:cd07083 271 GGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEnGTDLGPVIDAEQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 333 FDAMQDALEQALSEGGKVFGGKRQLEdkfpNAYYVSPAIVEM-PEQSDVVCTETFAPILYVVGYK--DFAEALRLNNAVP 409
Cdd:cd07083 351 EAKVLSYIEHGKNEGQLVLGGKRLEG----EGYFVAPTVVEEvPPKARIAQEEIFGPVLSVIRYKddDFAEALEVANSTP 426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 410 QGLSSCIFTTDVREAEQfmsaVGSDCGIANVNIgpsGAEIGGAFGGEKETGGGRESGSDAWRG---YMRR 476
Cdd:cd07083 427 YGLTGGVYSRKREHLEE----ARREFHVGNLYI---NRKITGALVGVQPFGGFKLSGTNAKTGgphYLRR 489
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
22-475 |
1.79e-62 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 211.28 E-value: 1.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGL-G 100
Cdd:PRK13252 25 EVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSvV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 101 EVQEMIDICDFAVGLSRQLYGLTIaSERPG---HHMREtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEK 177
Cdd:PRK13252 105 DIVTGADVLEYYAGLAPALEGEQI-PLRGGsfvYTRRE---PLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 178 TPLTALacqalfeRVLKNFKDA--PQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGG 255
Cdd:PRK13252 181 TPLTAL-------KLAEIYTEAglPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 256 NNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNL-IGPLIDKHGFD 334
Cdd:PRK13252 254 KSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATnFGPLVSFAHRD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 335 AMQDALEQALSEGGK-VFGGKRQLEDKFPNAYYVSPAIV-----EMPeqsdVVCTETFAPILYVVGYKDFAEALRLNNAV 408
Cdd:PRK13252 334 KVLGYIEKGKAEGARlLCGGERLTEGGFANGAFVAPTVFtdctdDMT----IVREEIFGPVMSVLTFDDEDEVIARANDT 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224333486 409 PQGLSSCIFTTDVREAEQFMSAVgsDCGIANVNI-GPSGAEIggAFGGEKETGGGRESGSDAWRGYMR 475
Cdd:PRK13252 410 EYGLAAGVFTADLSRAHRVIHQL--EAGICWINTwGESPAEM--PVGGYKQSGIGRENGIATLEHYTQ 473
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
17-424 |
2.97e-62 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 210.54 E-value: 2.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 17 QAGKQPVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQ 96
Cdd:PRK13473 15 EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 97 EGLG-EVQEMIDICDFAVGLSRQLYGLTIASERPGH-HM--REtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIW 172
Cdd:PRK13473 95 LALNdEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHtSMirRD---PVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 173 KPSEKTPLTALACQALFERVLknfkdaPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSIL 251
Cdd:PRK13473 172 KPSEITPLTALKLAELAADIL------PPGVLNVVTGrGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 252 ELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDK 330
Cdd:PRK13473 246 ELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDdEDTELGPLISA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 331 HGFDAMQDALEQALSEG-GKVFGGKRQLEDkfPNAYYVSPAIVEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVP 409
Cdd:PRK13473 326 AHRDRVAGFVERAKALGhIRVVTGGEAPDG--KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSD 403
|
410
....*....|....*
gi 1224333486 410 QGLSSCIFTTDVREA 424
Cdd:PRK13473 404 YGLASSVWTRDVGRA 418
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
22-481 |
6.29e-62 |
|
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: 209.90 E-value: 6.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFE---AWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEG 98
Cdd:cd07141 25 PTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 99 -LGEVQEMIDICDFAVGLSRQLYGLTIASErpGHHMRETWH-PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSE 176
Cdd:cd07141 105 yLVDLPGAIKVLRYYAGWADKIHGKTIPMD--GDFFTYTRHePVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 177 KTPLTALACQALfervlknFKDA--PQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAA-RFARSILE 252
Cdd:cd07141 183 QTPLTALYLASL-------IKEAgfPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 253 LGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDKH 331
Cdd:cd07141 256 LGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDpKTEQGPQIDEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 332 GFDAMQDALEQALSEGGK-VFGGKRqLEDKfpnAYYVSPAIVempeqSDV------VCTETFAPILYVVGYKDFAEALRL 404
Cdd:cd07141 336 QFKKILELIESGKKEGAKlECGGKR-HGDK---GYFIQPTVF-----SDVtddmriAKEEIFGPVQQIFKFKTIDEVIER 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1224333486 405 NNAVPQGLSSCIFTTDVREAEQFMSAVgsDCGIANVNIgPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQTNTV 481
Cdd:cd07141 407 ANNTTYGLAAAVFTKDIDKAITFSNAL--RAGTVWVNC-YNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
22-464 |
1.60e-61 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 208.74 E-value: 1.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGe 101
Cdd:cd07559 19 DNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 vqemIDIcDFAV--------------GLSRQLYGLTIAserpgHHMREtwhPLGVVGVISAFNFPVAVWAWNTTLALVCG 167
Cdd:cd07559 98 ----ADI-PLAIdhfryfagviraqeGSLSEIDEDTLS-----YHFHE---PLGVVGQIIPWNFPLLMAAWKLAPALAAG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 168 NAVIWKPSEKTPLTALACQALFERVLknfkdaPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARF 246
Cdd:cd07559 165 NTVVLKPASQTPLSILVLMELIGDLL------PKGVVNVVTGfGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 247 ARSILELGGNNAMILgpSADLDMAVRAILFSAVGTA-------GQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL 319
Cdd:cd07559 239 IPVTLELGGKSPNIF--FDDAMDADDDFDDKAEEGQlgfafnqGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 320 E-GNLIGPLIDKHGFDAMQDALEQALSEGGKVF-GGKRQLEDKFPNAYYVSPAIVEMP-EQSDVVCTETFAPILYVVGYK 396
Cdd:cd07559 317 DpETMMGAQVSKDQLEKILSYVDIGKEEGAEVLtGGERLTLGGLDKGYFYEPTLIKGGnNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1224333486 397 DFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVGS-----DCgianVNIGPSGAeiggAFGGEKETGGGRE 464
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTgrvwvNC----YHQYPAHA----PFGGYKKSGIGRE 461
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
22-483 |
4.46e-61 |
|
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: 207.43 E-value: 4.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGE 101
Cdd:TIGR01722 19 PVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLT 181
Cdd:TIGR01722 99 VARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 182 ALACQALFERvlknfKDAPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMIL 261
Cdd:TIGR01722 179 AVKLAELFSE-----AGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 262 GPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKE---EIVTRLKaaysKVRIGHPLE-GNLIGPLIDKHGFDAMQ 337
Cdd:TIGR01722 254 MPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAADEwvpEIRERAE----KIRIGPGDDpGAEMGPLITPQAKDRVA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 338 DALEQALSEGGKV-FGGKRQLEDKFPNAYYVSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSC 415
Cdd:TIGR01722 330 SLIAGGAAEGAEVlLDGRGYKVDGYEEGNWVGPTLLErVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTA 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224333486 416 IFTTDVREAEQFMSAVgsDCGIANVNIgPSGAEIG-GAFGGEKET--GGGRESGSDAWRGYMRRQTNTVNY 483
Cdd:TIGR01722 410 IFTRDGAAARRFQHEI--EVGQVGVNV-PIPVPLPyFSFTGWKDSffGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
23-485 |
4.50e-61 |
|
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: 207.38 E-value: 4.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFE-AW-RNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGK-ITQEGL 99
Cdd:cd07143 26 VYNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWgLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKtFGTAKR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 100 GEVQEMIDICDFAVGLSRQLYGLTIasERPGHHMRETWH-PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKT 178
Cdd:cd07143 106 VDVQASADTFRYYGGWADKIHGQVI--ETDIKKLTYTRHePIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 179 PLTALacqalfeRVLKNFKDA--PQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVA-ARFARSILELG 254
Cdd:cd07143 184 PLSAL-------YMTKLIPEAgfPPGVINVVSGyGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAkSNLKKVTLELG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 255 GNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNLI-GPLIDKHGF 333
Cdd:cd07143 257 GKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFqGPQVSQIQY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 334 DAMQDALEQALSEGGKV-FGGKRQLEDkfpnAYYVSPAIV-EMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQG 411
Cdd:cd07143 337 ERIMSYIESGKAEGATVeTGGKRHGNE----GYFIEPTIFtDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYG 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224333486 412 LSSCIFTTDVREAEQFMSAVgsDCGIANVN----IGPsgaeiGGAFGGEKETGGGRESGSDAWRGYMrrQTNTVNYSL 485
Cdd:cd07143 413 LAAAVFTNNINNAIRVANAL--KAGTVWVNcynlLHH-----QVPFGGYKQSGIGRELGEYALENYT--QIKAVHINL 481
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
22-465 |
2.13e-60 |
|
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: 205.77 E-value: 2.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGe 101
Cdd:cd07117 19 DSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 vqemIDIcDFAVGLSRQLYGLTIASERPGHHMRETW------HPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPS 175
Cdd:cd07117 98 ----VDI-PLAADHFRYFAGVIRAEEGSANMIDEDTlsivlrEPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 176 EKTPLTALACQALFERVLknfkdaPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELG 254
Cdd:cd07117 173 STTSLSLLELAKIIQDVL------PKGVVNIVTGkGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 255 GNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNLI-GPLIDKHGF 333
Cdd:cd07117 247 GKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQmGAQVNKDQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 334 DAMQDALEQALSEGGKVF-GGKRQLEDKFPNAYYVSPAIVEMPEQ-SDVVCTETFAPILYVVGYKDFAEALRLNNAVPQG 411
Cdd:cd07117 327 DKILSYVDIAKEEGAKILtGGHRLTENGLDKGFFIEPTLIVNVTNdMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYG 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1224333486 412 LSSCIFTTDVREAEQFMSAVGSD-CGIANVNIGPSGAeiggAFGGEKETGGGRES 465
Cdd:cd07117 407 LGGGVFTKDINRALRVARAVETGrVWVNTYNQIPAGA----PFGGYKKSGIGRET 457
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
22-466 |
2.38e-60 |
|
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: 205.04 E-value: 2.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAG---KITQE- 97
Cdd:cd07138 17 DVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGapiTLARAa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 98 ----GLGEVQEMIDICDfavglsrqlyglTIASERPGHHMRETWHPLGVVGVISAFNFP-------VAVwawnttlALVC 166
Cdd:cd07138 97 qvglGIGHLRAAADALK------------DFEFEERRGNSLVVREPIGVCGLITPWNWPlnqivlkVAP-------ALAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 167 GNAVIWKPSEKTPLTALACQALFERVlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAAR 245
Cdd:cd07138 158 GCTVVLKPSEVAPLSAIILAEILDEA-----GLPAGVFNLVNGdGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 246 FARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLI 324
Cdd:cd07138 233 VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRdPATTL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 325 GPLIDKHGFDAMQDALEQALSEGGKVFGGKRQLEDKFPNAYYVSPAIVempeqSDVvcT--------ETFAPILYVVGYK 396
Cdd:cd07138 313 GPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEGLERGYFVKPTVF-----ADV--TpdmtiareEIFGPVLSIIPYD 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 397 DFAEALRLNNAVPQGLSSCIFTTDVREAEQFmsAVGSDCGIANVNIGPsgAEIGGAFGGEKETGGGRESG 466
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAV--ARRLRAGQVHINGAA--FNPGAPFGGYKQSGNGREWG 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
42-469 |
6.86e-60 |
|
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: 203.19 E-value: 6.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 42 EVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGkiTQEGLGE--VQEMIDICDFAVGLSRQL 119
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG--ATAAWAGfnVDLAAGMLREAASLITQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 120 YGLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTA-LACQAlfervlknFKD 198
Cdd:cd07105 79 IGGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHwLIGRV--------FHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 199 A---PQYLSQVIIGGRDAGA---ALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVR 272
Cdd:cd07105 151 AglpKGVLNVVTHSPEDAPEvveALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 273 AILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHplegNLIGPLIDKHGFDAMQDALEQALSEGGKVFG 352
Cdd:cd07105 231 AALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP----VVLGSLVSAAAADRVKELVDDALSKGAKLVV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 353 GKrqLEDKFPNAYYVSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAV 431
Cdd:cd07105 307 GG--LADESPSGTSMPPTILDnVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRI 384
|
410 420 430
....*....|....*....|....*....|....*....
gi 1224333486 432 gsDCGIANVNiGPS-GAEIGGAFGGEKETGGGRESGSDA 469
Cdd:cd07105 385 --ESGAVHIN-GMTvHDEPTLPHGGVKSSGYGRFNGKWG 420
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
18-396 |
5.66e-58 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 207.36 E-value: 5.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 18 AGKQPVHSPIDGSR-IGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQ 96
Cdd:PRK11904 561 GEARPVVSPADRRRvVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQ 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 97 EGLGEVQEMIDICDFAVGLSRQLYGLTIASERP-GHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPS 175
Cdd:PRK11904 641 DAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPtGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPA 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 176 EKTPLTA-LACQALFE-----RVLknfkdapqylsQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARfAR 248
Cdd:PRK11904 721 EQTPLIAaEAVKLLHEagipkDVL-----------QLLPGdGATVGAALTADPRIAGVAFTGSTETARIINRTLAAR-DG 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 249 SIL----ELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNL 323
Cdd:PRK11904 789 PIVpliaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLlSTD 868
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1224333486 324 IGPLIDKHGFDAMQDALEQALSEGGKVFggKRQLEDKFPNAYYVSPAIVEMPEQSDvVCTETFAPILYVVGYK 396
Cdd:PRK11904 869 VGPVIDAEAKANLDAHIERMKREARLLA--QLPLPAGTENGHFVAPTAFEIDSISQ-LEREVFGPILHVIRYK 938
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
70-424 |
9.25e-57 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 194.18 E-value: 9.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 70 RQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPLGVVGVISAF 149
Cdd:PRK10090 2 RKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 150 NFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTALACQALFERVlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISA 228
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI-----GLPKGVFNLVLGrGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 229 TGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKA 308
Cdd:PRK10090 157 TGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 309 AYSKVRIGHPLEGNLI--GPLIDKHGFDAMQDALEQALSEGGKVF-GGKRQLEDKFpnaYYVSPAIVEMPEQSDVVCTET 385
Cdd:PRK10090 237 AMQAVQFGNPAERNDIamGPLINAAALERVEQKVARAVEEGARVAlGGKAVEGKGY---YYPPTLLLDVRQEMSIMHEET 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 1224333486 386 FAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREA 424
Cdd:PRK10090 314 FGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVA 352
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
22-476 |
6.51e-56 |
|
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: 193.77 E-value: 6.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKitqeglgE 101
Cdd:cd07111 40 PTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK-------P 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDiCDFAVgLSRQLYGLTIASERPGHHMREtWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLT 181
Cdd:cd07111 113 IRESRD-CDIPL-VARHFYHHAGWAQLLDTELAG-WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 182 ALACQALFERVlknfkDAPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMIL 261
Cdd:cd07111 190 ALLFAEICAEA-----GLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 262 GPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNL-IGPLIDKHGFDAMQDAL 340
Cdd:cd07111 265 FDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIdMGAIVDPAQLKRIRELV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 341 EQALSEGGKVFggkrQLEDKFPN-AYYVSPAIVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFT 418
Cdd:cd07111 345 EEGRAEGADVF----QPGADLPSkGPFYPPTLFTnVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWS 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1224333486 419 TDVREAeqFMSAVGSDCGIANVNiGPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRR 476
Cdd:cd07111 421 ENLSLA--LEVALSLKAGVVWIN-GHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRP 475
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
21-396 |
1.82e-55 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 200.16 E-value: 1.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 21 QPVHSPIDGSR-IGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGL 99
Cdd:COG4230 572 RPVRNPADHSDvVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAI 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 100 GEVQEMIDICDFAVGLSRQLYGltiaserpghhMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTP 179
Cdd:COG4230 652 AEVREAVDFCRYYAAQARRLFA-----------APTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTP 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 180 LTALACQALF------ERVLknfkdapqylsQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARS--- 249
Cdd:COG4230 721 LIAARAVRLLheagvpADVL-----------QLLPGdGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIvpl 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 250 ILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLegNL---IGP 326
Cdd:COG4230 790 IAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPA--DLstdVGP 867
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 327 LIDKHGFDAMQDALEQALSEGGKVFGGKrqLEDKFPNAYYVSPAIVEMPEQSDVVcTETFAPILYVVGYK 396
Cdd:COG4230 868 VIDAEARANLEAHIERMRAEGRLVHQLP--LPEECANGTFVAPTLIEIDSISDLE-REVFGPVLHVVRYK 934
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
24-472 |
3.00e-55 |
|
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: 191.74 E-value: 3.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 24 HSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEG-LGEV 102
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 103 qemIDICDFAVGLSRqlYGLTI--ASERPGHHM------RETWHPLGVVGVISAFNFPVAVwAWNTTL-ALVCGNAVIWK 173
Cdd:cd07098 81 ---LVTCEKIRWTLK--HGEKAlrPESRPGGLLmfykraRVEYEPLGVVGAIVSWNYPFHN-LLGPIIaALFAGNAIVVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 174 PSEKTPLTALACQALFERVLKNFKDAPQyLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILEL 253
Cdd:cd07098 155 VSEQVAWSSGFFLSIIRECLAACGHDPD-LVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 254 GGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNL-IGPLIDKHG 332
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVdVGAMISPAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 333 FDAMQDALEQALSEGGK-VFGGKRQLEDKFPNAYYVSPAI-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQ 410
Cdd:cd07098 314 FDRLEELVADAVEKGARlLAGGKRYPHPEYPQGHYFPPTLlVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEY 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224333486 411 GLSSCIFTTDVREAEQFMSAVgsDCGIANVNigpsgaEIGGA-------FGGEKETGGGRESGSDAWRG 472
Cdd:cd07098 394 GLGASVFGKDIKRARRIASQL--ETGMVAIN------DFGVNyyvqqlpFGGVKGSGFGRFAGEEGLRG 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
25-483 |
5.54e-55 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 191.55 E-value: 5.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 25 SPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEA--WRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLG-E 101
Cdd:cd07140 27 NPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALKtH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 102 VQEMIDICDFAVGLSRQLYGLTIA--SERPGHHMRETW-HPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKT 178
Cdd:cd07140 107 VGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLTLTKrEPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 179 PLTALACQALfeRVLKNFkdaPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSI-LELGGN 256
Cdd:cd07140 187 PLTALKFAEL--TVKAGF---PKGVINILPGsGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSNLKKVsLELGGK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 257 NAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNLI-GPLIDKHGFDA 335
Cdd:cd07140 262 SPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDhGPQNHKAHLDK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 336 MQDALEQALSEGGKVFGGKRQLEDKfpnAYYVSPAIV-EMPEQSDVVCTETFAPILYVVGYK--DFAEALRLNNAVPQGL 412
Cdd:cd07140 342 LVEYCERGVKEGATLVYGGKQVDRP---GFFFEPTVFtDVEDHMFIAKEESFGPIMIISKFDdgDVDGVLQRANDTEYGL 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224333486 413 SSCIFTTDVREAEQFMSAVgsDCGIANVNIgPSGAEIGGAFGGEKETGGGRESGSDAWRGYMRRQTNTVNY 483
Cdd:cd07140 419 ASGVFTKDINKALYVSDKL--EAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIEY 486
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
17-474 |
1.21e-54 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 191.10 E-value: 1.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 17 QAGKQPVHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEA-----WRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEA 91
Cdd:PLN02467 21 LGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKSELAKLETLDC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 92 GKITQEGLGEvqeMIDI--C-----DFAVGL-SRQLYGLTIASERPGHHMRetWHPLGVVGVISAFNFPVAVWAWNTTLA 163
Cdd:PLN02467 101 GKPLDEAAWD---MDDVagCfeyyaDLAEALdAKQKAPVSLPMETFKGYVL--KEPLGVVGLITPWNYPLLMATWKVAPA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 164 LVCGNAVIWKPSEktpLTALACQALFErVLKNFKDAPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVA 243
Cdd:PLN02467 176 LAAGCTAVLKPSE---LASVTCLELAD-ICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 244 ARFARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GN 322
Cdd:PLN02467 252 QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEeGC 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 323 LIGPLIDKHGFDAMQDALEQALSEGGKV-FGGKRqlEDKFPNAYYVSPAIVEMPEQSDVVCT-ETFAPILYVVGYKDFAE 400
Cdd:PLN02467 332 RLGPVVSEGQYEKVLKFISTAKSEGATIlCGGKR--PEHLKKGFFIEPTIITDVTTSMQIWReEVFGPVLCVKTFSTEDE 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224333486 401 ALRLNNAVPQGLSSCIFTTDVREAEQFMSAVgsDCGIANVNIG-PSGAEigGAFGGEKETGGGRESGSDAWRGYM 474
Cdd:PLN02467 410 AIELANDSHYGLAGAVISNDLERCERVSEAF--QAGIVWINCSqPCFCQ--APWGGIKRSGFGRELGEWGLENYL 480
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
19-396 |
1.69e-54 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 197.39 E-value: 1.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 19 GKQPVHSPID-GSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQE 97
Cdd:PRK11905 567 GTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLAN 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 98 GLGEVQEMIDICDFavglsrqlYGLTIASERPGhhmrETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEK 177
Cdd:PRK11905 647 AIAEVREAVDFLRY--------YAAQARRLLNG----PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQ 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 178 TPLTALACQALFERVlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARS---ILEL 253
Cdd:PRK11905 715 TPLIAARAVRLLHEA-----GVPKDALQLLPGdGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPvplIAET 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 254 GGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPleGNL---IGPLIDK 330
Cdd:PRK11905 790 GGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDP--WRLstdVGPVIDA 867
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224333486 331 HGFDAMQDALEQALSEGGKVFggKRQLEDKFPNAYYVSPAIVEMPEQSDVVcTETFAPILYVVGYK 396
Cdd:PRK11905 868 EAQANIEAHIEAMRAAGRLVH--QLPLPAETEKGTFVAPTLIEIDSISDLE-REVFGPVLHVVRFK 930
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
21-466 |
1.07e-53 |
|
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: 188.20 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 21 QPVHSPID-GSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGL 99
Cdd:TIGR01238 53 QPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 100 GEVQEMIDICDFAVGLSRQLYGltiaserpghhmRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTP 179
Cdd:TIGR01238 133 AEVREAVDFCRYYAKQVRDVLG------------EFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 180 LTALACQALFERVlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARS---ILELGG 255
Cdd:TIGR01238 201 LIAYRAVELMQEA-----GFPAGTIQLLPGrGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPvplIAETGG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 256 NNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHP-LEGNLIGPLIDKHGFD 334
Cdd:TIGR01238 276 QNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPhLLTTDVGPVIDAEAKQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 335 AMQDALEQALSEGGKVFGGKRQLEDKFPNAYYVSPAIVEMpEQSDVVCTETFAPILYVVGYK--DFAEALRLNNAVPQGL 412
Cdd:TIGR01238 356 NLLAHIEHMSQTQKKIAQLTLDDSRACQHGTFVAPTLFEL-DDIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGL 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1224333486 413 SSCIFT---TDVREAEQFMSAvgsdcGIANVNIGPSGAEIG-GAFGGEKETGGGRESG 466
Cdd:TIGR01238 435 TMGVHSrieTTYRWIEKHARV-----GNCYVNRNQVGAVVGvQPFGGQGLSGTGPKAG 487
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
22-488 |
4.45e-53 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 187.32 E-value: 4.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 22 PVHSPIDGSRIGSVHwEGAAE-VEQQVSRAEHAFE--AWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEG 98
Cdd:PLN02466 76 PTLDPRTGEVIAHVA-EGDAEdVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 99 LG-EVQEMIDICDFAVGLSRQLYGLTIASERPgHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEK 177
Cdd:PLN02466 155 AKaELPMFARLFRYYAGWADKIHGLTVPADGP-HHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQ 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 178 TPLTALACQALFERVlknfkDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSI-LELGG 255
Cdd:PLN02466 234 TPLSALYAAKLLHEA-----GLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVtLELGG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 256 NNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFD 334
Cdd:PLN02466 309 KSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFkKGVEQGPQIDSEQFE 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 335 AMQDALEQALSEGGKVFGGKRQLEDKfpnAYYVSPAIVEMPEQSDVVCT-ETFAPILYVVGYKDFAEALRLNNAVPQGLS 413
Cdd:PLN02466 389 KILRYIKSGVESGATLECGGDRFGSK---GYYIQPTVFSNVQDDMLIAQdEIFGPVQSILKFKDLDEVIRRANNTRYGLA 465
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224333486 414 SCIFTTDVREAEQFMSAVgsDCGIANVN-IGPSGAEIggAFGGEKETGGGRESGSDAWRGYMrrQTNTVNYSLELP 488
Cdd:PLN02466 466 AGVFTQNLDTANTLSRAL--RVGTVWVNcFDVFDAAI--PFGGYKMSGIGREKGIYSLNNYL--QVKAVVTPLKNP 535
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
23-424 |
7.74e-51 |
|
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: 179.54 E-value: 7.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 23 VHSPIDGSRIGSVHWEGAAEVEQQVSRAEHAF---EAWrnVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGL 99
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFldrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 100 GEVQEMIDICDFAVGLSRQLYG------LTIASE-RPGHHMREtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIW 172
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGreipmgLTPASAgRIAFTTRE---PIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 173 KPSEKTPLTalaCQALFERVlknfKDA--PQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARfARSI 250
Cdd:cd07148 158 KPALATPLS---CLAFVDLL----HEAglPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 251 LELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHP-LEGNLIGPLID 329
Cdd:cd07148 230 LEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPtDPDTEVGPLIR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 330 KHGFDAMQDALEQALSEGGKVFGGKRQLEDKFpnayyVSPAIVEMPEQSDVVCT-ETFAPILYVVGYKDFAEALRLNNAV 408
Cdd:cd07148 310 PREVDRVEEWVNEAVAAGARLLCGGKRLSDTT-----YAPTVLLDPPRDAKVSTqEIFGPVVCVYSYDDLDEAIAQANSL 384
|
410
....*....|....*.
gi 1224333486 409 PQGLSSCIFTTDVREA 424
Cdd:cd07148 385 PVAFQAAVFTKDLDVA 400
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
25-464 |
1.04e-49 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 176.59 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 25 SPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQE 104
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 105 MIDICDFAVGlsrqlYGLTIASERP----GHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEktpl 180
Cdd:PRK13968 93 SANLCDWYAE-----HGPAMLKAEPtlveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAP---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 181 TALACQALFERVlknFKDA--PQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNA 258
Cdd:PRK13968 164 NVMGCAQLIAQV---FKDAgiPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 259 MILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQ 337
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRdEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 338 DALEQALSEGGKVFGGKRQLEDKfpNAYYVSPAIVEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIF 417
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKIAGA--GNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1224333486 418 TTDVREAEQFMSAVgsDCGIANVNiGPSGAEIGGAFGGEKETGGGRE 464
Cdd:PRK13968 399 TTDETQARQMAARL--ECGGVFIN-GYCASDARVAFGGVKKSGFGRE 442
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
26-481 |
6.32e-48 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 172.70 E-value: 6.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 26 PIDGSRIGSVHWEGAAEVEQQVSRAEHAFE--AWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGlgevq 103
Cdd:PLN02766 43 PRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALG----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 104 EMIDICDFA------VGLSRQLYGLTIASERP--GHHMREtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPS 175
Cdd:PLN02766 118 KAVDIPAAAgllryyAGAADKIHGETLKMSRQlqGYTLKE---PIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 176 EKTPLTalacqALFERVLKNFKDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSI-LEL 253
Cdd:PLN02766 195 EQTPLS-----ALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNLKQVsLEL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 254 GGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNL-IGPLIDKHG 332
Cdd:PLN02766 270 GGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRArQGPQVDKQQ 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 333 FDAMQDALEQALSEGGKVFGGKRQLEDKfpnAYYVSPAI-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQG 411
Cdd:PLN02766 350 FEKILSYIEHGKREGATLLTGGKPCGDK---GYYIEPTIfTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYG 426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 412 LSSCIFTTDVREAEQFMSAVGSdcGIANVNIgPSGAEIGGAFGGEKETGGGRESGSDAWRGYMrrQTNTV 481
Cdd:PLN02766 427 LAAGIVTKDLDVANTVSRSIRA--GTIWVNC-YFAFDPDCPFGGYKMSGFGRDQGMDALDKYL--QVKSV 491
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
25-465 |
6.51e-47 |
|
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: 169.56 E-value: 6.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 25 SPIDGSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLG-EVQ 103
Cdd:cd07116 22 TPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAaDIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 104 EMIDICDFAVGLSRQLYG--LTIASERPGHHMREtwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLT 181
Cdd:cd07116 102 LAIDHFRYFAGCIRAQEGsiSEIDENTVAYHFHE---PLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPAS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 182 ALACQALFERVLknfkdaPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMI 260
Cdd:cd07116 179 ILVLMELIGDLL------PPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 261 LGPS------ADLDMAVRAILFSAVgTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLE-GNLIGPLIDKHGF 333
Cdd:cd07116 253 FFADvmdaddAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDtETMIGAQASLEQL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 334 DAMQDALEQALSEGGKVF-GGKRQLEDKFPNAYYVSPAIVEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGL 412
Cdd:cd07116 332 EKILSYIDIGKEEGAEVLtGGERNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGL 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1224333486 413 SSCIFTTDVREAEQFMSAVGSdcGIANVN---IGPSGAeiggAFGGEKETGGGRES 465
Cdd:cd07116 412 GAGVWTRDGNTAYRMGRGIQA--GRVWTNcyhLYPAHA----AFGGYKQSGIGREN 461
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
39-464 |
2.21e-46 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 167.61 E-value: 2.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 39 GAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQEMIDICDF------- 111
Cdd:PRK09406 21 TDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYyaehaea 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 112 ----------AVGLSRQLygltiaserpghhMRetWHPLGVVGVISAFNFPVavwaWNTTL----ALVCGNAVIWKPSEK 177
Cdd:PRK09406 101 lladepadaaAVGASRAY-------------VR--YQPLGVVLAVMPWNFPL----WQVVRfaapALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 178 TPLTALACQALFERVlkNFkdaPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNN 257
Cdd:PRK09406 162 VPQTALYLADLFRRA--GF---PDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 258 AMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAM 336
Cdd:PRK09406 237 PFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTdPDTDVGPLATEQGRDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 337 QDALEQALSEGGKVFGGKRQLEDkfPNAYYVSPAIVEMPEQSDVVCTETFAPI--LYVVGykDFAEALRLNNAVPQGLSS 414
Cdd:PRK09406 317 EKQVDDAVAAGATILCGGKRPDG--PGWFYPPTVITDITPDMRLYTEEVFGPVasLYRVA--DIDEAIEIANATTFGLGS 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1224333486 415 CIFTTDVREAEQFMSAVgsDCGIANVN-IGPSGAEIGgaFGGEKETGGGRE 464
Cdd:PRK09406 393 NAWTRDEAEQERFIDDL--EAGQVFINgMTVSYPELP--FGGVKRSGYGRE 439
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
138-433 |
2.23e-44 |
|
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: 161.54 E-value: 2.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 138 HPLGVVGVISAFNFPVavwawNTTL-----ALVCGNAVIWKPSEKTPLTAlacqALFERVLknfkdaPQYLS----QVII 208
Cdd:cd07087 99 EPLGVVLIIGPWNYPL-----QLALapligAIAAGNTVVLKPSELAPATS----ALLAKLI------PKYFDpeavAVVE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 209 GGRDAGAALVDDPrVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTT 288
Cdd:cd07087 164 GGVEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 289 LRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNLIGPLIDKHGFDAMQDALEQalsegGKV-FGGKRQLEDKfpnayYV 367
Cdd:cd07087 243 PDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDD-----GKVvIGGQVDKEER-----YI 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1224333486 368 SPAIVEMPE-QSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVGS 433
Cdd:cd07087 313 APTILDDVSpDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSS 379
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
4-464 |
6.42e-42 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 156.21 E-value: 6.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 4 ALLDRLGVNPALYQAGKQPVHSPID---GSRIGSVHWEGAAEVEQQVSRAEHAFEA--WRNVPAPRRGELVRQFGDVLRQ 78
Cdd:PRK09847 17 AIENRLFINGEYTAAAENETFETVDpvtQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 79 YKADLGELVSWEAGKITQEGLGEvqemiDICDFAVGLS------RQLYGlTIASERPGHHMRETWHPLGVVGVISAFNFP 152
Cdd:PRK09847 97 HAEELALLETLDTGKPIRHSLRD-----DIPGAARAIRwyaeaiDKVYG-EVATTSSHELAMIVREPVGVIAAIVPWNFP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 153 VAVWAWNTTLALVCGNAVIWKPSEKTPLTALacqalfeRVLKNFKDA--PQYLSQVIIG-GRDAGAALVDDPRVALISAT 229
Cdd:PRK09847 171 LLLTCWKLGPALAAGNSVILKPSEKSPLSAI-------RLAGLAKEAglPDGVLNVVTGfGHEAGQALSRHNDIDAIAFT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 230 GSTRMGREVAPKVA-ARFARSILELGGNNA-MILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLK 307
Cdd:PRK09847 244 GSTRTGKQLLKDAGdSNMKRVWLEAGGKSAnIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 308 AAYSKVRIGHPLE-GNLIGPLIDKHGFDAMQDALEQALSEGGKVFGGKRQledkfPNAYYVSPAI-VEMPEQSDVVCTET 385
Cdd:PRK09847 324 QQAQNWQPGHPLDpATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNA-----GLAAAIGPTIfVDVDPNASLSREEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 386 FAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQfMS---AVGSdCGIANVNIGpsgaEIGGAFGGEKETGGG 462
Cdd:PRK09847 399 FGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHR-MSrrlKAGS-VFVNNYNDG----DMTVPFGGYKQSGNG 472
|
..
gi 1224333486 463 RE 464
Cdd:PRK09847 473 RD 474
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
14-396 |
1.69e-41 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 158.98 E-value: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 14 ALYQAGKQPVHSPIDGSRI-GSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAG 92
Cdd:PRK11809 654 PVAAGEMSPVINPADPRDIvGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAG 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 93 KITQEGLGEVQEMIDICDFAVGLSRQLYGltiaserpghhmRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIW 172
Cdd:PRK11809 734 KTFSNAIAEVREAVDFLRYYAGQVRDDFD------------NDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLA 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 173 KPSEKTPLtaLACQALfeRVLKnfkDA--PQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARS 249
Cdd:PRK11809 802 KPAEQTPL--IAAQAV--RILL---EAgvPAGVVQLLPGrGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQ 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 250 ------ILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPleGNL 323
Cdd:PRK11809 875 grpiplIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNP--DRL 952
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224333486 324 ---IGPLIDKHGFDAMQDALEQALSEGGKVFGGKRQLEDKFPNAYYVSPAIVEMpEQSDVVCTETFAPILYVVGYK 396
Cdd:PRK11809 953 stdIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEDWQSGTFVPPTLIEL-DSFDELKREVFGPVLHVVRYN 1027
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
42-442 |
2.55e-40 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 153.36 E-value: 2.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 42 EVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQEMIDICDFAVGLSRQLYG 121
Cdd:PLN02419 152 EFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMG 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 122 LTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTP-----LTALACQAlfervlknf 196
Cdd:PLN02419 232 EYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPgasviLAELAMEA--------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 197 kDAPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILF 276
Cdd:PLN02419 303 -GLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 277 SAVGTAGQRCTTLRRLI---AHESVKEEIVTRLKAAysKVRIGHPLEGNLiGPLIDKHGFDAMQDALEQALSEGGK-VFG 352
Cdd:PLN02419 382 AGFGAAGQRCMALSTVVfvgDAKSWEDKLVERAKAL--KVTCGSEPDADL-GPVISKQAKERICRLIQSGVDDGAKlLLD 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 353 GKRQLEDKFPNAYYVSPAIVEmPEQSDVVC--TETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSA 430
Cdd:PLN02419 459 GRDIVVPGYEKGNFIGPTILS-GVTPDMECykEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMD 537
|
410
....*....|..
gi 1224333486 431 VgsDCGIANVNI 442
Cdd:PLN02419 538 I--EAGQIGINV 547
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
139-455 |
2.27e-39 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 149.02 E-value: 2.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 139 PLGVVGVISAFNFPVavwawNTTL-----ALVCGNAVIWKPSEKTPLTALACQALFervlknfkdaPQYLSQ----VIIG 209
Cdd:PTZ00381 109 PLGVVLVIGAWNYPL-----NLTLiplagAIAAGNTVVLKPSELSPHTSKLMAKLL----------TKYLDPsyvrVIEG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 210 GRDAGAALVDDPrVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTL 289
Cdd:PTZ00381 174 GVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 290 RRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNLIGPLIDKHGFDAMQDALEQalsEGGKV-FGGKRQLEDKfpnayYVS 368
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVvYGGEVDIENK-----YVA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 369 PAIVEMPEQSDVVCT-ETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVGS------DC--GIAN 439
Cdd:PTZ00381 325 PTIIVNPDLDSPLMQeEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSgavvinDCvfHLLN 404
|
330 340
....*....|....*....|.
gi 1224333486 440 VN-----IGPSGAeigGAFGG 455
Cdd:PTZ00381 405 PNlpfggVGNSGM---GAYHG 422
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
139-456 |
8.89e-39 |
|
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: 146.21 E-value: 8.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 139 PLGVVGVISAFNFPVAVwawntTL-----ALVCGNAVIWKPSEKTPltalACQALFERVLKNFKDAPQYlsQVIIGGRDA 213
Cdd:cd07135 108 PLGVVLIIGPWNYPVLL-----ALsplvgAIAAGCTVVLKPSELTP----HTAALLAELVPKYLDPDAF--QVVQGGVPE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 214 GAALVDDpRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLI 293
Cdd:cd07135 177 TTALLEQ-KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 294 AHESVKEEIVTRLKAAYSKVRIGHPLEGNLIGPLIDKHGFDAMQDALEQalSEGGKVFGGKRQLEDKFpnayyVSPAIVE 373
Cdd:cd07135 256 VDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT--TKGKVVIGGEMDEATRF-----IPPTIVS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 374 MPEQSDVVCT-ETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVGSdcGIANVN----------- 441
Cdd:cd07135 329 DVSWDDSLMSeELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRS--GGVVINdtlihvgvdna 406
|
330
....*....|....*....
gi 1224333486 442 ----IGPSGAeigGAFGGE 456
Cdd:cd07135 407 pfggVGDSGY---GAYHGK 422
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
15-467 |
1.55e-37 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 144.27 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 15 LYQAGKQPVHSPID-GSRIGSVHWEGAAEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLR-QYKADLGELVSWEAG 92
Cdd:cd07123 42 VRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 93 K-ITQEGLGEVQEMIDICDFAVGLSRQLYGLTIASERPGHHMRETWHPL-GVVGVISAFNFpVAVwAWN--TTLALVcGN 168
Cdd:cd07123 122 KnVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNF-TAI-GGNlaGAPALM-GN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 169 AVIWKPSEktplTALACQALferVLKNFKDA--PQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAAR 245
Cdd:cd07123 199 VVLWKPSD----TAVLSNYL---VYKILEEAglPPGVINFVPGdGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGEN 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 246 ------FARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL 319
Cdd:cd07123 272 ldryrtYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 320 E-GNLIGPLIDKHGFDAMQDALEQALSEGG--KVFGGKrqlEDKfPNAYYVSPAIVEMPE-QSDVVCTETFAPILYVVGY 395
Cdd:cd07123 352 DfSNFMGAVIDEKAFDRIKGYIDHAKSDPEaeIIAGGK---CDD-SVGYFVEPTVIETTDpKHKLMTEEIFGPVLTVYVY 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224333486 396 KD--FAEALRL-NNAVPQGLSSCIFTTDVREAEQFMSAVGSDCGIANVNIGPSGAEIggafgGEKETGGGRESGS 467
Cdd:cd07123 428 PDsdFEETLELvDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKPTGAVV-----GQQPFGGARASGT 497
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
139-440 |
2.47e-35 |
|
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: 136.59 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 139 PLGVVGVISAFNFPVavwawNTTL-----ALVCGNAVIWKPSEKTPLTALACQALFERVLknfkdaPQYLSQVIIGGRDA 213
Cdd:cd07134 100 PKGVCLIISPWNYPF-----NLAFgplvsAIAAGNTAILKPSELTPHTSAVIAKIIREAF------DEDEVAVFEGDAEV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 214 GAALVDDPrVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRLI 293
Cdd:cd07134 169 AQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVF 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 294 AHESVKEEIVTRLKAAYSKV--RIGHPLEGNLIGPLIDKHGFDAMQDALEQALSEGGKV-FGGKRQLEDKfpnayYVSPA 370
Cdd:cd07134 248 VHESVKDAFVEHLKAEIEKFygKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVeFGGQFDAAQR-----YIAPT 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224333486 371 IVE-MPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVGS-DCGIANV 440
Cdd:cd07134 323 VLTnVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSgGVVVNDV 394
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
139-446 |
4.12e-35 |
|
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: 136.08 E-value: 4.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 139 PLGVVGVISAFNFPVavwawNTTL-----ALVCGNAVIWKPSEKTPLTAlacqALFERVL-KNFkdAPQYLSqVIIGGRD 212
Cdd:cd07133 101 PLGVVGIIVPWNYPL-----YLALgpliaALAAGNRVMIKPSEFTPRTS----ALLAELLaEYF--DEDEVA-VVTGGAD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 213 AGAAlvddprvalISA--------TGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQ 284
Cdd:cd07133 169 VAAA---------FSSlpfdhllfTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 285 RCTTLRRLIAHESVKEEIVTRLKAAYSKvRIGHPLEGNLIGPLIDKHGFDAMQDALEQALSEGGKV---------FGGKR 355
Cdd:cd07133 240 TCVAPDYVLVPEDKLEEFVAAAKAAVAK-MYPTLADNPDYTSIINERHYARLQGLLEDARAKGARVielnpagedFAATR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 356 qledKFPnayyvsPAIV-EMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVGS- 433
Cdd:cd07133 319 ----KLP------PTLVlNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSg 388
|
330 340
....*....|....*....|....*
gi 1224333486 434 -----DCG--IANVN-----IGPSG 446
Cdd:cd07133 389 gvtinDTLlhVAQDDlpfggVGASG 413
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
42-462 |
6.61e-35 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 136.42 E-value: 6.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 42 EVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGKITQEGLGEVQEMIDICDFAVGLSRQLYG 121
Cdd:PLN00412 54 EVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 122 ---LTIASERPGHHMRE----TWHPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTALACQALFErvLK 194
Cdd:PLN00412 134 egkFLVSDSFPGNERNKycltSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFH--LA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 195 NFkdaPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTrMGREVAPKvaARFARSILELGGNNAMILGPSADLDMAVRA 273
Cdd:PLN00412 212 GF---PKGLISCVTGkGSEIGDFLTMHPGVNCISFTGGD-TGIAISKK--AGMVPLQMELGGKDACIVLEDADLDLAAAN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 274 ILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNLIGPLIDKHGFDAMQDALEQALSEGGKvFGG 353
Cdd:PLN00412 286 IIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGAT-FCQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 354 KRQLEDKFpnayyVSPAIVEMPEQSDVVC-TETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVg 432
Cdd:PLN00412 365 EWKREGNL-----IWPLLLDNVRPDMRIAwEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAM- 438
|
410 420 430
....*....|....*....|....*....|
gi 1224333486 433 sDCGIANVNIGPSGAEIGGAFGGEKETGGG 462
Cdd:PLN00412 439 -ETGTVQINSAPARGPDHFPFQGLKDSGIG 467
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
139-435 |
1.31e-33 |
|
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: 132.24 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 139 PLGVVGVISAFNFPvavwaWNTTL-----ALVCGNAVIWKPSEKTPLTAlacqALFERVLKNFKDaPQYLSqVIIGGRDA 213
Cdd:cd07136 100 PYGVVLIIAPWNYP-----FQLALapligAIAAGNTAVLKPSELTPNTS----KVIAKIIEETFD-EEYVA-VVEGGVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 214 GAALVDDPrVALISATGSTRMGREVApKVAARFARSI-LELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRL 292
Cdd:cd07136 169 NQELLDQK-FDYIFFTGSVRVGKIVM-EAAAKHLTPVtLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 293 IAHESVKEEIVTRLKAAYSKVRIGHPLEGNLIGPLIDKHGFDAmqdaLEQALSEGGKVFGGKRQLEDKfpnayYVSPAIV 372
Cdd:cd07136 247 LVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDR----LAGLLDNGKIVFGGNTDRETL-----YIEPTIL 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224333486 373 -EMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAV--GSDC 435
Cdd:cd07136 318 dNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLsfGGGC 383
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
43-476 |
1.55e-29 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 120.42 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 43 VEQQVSRAEHAFEAWRNVPAPRRGELVRqfgDVLRQYKADLGELVsweAGKITQEGLGEvQEMIDICdfavGLSRQLYGL 122
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLA---RIIQRLAAKSYDIA---AGAVLVTGKGW-MFAENIC----GDQVQLRAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 123 TIASERPGHHMRETWH--------------PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTALACQAL 188
Cdd:cd07084 70 AFVIYSYRIPHEPGNHlgqglkqqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 189 FERVLKnfkdAPQYLSQVIIGGRDAGAALVDDPRVALISATGSTRMGREVApkVAARFARSILELGGNNAMILGPSAD-L 267
Cdd:cd07084 150 LHYAGL----LPPEDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLA--LDAKQARIYLELAGFNWKVLGPDAQaV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 268 DMAVRAILFSAVGTAGQRCTTLRRLIAHES-VKEEIVTRLKAAYSKVRighpLEGNLIGPLIdkhgFDAMQDALEQALSE 346
Cdd:cd07084 224 DYVAWQCVQDMTACSGQKCTAQSMLFVPENwSKTPLVEKLKALLARRK----LEDLLLGPVQ----TFTTLAMIAHMENL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 347 GGKV--FGGK---RQLEDKFPNAYYVSPAIV---EMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAV-PQG-LSSCI 416
Cdd:cd07084 296 LGSVllFSGKelkNHSIPSIYGACVASALFVpidEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLErMHGsLTAAI 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224333486 417 FTTDVREAEQFMSAVGSDCGIANVNIGPSGAEIGGAFGGEKETGGGRES--GSDAWRGYMRR 476
Cdd:cd07084 376 YSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGigGPEAIKLVWRC 437
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
139-466 |
1.80e-29 |
|
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: 120.21 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 139 PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTAlacqALFERVLknfkdaPQYLS----QVIIGGRDAG 214
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATS----ALLAKLI------PEYLDtkaiKVIEGGVPET 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 215 AALVDDpRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVGT-AGQRCTTLRRLI 293
Cdd:cd07137 171 TALLEQ-KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 294 AHESVKEEIVTRLKAAYSKVRIGHPLEGNLIGPLIDKHGFDAMQDALEQALSEGGKVFGGKRQlEDKFpnayYVSPAIV- 372
Cdd:cd07137 250 VEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERD-EKNL----YIEPTILl 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 373 EMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVGS------DCGIANVNIG-Ps 445
Cdd:cd07137 325 DPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSggvtfnDTVVQYAIDTlP- 403
|
330 340
....*....|....*....|.
gi 1224333486 446 gaeiggaFGGEKETGGGRESG 466
Cdd:cd07137 404 -------FGGVGESGFGAYHG 417
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
137-429 |
6.27e-28 |
|
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: 115.78 E-value: 6.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 137 WHPLGVVGVISAFNFPVAVwawntTL-----ALVCGNAVIWKPSEKTPLTAlacqALFERVLknfkdaPQYLSQ----VI 207
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQL-----TLvplvgAIAAGNCVVIKPSEVSPATA----KLLAELI------PKYLDKecypVV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 208 IGGRDAGAALVDDpRVALISATGSTRMGREVApKVAARF-ARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRC 286
Cdd:cd07132 163 LGGVEETTELLKQ-RFDYIFYTGSTSVGKIVM-QAAAKHlTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 287 TTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNLIGPLIDKHGFDAMqdaleQALSEGGKV-FGGKRQLEDKfpnay 365
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRL-----KKLLSGGKVaIGGQTDEKER----- 310
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224333486 366 YVSPAI-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMS 429
Cdd:cd07132 311 YIAPTVlTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILS 375
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
139-477 |
6.91e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 110.52 E-value: 6.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 139 PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPltalACQALFERVLKNFKDAPqyLSQVIIGGRDAGAALV 218
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAP----ASSALLAKLLEQYLDSS--AVRVVEGAVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 219 DDpRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVG-TAGQRCTTLRRLIAHES 297
Cdd:PLN02174 186 EQ-KWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 298 VKEEIVTRLKAAYSKVRIGHPLEGNLIGPLIDKHGFDAMQDALEQALSEGGKVFGGKRQLEDkfpnaYYVSPAI-VEMPE 376
Cdd:PLN02174 265 YAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDREN-----LKIAPTIlLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 377 QSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVgSDCGIANVNIGPSGAEIGGAFGGE 456
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATV-SAGGIVVNDIAVHLALHTLPFGGV 418
|
330 340
....*....|....*....|.
gi 1224333486 457 KETGGGRESGSDAWRGYMRRQ 477
Cdd:PLN02174 419 GESGMGAYHGKFSFDAFSHKK 439
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
130-476 |
2.48e-25 |
|
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: 108.90 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 130 GHHMretWHPLGVVGV-ISAFNFPVavWAWNTTLA--LVCGNAVIWKPSEKTPLTAlacqalfERVLKNFKDA---PQYL 203
Cdd:cd07128 137 GQHI---LTPRRGVAVhINAFNFPV--WGMLEKFApaLLAGVPVIVKPATATAYLT-------EAVVKDIVESgllPEGA 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 204 SQVIIGGrdaGAALVD--DPRvALISATGSTRMGRE--VAPKVAARFARSILELGGNNAMILGPSA-----DLDMAVRAI 274
Cdd:cd07128 205 LQLICGS---VGDLLDhlGEQ-DVVAFTGSAATAAKlrAHPNIVARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEV 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 275 LFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHP-LEGNLIGPLIDKHGFDAMQDALEQALSEGGKVFGG 353
Cdd:cd07128 281 AREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPrLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 354 KRQLEDKFPNA---YYVSPAIV--EMPEQSDVV-CTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQF 427
Cdd:cd07128 361 PDRFEVVGADAekgAFFPPTLLlcDDPDAATAVhDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFAREL 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1224333486 428 MSAVGSDCGIANVNIGPSGAEIGG--------AFGGEKETGGGRE-SGSDAWRGYMRR 476
Cdd:cd07128 441 VLGAAPYHGRLLVLNRDSAKESTGhgsplpqlVHGGPGRAGGGEElGGLRGVKHYMQR 498
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
139-466 |
3.42e-24 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 105.19 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 139 PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPltalACQALFERVLknfkdaPQYLS----QVIIGGRDAG 214
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAP----ATSAFLAANI------PKYLDskavKVIEGGPAVG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 215 AALVDDpRVALISATGSTRMGREVAPKVAARFARSILELGGNNAMI---LGPSADLDMAVRAILFSAVGT-AGQRCTTLR 290
Cdd:PLN02203 178 EQLLQH-KWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIAID 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 291 RLIAHESVKEEIVTRLKAAYSKVRIGHPLEGNLIGPLIDKHGFDAMQDALEQALSEGGKVFGGKRQledkfPNAYYVSPA 370
Cdd:PLN02203 257 YVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSID-----EKKLFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 371 I-VEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVGSDCGIANVNIGPSGAEi 449
Cdd:PLN02203 332 IlLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACD- 410
|
330
....*....|....*..
gi 1224333486 450 GGAFGGEKETGGGRESG 466
Cdd:PLN02203 411 SLPFGGVGESGFGRYHG 427
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
141-476 |
5.83e-20 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 92.85 E-value: 5.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 141 GVVGVISAFNFPvavwAW----NTTLALVCGNAVIWKPSEKTPLtalacqaLFERVLKNFKDA---PQYLSQVIIGGrda 213
Cdd:PRK11903 150 GVALFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAW-------LTQRMVKDVVAAgilPAGALSVVCGS--- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 214 GAALVDDPR-VALISATGSTRMGREV--APKVAARFARSILELGGNNAMILGP-----SADLDMAVRAILFSAVGTAGQR 285
Cdd:PRK11903 216 SAGLLDHLQpFDVVSFTGSAETAAVLrsHPAVVQRSVRVNVEADSLNSALLGPdaapgSEAFDLFVKEVVREMTVKSGQK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 286 CTTLRRLIAHESVKEEIVTRLKAAYSKVRIGHPL-EGNLIGPLIDKHGFDAMQDALEQALSEGGKVFGGKRQ-LEDKFPN 363
Cdd:PRK11903 296 CTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRnDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFaLVDADPA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 364 -AYYVSPAI--VEMPEQSDVVC-TETFAPILYVVGYKDFAEALRLNNAVPQGLSSCIFTTDVREAEQFMSAVGSDCG--- 436
Cdd:PRK11903 376 vAACVGPTLlgASDPDAATAVHdVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADSHGrvh 455
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1224333486 437 -----IANVNIGPSGAEIGGAFGGEKETGGGRESGsdAWRG---YMRR 476
Cdd:PRK11903 456 vispdVAALHTGHGNVMPQSLHGGPGRAGGGEELG--GLRAlafYHRR 501
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
129-422 |
5.39e-15 |
|
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: 77.15 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 129 PGHHMRETWH----PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTAlacqALFERVLKNFKDAPQYLS 204
Cdd:cd07126 128 PGDHQGQQSSgyrwPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVM----EQFLRLLHLCGMPATDVD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 205 QVIIGGRDAGAALVD-DPRVALIsaTGSTRmgrevapkVAARFARSI-----LELGGNNAMILGPS-ADLDMAVRAILFS 277
Cdd:cd07126 204 LIHSDGPTMNKILLEaNPRMTLF--TGSSK--------VAERLALELhgkvkLEDAGFDWKILGPDvSDVDYVAWQCDQD 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 278 AVGTAGQRCTTLRRLIAHES-VKEEIVTRLKAAYSKVRighpLEGNLIGPLIDKHGfDAMQDALEQALS-EGGKV-FGGK 354
Cdd:cd07126 274 AYACSGQKCSAQSILFAHENwVQAGILDKLKALAEQRK----LEDLTIGPVLTWTT-ERILDHVDKLLAiPGAKVlFGGK 348
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224333486 355 RQLEDKFPNAY--------YVSPAIVEMPEQSDVVCTETFAPILYVVGYKDFAEALRLN--NAVPQGLSSCIFTTDVR 422
Cdd:cd07126 349 PLTNHSIPSIYgayeptavFVPLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEalERMHAHLTAAVVSNDIR 426
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
43-420 |
1.34e-14 |
|
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: 75.66 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 43 VEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAGkitqegLGEVQemidicdfAVG-LSR---Q 118
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG------LPEAR--------LQGeLGRttgQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 119 L------------YGLTI---ASER---PGHHMRETWHPLGVVGVISAFNFPVA--VWAWNTTLALVCGNAVIWKPSEKT 178
Cdd:cd07129 67 LrlfadlvregswLDARIdpaDPDRqplPRPDLRRMLVPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 179 PLTALACQALFERVLKNfKDAPQYLSQVIIG-GRDAGAALVDDPRVALISATGSTRMGREVAPKVAAR------FArsil 251
Cdd:cd07129 147 PGTSELVARAIRAALRA-TGLPAGVFSLLQGgGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARpepipfYA---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 252 ELGGNNAMILGPSAdldMAVRA------ILFSAVGTAGQRCTTLRRLIAHESVK-EEIVTRLKAAYSKVRighplegnlI 324
Cdd:cd07129 222 ELGSVNPVFILPGA---LAERGeaiaqgFVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAP---------A 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 325 GPLIDKHGFDAMQDALEQALSEGG-KVFGGKRQLEDkfpnAYYVSPAIVEMPEQS----DVVCTETFAPILYVVGYKDFA 399
Cdd:cd07129 290 QTMLTPGIAEAYRQGVEALAAAPGvRVLAGGAAAEG----GNQAAPTLFKVDAAAfladPALQEEVFGPASLVVRYDDAA 365
|
410 420
....*....|....*....|.
gi 1224333486 400 EALRLNNAVPQGLSSCIFTTD 420
Cdd:cd07129 366 ELLAVAEALEGQLTATIHGEE 386
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
133-430 |
1.60e-12 |
|
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: 69.81 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 133 MRETWH--PLGVVGVISAFNFPVavwaWNTT----LALVCGNAVIWKPSEKTPL-TALACQALFErVLKNFKDAPQYLSQ 205
Cdd:cd07127 185 MEKTFTvvPRGVALVIGCSTFPT----WNGYpglfASLATGNPVIVKPHPAAILpLAITVQVARE-VLAEAGFDPNLVTL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 206 VI-IGGRDAGAALVDDPRVALISATGSTRMGREVapKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQ 284
Cdd:cd07127 260 AAdTPEEPIAQTLATRPEVRIIDFTGSNAFGDWL--EANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 285 RCTTLRRLIAHesvKEEIVTRL-KAAYSKVR--IGHPLEGNLIGPLIDKHGFDAMQ-----DALEQALSEGGKVFGGKRQ 356
Cdd:cd07127 338 MCTTPQNIYVP---RDGIQTDDgRKSFDEVAadLAAAIDGLLADPARAAALLGAIQspdtlARIAEARQLGEVLLASEAV 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224333486 357 LEDKFPNAYYVSPAIVEM-PEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQ---GLSSCIFTTDVREAEQFMSA 430
Cdd:cd07127 415 AHPEFPDARVRTPLLLKLdASDEAAYAEERFGPIAFVVATDSTDHSIELARESVRehgAMTVGVYSTDPEVVERVQEA 492
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
139-472 |
1.27e-10 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, 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. This group includes families ALDH18, ALDH19, and ALDH20 and represents 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: 143396 [Multi-domain] Cd Length: 397 Bit Score: 63.01 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 139 PLGVVGVISAFNFPVAVwAWNTTLALVCGNAVIWKPSEKTPLTALACQALFERVLKNF--KDAPQYLSQVIIggrDAGAA 216
Cdd:cd07077 100 PIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHgpKILVLYVPHPSD---ELAEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 217 LVDDPRVALISATGSTRMGRevAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVgTAGQRCTTLRRLIAHE 296
Cdd:cd07077 176 LLSHPKIDLIVATGGRDAVD--AAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNLYVVD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 297 SVKEEIVTRLKaayskvrighplegnligpliDKHGFdamqdaleqalsEGGKVFGGKRqledkfpnayyvsPAIVEMPE 376
Cdd:cd07077 253 DVLDPLYEEFK---------------------LKLVV------------EGLKVPQETK-------------PLSKETTP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 377 QSDVVCTETFAPILYVVGYKDFAEALRLNNAV----PQGLSSCIFTTDVREAEQFMSAVGSDCGIANvniGPSGAEIGGA 452
Cdd:cd07077 287 SFDDEALESMTPLECQFRVLDVISAVENAWMIiesgGGPHTRCVYTHKINKVDDFVQYIDTASFYPN---ESSKKGRGAF 363
|
330 340
....*....|....*....|
gi 1224333486 453 FGGEKETggGRESGSDAWRG 472
Cdd:cd07077 364 AGKGVER--IVTSGMNNIFG 381
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
139-427 |
3.80e-08 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, 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: 143440 [Multi-domain] Cd Length: 436 Bit Score: 55.58 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 139 PLGVV-GVISAFNfPVAVWAWNTTLALVCGNAVIWKPSektPLTALACQALFERVLKNFK--DAPQYLSQVI-IGGRDAG 214
Cdd:cd07122 95 PVGVIaALIPSTN-PTSTAIFKALIALKTRNAIIFSPH---PRAKKCSIEAAKIMREAAVaaGAPEGLIQWIeEPSIELT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 215 AALVDDPRVALISATGSTRMgrevapkVAArfARS----ILELG-GNNAMILGPSADLDMAVRAILFSAV---GTAgqrC 286
Cdd:cd07122 171 QELMKHPDVDLILATGGPGM-------VKA--AYSsgkpAIGVGpGNVPAYIDETADIKRAVKDIILSKTfdnGTI---C 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 287 TTLRRLIAHESVKEEIVTRLKA--AY-------SKVR-----IGHPLEGNLIGplidkhgfdamQDALEQALSEGGKVFG 352
Cdd:cd07122 239 ASEQSVIVDDEIYDEVRAELKRrgAYflneeekEKLEkalfdDGGTLNPDIVG-----------KSAQKIAELAGIEVPE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 353 GKRQLedkfpnayyvspaIVEMPE--QSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQ----GLSSCIFTTDVREAEQ 426
Cdd:cd07122 308 DTKVL-------------VAEETGvgPEEPLSREKLSPVLAFYRAEDFEEALEKARELLEyggaGHTAVIHSNDEEVIEE 374
|
.
gi 1224333486 427 F 427
Cdd:cd07122 375 F 375
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
41-456 |
9.61e-07 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 51.08 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 41 AEVEQQVSRAEHAFEAWRNVPAPRRGELVRQFGDVLRQYKADLGELVSWEAG------KITQ-EGLGEVQEMIDICDfAV 113
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGmgrvedKIAKnHLAAEKTPGTEDLT-TT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 114 GLSRQlYGLTIAsERPghhmretwhPLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSektPLTALACQALFERVL 193
Cdd:cd07121 83 AWSGD-NGLTLV-EYA---------PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPH---PGAKKVSAYAVELIN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 194 KNFKDA--PQYLSQVI----IggrDAGAALVDDPRVALISATGstrmGREVAPKVAARFARSILELGGNNAMILGPSADL 267
Cdd:cd07121 149 KAIAEAggPDNLVVTVeeptI---ETTNELMAHPDINLLVVTG----GPAVVKAALSSGKKAIGAGAGNPPVVVDETADI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 268 DMAVRAILFSAVGTAGQRCTTLRRLIAHESVKEEIVTRLKAaYSKVRIGHPLEGNLIGPLIDKHGFDAM------QDALE 341
Cdd:cd07121 222 EKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQR-NGAYVLNDEQAEQLLEVVLLTNKGATPnkkwvgKDASK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 342 QALSEGGKVFGGKRQLedkfpnayyvspaIVEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGL--SSCIFTT 419
Cdd:cd07121 301 ILKAAGIEVPADIRLI-------------IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSK 367
|
410 420 430
....*....|....*....|....*....|....*..
gi 1224333486 420 DVREAEQFMSAVgsDCGIANVNiGPSGAEIGgaFGGE 456
Cdd:cd07121 368 NVENLTKMARAM--QTTIFVKN-GPSYAGLG--VGGE 399
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
139-455 |
2.29e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 49.96 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 139 PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTP-LTALACQALFERVLKnfKDAPQYLsqviIGGRD----- 212
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKkVTQRAATLLLQAAVA--AGAPENL----IGWIDnpsie 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 213 AGAALVDDPRVALISATGstrmGREVAPKVAARFARSILELGGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRRL 292
Cdd:cd07081 169 LAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 293 IAHESVKEEIVTRLKAAYskvrighplegnliGPLIDKHGFDAMQDALEQALSEGGKVFGgkrqledkfPNAYYVSPAI- 371
Cdd:cd07081 245 IVVDSVYDEVMRLFEGQG--------------AYKLTAEELQQVQPVILKNGDVNRDIVG---------QDAYKIAAAAg 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 372 VEMPEQSDVV-------------CTETFAPILYVVGYKDFAEALRLNNAVPQ----GLSSCIFTTDVREAE---QFMSAV 431
Cdd:cd07081 302 LKVPQETRILigevtslaehepfAHEKLSPVLAMYRAANFADADAKALALKLeggcGHTSAMYSDNIKAIEnmnQFANAM 381
|
330 340
....*....|....*....|....
gi 1224333486 432 GSDCGIANVNIGPSGAEIGGAFGG 455
Cdd:cd07081 382 KTSRFVKNGPCSQGGLGDLYNFRG 405
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
139-456 |
8.74e-05 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 44.89 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 139 PLGVVGVISAFNFPVAVWAWNTTLALVCGNAVIWKPSEKTPLTALACQALFERVLKNfKDAPQYLSQVI----IggrDAG 214
Cdd:PRK15398 129 PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVA-AGGPENLVVTVaeptI---ETA 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 215 AALVDDPRVALISATGST---RMGREVAPKVAARFArsilelgGNNAMILGPSADLDMAVRAILFSAVGTAGQRCTTLRR 291
Cdd:PRK15398 205 QRLMKHPGIALLVVTGGPavvKAAMKSGKKAIGAGA-------GNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 292 LIAHESVKEEIVTRLKAayskvrighplEGNLigpLIDKHGFDAMQDAleqALSEGGKVfggKRQLEDKfpNAYYVSPA- 370
Cdd:PRK15398 278 VIVVDSVADELMRLMEK-----------NGAV---LLTAEQAEKLQKV---VLKNGGTV---NKKWVGK--DAAKILEAa 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224333486 371 -----------IVEMPEQSDVVCTETFAPILYVVGYKDFAEALRLNNAVPQGL--SSCIFTTDVREAEQFMSAVgsDCGI 437
Cdd:PRK15398 336 ginvpkdtrllIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNKMARAI--QTSI 413
|
330
....*....|....*....
gi 1224333486 438 ANVNiGPSGAEIGgaFGGE 456
Cdd:PRK15398 414 FVKN-GPSYAGLG--LGGE 429
|
|
| |
