|
Name |
Accession |
Description |
Interval |
E-value |
| G3PDH_Arch |
NF040869 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; |
1-500 |
0e+00 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468806 Cd Length: 502 Bit Score: 861.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 1 MRAGLLEGVIKEK-GGVPVYPSYLAGEWGGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFKRGRWSARDMPGTER 79
Cdd:NF040869 1 EKSPLFKDIYRIGeDGVPEFKTYVAGEWVFGGEFADVKSPIDGSVIARVSRLSREQVEEAIETIYEKGRWKIRDTPGEKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 80 LAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGLVRREPLG 159
Cdd:NF040869 81 LEIFLRAADLLEKHRDDFVNVLVLNAGKTRSAAEGEVNASIERLRKATLDVRKIYGDYIPGDWSEETLESEAIVRREPYG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 160 VVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAV 239
Cdd:NF040869 161 VVLAITPFNYPLFDTVNKIVYSLLAGNAVILKPASADPLPALLFARVLELAGFPKESLALLTIPGREMDKVVADRRISAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 240 SFTGSTEVGERVVKVGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAK 319
Cdd:NF040869 241 SFTGSTETGEHVLRTGGIKQYIMELGGGDPAIVLDDADLELAAEKIVTGITSYSGQRCDAIKLILAEEKIYDELKKRLVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 320 RLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPTYVQPTFVEAPADRVKDMVLYKREVFAP 399
Cdd:NF040869 321 ELSKVKVGDPRDENVVMGPLIDEKTADEIEEAIKDAVEKGGKILYGGRRLGGNYVEPTLIEVDKEKLKDLRLYNEEVFAP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 400 VALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAV 479
Cdd:NF040869 401 VALLVKVKDLDEAIELANSRRYGLDAAIFGEDINRIRKVIRLLEVGAVYINDYPRHGIGYYPFGGRKDSGIGREGIGYSI 480
|
490 500
....*....|....*....|.
1UXU_A 480 EAVTAYKTIVFNYKGKGVWKY 500
Cdd:NF040869 481 EYVTAYKTIVYNYRGKGVWEY 501
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
18-491 |
0e+00 |
|
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: 645.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 18 VYPSYLAGEW-GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFKRGRWSARDMPGTERLAVLRKAADIIERNLDV 96
Cdd:cd07082 1 QFKYLINGEWkESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 97 FAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGLVRREPLGVVAAITPFNYPLFDAVN 176
Cdd:cd07082 81 VANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 177 KITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVSFTGSTEVGERVVKVG 255
Cdd:cd07082 161 KLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREiGDPLVTHGRIDVISFTGSTEVGNRLKKQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 256 GVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVD 335
Cdd:cd07082 241 PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 336 VGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPTYVQPTFVEAPADrvkDMVLYKREVFAPVALAVEVKDLDQAIEL 415
Cdd:cd07082 321 ITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGNLIYPTLLDPVTP---DMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1UXU_A 416 ANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVFN 491
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
17-492 |
3.17e-160 |
|
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: 463.06 E-value: 3.17e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 17 PVYPSYLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLfKRGRWSARDMPGTERLAVLRKAADIIERNL 94
Cdd:COG1012 4 PEYPLFIGGEWvaAASGETFDVINPATGEVLARVPAATAEDVDAAVAAA-RAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 95 DVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTydtlETEGLVRREPLGVVAAITPFNYPLFDA 174
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAP----GTRAYVRREPLGVVGAITPWNFPLALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 175 VNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVK 253
Cdd:COG1012 159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVgAALVAHPDVDKISFTGSTAVGRRIAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 254 VGG--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRD 331
Cdd:COG1012 239 AAAenLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 332 PTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRL---GPTYVQPTFVEAPADrvkDMVLYKREVFAPVALAVEVKD 408
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdgeGGYFVEPTVLADVTP---DMRIAREEIFGPVLSVIPFDD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 409 LDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTI 488
Cdd:COG1012 396 EEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTV 475
|
....
1UXU_A 489 VFNY 492
Cdd:COG1012 476 TIRL 479
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
70-490 |
7.18e-152 |
|
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: 440.11 E-value: 7.18e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 70 SARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPgdwtYDTLET 149
Cdd:cd07078 13 AWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIP----SPDPGE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 150 EGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-E 228
Cdd:cd07078 89 LAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVgA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 229 KIVADDRVAAVSFTGSTEVGERVVKVGG--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAE 306
Cdd:cd07078 169 ALASHPRVDKISFTGSTAVGKAIMRAAAenLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 307 RPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT---YVQPTFVEAPA 383
Cdd:cd07078 249 ESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkgyFVPPTVLTDVD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 384 DrvkDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFG 463
Cdd:cd07078 329 P---DMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPSAPFG 405
|
410 420
....*....|....*....|....*..
1UXU_A 464 GRKKSGVFREGIGYAVEAVTAYKTIVF 490
Cdd:cd07078 406 GVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
29-488 |
1.08e-146 |
|
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: 428.10 E-value: 1.08e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 29 GSGQEIEVKSPIDLATIAKVISPSREEVERTLDVL---FKRgrWsaRDMPGTERLAVLRKAADIIERNLDVFAEVLVMNA 105
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAAraaFPA--W--RKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 106 GKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLeteglVRREPLGVVAAITPFNYPLFDAVNKITYSFIYG 185
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAY-----TRREPLGVVGAITPWNFPLLLPAWKIAPALAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 186 NAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEK-IVADDRVAAVSFTGSTEVGERVVKVGG--VKQYVM 262
Cdd:pfam00171 155 NTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEaLVEHPDVRKVSFTGSTAVGRHIAEAAAqnLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 263 ELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISP 342
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 343 SAVDEMMAAIEDAVEKGGRVLAGGRRLGPT--YVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRP 420
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNgyFVEPTVL---ANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1UXU_A 421 YGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTI 488
Cdd:pfam00171 392 YGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
34-489 |
4.46e-134 |
|
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: 395.56 E-value: 4.46e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 34 IEVKSPIDLATIAKVISPSREEVERTLDVLFKrGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAV 113
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEK-AKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 114 GEVKAAVDRLRLAELDLKKIGGDYIPGDwTYDTLETE-GLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKP 192
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVD-AYEYNERRiAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 193 SISDPLPAAMAVKALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVSFTGSTEVGERVVK--VGGVKQYVMELGGGDP 269
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEvGDEIVTNPKVNMISFTGSTAVGLLIASkaGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 270 AIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMM 349
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 350 AAIEDAVEKGGRVLAGGRRLGPTYVQPTFVEAPAdrvKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFG 429
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKRDEGSFFPPTVLENDT---PDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 430 RDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIV 489
Cdd:cd07145 396 NDINRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIV 455
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
34-490 |
1.29e-132 |
|
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: 391.96 E-value: 1.29e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 34 IEVKSPIDLATIAKVISPSREEVERTLDVLfKRGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAV 113
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAA-KEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 114 GEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPS 193
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRLAGETIPFDASPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 194 ISDPLPAAMAVKALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVSFTGSTEVGERVVKVGGVKQYVMELGGGDPAIV 272
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETvGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKVTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 273 LEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAI 352
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 353 EDAVEKGGRVLAGGRRLGpTYVQPTFVEAPAdrvKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDV 432
Cdd:cd07149 320 EEAVEGGARLLTGGKRDG-AILEPTVLTDVP---PDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
1UXU_A 433 VKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVF 490
Cdd:cd07149 396 QKALKAARELEVGGVMINDSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
34-490 |
3.31e-127 |
|
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: 377.93 E-value: 3.31e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 34 IEVKSPIDLATIAKVISPSREEVERTLDVLFKRGRWSaRDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAV 113
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENR-RALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 114 GEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPS 193
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 194 ISDPLPAAMAVKALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVSFTGSTEVGERVVKVGGVKQYVMELGGGDPAIV 272
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVlGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 273 LEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAI 352
Cdd:cd07094 240 DRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 353 EDAVEKGGRVLAGGRRLGPTYvQPTFVEAPAdrvKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDV 432
Cdd:cd07094 320 EEAVEAGARLLCGGERDGALF-KPTVLEDVP---RDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
1UXU_A 433 VKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVF 490
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| lactal_redase_Meth |
NF040648 |
lactaldehyde dehydrogenase; |
25-491 |
8.73e-120 |
|
lactaldehyde dehydrogenase;
Pssm-ID: 468615 [Multi-domain] Cd Length: 463 Bit Score: 359.30 E-value: 8.73e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 25 GEWGGSgQEIEVKSPIDLATIAKVISPSREEVERTLDVLfKRGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMN 104
Cdd:NF040648 5 GKWIDR-EDIDVINPYNLEVIDKIPSLSREEVKEAIEIA-NEAKEVMKNLSPRKRYNILMDIAEELKKNKEELAKLITID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 105 AGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDwtydtlETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIY 184
Cdd:NF040648 83 AGKPIKQSIIEVDRSIETFKLAAFYAKEIRGETIPSD------AGLIFTKKEPLGVVGAITPFNYPLNLAAHKIAPAIAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 185 GNAVVVKPSISDPLPAAMAVK----ALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVSFTGSTEVGERVVKVGGVKQ 259
Cdd:NF040648 157 GNSVVLHPSSKAPLAAIELAKiiekVLKKMNIPLGVFNLVTGYGEVvGDEIVKNEKVNKISFTGSVEVGESISKKAGMKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 260 YVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPL 339
Cdd:NF040648 237 ITLELGGNNPLIVLKDADIEKAVESAVKGSFLNSGQVCISVGRVIVEEEIADEFIKKLVEETKKLKVGNPLDEKTDIGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 340 ISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGpTYVQPTFVEAPAdrvkDMVLYKREVFAPVALAVEVKDLDQAIELANGR 419
Cdd:NF040648 317 ITEEAAIRVENLVNEAIEEGAKLLCGGNREG-SLFYPTVLDVDE----DNILVKVETFGPVLPIIRVKDIDEAIEIANNT 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1UXU_A 420 PYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVFN 491
Cdd:NF040648 392 KYGLQAGVFTNDINKALKFADELEYGGVIINKSSTFRTDNMPFGGFKKSGLGKEGIKYAVEEMTEIKTIVIN 463
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
34-490 |
4.36e-115 |
|
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: 346.93 E-value: 4.36e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 34 IEVKSPIDLATIAKVISPSREEVERTLDVLFKrGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAV 113
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVK-AFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 114 GEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPS 193
Cdd:cd07147 80 GEVARAIDTFRIAAEEATRIYGEVLPLDISARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 194 ISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVVKVGGVKQYVMELGGGDPAIVL 273
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKKVVLELGGNAAVIVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 274 EDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIE 353
Cdd:cd07147 240 SDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 354 DAVEKGGRVLAGGRRLGPTYvQPTFVEapaDRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVV 433
Cdd:cd07147 320 EAVDAGAKLLTGGKRDGALL-EPTILE---DVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLE 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
1UXU_A 434 KIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVF 490
Cdd:cd07147 396 KALRAWDELEVGGVVINDVPTFRVDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
35-488 |
1.59e-114 |
|
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: 345.47 E-value: 1.59e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 35 EVKSPIDLATIAKVISPSREEVERTLDVLFK-RGRWSarDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAV 113
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDaFPAWA--ATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 114 GEVKAAVDRLRLAELDLKKIGGDYIPGDWTydtlETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPS 193
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRGETLPSDSP----GTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 194 ISDPLPAAMAVKALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVSFTGSTEVGERVVKVGGV--KQYVMELGGGDPA 270
Cdd:cd07150 156 EETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEvGDELVDDPRVRMVTFTGSTAVGREIAEKAGRhlKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 271 IVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMA 350
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 351 AIEDAVEKGGRVLAGGRRLGPtYVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGR 430
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKYDGN-FYQPTVL---TDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
1UXU_A 431 DVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTI 488
Cdd:cd07150 392 DLQRAFKLAERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
34-489 |
2.20e-112 |
|
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: 340.11 E-value: 2.20e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 34 IEVKSPIDLATIAKVISPSREEVERTLD-VLFKRGRWSARDmpgteRLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAA 112
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALAlAASYRSTLTRYQ-----RSAILNKAAALLEARREEFARLITLESGLCLKDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 113 VGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKP 192
Cdd:cd07146 76 RYEVGRAADVLRFAAAEALRDDGESFSCDLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 193 SISDPLPAAMAVKALLDAGFPPDAIALL-NLPGKEAEKIVADDRVAAVSFTGSTEVGERVVKVGGVKQYVMELGGGDPAI 271
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVtGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 272 VLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAA 351
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 352 IEDAVEKGGRVLAGGRRLGPTYvQPTFVeapaDRV-KDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGR 430
Cdd:cd07146 316 VEEAIAQGARVLLGNQRQGALY-APTVL----DHVpPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTN 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 431 DVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSG-VFREGIGYAVEAVTAYKTIV 489
Cdd:cd07146 391 DLDTIKRLVERLDVGTVNVNEVPGFRSELSPFGGVKDSGlGGKEGVREAMKEMTNVKTYS 450
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
69-483 |
8.09e-112 |
|
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: 337.97 E-value: 8.09e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 69 WSArdMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPgdwtYDTLE 148
Cdd:cd07104 16 WAA--TPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILP----SDVPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 149 TEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAV-KALLDAGFPPdaiALLN-LPGKE 226
Cdd:cd07104 90 KESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPK---GVLNvVPGGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 227 AE---KIVADDRVAAVSFTGSTEVGERVVKVGG--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIK 301
Cdd:cd07104 167 SEigdALVEHPRVRMISFTGSTAVGRHIGELAGrhLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 302 LVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPtYVQPT-FVE 380
Cdd:cd07104 247 RILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEGL-FYQPTvLSD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 381 APAdrvkDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYY 460
Cdd:cd07104 326 VTP----DMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDEPHV 401
|
410 420
....*....|....*....|...
1UXU_A 461 PFGGRKKSGVFREGIGYAVEAVT 483
Cdd:cd07104 402 PFGGVKASGGGRFGGPASLEEFT 424
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
72-490 |
1.02e-111 |
|
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: 335.35 E-value: 1.02e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 72 RDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDyipgDWTYDTLETEG 151
Cdd:cd06534 11 AALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGP----ELPSPDPGGEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 152 LVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKI 230
Cdd:cd06534 87 YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVgAAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 231 VADDRVAAVSFTGSTEVGERVVKVGG--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERP 308
Cdd:cd06534 167 LSHPRVDKISFTGSTAVGKAIMKAAAenLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHES 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 309 VYGKLVEEVAKRLsslrvgdprdptVDVGPlispsavdemmaaiedavekggrvlaggrrlgptyvqptfveapadrvkD 388
Cdd:cd06534 247 IYDEFVEKLVTVL------------VDVDP-------------------------------------------------D 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 389 MVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKS 468
Cdd:cd06534 266 MPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFGGVKNS 345
|
410 420
....*....|....*....|..
1UXU_A 469 GVFREGIGYAVEAVTAYKTIVF 490
Cdd:cd06534 346 GIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
36-490 |
4.85e-109 |
|
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: 331.32 E-value: 4.85e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 36 VKSPIDLATIAKVISPSREEVERTLDVL---FKRgrWsaRDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAA 112
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAaaaFKT--W--RKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 113 VGEVKAAVDRLR-LAElDLKKIGGDYIPGDwtydTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVK 191
Cdd:cd07103 77 RGEVDYAASFLEwFAE-EARRIYGRTIPSP----APGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 192 PSISDPLPAAMAVKALLDAGFPPDAIALLnlPGKEAE---KIVADDRVAAVSFTGSTEVGERVVK--VGGVKQYVMELGG 266
Cdd:cd07103 152 PAEETPLSALALAELAEEAGLPAGVLNVV--TGSPAEigeALCASPRVRKISFTGSTAVGKLLMAqaADTVKRVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 267 GDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVD 346
Cdd:cd07103 230 NAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 347 EMMAAIEDAVEKGGRVLAGGRR--LGPTYVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLD 424
Cdd:cd07103 310 KVEALVEDAVAKGAKVLTGGKRlgLGGYFYEPTVL---TDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1UXU_A 425 AAVFGRDVVKIRRAVRLLEVGAIYINdmprHGIGYY---PFGGRKKSGVFREGIGYAVEAVTAYKTIVF 490
Cdd:cd07103 387 AYVFTRDLARAWRVAEALEAGMVGIN----TGLISDaeaPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
19-488 |
1.98e-105 |
|
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: 323.05 E-value: 1.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 19 YPSYLAGEWGGSGQEIEVKSPIDLA-TIAKVISPSREEVERTLDVLFKRGR-WsaRDMPGTERLAVLRKAADIIERNLDV 96
Cdd:cd07097 1 YRNYIDGEWVAGGDGEENRNPSDTSdVVGKYARASAEDADAAIAAAAAAFPaW--RRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 97 FAEVLVMNAGKPKSAAVGEVKAAVDRLR-LAELDLKkIGGDYIPGDWTydtlETEGLVRREPLGVVAAITPFNYPLFDAV 175
Cdd:cd07097 79 LARLLTREEGKTLPEARGEVTRAGQIFRyYAGEALR-LSGETLPSTRP----GVEVETTREPLGVVGLITPWNFPIAIPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 176 NKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVSFTGSTEVGERVVK- 253
Cdd:cd07097 154 WKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEvGQALVEHPDVDAVSFTGSTAVGRRIAAa 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 254 -VGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDP 332
Cdd:cd07097 234 aAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 333 TVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRL-GPT---YVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKD 408
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkRPDegyYLAPALF---AGVTNDMRIAREEIFGPVAAVIRVRD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 409 LDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINdMPRHGIGYY-PFGGRKKSGV-FREGIGYAVEAVTAYK 486
Cdd:cd07097 391 YDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVN-LPTAGVDYHvPFGGRKGSSYgPREQGEAALEFYTTIK 469
|
..
1UXU_A 487 TI 488
Cdd:cd07097 470 TV 471
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
21-492 |
3.85e-102 |
|
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: 314.50 E-value: 3.85e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 21 SYLAGEWGGSGQE-IEVKSPIDLATIAKVISPSREEVERTLDVL---FKRgrWsaRDMPGTERLAVLRKAADIIERNLDV 96
Cdd:cd07086 1 GVIGGEWVGSGGEtFTSRNPANGEPIARVFPASPEDVEAAVAAAreaFKE--W--RKVPAPRRGEIVRQIGEALRKKKEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 97 FAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGdwtydtlETEG---LVRREPLGVVAAITPFNYPLfd 173
Cdd:cd07086 77 LGRLVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPS-------ERPGhrlMEQWNPLGVVGVITAFNFPV-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 174 AVN--KITYSFIYGNAVVVKPSISDPLPA----AMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEV 247
Cdd:cd07086 148 AVPgwNAAIALVCGNTVVWKPSETTPLTAiavtKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 248 GERV-VKVGG-VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLR 325
Cdd:cd07086 228 GRRVgETVARrFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 326 VGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT----YVQPTFVEAPADrvkDMVLYKREVFAPVA 401
Cdd:cd07086 308 IGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGepgnYVEPTIVTGVTD---DARIVQEETFAPIL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 402 LAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVR--LLEVGAIYINdMPRHG--IGyYPFGGRKKSGVFREGIGY 477
Cdd:cd07086 385 YVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGpkGSDCGIVNVN-IPTSGaeIG-GAFGGEKETGGGRESGSD 462
|
490
....*....|....*
1UXU_A 478 AVEAVTAYKTIVFNY 492
Cdd:cd07086 463 AWKQYMRRSTCTINY 477
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
38-488 |
6.06e-101 |
|
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: 310.65 E-value: 6.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 38 SPIDLATIAKVISPSREEVERTLDVL---FKRgrWSArdMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKP-KSAAV 113
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAkeaFPG--WSR--MSPAERARILHKVADLIEARADELALLESLDTGKPiTLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 114 GEVKAAVDRLRL-AELDLKKIGGDY--IPGDWTYdtleteglVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVV 190
Cdd:cd07093 79 RDIPRAAANFRFfADYILQLDGESYpqDGGALNY--------VLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 191 KPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVKVG--GVKQYVMELGGG 267
Cdd:cd07093 151 KPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAgAALVAHPDVDLISFTGETATGRTIMRAAapNLKPVSLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 268 DPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDE 347
Cdd:cd07093 231 NPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 348 MMAAIEDAVEKGGRVLAGGRRL------GPTYVQPTFVEAPADrvkDMVLYKREVFAPVALAVEVKDLDQAIELANGRPY 421
Cdd:cd07093 311 VLGYVELARAEGATILTGGGRPelpdleGGYFVEPTVITGLDN---DSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPY 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1UXU_A 422 GLDAAVFGRDVVKIRRAVRLLEVGAIYIN-----DMPRhgigyyPFGGRKKSGVFREGIGYAVEAVTAYKTI 488
Cdd:cd07093 388 GLAAYVWTRDLGRAHRVARRLEAGTVWVNcwlvrDLRT------PFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
72-489 |
4.38e-100 |
|
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: 307.46 E-value: 4.38e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 72 RDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRL----AELDLKkiggdyipgDWTYDTL 147
Cdd:cd07100 16 RKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyaenAEAFLA---------DEPIETD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 148 ETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA 227
Cdd:cd07100 87 AGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 228 EKIVADDRVAAVSFTGSTEVGERVVKVGG--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLA 305
Cdd:cd07100 167 EAIIADPRVRGVTLTGSERAGRAVAAEAGknLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 306 ERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT--YVQPTFVEapa 383
Cdd:cd07100 247 HEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPgaFYPPTVLT--- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 384 DRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDM----PRhgigy 459
Cdd:cd07100 324 DVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMvksdPR----- 398
|
410 420 430
....*....|....*....|....*....|
1UXU_A 460 YPFGGRKKSGVFREGIGYAVEAVTAYKTIV 489
Cdd:cd07100 399 LPFGGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
39-490 |
7.22e-95 |
|
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: 295.23 E-value: 7.22e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 39 PIDLATIAKVISPSREEVER---TLDVLFKRGRWsaRDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGE 115
Cdd:cd07114 4 PATGEPWARVPEASAADVDRavaAARAAFEGGAW--RKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 116 VKAAVDRLR----LAEldlkKIGGDYIPGDwtydTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVK 191
Cdd:cd07114 82 VRYLAEWYRyyagLAD----KIEGAVIPVD----KGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 192 PSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVKVGG--VKQYVMELGGGD 268
Cdd:cd07114 154 PSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETgEALVEHPLVAKIAFTGGTETGRHIARAAAenLAPVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 269 PAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEM 348
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 349 MAAIEDAVEKGGRVLAGGRRLGPT------YVQPTFVEAPADrvkDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYG 422
Cdd:cd07114 314 ERYVARAREEGARVLTGGERPSGAdlgagyFFEPTILADVTN---DMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYG 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1UXU_A 423 LDAAVFGRDVVKIRRAVRLLEVGAIYINDMprHGIGYY-PFGGRKKSGVFREGigyAVEAVTAY---KTIVF 490
Cdd:cd07114 391 LAAGIWTRDLARAHRVARAIEAGTVWVNTY--RALSPSsPFGGFKDSGIGREN---GIEAIREYtqtKSVWI 457
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
19-470 |
5.58e-94 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 294.52 E-value: 5.58e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 19 YPSYLAGEWGGSGQEIEVKSPIDLA-TIAKVISPSREEVERTLDVLfKRGRWSARDMPGTERLAVLRKAADIIERNLDVF 97
Cdd:cd07124 33 YPLVIGGKEVRTEEKIESRNPADPSeVLGTVQKATKEEAEAAVQAA-RAAFPTWRRTPPEERARLLLRAAALLRRRRFEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 98 AEVLVMNAGKPKSAAVGEVKAAVDRLRL-AELDLKKIGGDYIPGDWTYDTLeteglvRREPLGVVAAITPFNYPLFDAVN 176
Cdd:cd07124 112 AAWMVLEVGKNWAEADADVAEAIDFLEYyAREMLRLRGFPVEMVPGEDNRY------VYRPLGVGAVISPWNFPLAILAG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 177 KITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVG----ERV 251
Cdd:cd07124 186 MTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGlriyERA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 252 VKV----GGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVG 327
Cdd:cd07124 266 AKVqpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 328 DPRDPTVDVGPLISPSAVDEMMAAIEDAvEKGGRVLAGGRRLGPT----YVQPT-FVEAPADRvkdmVLYKREVFAPVAL 402
Cdd:cd07124 346 DPEDPEVYMGPVIDKGARDRIRRYIEIG-KSEGRLLLGGEVLELAaegyFVQPTiFADVPPDH----RLAQEEIFGPVLA 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1UXU_A 403 AVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINdmpRHG----IGYYPFGGRKKSGV 470
Cdd:cd07124 421 VIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYAN---RKItgalVGRQPFGGFKMSGT 489
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
34-490 |
1.95e-93 |
|
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: 291.24 E-value: 1.95e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 34 IEVKSPIDLATIAKVISPSREEVERTLDV---LFK-RGRWsardMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPK 109
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTahaLFLdRNNW----LPAHERIAILERLADLMEERADELALLIAREGGKPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 110 SAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVV 189
Cdd:cd07148 77 VDAKVEVTRAIDGVELAADELGQLGGREIPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 190 VKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERV-VKVGGVKQYVMELGGGD 268
Cdd:cd07148 157 VKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLrSKLAPGTRCALEHGGAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 269 PAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEM 348
Cdd:cd07148 237 PVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 349 MAAIEDAVEKGGRVLAGGRRLGPTYVQPTFVEAPADRVKdmvLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVF 428
Cdd:cd07148 317 EEWVNEAVAAGARLLCGGKRLSDTTYAPTVLLDPPRDAK---VSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
1UXU_A 429 GRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVF 490
Cdd:cd07148 394 TKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
36-490 |
2.13e-93 |
|
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: 291.45 E-value: 2.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 36 VKSPIDLATIAKVISPSREEVERTLDVL---FKRGRWSardMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAA 112
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAArraFDTGDWS---TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 113 VG-EVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVK 191
Cdd:cd07089 78 RAmQVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 192 PSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVKVGG--VKQYVMELGGGD 268
Cdd:cd07089 158 PAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVgEALTTDPRVDMVSFTGSTAVGRRIMAQAAatLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 269 PAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEM 348
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 349 MAAIEDAVEKGGRVLAGGRRLGPT----YVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLD 424
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRPAGLdkgfYVEPTLF---ADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLS 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 425 AAVFGRDVVKIRRAVRLLEVGAIYINdmprhGIGYY----PFGGRKKSGVFREGIGYAVEAVTAYKTIVF 490
Cdd:cd07089 395 GGVWSADVDRAYRVARRIRTGSVGIN-----GGGGYgpdaPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
22-490 |
1.57e-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: 286.85 E-value: 1.57e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 22 YLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLfKRGRWSARDMPGTERLAVLRKAADIIERNLDVFAE 99
Cdd:cd07088 1 YINGEFvpSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAA-EAAQKAWERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 100 VLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLetegLVRREPLGVVAAITPFNYPLFDAVNKIT 179
Cdd:cd07088 80 LIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENI----FIFKVPIGVVAGILPWNFPFFLIARKLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 180 YSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVSFTGSTEVGERVVKVGG-- 256
Cdd:cd07088 156 PALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVvGDALVAHPKVGMISLTGSTEAGQKIMEAAAen 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 257 VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDV 336
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 337 GPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT---YVQPTFVEapaDRVKDMVLYKREVFAPVALAVEVKDLDQAI 413
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEkgyFYEPTVLT---NVRQDMEIVQEEIFGPVLPVVKFSSLDEAI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1UXU_A 414 ELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGI-GYYpfGGRKKSGVFREGIGYAVEAVTAYKTIVF 490
Cdd:cd07088 393 ELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMqGFH--AGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
21-492 |
3.43e-90 |
|
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: 283.85 E-value: 3.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 21 SYLAGEW--GGSGQEIEVKSPIDLAT-IAKVISPSREEVERTLDVLFK-RGRWSArdMPGTERLAVLRKAADIIERNLDV 96
Cdd:cd07131 1 NYIGGEWvdSASGETFDSRNPADLEEvVGTFPLSTASDVDAAVEAAREaFPEWRK--VPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 97 FAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTydtlETEGLVRREPLGVVAAITPFNYPLFDAVN 176
Cdd:cd07131 79 LARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELP----NKDAMTRRQPIGVVALITPWNFPVAIPSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 177 KITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVKVG 255
Cdd:cd07131 155 KIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 256 G--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPT 333
Cdd:cd07131 235 ArpNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 334 VDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT------YVQPTFVEapaDRVKDMVLYKREVFAPVALAVEVK 407
Cdd:cd07131 315 TDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGgyekgyFVEPTVFT---DVTPDMRIAQEEIFGPVVALIEVS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 408 DLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINdMPRhgIG---YYPFGGRKKSGV-FREGIGYAVEAVT 483
Cdd:cd07131 392 SLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN-APT--IGaevHLPFGGVKKSGNgHREAGTTALDAFT 468
|
....*....
1UXU_A 484 AYKTIVFNY 492
Cdd:cd07131 469 EWKAVYVDY 477
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
25-488 |
6.99e-90 |
|
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: 282.66 E-value: 6.99e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 25 GEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFKRGR-WSArdMPGTERLAVLRKAADIIERNLDVFAEVL 101
Cdd:cd07151 1 GEWrdGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKeWAA--TLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 102 VMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPgdwtYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYS 181
Cdd:cd07151 79 IRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILP----SDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 182 FIYGNAVVVKPSISDPLPAAMAV-KALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAV-SFTGSTEVGERVVKVGG--V 257
Cdd:cd07151 155 LALGNAVVLKPASDTPITGGLLLaKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLiSFTGSTPVGRHIGELAGrhL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 258 KQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVG 337
Cdd:cd07151 235 KKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 338 PLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGpTYVQPT-FVEAPAdrvkDMVLYKREVFAPVALAVEVKDLDQAIELA 416
Cdd:cd07151 315 PLINESQVDGLLDKIEQAVEEGATLLVGGEAEG-NVLEPTvLSDVTN----DMEIAREEIFGPVAPIIKADDEEEALELA 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1UXU_A 417 NGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTI 488
Cdd:cd07151 390 NDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
44-486 |
1.04e-88 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 278.83 E-value: 1.04e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 44 TIAKVISPSREEVERTLDVL---FKRGRWSArdmPGtERLAVLRKAADIIERNLDVFAEVLVMNAGKP-KSAAVGEVKAA 119
Cdd:cd07092 9 EIATVPDASAADVDAAVAAAhaaFPSWRRTT---PA-ERSKALLKLADAIEENAEELAALESRNTGKPlHLVRDDELPGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 120 VDRLRL---AELDLK-KIGGDYIPGdwtydtleTEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSIS 195
Cdd:cd07092 85 VDNFRFfagAARTLEgPAAGEYLPG--------HTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 196 DPLPAAMaVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVKV--GGVKQYVMELGGGDPAIV 272
Cdd:cd07092 157 TPLTTLL-LAELAAEVLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAaaDTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 273 LEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAI 352
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 353 EDAvEKGGRVLAGGRRLGPT--YVQPTFVEAPADrvkDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGR 430
Cdd:cd07092 316 ERA-PAHARVLTGGRRAEGPgyFYEPTVVAGVAQ---DDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
1UXU_A 431 DVVKIRRAVRLLEVGAIYINDmprHG--IGYYPFGGRKKSGVFREGIGYAVEAVTAYK 486
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNT---HIplAAEMPHGGFKQSGYGKDLSIYALEDYTRIK 446
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
25-490 |
1.25e-88 |
|
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: 279.48 E-value: 1.25e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 25 GEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVL---FKRGRWsaRDMPGTERLAVLRKAADIIERNLDVFAE 99
Cdd:cd07091 10 NEFvdSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAAraaFETGWW--RKMDPRERGRLLNKLADLIERDRDELAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 100 VLVMNAGKPKS-AAVGEVKAAVDRLR----LAEldlkKIGGDYIPGDWTYDTLeteglVRREPLGVVAAITPFNYPLFDA 174
Cdd:cd07091 88 LESLDNGKPLEeSAKGDVALSIKCLRyyagWAD----KIQGKTIPIDGNFLAY-----TRREPIGVCGQIIPWNFPLLML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 175 VNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVK 253
Cdd:cd07091 159 AWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAgAAISSHMDVDKIAFTGSTAVGRTIME 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 254 VGG---VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPR 330
Cdd:cd07091 239 AAAksnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 331 DPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLG--PTYVQPT-FveapADRVKDMVLYKREVFAPVALAVEVK 407
Cdd:cd07091 319 DPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGskGYFIQPTvF----TDVKDDMKIAKEEIFGPVVTILKFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 408 DLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN--DMPRHGIgyyPFGGRKKSGVFREGIGYAVEAVTAY 485
Cdd:cd07091 395 TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNtyNVFDAAV---PFGGFKQSGFGRELGEEGLEEYTQV 471
|
....*
1UXU_A 486 KTIVF 490
Cdd:cd07091 472 KAVTI 476
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
22-473 |
3.67e-88 |
|
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: 278.43 E-value: 3.67e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 22 YLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDV---LFKRGRWSArdMPGTERLAVLRKAADIIERNLDV 96
Cdd:cd07119 1 YIDGEWveAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAarrAFDSGEWPH--LPAQERAALLFRIADKIREDAEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 97 FAEVLVMNAGKPKSAAVGEVKAAVDRLR-LAELdLKKIGGDYIPGDwtydtLETEGLVRREPLGVVAAITPFNYPLFDAV 175
Cdd:cd07119 79 LARLETLNTGKTLRESEIDIDDVANCFRyYAGL-ATKETGEVYDVP-----PHVISRTVREPVGVCGLITPWNYPLLQAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 176 NKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVK- 253
Cdd:cd07119 153 WKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRa 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 254 -VGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDP 332
Cdd:cd07119 233 aAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 333 TVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT------YVQPTFVeapADRVKDMVLYKREVFAPVALAVEV 406
Cdd:cd07119 313 DTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakgyFVEPTIF---DDVDRTMRIVQEEIFGPVLTVERF 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1UXU_A 407 KDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMprhgiGYY----PFGGRKKSGVFRE 473
Cdd:cd07119 390 DTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDY-----HPYfaeaPWGGYKQSGIGRE 455
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
69-473 |
1.18e-87 |
|
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: 275.95 E-value: 1.18e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 69 WSARDMpgTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLR-LAELDLkkiggdyiPGDWTYDTL 147
Cdd:cd07106 35 WSATPL--EERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRyTASLDL--------PDEVIEDDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 148 ETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAgFPPDAIALLNLPGKEA 227
Cdd:cd07106 105 TRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGDELG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 228 EKIVADDRVAAVSFTGSTEVGERVVK--VGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLA 305
Cdd:cd07106 184 PALTSHPDIRKISFTGSTATGKKVMAsaAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 306 ERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRL-GPTY-VQPTFVEAPA 383
Cdd:cd07106 264 HESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLdGPGYfIPPTIVDDPP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 384 DrvkDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGyYPFG 463
Cdd:cd07106 344 E---GSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGALDPD-APFG 419
|
410
....*....|
1UXU_A 464 GRKKSGVFRE 473
Cdd:cd07106 420 GHKQSGIGVE 429
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
31-488 |
2.47e-86 |
|
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: 273.32 E-value: 2.47e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 31 GQEIEVKSPIDLATIAKVISPSREEVERTLDV---LFKRGRWSarDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGK 107
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAarrAFESGVWS--RLSPAERKAVLLRLADLIEAHRDELALLETLDMGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 108 PKSAAV-GEVKAAVDRLR-LAELdLKKIGGDYIPGDwtYDTLeteGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYG 185
Cdd:cd07112 79 PISDALaVDVPSAANTFRwYAEA-IDKVYGEVAPTG--PDAL---ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 186 NAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVA--DDrVAAVSFTGSTEVGERVVKVGG---VKQY 260
Cdd:cd07112 153 NSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGlhMD-VDALAFTGSTEVGRRFLEYSGqsnLKRV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 261 VMELGGGDPAIVLEDA-DLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPL 339
Cdd:cd07112 232 WLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 340 ISPSAVDEMMAAIEDAVEKGGRVLAGGRRL----GPTYVQPTFVeapaDRVK-DMVLYKREVFAPVALAVEVKDLDQAIE 414
Cdd:cd07112 312 VSEAHFDKVLGYIESGKAEGARLVAGGKRVltetGGFFVEPTVF----DGVTpDMRIAREEIFGPVLSVITFDSEEEAVA 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1UXU_A 415 LANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN-----DMPrhgigyYPFGGRKKSGVFREGIGYAVEAVTAYKTI 488
Cdd:cd07112 388 LANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNcfdegDIT------TPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
69-488 |
3.71e-86 |
|
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: 271.76 E-value: 3.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 69 WSArdMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDwTYDTLe 148
Cdd:cd07105 16 WSK--TPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIPSD-KPGTL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 149 teGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAE 228
Cdd:cd07105 92 --AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSPEDAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 229 KIV----ADDRVAAVSFTGSTEVGERVVKVGG--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKL 302
Cdd:cd07105 170 EVVealiAHPAVRKVNFTGSTRVGRIIAETAAkhLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTER 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 303 VLAERPVYGKLVEEVAKRLSSLRVGDprdptVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRR---LGPTYVQPTFV 379
Cdd:cd07105 250 IIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLAdesPSGTSMPPTIL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 380 eapaDRV-KDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIG 458
Cdd:cd07105 325 ----DNVtPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDEP 400
|
410 420 430
....*....|....*....|....*....|
1UXU_A 459 YYPFGGRKKSGVFREGIGYAVEAVTAYKTI 488
Cdd:cd07105 401 TLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
64-488 |
4.91e-86 |
|
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: 272.29 E-value: 4.91e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 64 FKRGRWSArdMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDyipgdwT 143
Cdd:cd07118 32 FDKGPWPR--MSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGD------S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 144 YDTL--ETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLN 221
Cdd:cd07118 104 YNNLgdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 222 LPGKEA-EKIVADDRVAAVSFTGSTEVGERVVKVGG--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCD 298
Cdd:cd07118 184 GYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAArnLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 299 AIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT---YVQ 375
Cdd:cd07118 264 SGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAaglFYQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 376 PTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMpRH 455
Cdd:cd07118 344 PTIF---TDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTF-LD 419
|
410 420 430
....*....|....*....|....*....|...
1UXU_A 456 GIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTI 488
Cdd:cd07118 420 GSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
25-491 |
1.69e-85 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 271.40 E-value: 1.69e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 25 GEW-GGSGQEIEVKSPIDLATIAKVISPSREEVERTL---DVLFkrGRWSaRDMPGtERLAVLRKAADIIERNLDVFAEV 100
Cdd:PRK13473 9 GELvAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVaaaDAAF--PEWS-QTTPK-ERAEALLKLADAIEENADEFARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 101 LVMNAGKPKSAAVG-EVKAAVDRLRL---AELDLK-KIGGDYIPGDWTYdtleteglVRREPLGVVAAITPFNYPLFDAV 175
Cdd:PRK13473 85 ESLNCGKPLHLALNdEIPAIVDVFRFfagAARCLEgKAAGEYLEGHTSM--------IRRDPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 176 NKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAgFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVK- 253
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIATGKHVLSa 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 254 -VGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDP 332
Cdd:PRK13473 236 aADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 333 TVDVGPLISPSAVDEMMAAIEDAVEKG-GRVLAGGRRLGPT--YVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDL 409
Cdd:PRK13473 316 DTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKgyYYEPTLL---AGARQDDEIVQREVFGPVVSVTPFDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 410 DQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDmprHG--IGYYPFGGRKKSGVFREGIGYAVEAVTAYKT 487
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT---HFmlVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRH 469
|
....
1UXU_A 488 IVFN 491
Cdd:PRK13473 470 VMVK 473
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
21-480 |
2.16e-85 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 271.95 E-value: 2.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 21 SYLAGEWGGS--GQEIEVKSPIDLATIAKVISPSREEVERTLD---VLFKRgrWSARdmPGTERLAVLRKAADIIERNLD 95
Cdd:PLN02278 27 GLIGGKWTDAydGKTFPVYNPATGEVIANVPCMGRAETNDAIAsahDAFPS--WSKL--TASERSKILRRWYDLIIANKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 96 VFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTydtlETEGLVRREPLGVVAAITPFNYPLFDAV 175
Cdd:PLN02278 103 DLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFP----DRRLLVLKQPVGVVGAITPWNFPLAMIT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 176 NKITYSFIYGNAVVVKPSISDPLPA-AMAVKALlDAGFPPDAialLNLPGKEAEKI----VADDRVAAVSFTGSTEVGER 250
Cdd:PLN02278 179 RKVGPALAAGCTVVVKPSELTPLTAlAAAELAL-QAGIPPGV---LNVVMGDAPEIgdalLASPKVRKITFTGSTAVGKK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 251 VVK--VGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGD 328
Cdd:PLN02278 255 LMAgaAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 329 PRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRR--LGPTYVQPTFVeapADRVKDMVLYKREVFAPVALAVEV 406
Cdd:PLN02278 335 GFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRhsLGGTFYEPTVL---GDVTEDMLIFREEVFGPVAPLTRF 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1UXU_A 407 KDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDmprhGI---GYYPFGGRKKSGVFREGIGYAVE 480
Cdd:PLN02278 412 KTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNE----GListEVAPFGGVKQSGLGREGSKYGID 484
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
22-490 |
2.80e-85 |
|
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: 270.60 E-value: 2.80e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 22 YLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDV---LFKRGRWsaRDMPGTERLAVLRKAADIIERNLDV 96
Cdd:cd07139 2 FIGGRWvaPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAarrAFDNGPW--PRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 97 FAEVLVMNAGKPKSA---AVGEVKAAVDR--LRLAEldlkkiggdyipgDWTYDTLET-----EGLVRREPLGVVAAITP 166
Cdd:cd07139 80 LARLWTAENGMPISWsrrAQGPGPAALLRyyAALAR-------------DFPFEERRPgsgggHVLVRREPVGVVAAIVP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 167 FNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTE 246
Cdd:cd07139 147 WNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 247 VGERVVKVGG--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSL 324
Cdd:cd07139 227 AGRRIAAVCGerLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 325 RVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGG-RRLGPT---YVQPTFVeapADRVKDMVLYKREVFAPV 400
Cdd:cd07139 307 KVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGgRPAGLDrgwFVEPTLF---ADVDNDMRIAQEEIFGPV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 401 ALAVEVKDLDQAIELANGRPYGLDAAVFGRDV---VKIRRAVRlleVGAIYINdMPRHGIGyYPFGGRKKSGVFREGIGY 477
Cdd:cd07139 384 LSVIPYDDEDDAVRIANDSDYGLSGSVWTADVergLAVARRIR---TGTVGVN-GFRLDFG-APFGGFKQSGIGREGGPE 458
|
490
....*....|...
1UXU_A 478 AVEAVTAYKTIVF 490
Cdd:cd07139 459 GLDAYLETKSIYL 471
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
38-491 |
1.20e-84 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 268.54 E-value: 1.20e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 38 SPIDLATIAKVISPSREEVERTLDVLfKRG--RWSArdMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVG- 114
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAA-RAAfeAWSA--MDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 115 EVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLeteglVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSI 194
Cdd:cd07115 80 DVPRAADTFRYYAGWADKIEGEVIPVRGPFLNY-----TVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 195 SDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVK--VGGVKQYVMELGGGDPAI 271
Cdd:cd07115 155 LTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAgAALVEHPDVDKITFTGSTAVGRKIMQgaAGNLKRVSLELGGKSANI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 272 VLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAA 351
Cdd:cd07115 235 VFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 352 IEDAVEKGGRVLAGGRRLGPT--YVQPTFVEA--PADRVKdmvlyKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAV 427
Cdd:cd07115 315 VDVGREEGARLLTGGKRPGARgfFVEPTIFAAvpPEMRIA-----QEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
1UXU_A 428 FGRDVVKIRRAVRLLEVGAIYINDMPRHGIGyYPFGGRKKSGVFREGIGYAVEAVTAYKTIVFN 491
Cdd:cd07115 390 WTRDLGRAHRVAAALKAGTVWINTYNRFDPG-SPFGGYKQSGFGREMGREALDEYTEVKSVWVN 452
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
36-490 |
3.87e-84 |
|
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: 267.18 E-value: 3.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 36 VKSPIDLATIAKVISPSREEVERTLDVLFKRGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGE 115
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 116 VKAAVDRLRLAELDLKKIGGDYIP--GDWTydtleteGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPS 193
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPlgPGYF-------VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 194 ISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEK-IVADDRVAAVSFTGSTEVGERVVKVGG--VKQYVMELGGGDPA 270
Cdd:cd07109 154 EDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAaLVAHPGVDHISFTGSVETGIAVMRAAAenVVPVTLELGGKSPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 271 IVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDpTVDVGPLISPSAVDEMMA 350
Cdd:cd07109 234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 351 AIEDAVEKGGRVLAGGRRLGPT-----YVQPTFVEapaDRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDA 425
Cdd:cd07109 313 FVARARARGARIVAGGRIAEGApaggyFVAPTLLD---DVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVA 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
1UXU_A 426 AVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVF 490
Cdd:cd07109 390 GVWTRDGDRALRVARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
69-469 |
1.75e-83 |
|
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: 265.31 E-value: 1.75e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 69 WSArdMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIP---GDWTYd 145
Cdd:cd07152 29 WAA--TPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQGEILPsapGRLSL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 146 tleteglVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALL-DAGFPPDAIALLNLPG 224
Cdd:cd07152 106 -------ARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARLFeEAGLPAGVLHVLPGGA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 225 KEAEKIVADDRVAAVSFTGSTEVGERVVKVGG--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKL 302
Cdd:cd07152 179 DAGEALVEDPNVAMISFTGSTAVGRKVGEAAGrhLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 303 VLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPTYvQPTFVeap 382
Cdd:cd07152 259 HLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTYDGLFY-RPTVL--- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 383 aDRVK-DMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVvkiRRAVRL---LEVGAIYINDMPRHGIG 458
Cdd:cd07152 335 -SGVKpGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDV---GRAMALadrLRTGMLHINDQTVNDEP 410
|
410
....*....|.
1UXU_A 459 YYPFGGRKKSG 469
Cdd:cd07152 411 HNPFGGMGASG 421
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
38-469 |
1.97e-83 |
|
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: 265.24 E-value: 1.97e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 38 SPIDLATIAKVISPSREEVERTLDVLFKRGRWSARdMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVK 117
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAA-LGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 118 AAVDRLRLAELDLKKIGGD-YIPGDWTYDTLETEglVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISD 196
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPrKVPTGLLMPNKKAT--VEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 197 PLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVaDDRVAAVSFTGSTEVGERVVKVGGVK--QYVMELGGGDPAIVLE 274
Cdd:cd07099 159 PLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERliPVVLELGGKDPMIVLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 275 DADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIED 354
Cdd:cd07099 238 DADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 355 AVEKGGRVLAGGRRL--GPTYVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDV 432
Cdd:cd07099 318 AVAKGAKALTGGARSngGGPFYEPTVL---TDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430
....*....|....*....|....*....|....*...
1UXU_A 433 VKIRRAVRLLEVGAIYIND-MPRHGIGYYPFGGRKKSG 469
Cdd:cd07099 395 ARAEAIARRLEAGAVSINDvLLTAGIPALPFGGVKDSG 432
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
22-490 |
3.34e-83 |
|
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: 265.14 E-value: 3.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 22 YLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTldVLFKR---GRWSArdMPGTERLAVLRKAADIIERNLDV 96
Cdd:cd07138 2 YIDGAWvaPAGTETIDVINPATEEVIGTVPLGTAADVDRA--VAAARrafPAWSA--TSVEERAALLERIAEAYEARADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 97 FAEVLVMNAGKPKS-AAVGEVKAAVDRLRLAELDLKkiggdyipgdwTYDTLETEG--LVRREPLGVVAAITPFNYPLFD 173
Cdd:cd07138 78 LAQAITLEMGAPITlARAAQVGLGIGHLRAAADALK-----------DFEFEERRGnsLVVREPIGVCGLITPWNWPLNQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 174 AVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVV 252
Cdd:cd07138 147 IVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 253 KVGG--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPR 330
Cdd:cd07138 227 EAAAdtVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 331 DPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGrrLGPT-------YVQPT-FveapADRVKDMVLYKREVFAPVAL 402
Cdd:cd07138 307 DPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG--PGRPeglergyFVKPTvF----ADVTPDMTIAREEIFGPVLS 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 403 AVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHgiGYYPFGGRKKSGVFREGIGYAVEAV 482
Cdd:cd07138 381 IIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFN--PGAPFGGYKQSGNGREWGRYGLEEF 458
|
....*...
1UXU_A 483 TAYKTIVF 490
Cdd:cd07138 459 LEVKSIQG 466
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
20-488 |
1.25e-82 |
|
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: 263.99 E-value: 1.25e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 20 PSYLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLfKRGRWSARDMPGTERLAVLRKAADIIERNLDVF 97
Cdd:cd07085 2 KLFINGEWveSKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAA-KAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 98 AEVLVMNAGKPKSAAVGEVKAAVDRLRLA----ELDLkkigGDYIPGDWT-YDTLeteglVRREPLGVVAAITPFNYPLF 172
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFAcsipHLLK----GEYLENVARgIDTY-----SYRQPLGVVAGITPFNFPAM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 173 DAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVV 252
Cdd:cd07085 152 IPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 253 KVGGVK-QYVMELGGG-DPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPR 330
Cdd:cd07085 232 ERAAANgKRVQALGGAkNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 331 DPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT------YVQPTFVeapaDRVK-DMVLYKREVFAPVALA 403
Cdd:cd07085 312 DPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPgyengnFVGPTIL----DNVTpDMKIYKEEIFGPVLSI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 404 VEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN---DMPRhgiGYYPFGGRKKSgVFREGIGYAVE 480
Cdd:cd07085 388 VRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINvpiPVPL---AFFSFGGWKGS-FFGDLHFYGKD 463
|
490
....*....|.
1UXU_A 481 AVTAY---KTI 488
Cdd:cd07085 464 GVRFYtqtKTV 474
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
22-491 |
2.48e-82 |
|
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: 263.50 E-value: 2.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 22 YLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFK--RGRWSarDMPGTERLAVLRKAADIIERNLDVF 97
Cdd:cd07144 11 FINNEFvkSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKafESWWS--KVTGEERGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 98 AEVLVMNAGKPK-SAAVGEVKAAVDRLRLAELDLKKIGGDYIPgdwtyDTLETEGLVRREPLGVVAAITPFNYPLFDAVN 176
Cdd:cd07144 89 AAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIP-----TSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 177 KITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVAD-DRVAAVSFTGSTEVGERVVKVG 255
Cdd:cd07144 164 KLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEhPDVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 256 G--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVE---EVAKRLSslRVGDPR 330
Cdd:cd07144 244 AqnLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEkfvEHVKQNY--KVGSPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 331 DPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT-----YVQPTFVeapADRVKDMVLYKREVFAPVALAVE 405
Cdd:cd07144 322 DDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGlgkgyFIPPTIF---TDVPQDMRIVKEEIFGPVVVISK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 406 VKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGyYPFGGRKKSGVFREGIGYAVEAVTAY 485
Cdd:cd07144 399 FKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVG-VPFGGFKMSGIGRELGEYGLETYTQT 477
|
....*.
1UXU_A 486 KTIVFN 491
Cdd:cd07144 478 KAVHIN 483
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
48-469 |
1.12e-81 |
|
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: 261.08 E-value: 1.12e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 48 VISPSREEVERTLDVLFKRGR-WSARDMpgTERLAVLRKAADIIERNLDVFAEVLVMNAGKPK-SAAVGEVKAAVDRLRl 125
Cdd:cd07098 12 VPADTPEDVDEAIAAARAAQReWAKTSF--AERRKVLRSLLKYILENQEEICRVACRDTGKTMvDASLGEILVTCEKIR- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 126 aeldlkkiggdyipgdWTYD----TLETE------------GLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVV 189
Cdd:cd07098 89 ----------------WTLKhgekALRPEsrpggllmfykrARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 190 VKPS----ISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVVKVGG--VKQYVME 263
Cdd:cd07098 153 VKVSeqvaWSSGFFLSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAesLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 264 LGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPS 343
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 344 AVDEMMAAIEDAVEKGGRVLAGGRRL-GPTYVQ-----PTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELAN 417
Cdd:cd07098 313 RFDRLEELVADAVEKGARLLAGGKRYpHPEYPQghyfpPTLL---VDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIAN 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
1UXU_A 418 GRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMprhGIGYY----PFGGRKKSG 469
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAINDF---GVNYYvqqlPFGGVKGSG 442
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
36-473 |
7.32e-81 |
|
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: 258.84 E-value: 7.32e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 36 VKSPIDLATIAKVISPSREEVERTLDVLfKRGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGE 115
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAA-RAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 116 VKAAVDRLRLAELDLKKIGGDYIP---GDWTYdtleteglVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKP 192
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKGETIPvggRNLHY--------TLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 193 SISDPLPAAMAVKaLLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVKVG--GVKQYVMELGGGDP 269
Cdd:cd07107 152 PEQAPLSALRLAE-LAREVLPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAaeGIKHVTLELGGKNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 270 AIVLEDADLDLAADKIARGI-YSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEM 348
Cdd:cd07107 231 LIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 349 MAAIEDAVEKGGRVLAGGRR-LGPT-----YVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYG 422
Cdd:cd07107 311 MHYIDSAKREGARLVTGGGRpEGPAleggfYVEPTVF---ADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
1UXU_A 423 LDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGyYPFGGRKKSGVFRE 473
Cdd:cd07107 388 LTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFLG-APFGGVKNSGIGRE 437
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
22-473 |
3.34e-79 |
|
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: 255.21 E-value: 3.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 22 YLAGEWGGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVL---FKrgRWsaRDMPGTERLAVLRKAADIIERNLDVFA 98
Cdd:cd07130 2 VYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAqeaFK--EW--RDVPAPKRGEIVRQIGDALRKKKEALG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 99 EVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGdwtydtlETEGLVRRE---PLGVVAAITPFNYPLfdAV 175
Cdd:cd07130 78 KLVSLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPS-------ERPGHRMMEqwnPLGVVGVITAFNFPV--AV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 176 ---NKiTYSFIYGNAVVVKPSISDPLPA----AMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVG 248
Cdd:cd07130 149 wgwNA-AIALVCGNVVVWKPSPTTPLTAiavtKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 249 ERV-VKVGG-VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRV 326
Cdd:cd07130 228 RQVgQAVAArFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 327 GDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRL--GPTYVQPTFVEAPadrvKDMVLYKREVFAPVALAV 404
Cdd:cd07130 308 GDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIdgPGNYVEPTIVEGL----SDAPIVKEETFAPILYVL 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1UXU_A 405 EVKDLDQAIELANGRPYGLDAAVFGRDvvkIRRAVRLL-----EVGAIYINdMPRHG--IGyYPFGGRKKSGVFRE 473
Cdd:cd07130 384 KFDTLEEAIAWNNEVPQGLSSSIFTTD---LRNAFRWLgpkgsDCGIVNVN-IGTSGaeIG-GAFGGEKETGGGRE 454
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
18-491 |
1.40e-78 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 254.30 E-value: 1.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 18 VYPSYLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFKRGRWSARdMPGTERLAVLRKAADIIERNLD 95
Cdd:PLN00412 15 VYKYYADGEWrtSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAK-TPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 96 VFAEVLVMNAGKPKSAAVGEVKAAVDRLRL-AELDLKKIG-GDYIPGD-WTYDTLETEGLVRREPLGVVAAITPFNYPLF 172
Cdd:PLN00412 94 PIAECLVKEIAKPAKDAVTEVVRSGDLISYtAEEGVRILGeGKFLVSDsFPGNERNKYCLTSKIPLGVVLAIPPFNYPVN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 173 DAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDR-VAAVSFTGStEVGERV 251
Cdd:PLN00412 174 LAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPgVNCISFTGG-DTGIAI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 252 VKVGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRD 331
Cdd:PLN00412 253 SKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 332 pTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGpTYVQPTFVeapaDRVK-DMVLYKREVFAPVALAVEVKDLD 410
Cdd:PLN00412 333 -DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREG-NLIWPLLL----DNVRpDMRIAWEEPFGPVLPVIRINSVE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 411 QAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVF 490
Cdd:PLN00412 407 EGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKSTVI 486
|
.
1UXU_A 491 N 491
Cdd:PLN00412 487 N 487
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
19-492 |
1.58e-78 |
|
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: 253.42 E-value: 1.58e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 19 YPSYLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFK-RGRWSARDMpgTERLAVLRKAADIIERNLD 95
Cdd:cd07559 1 YDNFINGEWvaPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEaFKTWGKTSV--AERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 96 VFAEVLVMNAGKP-KSAAVGEVKAAVDRLR------------LAELDLkkiggdyipgdwtydtlETEGLVRREPLGVVA 162
Cdd:cd07559 79 LLAVAETLDNGKPiRETLAADIPLAIDHFRyfagviraqegsLSEIDE-----------------DTLSYHFHEPLGVVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 163 AITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLpAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVAD-DRVAAVSF 241
Cdd:cd07559 142 QIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPL-SILVLMELIGDLLPKGVVNVVTGFGSEAGKPLAShPRIAKLAF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 242 TGSTEVGERVVkvggvkQY--------VMELGGGDPAIVLEDA-----DLDLAADKIARGIYSYAGQRCDAIKLVLAERP 308
Cdd:cd07559 221 TGSTTVGRLIM------QYaaenlipvTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQES 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 309 VYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRR------LGPTYVQPTFVEAP 382
Cdd:cd07559 295 IYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERltlgglDKGYFYEPTLIKGG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 383 ADrvkDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN---DMPRHGigy 459
Cdd:cd07559 375 NN---DMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcyhQYPAHA--- 448
|
490 500 510
....*....|....*....|....*....|...
1UXU_A 460 yPFGGRKKSGVFREGIGYAVEAVTAYKTIVFNY 492
Cdd:cd07559 449 -PFGGYKKSGIGRETHKMMLDHYQQTKNILVSY 480
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
38-469 |
1.93e-78 |
|
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: 252.55 E-value: 1.93e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 38 SPIDLATIAKVISPSREEVERTLDVLFKRGR-WSARDMpgTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEV 116
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKgWRAVPL--EERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 117 KAAVDR----LRLAELDLKKIggdyipgdwtyDTLETEGL---VRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVV 189
Cdd:cd07102 80 RGMLERarymISIAEEALADI-----------RVPEKDGFeryIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 190 VKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVVKV--GGVKQYVMELGGG 267
Cdd:cd07102 149 LKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAaaGRFIKVGLELGGK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 268 DPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDE 347
Cdd:cd07102 229 DPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 348 MMAAIEDAVEKGGRVLAGGRRL-----GPTYVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYG 422
Cdd:cd07102 309 VRAQIADAIAKGARALIDGALFpedkaGGAYLAPTVL---TNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
1UXU_A 423 LDAAVFGRDVVKIRRAVRLLEVGAIYIN--DMPRHGIgyyPFGGRKKSG 469
Cdd:cd07102 386 LTASVWTKDIARAEALGEQLETGTVFMNrcDYLDPAL---AWTGVKDSG 431
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
30-489 |
1.98e-78 |
|
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: 253.42 E-value: 1.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 30 SGQEIEVKSPIDLATIAKVISPSREEVERTLDVL---FKRGR-WsaRDMPGTERLAVLRKAADIIERNLDVFAEVLVMNA 105
Cdd:cd07141 20 SGKTFPTINPATGEKICEVQEGDKADVDKAVKAAraaFKLGSpW--RTMDASERGRLLNKLADLIERDRAYLASLETLDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 106 GKPKS-AAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLeteglVRREPLGVVAAITPFNYPLFDAVNKITYSFIY 184
Cdd:cd07141 98 GKPFSkSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTY-----TRHEPVGVCGQIIPWNFPLLMAAWKLAPALAC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 185 GNAVVVKPSISDPLpAAMAVKALL-DAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVKVGG---VKQ 259
Cdd:cd07141 173 GNTVVLKPAEQTPL-TALYLASLIkEAGFPPGVVNVVPGYGPTAgAAISSHPDIDKVAFTGSTEVGKLIQQAAGksnLKR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 260 YVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPL 339
Cdd:cd07141 252 VTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 340 ISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT--YVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELAN 417
Cdd:cd07141 332 IDEEQFKKILELIESGKKEGAKLECGGKRHGDKgyFIQPTVF---SDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERAN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1UXU_A 418 GRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINdMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIV 489
Cdd:cd07141 409 NTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN-CYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
22-491 |
2.56e-78 |
|
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: 252.83 E-value: 2.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 22 YLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFK--RGRWsARDMPGTERLAVLRKAADIIERNLDVF 97
Cdd:cd07143 10 FINGEFvdSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAafETDW-GLKVSGSKRGRCLSKLADLMERNLDYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 98 AEVLVMNAGKP-KSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDwtydtLETEGLVRREPLGVVAAITPFNYPLFDAVN 176
Cdd:cd07143 89 ASIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETD-----IKKLTYTRHEPIGVCGQIIPWNFPLLMCAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 177 KITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVKVG 255
Cdd:cd07143 164 KIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 256 G---VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDP 332
Cdd:cd07143 244 AksnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 333 TVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT--YVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLD 410
Cdd:cd07143 324 DTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEgyFIEPTIF---TDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 411 QAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN--DMPRHGIgyyPFGGRKKSGVFREGIGYAVEAVTAYKTI 488
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcyNLLHHQV---PFGGYKQSGIGRELGEYALENYTQIKAV 477
|
...
1UXU_A 489 VFN 491
Cdd:cd07143 478 HIN 480
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
17-488 |
7.75e-78 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 251.72 E-value: 7.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 17 PVYPSYLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLfKRGR--WSArdMPGTERLAVLRKAADII-E 91
Cdd:PRK13252 5 PLQSLYIDGAYveATSGETFEVINPATGEVLATVQAATPADVEAAVASA-KQGQkiWAA--MTAMERSRILRRAVDILrE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 92 RNlDVFAEVLVMNAGKPKS-AAVGEVKAAVDRLR----LAEldlkKIGGDYIP---GDWTYdtleteglVRREPLGVVAA 163
Cdd:PRK13252 82 RN-DELAALETLDTGKPIQeTSVVDIVTGADVLEyyagLAP----ALEGEQIPlrgGSFVY--------TRREPLGVCAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 164 ITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTG 243
Cdd:PRK13252 149 IGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 244 STEVGERVVK--VGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRL 321
Cdd:PRK13252 229 GVPTGKKVMAaaAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 322 SSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGP------TYVQPT-FveapADRVKDMVLYKR 394
Cdd:PRK13252 309 ERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfangAFVAPTvF----TDCTDDMTIVRE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 395 EVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN-------DMprhgigyyPFGGRKK 467
Cdd:PRK13252 385 EIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINtwgespaEM--------PVGGYKQ 456
|
490 500
....*....|....*....|.
1UXU_A 468 SGVFREGIGYAVEAVTAYKTI 488
Cdd:PRK13252 457 SGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
36-473 |
9.15e-78 |
|
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: 250.73 E-value: 9.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 36 VKSPIDLATIAKVISPSREEVE---RTLDVLFKRGRwsarDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAA 112
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDaavRAARRAFPRWK----KTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 113 ---VGEVKAAVDRL-RLAElDLKKIGGDYIPgdwtydtLETEGL---VRREPLGVVAAITPFNYPLFDAVNKITYSFIYG 185
Cdd:cd07110 77 awdVDDVAGCFEYYaDLAE-QLDAKAERAVP-------LPSEDFkarVRREPVGVVGLITPWNFPLLMAAWKVAPALAAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 186 NAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVKVG--GVKQYVM 262
Cdd:cd07110 149 CTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAgAPLAAHPGIDKISFTGSTATGSQVMQAAaqDIKPVSL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 263 ELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISP 342
Cdd:cd07110 229 ELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 343 SAVDEMMAAIEDAVEKGGRVLAGGRR---LGPTY-VQPT-FVEAPadrvKDMVLYKREVFAPVALAVEVKDLDQAIELAN 417
Cdd:cd07110 309 AQYEKVLSFIARGKEEGARLLCGGRRpahLEKGYfIAPTvFADVP----TDSRIWREEIFGPVLCVRSFATEDEAIALAN 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
1UXU_A 418 GRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINdMPRHGIGYYPFGGRKKSGVFRE 473
Cdd:cd07110 385 DSEYGLAAAVISRDAERCDRVAEALEAGIVWIN-CSQPCFPQAPWGGYKRSGIGRE 439
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
52-488 |
1.17e-77 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 250.43 E-value: 1.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 52 SREEVERTLDVLFKRGRwSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLR------- 124
Cdd:PRK09406 21 TDDEVDAAIARAHARFR-DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRyyaehae 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 125 --LAE--LDLKKIGGdyipgdwtydtleTEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPA 200
Cdd:PRK09406 100 alLADepADAAAVGA-------------SRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 201 AMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVVKVGG--VKQYVMELGGGDPAIVLEDADL 278
Cdd:PRK09406 167 LYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGdeIKKTVLELGGSDPFIVMPSADL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 279 DLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEK 358
Cdd:PRK09406 247 DRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 359 GGRVLAGGRRL-GPT-YVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIR 436
Cdd:PRK09406 327 GATILCGGKRPdGPGwFYPPTVI---TDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQE 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
1UXU_A 437 RAVRLLEVGAIYINDMPrhgIGY--YPFGGRKKSGVFREGIGYAVEAVTAYKTI 488
Cdd:PRK09406 404 RFIDDLEAGQVFINGMT---VSYpeLPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
44-488 |
1.27e-76 |
|
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: 247.99 E-value: 1.27e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 44 TIAKVISPSREEVERTL---DVLFKRgrWSArdMPGTERLAVLRKAADII-ERNLDVfAEVLVMNAGKPKSAAVGEVKAA 119
Cdd:cd07090 9 VLATVHCAGAEDVDLAVksaKAAQKE--WSA--TSGMERGRILRKAADLLrERNDEI-ARLETIDNGKPIEEARVDIDSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 120 VDRLRLAELDLKKIGGDYIP---GDWTYdtleteglVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISD 196
Cdd:cd07090 84 ADCLEYYAGLAPTLSGEHVPlpgGSFAY--------TRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 197 PLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVVKV--GGVKQYVMELGGGDPAIVLE 274
Cdd:cd07090 156 PLTALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAaaKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 275 DADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIED 354
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 355 AVEKGGRVLAGGRRLGPT-------YVQPTFVEAPADrvkDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAV 427
Cdd:cd07090 316 AKQEGAKVLCGGERVVPEdglengfYVSPCVLTDCTD---DMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
1UXU_A 428 FGRDVVKIRRAVRLLEVGAIYINDMPRHGIGyYPFGGRKKSGVFREGIGYAVEAVTAYKTI 488
Cdd:cd07090 393 FTRDLQRAHRVIAQLQAGTCWINTYNISPVE-VPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
38-483 |
4.66e-76 |
|
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: 246.07 E-value: 4.66e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 38 SPIDLATIAKVISPSREEVERTldvlFKRGR-----WSARdmPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAA 112
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAA----FARARaaqraWAAR--PFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 113 VGEV--KAAVDR--LRLAELDLK---KIGGdyIPgdwtydtLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYG 185
Cdd:cd07101 76 FEEVldVAIVARyyARRAERLLKprrRRGA--IP-------VLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 186 NAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKE-AEKIVadDRVAAVSFTGSTEVGERVVKVGGVK--QYVM 262
Cdd:cd07101 147 NAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEvGGAIV--DNADYVMFTGSTATGRVVAERAGRRliGCSL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 263 ELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISP 342
Cdd:cd07101 225 ELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 343 SAVDEMMAAIEDAVEKGGRVLAGGRR---LGPTYVQPTFVEapaDRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGR 419
Cdd:cd07101 305 AQLDRVTAHVDDAVAKGATVLAGGRArpdLGPYFYEPTVLT---GVTEDMELFAEETFGPVVSIYRVADDDEAIELANDT 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 420 PYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYY--PFGGRKKSGVFR----EGIGYAVEAVT 483
Cdd:cd07101 382 DYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAAAWASIdaPMGGMKDSGLGRrhgaEGLLKYTETQT 451
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
30-489 |
3.52e-75 |
|
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: 244.71 E-value: 3.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 30 SGQEIEVKSPIDLATIAKVISPSREEVERTLDVL---FKRGRWSArdMPGTERLAVLRKAADIIERNLDVFAEVLVMNAG 106
Cdd:cd07142 17 SGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAArkaFDEGPWPR--MTGYERSRILLRFADLLEKHADELAALETWDNG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 107 KP-KSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYdtletEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYG 185
Cdd:cd07142 95 KPyEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPH-----HVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 186 NAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDR-VAAVSFTGSTEVGERVVKVGG---VKQYV 261
Cdd:cd07142 170 NTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMdVDKVAFTGSTEVGKIIMQLAAksnLKPVT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 262 MELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLIS 341
Cdd:cd07142 250 LELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 342 PSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT--YVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGR 419
Cdd:cd07142 330 KEQFEKILSYIEHGKEEGATLITGGDRIGSKgyYIQPTIF---SDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNS 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1UXU_A 420 PYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN--DMPRHGIgyyPFGGRKKSGVFREGIGYAVEAVTAYKTIV 489
Cdd:cd07142 407 KYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDVFDASI---PFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
23-470 |
1.29e-73 |
|
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: 241.72 E-value: 1.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 23 LAGEWGGSGQEIEVKSPIDL-ATIAKVISPSREEVERTLDVLFK-RGRWSArdMPGTERLAVLRKAADIIERNLDVFAEV 100
Cdd:cd07125 37 INGEETETGEGAPVIDPADHeRTIGEVSLADAEDVDAALAIAAAaFAGWSA--TPVEERAEILEKAADLLEANRGELIAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 101 LVMNAGKPKSAAVGEVKAAVDRLRL-AELDLKKIGGDYIPGDWTydtlETEGLvRREPLGVVAAITPFNYPLFDAVNKIT 179
Cdd:cd07125 115 AAAEAGKTLADADAEVREAIDFCRYyAAQARELFSDPELPGPTG----ELNGL-ELHGRGVFVCISPWNFPLAIFTGQIA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 180 YSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVKV---- 254
Cdd:cd07125 190 AALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAKLINRAlaer 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 255 -GGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPT 333
Cdd:cd07125 270 dGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 334 VDVGPLISPSAvDEMMAAIEDAVEKGGRVLAGGR--RLGPTYVQPTFVEAPADRVkdmvlYKREVFAPVaLAV---EVKD 408
Cdd:cd07125 350 TDVGPLIDKPA-GKLLRAHTELMRGEAWLIAPAPldDGNGYFVAPGIIEIVGIFD-----LTTEVFGPI-LHVirfKAED 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1UXU_A 409 LDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINdmpRHGIG----YYPFGGRKKSGV 470
Cdd:cd07125 423 LDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN---RNITGaivgRQPFGGWGLSGT 485
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
22-492 |
1.74e-73 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 240.42 E-value: 1.74e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 22 YLAGEWGGSGQE--IEVKSPIDLATIAKVISPSREEVERTLDVLFK--RGRWsaRDMPGTERLAVLRKAADIIERNLDVF 97
Cdd:cd07113 3 FIDGRPVAGQSEkrLDITNPATEQVIASVASATEADVDAAVASAWRafVSAW--AKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 98 AEVLVMNAGKPKSAAVG-EVKAAVDRLRLAELDLKKIGGDYIpgDWTYDTLETE---GLVRREPLGVVAAITPFNYPLFD 173
Cdd:cd07113 81 AQLETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETL--APSIPSMQGErytAFTRREPVGVVAGIVPWNFSVMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 174 AVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVVK 253
Cdd:cd07113 159 AVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 254 --VGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRD 331
Cdd:cd07113 239 qaASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 332 PTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT--YVQPTFVEAPAdrvKDMVLYKREVFAPVALAVEVKDL 409
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEgyFVQPTLVLARS---ADSRLMREETFGPVVSFVPYEDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 410 DQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINdmpRHGI--GYYPFGGRKKSGVFREGIGYAVEAVTAYKT 487
Cdd:cd07113 396 EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFldPAVPFGGMKQSGIGREFGSAFIDDYTELKS 472
|
....*
1UXU_A 488 IVFNY 492
Cdd:cd07113 473 VMIRY 477
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
19-469 |
7.48e-72 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 237.14 E-value: 7.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 19 YPSYLAGEWGGSGQEIEVKSPIDLA-TIAKVISPSREEVERTLDvlfkrGRWSA----RDMPGTERLAVLRKAADIIERN 93
Cdd:PRK03137 37 YPLIIGGERITTEDKIVSINPANKSeVVGRVSKATKELAEKAMQ-----AALEAfetwKKWSPEDRARILLRAAAIIRRR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 94 LDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRL---AELDLKKiGGDYIPGDWTYDTLeteglvRREPLGVVAAITPFNYP 170
Cdd:PRK03137 112 KHEFSAWLVKEAGKPWAEADADTAEAIDFLEYyarQMLKLAD-GKPVESRPGEHNRY------FYIPLGVGVVISPWNFP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 171 LFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVSFTGSTEVG- 248
Cdd:PRK03137 185 FAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEvGDYLVDHPKTRFITFTGSREVGl 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 249 ---ERVVKV--GGV--KQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRL 321
Cdd:PRK03137 265 riyERAAKVqpGQIwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 322 SSLRVGDPRDPTvDVGPLISPSAVDEMMAAIEDAvEKGGRVLAGGRRLGPT--YVQPTFVE--APADRvkdmvLYKREVF 397
Cdd:PRK03137 345 KELTVGNPEDNA-YMGPVINQASFDKIMSYIEIG-KEEGRLVLGGEGDDSKgyFIQPTIFAdvDPKAR-----IMQEEIF 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1UXU_A 398 APVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGI-GYYPFGGRKKSG 469
Cdd:PRK03137 418 GPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIvGYHPFGGFNMSG 490
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
28-475 |
2.80e-71 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 235.54 E-value: 2.80e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 28 GGSGQEIEVKSPIDLATIAKVISPSREEVERTldvlFKRGR-----WSARdmPGTERLAVLRKAADIIERNLDVFAEVLV 102
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAA----FARARaaqraWAAT--PVRERAAVLLRFHDLVLENREELLDLVQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 103 MNAGKPKSAAVGEVK--AAVDR--LRLAE--LDLKKIGGdYIPgdwtydtLETEGLVRREPLGVVAAITPFNYPLFDAVN 176
Cdd:PRK09407 102 LETGKARRHAFEEVLdvALTARyyARRAPklLAPRRRAG-ALP-------VLTKTTELRQPKGVVGVISPWNYPLTLAVS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 177 KITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKE-AEKIVadDRVAAVSFTGSTEVGeRVVKVG 255
Cdd:PRK09407 174 DAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVvGTALV--DNADYLMFTGSTATG-RVLAEQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 256 GVKQYV---MELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDP 332
Cdd:PRK09407 251 AGRRLIgfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 333 TVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRR---LGPTYVQPTFVEapaDRVKDMVLYKREVFAPVaLAVE-VKD 408
Cdd:PRK09407 331 SADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKArpdLGPLFYEPTVLT---GVTPDMELAREETFGPV-VSVYpVAD 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1UXU_A 409 LDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDmprhgiGY--------YPFGGRKKSGVFR----EGI 475
Cdd:PRK09407 407 VDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNE------GYaaawgsvdAPMGGMKDSGLGRrhgaEGL 479
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
19-491 |
7.32e-71 |
|
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: 233.50 E-value: 7.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 19 YPSYLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLfKRGRWSARDMPGTERLAVLRKAADIIERNLDV 96
Cdd:cd07117 1 YGLFINGEWvkGSSGETIDSYNPANGETLSEITDATDADVDRAVKAA-QEAFKTWRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 97 FAEVLVMNAGKP--KSAAVgEVKAAVDRLR-LAELdlkkIGGDyiPGDWTYDTLETEGLVRREPLGVVAAITPFNYPLFD 173
Cdd:cd07117 80 LAMVETLDNGKPirETRAV-DIPLAADHFRyFAGV----IRAE--EGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 174 AVNKITYSFIYGNAVVVKPSISDPLpAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVV 252
Cdd:cd07117 153 AAWKLAPALAAGNTVVIKPSSTTSL-SLLELAKIIQDVLPKGVVNIVTGKGSKSgEYLLNHPGLDKLAFTGSTEVGRDVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 253 KVGGVK--QYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPR 330
Cdd:cd07117 232 IAAAKKliPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 331 DPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRL------GPTYVQPTFVEAPADrvkDMVLYKREVFAPVALAV 404
Cdd:cd07117 312 DPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLtengldKGFFIEPTLIVNVTN---DMRVAQEEIFGPVATVI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 405 EVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN---DMPRHGigyyPFGGRKKSGVFREGIGYAVEA 481
Cdd:cd07117 389 KFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNtynQIPAGA----PFGGYKKSGIGRETHKSMLDA 464
|
490
....*....|
1UXU_A 482 VTAYKTIVFN 491
Cdd:cd07117 465 YTQMKNIYID 474
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
79-489 |
6.62e-68 |
|
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: 224.92 E-value: 6.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 79 RLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIpgDWTYDTLeteGLVRREPL 158
Cdd:cd07120 44 RARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARTEAGRMI--EPEPGSF---SLVLREPM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 159 GVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDA-GFPPDAIALLNLPGKE-AEKIVADDRV 236
Cdd:cd07120 119 GVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEgAAHLVASPDV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 237 AAVSFTGSTEVGERVVKVGG--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLV 314
Cdd:cd07120 199 DVISFTGSTATGRAIMAAAAptLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 315 EEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPTY-----VQPTFVEapaDRVKDM 389
Cdd:cd07120 279 DRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPVTEGLakgafLRPTLLE---VDDPDA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 390 VLYKREVFAPVaLAVEV-KDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDmprHGIGY--YPFGGRK 466
Cdd:cd07120 356 DIVQEEIFGPV-LTLETfDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND---WNKLFaeAEEGGYR 431
|
410 420
....*....|....*....|....
1UXU_A 467 KSGVFR-EGIGyAVEAVTAYKTIV 489
Cdd:cd07120 432 QSGLGRlHGVA-ALEDFIEYKHIY 454
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
36-489 |
1.99e-66 |
|
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: 221.08 E-value: 1.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 36 VKSPIDLATIAKVISPSREEVERTLDVLFKR-GRWsaRDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKP-KSAAV 113
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAfPEW--AATPARERGKLLARIADALEARSEELARLLALETGNAlRTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 114 GEVKAAVDRLRLAELDLKKIGGDYIPGDwtYDTLEtegLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPS 193
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELKGETLPFG--PDVLT---YTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 194 ISDPLpAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVGERVVKVGGVK--QYVMELGGGDPA 270
Cdd:cd07108 154 EDAPL-AVLLLAEILAQVLPAGVLNVITGYGEECgAALVDHPDVDKVTFTGSTEVGKIIYRAAADRliPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 271 IVLEDADLDLAADKIARGI-YSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMM 349
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 350 AAIEDAVE-KGGRVLAGGR-----RLGPTY-VQPT-FVEAPAdrvkDMVLYKREVFAPVALAVEVKDLDQAIELANGRPY 421
Cdd:cd07108 313 GYIDLGLStSGATVLRGGPlpgegPLADGFfVQPTiFSGVDN----EWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHY 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1UXU_A 422 GLDAAVFGRDVVKIRRAVRLLEVGAIYIND--MPRHGIGYypfGGRKKSGVFREgigYAVEAV----TAYKTIV 489
Cdd:cd07108 389 GLAAYVWTRDLGRALRAAHALEAGWVQVNQggGQQPGQSY---GGFKQSGLGRE---ASLEGMlehfTQKKTVN 456
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
21-480 |
4.54e-64 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 215.54 E-value: 4.54e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 21 SYLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLfKRGRWSARDMPGTERLAVLRKAADIIERNLDVFA 98
Cdd:PRK11241 13 ALINGEWldANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAA-NRALPAWRALTAKERANILRRWFNLMMEHQDDLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 99 EVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLetegLVRREPLGVVAAITPFNYPLFDAVNKI 178
Cdd:PRK11241 92 RLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRL----IVIKQPIGVTAAITPWNFPAAMITRKA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 179 TYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLN-LPGKEAEKIVADDRVAAVSFTGSTEVGERVVK--VG 255
Cdd:PRK11241 168 GPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTgSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEqcAK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 256 GVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVD 335
Cdd:PRK11241 248 DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 336 VGPLISPSAVDEMMAAIEDAVEKGGRVLAGGR--RLGPTYVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAI 413
Cdd:PRK11241 328 IGPLIDEKAVAKVEEHIADALEKGARVVCGGKahELGGNFFQPTIL---VDVPANAKVAKEETFGPLAPLFRFKDEADVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 414 ELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDmprhGI---GYYPFGGRKKSGVFREGIGYAVE 480
Cdd:PRK11241 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINT----GIisnEVAPFGGIKASGLGREGSKYGIE 470
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
16-473 |
3.01e-63 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 213.83 E-value: 3.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 16 VPVYPSYLAGEWGGS--GQEIEVKSPIDLATIAKVISPSREEVERTLDVL---FKRGR---WSArdMPGTERLAVLRKAA 87
Cdd:PLN02467 5 VPRRQLFIGGEWREPvlGKRIPVVNPATEETIGDIPAATAEDVDAAVEAArkaFKRNKgkdWAR--TTGAVRAKYLRAIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 88 DIIERNLDVFAEVLVMNAGKPKSAAVGE---VKAAVDRLR-LAE-LDLKKiggdYIPGDWTYDTLEteGLVRREPLGVVA 162
Cdd:PLN02467 83 AKITERKSELAKLETLDCGKPLDEAAWDmddVAGCFEYYAdLAEaLDAKQ----KAPVSLPMETFK--GYVLKEPLGVVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 163 AITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEA-EKIVADDRVAAVSF 241
Cdd:PLN02467 157 LITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAgAPLASHPGVDKIAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 242 TGSTEVGERVVKVGG--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAK 319
Cdd:PLN02467 237 TGSTATGRKIMTAAAqmVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 320 RLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT----YVQPTFveaPADRVKDMVLYKRE 395
Cdd:PLN02467 317 WAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLkkgfFIEPTI---ITDVTTSMQIWREE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1UXU_A 396 VFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN-DMPrhGIGYYPFGGRKKSGVFRE 473
Cdd:PLN02467 394 VFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINcSQP--CFCQAPWGGIKRSGFGRE 470
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
66-478 |
1.78e-61 |
|
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: 207.51 E-value: 1.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 66 RGRWSARDMpgTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYipgdwTYD 145
Cdd:cd07095 13 FPGWAALSL--EERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTGER-----ATP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 146 TLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGK 225
Cdd:cd07095 86 MAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 226 EAEKIVADDRVAAVSFTGSTEVGERVVKVGG---VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCD-AIK 301
Cdd:cd07095 166 TGEALAAHEGIDGLLFTGSAATGLLLHRQFAgrpGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTcARR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 302 LVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRL--GPTYVQPTFV 379
Cdd:cd07095 246 LIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLvaGTAFLSPGII 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 380 eapaDRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINdMPRHGI-G 458
Cdd:cd07095 326 ----DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWN-RPTTGAsS 400
|
410 420
....*....|....*....|
1UXU_A 459 YYPFGGRKKSGVFREGIGYA 478
Cdd:cd07095 401 TAPFGGVGLSGNHRPSAYYA 420
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
30-489 |
2.85e-61 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 209.66 E-value: 2.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 30 SGQEIEVKSPIDLATIAKVISPSREEVERTLDVL---FKRGRWSArdMPGTERLAVLRKAADIIERNLDVFAEVLVMNAG 106
Cdd:PLN02466 71 SGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAArkaFDEGPWPK--MTAYERSRILLRFADLLEKHNDELAALETWDNG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 107 KP-KSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTY--DTLEteglvrrEPLGVVAAITPFNYPLFDAVNKITYSFI 183
Cdd:PLN02466 149 KPyEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHhvQTLH-------EPIGVAGQIIPWNFPLLMFAWKVGPALA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 184 YGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDR-VAAVSFTGSTEVGERVVKVGG---VKQ 259
Cdd:PLN02466 222 CGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMdVDKLAFTGSTDTGKIVLELAAksnLKP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 260 YVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPL 339
Cdd:PLN02466 302 VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQ 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 340 ISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT--YVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELAN 417
Cdd:PLN02466 382 IDSEQFEKILRYIKSGVESGATLECGGDRFGSKgyYIQPTVF---SNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRAN 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1UXU_A 418 GRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN--DMPRHGIgyyPFGGRKKSGVFREGIGYAVEAVTAYKTIV 489
Cdd:PLN02466 459 NTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVFDAAI---PFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
22-488 |
2.40e-60 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 206.29 E-value: 2.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 22 YLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDV---LFKRGRWSaRDMPGtERLAVLRKAADIIERNLDV 96
Cdd:PRK09847 23 FINGEYtaAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAargVFERGDWS-LSSPA-KRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 97 FAEVLVMNAGKP-KSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDwtYDTLeteGLVRREPLGVVAAITPFNYPLFDAV 175
Cdd:PRK09847 101 LALLETLDTGKPiRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTS--SHEL---AMIVREPVGVIAAIVPWNFPLLLTC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 176 NKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVA-DDRVAAVSFTGSTEVGERVVKV 254
Cdd:PRK09847 176 WKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSrHNDIDAIAFTGSTRTGKQLLKD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 255 GG---VKQYVMELGGGDPAIVLEDA-DLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPR 330
Cdd:PRK09847 256 AGdsnMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 331 DPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPTYVQPT-FVEA-PADRVKdmvlyKREVFAPVALAVEVKD 408
Cdd:PRK09847 336 DPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIGPTiFVDVdPNASLS-----REEIFGPVLVVTRFTS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 409 LDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMpRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTI 488
Cdd:PRK09847 411 EEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNY-NDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
83-450 |
5.65e-60 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 202.66 E-value: 5.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 83 LRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLR-LAELdLKKIGGDYIPGDWTYDTLetegLVRREPLGVV 161
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDyMAEW-ARRYEGEIIQSDRPGENI----LLFKRALGVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 162 AAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVS 240
Cdd:PRK10090 76 TGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETvGQELAGNPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 241 FTGSTEVGERVVKVGG--VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVA 318
Cdd:PRK10090 156 MTGSVSAGEKIMAAAAknITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 319 KRLSSLRVGDPRD-PTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT--YVQPTFVeapADRVKDMVLYKRE 395
Cdd:PRK10090 236 EAMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKgyYYPPTLL---LDVRQEMSIMHEE 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
1UXU_A 396 VFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN 450
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
30-489 |
8.53e-60 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 204.67 E-value: 8.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 30 SGQEIEVKSPIDLATIAKVISPSREEVERTLDV---LFKRGRWSArdMPGTERLAVLRKAADIIERNLDVFAEVLVMNAG 106
Cdd:PLN02766 34 SGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAareAFDHGPWPR--MSGFERGRIMMKFADLIEEHIEELAALDTIDAG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 107 K-PKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGdwtydTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYG 185
Cdd:PLN02766 112 KlFALGKAVDIPAAAGLLRYYAGAADKIHGETLKM-----SRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 186 NAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDR-VAAVSFTGSTEVGERVVKVGG---VKQYV 261
Cdd:PLN02766 187 CTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMdVDKVSFTGSTEVGRKIMQAAAtsnLKQVS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 262 MELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLIS 341
Cdd:PLN02766 267 LELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 342 PSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT--YVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGR 419
Cdd:PLN02766 347 KQQFEKILSYIEHGKREGATLLTGGKPCGDKgyYIEPTIF---TDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNT 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1UXU_A 420 PYGLDAAVFGRDVVKIRRAVRLLEVGAIYINdmprhgiGYY------PFGGRKKSGVFREGIGYAVEAVTAYKTIV 489
Cdd:PLN02766 424 KYGLAAGIVTKDLDVANTVSRSIRAGTIWVN-------CYFafdpdcPFGGYKMSGFGRDQGMDALDKYLQVKSVV 492
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
19-474 |
6.08e-59 |
|
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: 201.91 E-value: 6.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 19 YPSYLAGEWGG--SGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFK-RGRWSARDMpgTERLAVLRKAADIIERNLD 95
Cdd:cd07116 1 YDNFIGGEWVApvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAaKEAWGKTSV--AERANILNKIADRMEANLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 96 VFAEVLVMNAGKP-KSAAVGEVKAAVDRLR------------LAELDLKKIGGDYipgdwtydtleteglvrREPLGVVA 162
Cdd:cd07116 79 MLAVAETWDNGKPvRETLAADIPLAIDHFRyfagciraqegsISEIDENTVAYHF-----------------HEPLGVVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 163 AITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAgFPPDAIALLNLPGKEAEK-IVADDRVAAVSF 241
Cdd:cd07116 142 QIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKpLASSKRIAKVAF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 242 TGSTEVGERVVkvggvkQY--------VMELGGGDPAIVLED--ADLDLAADKIARGIYSYA---GQRCDAIKLVLAERP 308
Cdd:cd07116 221 TGETTTGRLIM------QYaseniipvTLELGGKSPNIFFADvmDADDAFFDKALEGFVMFAlnqGEVCTCPSRALIQES 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 309 VYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRR------LGPTYVQPTFVEAP 382
Cdd:cd07116 295 IYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelgglLGGGYYVPTTFKGG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 383 adrvKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN---DMPRHGigy 459
Cdd:cd07116 375 ----NKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNcyhLYPAHA--- 447
|
490
....*....|....*
1UXU_A 460 yPFGGRKKSGVFREG 474
Cdd:cd07116 448 -AFGGYKQSGIGREN 461
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
28-469 |
7.51e-57 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 204.28 E-value: 7.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 28 GGSGQEIEVKSPIDLA-TIAKVISPSREEVERTLDVLFK-RGRWSARdmPGTERLAVLRKAADIIERNLDVFAEVLVMNA 105
Cdd:PRK11904 558 NGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAaFPAWSRT--PVEERAAILERAADLLEANRAELIALCVREA 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 106 GKPKSAAVGEVKAAVDRLR----LAELDLKKigGDYIPGDwtydTLETEGLvRREPLGVVAAITPFNYPLFDAVNKITYS 181
Cdd:PRK11904 636 GKTLQDAIAEVREAVDFCRyyaaQARRLFGA--PEKLPGP----TGESNEL-RLHGRGVFVCISPWNFPLAIFLGQVAAA 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 182 FIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVSFTGSTEVGERVVKV-----G 255
Cdd:PRK11904 709 LAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATvGAALTADPRIAGVAFTGSTETARIINRTlaardG 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 256 GVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVD 335
Cdd:PRK11904 789 PIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTD 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 336 VGPLISPSAVDEMMAAIEdAVEKGGRVLA----GGRRLGPTYVQPTFVEapADRVKDMvlyKREVFAPVaLAV---EVKD 408
Cdd:PRK11904 869 VGPVIDAEAKANLDAHIE-RMKREARLLAqlplPAGTENGHFVAPTAFE--IDSISQL---EREVFGPI-LHViryKASD 941
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
1UXU_A 409 LDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINdmpRHGIG----YYPFGGRKKSG 469
Cdd:PRK11904 942 LDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN---RNQIGavvgVQPFGGQGLSG 1003
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
19-469 |
1.61e-56 |
|
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: 195.88 E-value: 1.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 19 YPSYLAGEWGGSGQEIEVKSPIDLA-TIAKVISPSREEVERTLDVLFK-RGRWSarDMPGTERLAVLRKAADIIERNLDV 96
Cdd:cd07083 19 YPLVIGGEWVDTKERMVSVSPFAPSeVVGTTAKADKAEAEAALEAAWAaFKTWK--DWPQEDRARLLLKAADLLRRRRRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 97 FAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIggDYIPGDWTYDTLETEGLVRRePLGVVAAITPFNYPLFDAVN 176
Cdd:cd07083 97 LIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRL--RYPAVEVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIFTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 177 KITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVSFTGSTEVGERVVKV- 254
Cdd:cd07083 174 MIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEvGAYLTEHERIRGINFTGSLETGKKIYEAa 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 255 -------GGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVG 327
Cdd:cd07083 254 arlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 328 DPRDPTVDVGPLISPSAVDEMMAAIEDAvEKGGRVLAGGRRLGPT--YVQPTFVEAPADRVKDMvlyKREVFAPVALAVE 405
Cdd:cd07083 334 PPEENGTDLGPVIDAEQEAKVLSYIEHG-KNEGQLVLGGKRLEGEgyFVAPTVVEEVPPKARIA---QEEIFGPVLSVIR 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1UXU_A 406 VKDLD--QAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGI-GYYPFGGRKKSG 469
Cdd:cd07083 410 YKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALvGVQPFGGFKLSG 476
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
22-474 |
2.33e-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: 194.92 E-value: 2.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 22 YLAGEW--GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFKR-GRWSArdMPGTERLAVLRKAADIIERNLDVFA 98
Cdd:cd07111 25 FINGKWvkPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAfESWSA--LPGHVRARHLYRIARHIQKHQRLFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 99 EVLVMNAGKPksaaVGEVKAAVDRLRLAELdlkkiggdYIPGDWTyDTLETEgLVRREPLGVVAAITPFNYPLFDAVNKI 178
Cdd:cd07111 103 VLESLDNGKP----IRESRDCDIPLVARHF--------YHHAGWA-QLLDTE-LAGWKPVGVVGQIVPWNFPLLMLAWKI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 179 TYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGE--RVVKVGG 256
Cdd:cd07111 169 CPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRalRRATAGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 257 VKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDV 336
Cdd:cd07111 249 GKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 337 GPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRL---GPTYvQPTFVE--APADRVKdmvlyKREVFAPVALAVEVKDLDQ 411
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGADVFQPGADLpskGPFY-PPTLFTnvPPASRIA-----QEEIFGPVLVVLTFRTAKE 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
1UXU_A 412 AIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDmprHGI--GYYPFGGRKKSGVFREG 474
Cdd:cd07111 403 AVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING---HNLfdAAAGFGGYRESGFGREG 464
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
28-468 |
3.21e-56 |
|
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: 194.71 E-value: 3.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 28 GGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLfKRGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGK 107
Cdd:TIGR01722 12 GASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASA-RETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 108 PKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTydTLETEGLvrREPLGVVAAITPFNYPLFDAVNKITYSFIYGNA 187
Cdd:TIGR01722 91 THSDALGDVARGLEVVEHACGVNSLLKGETSTQVAT--RVDVYSI--RQPLGVCAGITPFNFPAMIPLWMFPIAIACGNT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 188 VVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVVKVGGV--KQYVMELG 265
Cdd:TIGR01722 167 FVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAhgKRVQALGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 266 GGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVyGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAV 345
Cdd:TIGR01722 247 AKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 346 DEMMAAIEDAVEKGGRVLAGGRRL------GPTYVQPTFVEapadRVK-DMVLYKREVFAPVALAVEVKDLDQAIELANG 418
Cdd:TIGR01722 326 DRVASLIAGGAAEGAEVLLDGRGYkvdgyeEGNWVGPTLLE----RVPpTMKAYQEEIFGPVLCVLEADTLEEAIALINA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
1UXU_A 419 RPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKS 468
Cdd:TIGR01722 402 SPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDS 451
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
30-492 |
1.59e-54 |
|
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: 190.40 E-value: 1.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 30 SGQEIEVKSPIDLATIAKVISPSREEVERTLDVL---FKRGRWsaRDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAG 106
Cdd:cd07140 19 GGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAkeaFENGEW--GKMNARDRGRLMYRLADLMEEHQEELATIESLDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 107 KPKSAAVG-EVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTlETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYG 185
Cdd:cd07140 97 AVYTLALKtHVGMSIQTFRYFAGWCDKIQGKTIPINQARPN-RNLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 186 NAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVAD-DRVAAVSFTGSTEVGERVVK---VGGVKQYV 261
Cdd:cd07140 176 NTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDhPDVRKLGFTGSTPIGKHIMKscaVSNLKKVS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 262 MELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLIS 341
Cdd:cd07140 256 LELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNH 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 342 PSAVDEMMAAIEDAVEKGGRVLAGGRRLGPT--YVQPTFVEAPADrvkDMVLYKREVFAPVALAVEVK--DLDQAIELAN 417
Cdd:cd07140 336 KAHLDKLVEYCERGVKEGATLVYGGKQVDRPgfFFEPTVFTDVED---HMFIAKEESFGPIMIISKFDdgDVDGVLQRAN 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1UXU_A 418 GRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGyYPFGGRKKSGvFREGIGYavEAVTAY---KTIVFNY 492
Cdd:cd07140 413 DTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVA-APFGGFKQSG-FGKDLGE--EALNEYlktKTVTIEY 486
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
38-473 |
8.19e-53 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 185.06 E-value: 8.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 38 SPIDLATIAKVISPSREEVERTLdVLFKRGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVK 117
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENAL-QLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 118 AAvdrlrlAELdlkkiggdyipGDWTYD----TLETE--------GLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYG 185
Cdd:PRK13968 92 KS------ANL-----------CDWYAEhgpaMLKAEptlvenqqAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 186 NAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVVKVGG--VKQYVME 263
Cdd:PRK13968 155 NGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGaaLKKCVLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 264 LGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPS 343
Cdd:PRK13968 235 LGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 344 AVDEMMAAIEDAVEKGGRVLAGGRRLG--PTYVQPTFVeapADRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPY 421
Cdd:PRK13968 315 LRDELHHQVEATLAEGARLLLGGEKIAgaGNYYAPTVL---ANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEF 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
1UXU_A 422 GLDAAVFGRDVVKIRRAVRLLEVGAIYINdmprhgiGY------YPFGGRKKSGVFRE 473
Cdd:PRK13968 392 GLSATIFTTDETQARQMAARLECGGVFIN-------GYcasdarVAFGGVKKSGFGRE 442
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
23-469 |
1.33e-52 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 192.08 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 23 LAGEwGGSGQEIEVKSPIDLA-TIAKVISPSREEVERTLDVL---FKRgrWSARdmPGTERLAVLRKAADIIERNLDVFA 98
Cdd:COG4230 562 IAGE-AASGEARPVRNPADHSdVVGTVVEATAADVEAALAAAqaaFPA--WSAT--PVEERAAILERAADLLEAHRAELM 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 99 EVLVMNAGKPKSAAVGEVKAAVDRLRlaeldlkkiggdyipgdwtYDTLETEGL----VRREPLGVVAAITPFNYPL--F 172
Cdd:COG4230 637 ALLVREAGKTLPDAIAEVREAVDFCR-------------------YYAAQARRLfaapTVLRGRGVFVCISPWNFPLaiF 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 173 daVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALlnLPGKEAE---KIVADDRVAAVSFTGSTEVGE 249
Cdd:COG4230 698 --TGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQL--LPGDGETvgaALVADPRIAGVAFTGSTETAR 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 250 RV-----VKVGGVKQYVMELGGGDPAIVledadlD-------LAADKIARGIYSyAGQRCDAIKLVLaerpvygkLVEEV 317
Cdd:COG4230 774 LInrtlaARDGPIVPLIAETGGQNAMIV------DssalpeqVVDDVLASAFDS-AGQRCSALRVLC--------VQEDI 838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 318 AKRL--------SSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRV----LAGGRRLGpTYVQPTFVEapADR 385
Cdd:COG4230 839 ADRVlemlkgamAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhqlpLPEECANG-TFVAPTLIE--IDS 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 386 VKDMvlyKREVFAPVaLAV---EVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN-DMprHG--IGY 459
Cdd:COG4230 916 ISDL---EREVFGPV-LHVvryKADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNrNI--IGavVGV 989
|
490
....*....|
1UXU_A 460 YPFGGRKKSG 469
Cdd:COG4230 990 QPFGGEGLSG 999
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
30-469 |
5.08e-52 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 190.46 E-value: 5.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 30 SGQEIEVKSPID-LATIAKVISPSREEVERTLDVLFKRGR-WSARdmPGTERLAVLRKAADIIERNLDVFAEVLVMNAGK 107
Cdd:PRK11905 565 DGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPeWSAT--PAAERAAILERAADLMEAHMPELFALAVREAGK 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 108 PKSAAVGEVKAAVDRLRlaeldlkkiggdyipgdwtYDTLETEGLV---RREPLGVVAAITPFNYPLFDAVNKITYSFIY 184
Cdd:PRK11905 643 TLANAIAEVREAVDFLR-------------------YYAAQARRLLngpGHKPLGPVVCISPWNFPLAIFTGQIAAALVA 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 185 GNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALlnLPGKEAE---KIVADDRVAAVSFTGSTEVGERVVKV-----GG 256
Cdd:PRK11905 704 GNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQL--LPGDGRTvgaALVADPRIAGVMFTGSTEVARLIQRTlakrsGP 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 257 VKQYVMELGGGDPAIVLEDAdldLA----ADKIARGIYSyAGQRCDAIKlVLAerpvygkLVEEVAKR--------LSSL 324
Cdd:PRK11905 782 PVPLIAETGGQNAMIVDSSA---LPeqvvADVIASAFDS-AGQRCSALR-VLC-------LQEDVADRvltmlkgaMDEL 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 325 RVGDPRDPTVDVGPLISPSAVDEMMAAIEdAVEKGGRVL----AGGRRLGPTYVQPTFVEapadrVKDMVLYKREVFAPV 400
Cdd:PRK11905 850 RIGDPWRLSTDVGPVIDAEAQANIEAHIE-AMRAAGRLVhqlpLPAETEKGTFVAPTLIE-----IDSISDLEREVFGPV 923
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1UXU_A 401 aLAV---EVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINdmpRHGI----GYYPFGGRKKSG 469
Cdd:PRK11905 924 -LHVvrfKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN---RNIIgavvGVQPFGGEGLSG 995
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
69-469 |
1.45e-50 |
|
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: 180.11 E-value: 1.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 69 WSArdMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRlaeldlkkiggdYIPGDwTYDTLE 148
Cdd:TIGR01238 90 WNA--TPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCR------------YYAKQ-VRDVLG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 149 TEGLvrrEPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALlnLPGKEAE 228
Cdd:TIGR01238 155 EFSV---ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQL--LPGRGAD 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 229 ---KIVADDRVAAVSFTGSTEVGERVVKVGGVKQ-----YVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAI 300
Cdd:TIGR01238 230 vgaALTSDPRIAGVAFTGSTEVAQLINQTLAQREdapvpLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSAL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 301 KLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPTYVQPTFVE 380
Cdd:TIGR01238 310 RVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACQHGTFVA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 381 APADRVKDMVLYKREVFAPVALAVEVK--DLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN-DMPRHGI 457
Cdd:TIGR01238 390 PTLFELDDIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNrNQVGAVV 469
|
410
....*....|..
1UXU_A 458 GYYPFGGRKKSG 469
Cdd:TIGR01238 470 GVQPFGGQGLSG 481
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
31-469 |
3.81e-49 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 182.10 E-value: 3.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 31 GQEIEVKSPIDLATI-AKVISPSREEVERTLDVLFKRGR-WSARdmPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKP 108
Cdd:PRK11809 658 GEMSPVINPADPRDIvGYVREATPAEVEQALESAVNAAPiWFAT--PPAERAAILERAADLMEAQMQTLMGLLVREAGKT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 109 KSAAVGEVKAAVDRLRLAeldlkkigGDYIPGDWTYDTleteglvrREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAV 188
Cdd:PRK11809 736 FSNAIAEVREAVDFLRYY--------AGQVRDDFDNDT--------HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSV 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 189 VVKPSISDPLPAAMAVKALLDAGFPPDAIALlnLPGKeAEKI----VADDRVAAVSFTGSTEVG--------ERVVKVGG 256
Cdd:PRK11809 800 LAKPAEQTPLIAAQAVRILLEAGVPAGVVQL--LPGR-GETVgaalVADARVRGVMFTGSTEVArllqrnlaGRLDPQGR 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 257 VKQYVMELGGGDPAIVLEDAdldLA----ADKIARGIYSyAGQRCDAIKLVLaerpvygkLVEEVAKR--------LSSL 324
Cdd:PRK11809 877 PIPLIAETGGQNAMIVDSSA---LTeqvvADVLASAFDS-AGQRCSALRVLC--------LQDDVADRtlkmlrgaMAEC 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 325 RVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVL------AGGRRLGpTYVQPTFVEapADRVKDMvlyKREVFA 398
Cdd:PRK11809 945 RMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFqaarenSEDWQSG-TFVPPTLIE--LDSFDEL---KREVFG 1018
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1UXU_A 399 PVALAVEVK--DLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIN-DMPRHGIGYYPFGGRKKSG 469
Cdd:PRK11809 1019 PVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrNMVGAVVGVQPFGGEGLSG 1092
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
21-473 |
7.09e-49 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 175.79 E-value: 7.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 21 SYLAGEWGGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFKRGR-WSArdMPGTERLAVLRKAADIIERNLDVFAE 99
Cdd:PLN02315 23 CYVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKiWMQ--VPAPKRGEIVRQIGDALRAKLDYLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 100 VLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLetegLVRREPLGVVAAITPFNYPLFDAVNKIT 179
Cdd:PLN02315 101 LVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMM----MEVWNPLGIVGVITAFNFPCAVLGWNAC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 180 YSFIYGNAVVVKPSISDPL-PAAMA--VKALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVSFTGSTEVGERVVKVG 255
Cdd:PLN02315 177 IALVCGNCVVWKGAPTTPLiTIAMTklVAEVLEKNNLPGAIFTSFCGGAEiGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 256 GVK--QYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPT 333
Cdd:PLN02315 257 NARfgKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 334 VDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGP--TYVQPTFVEAPADrvKDMVlyKREVFAPVALAVEVKDLDQ 411
Cdd:PLN02315 337 TLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESegNFVQPTIVEISPD--ADVV--KEELFGPVLYVMKFKTLEE 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1UXU_A 412 AIELANGRPYGLDAAVFGRDVVKIRRAVRLL--EVGAIYINdMPRHG--IGyYPFGGRKKSGVFRE 473
Cdd:PLN02315 413 AIEINNSVPQGLSSSIFTRNPETIFKWIGPLgsDCGIVNVN-IPTNGaeIG-GAFGGEKATGGGRE 476
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
2-469 |
1.76e-48 |
|
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: 174.70 E-value: 1.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 2 RAGLLEGVIKEKGGVPVYPSYLAGEWGGSGQEIEVKSPIDLA-TIAKVISPSREEVERTLDV-LFKRGRWSArdMPGTER 79
Cdd:cd07123 16 RAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAhVLATYHYADAALVEKAIEAaLEARKEWAR--MPFEDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 80 LAVLRKAADII--ERNLDVFAEVLVmnaGKPKSAAVGEVKAA---VDRLRLAELDLKKIGGD----YIPGDW---TYDTL 147
Cdd:cd07123 94 AAIFLKAADLLsgKYRYELNAATML---GQGKNVWQAEIDAAcelIDFLRFNVKYAEELYAQqplsSPAGVWnrlEYRPL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 148 EteglvrreplGVVAAITPFNyplFDAV--NKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGK 225
Cdd:cd07123 171 E----------GFVYAVSPFN---FTAIggNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 226 EAEKIVADDR-VAAVSFTGSTEVGERVVK-----VGGVKQY---VMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQR 296
Cdd:cd07123 238 VVGDTVLASPhLAGLHFTGSTPTFKSLWKqigenLDRYRTYpriVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 297 CDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGG-RVLAGGRRLGPT--Y 373
Cdd:cd07123 318 CSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEaEIIAGGKCDDSVgyF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 374 VQPTFVEAPADRVKDMvlyKREVFAPVaLAVEV---KDLDQAIELAN-GRPYGLDAAVFGRDVVKIRRAVRLLE--VGAI 447
Cdd:cd07123 398 VEPTVIETTDPKHKLM---TEEIFGPV-LTVYVypdSDFEETLELVDtTSPYALTGAIFAQDRKAIREATDALRnaAGNF 473
|
490 500
....*....|....*....|...
1UXU_A 448 YINDMPRHGI-GYYPFGGRKKSG 469
Cdd:cd07123 474 YINDKPTGAVvGQQPFGGARASG 496
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
79-469 |
4.36e-46 |
|
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: 166.16 E-value: 4.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 79 RLAVLRKAADIIERNLDVFAEVLVMNAGKPKS-AAVGEVKAAVDRLRLAELDLKK--------IGGDYIPGdwtydtlet 149
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAeAYLTEIAVVLGEIDHALKHLKKwmkprrvsVPLLLQPA--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 150 EGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPS-ISdplPAAMAVKA-LLDAGFPPDAIALLNLPGKEA 227
Cdd:cd07087 93 KAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSeLA---PATSALLAkLIPKYFDPEAVAVVEGGVEVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 228 EKIVADdRVAAVSFTGSTEVGeRVVKVGGVKQYV---MELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVL 304
Cdd:cd07087 170 TALLAE-PFDHIFFTGSPAVG-KIVMEAAAKHLTpvtLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 305 AERPVYGKLVEEVAKRLSSLRVGDPRDPTvDVGPLISPSAVDEMMAAIEDA-VEKGGRVLAGGRrlgptYVQPTFVEAPA 383
Cdd:cd07087 248 VHESIKDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLLDDGkVVIGGQVDKEER-----YIAPTILDDVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 384 DrvkDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRH-GIGYYPF 462
Cdd:cd07087 322 P---DSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHaAIPNLPF 398
|
....*..
1UXU_A 463 GGRKKSG 469
Cdd:cd07087 399 GGVGNSG 405
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
12-468 |
1.81e-44 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 165.30 E-value: 1.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 12 EKGGVPVYPSYLAGEWGGSGQEIEVKSPIDlatiakVISPSREEVER----TLDVLFKRGRWSA-------RDMPGTERL 80
Cdd:PLN02419 103 EQSTQPQMPPRVPNLIGGSFVESQSSSFID------VINPATQEVVSkvplTTNEEFKAAVSAAkqafplwRNTPITTRQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 81 AVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLR----LAELDLkkigGDYIPGdwTYDTLETEGLvrRE 156
Cdd:PLN02419 177 RVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEhacgMATLQM----GEYLPN--VSNGVDTYSI--RE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 157 PLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRV 236
Cdd:PLN02419 249 PLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDI 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 237 AAVSFTGSTEVGERVVKVGGVKQYVME--LGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVL---AERPVYG 311
Cdd:PLN02419 329 RAVSFVGSNTAGMHIYARAAAKGKRIQsnMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVfvgDAKSWED 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 312 KLVEevakRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRL-GPTYVQPTFVEAP--ADRVKD 388
Cdd:PLN02419 409 KLVE----RAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvVPGYEKGNFIGPTilSGVTPD 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 389 MVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKS 468
Cdd:PLN02419 485 MECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKAS 564
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
79-469 |
1.13e-41 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 155.57 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 79 RLAVLRKAADIIERNLDVFAEVLVMNAGKP----KSAAVGEVKAAVDRLrLAELDlkkiggdyipgDWTYD-TLETEGL- 152
Cdd:PTZ00381 31 RKQQLRNLLRMLEENKQEFSEAVHKDLGRHpfetKMTEVLLTVAEIEHL-LKHLD-----------EYLKPeKVDTVGVf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 153 ------VRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPlPAAMAVKALLDAGFPPDAIALLNlPGKE 226
Cdd:PTZ00381 99 gpgksyIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSP-HTSKLMAKLLTKYLDPSYVRVIE-GGVE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 227 AEKIVADDRVAAVSFTGSTEVGERVVKvGGVKQYV---MELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLV 303
Cdd:PTZ00381 177 VTTELLKEPFDHIFFTGSPRVGKLVMQ-AAAENLTpctLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 304 LAERPVYGKLVEEVAKRLSSLRVGDPRDPTvDVGPLISPSAVDEMMAAIEDaveKGGRVLAGGR-RLGPTYVQPTFVEAP 382
Cdd:PTZ00381 256 LVHRSIKDKFIEALKEAIKEFFGEDPKKSE-DYSRIVNEFHTKRLAELIKD---HGGKVVYGGEvDIENKYVAPTIIVNP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 383 AdrvKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIG-YYP 461
Cdd:PTZ00381 332 D---LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNpNLP 408
|
....*...
1UXU_A 462 FGGRKKSG 469
Cdd:PTZ00381 409 FGGVGNSG 416
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
22-431 |
1.12e-40 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 152.80 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 22 YLAGEW-GGSGQEIEVKSPIDLATIAKVISPSREEVERTLdvlfKRGR-----WSARDMpgTERLAVLRKAADIIERNLD 95
Cdd:PRK09457 4 WINGDWiAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAV----RAARaafpaWARLSF--EERQAIVERFAALLEENKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 96 VFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYipgdwTYDTLETEGLVRREPLGVVAAITPFNYPLFDAV 175
Cdd:PRK09457 78 ELAEVIARETGKPLWEAATEVTAMINKIAISIQAYHERTGEK-----RSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 176 NKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVVKvg 255
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHR-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 256 gvkQY--------VMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYG-KLVEEVAKRLSSLRV 326
Cdd:PRK09457 231 ---QFagqpekilALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGdAFLARLVAVAKRLTV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 327 GDP-RDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRL--GPTYVQPTFVEAPAdrVKDMVlyKREVFAPVALA 403
Cdd:PRK09457 308 GRWdAEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLqaGTGLLTPGIIDVTG--VAELP--DEEYFGPLLQV 383
|
410 420
....*....|....*....|....*...
1UXU_A 404 VEVKDLDQAIELANGRPYGLDAAVFGRD 431
Cdd:PRK09457 384 VRYDDFDEAIRLANNTRFGLSAGLLSDD 411
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
65-470 |
1.16e-39 |
|
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: 148.91 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 65 KRGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAA-VGEVKAAVDRLRLAELDLKKiggdyipgdW- 142
Cdd:cd07134 8 QAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVdLTEILPVLSEINHAIKHLKK---------Wm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 143 -------TYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAgFPPD 215
Cdd:cd07134 79 kpkrvrtPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 216 AIALLnlpgkEAEKIVA----DDRVAAVSFTGSTEVGeRVVKVGGVKQY---VMELGGGDPAIVLEDADLDLAADKIARG 288
Cdd:cd07134 158 EVAVF-----EGDAEVAqallELPFDHIFFTGSPAVG-KIVMAAAAKHLasvTLELGGKSPTIVDETADLKKAAKKIAWG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 289 IYSYAGQRCDAIKLVLAERPVYGKLVE----EVAKRLSSlrvGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLA 364
Cdd:cd07134 232 KFLNAGQTCIAPDYVFVHESVKDAFVEhlkaEIEKFYGK---DAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 365 GG-RRLGPTYVQPTFVEapaDRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLE 443
Cdd:cd07134 309 GGqFDAAQRYIAPTVLT---NVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTS 385
|
410 420
....*....|....*....|....*...
1UXU_A 444 VGAIYINDMPRHGI-GYYPFGGRKKSGV 470
Cdd:cd07134 386 SGGVVVNDVVLHFLnPNLPFGGVNNSGI 413
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
39-489 |
1.35e-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: 148.52 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 39 PIDLATIAKVISPSREevertldvLFKRGRwsARDMPgtERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAV-GEVK 117
Cdd:cd07135 1 YTPLDEIDSIHSRLRA--------TFRSGK--TKDLE--YRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 118 AAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDP 197
Cdd:cd07135 69 GVKNDILHMLKNLKKWAKDEKVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 198 lPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVaDDRVAAVSFTGSTEVGeRVVKVGGVKQY---VMELGGGDPAIVLE 274
Cdd:cd07135 149 -HTAALLAELVPKYLDPDAFQVVQGGVPETTALL-EQKFDKIFYTGSGRVG-RIIAEAAAKHLtpvTLELGGKSPVIVTK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 275 DADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTvDVGPLISPSAVDEMMAAIED 354
Cdd:cd07135 226 NADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSLLDT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 355 AvekGGRVLAGGRRLGPT-YVQPTFV--EAPADrvkdmVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRD 431
Cdd:cd07135 305 T---KGKVVIGGEMDEATrFIPPTIVsdVSWDD-----SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDD 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
1UXU_A 432 VVKIRRAVRLLEVGAIYINDMPRH-GIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIV 489
Cdd:cd07135 377 KSEIDHILTRTRSGGVVINDTLIHvGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
153-469 |
1.70e-33 |
|
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: 131.45 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 153 VRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMaVKALLDAGFPPDAIALLNlpGkEAEkiVA 232
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSAL-LAELLAEYFDEDEVAVVT--G-GAD--VA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 233 ddrvAAVS--------FTGSTEVGERVVK--------VggvkqyVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQR 296
Cdd:cd07133 171 ----AAFSslpfdhllFTGSTAVGRHVMRaaaenltpV------TLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 297 CDAIKLVLA----ERPVYGKLVEEVAKRLSSLRVGDprdptvDVGPLISPSAVDEMMAAIEDAVEKGGRV---------L 363
Cdd:cd07133 241 CVAPDYVLVpedkLEEFVAAAKAAVAKMYPTLADNP------DYTSIINERHYARLQGLLEDARAKGARVielnpagedF 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 364 AGGRRLGPTYVqptfVEAPAdrvkDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLE 443
Cdd:cd07133 315 AATRKLPPTLV----LNVTD----DMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTH 386
|
330 340 350
....*....|....*....|....*....|
1UXU_A 444 VGAIYIND----MPRHGIgyyPFGGRKKSG 469
Cdd:cd07133 387 SGGVTINDtllhVAQDDL---PFGGVGASG 413
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
70-469 |
8.67e-33 |
|
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: 129.67 E-value: 8.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 70 SARDMPGTERLAVLRKA---ADIIE----RNLDVFAEVlVMNAGKPKSAAvGEVKAAVDRLRLAELDLKKIGGDYIPGDW 142
Cdd:cd07084 8 ADISTKAARRLALPKRAdflARIIQrlaaKSYDIAAGA-VLVTGKGWMFA-ENICGDQVQLRARAFVIYSYRIPHEPGNH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 143 TYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAG-FPPDAIALLN 221
Cdd:cd07084 86 LGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLIN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 222 LPGKEAEKIVADDRVAAVSFTGSTEVGERVVKVGGVKQYVMELGGGDPAIVLEDAD-LDLAADKIARGIYSYAGQRCDAI 300
Cdd:cd07084 166 GDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 301 KLVL-----AERPVYGKLVEEVAKRlsslrvgdprdptVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPTYVQ 375
Cdd:cd07084 246 SMLFvpenwSKTPLVEKLKALLARR-------------KLEDLLLGPVQTFTTLAMIAHMENLLGSVLLFSGKELKNHSI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 376 PTFV---EAPADRV------KDMVLYKREVFAPVALAVEVKDLDQAIELANGRP---------YGLDAAVFGRDVVKIRR 437
Cdd:cd07084 313 PSIYgacVASALFVpideilKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERmhgsltaaiYSNDPIFLQELIGNLWV 392
|
410 420 430
....*....|....*....|....*....|....
1UXU_A 438 AVRLLEVGAIYINDMPR--HGIGYYPFGGRKKSG 469
Cdd:cd07084 393 AGRTYAILRGRTGVAPNqnHGGGPAADPRGAGIG 426
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
20-439 |
9.89e-29 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 119.04 E-value: 9.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 20 PSYLAGEW-GGSGQEIEVKSPIDLATIAKViSPSREEVERTLDVLFKRGRWSARDMPGTERLAVLRKAADIIERNLDVFA 98
Cdd:PRK11903 6 ANYVAGRWqAGSGAGTPLFDPVTGEELVRV-SATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 99 EVLVMNAGKPKSAAVGEVKAAVDRLR-LAELDlKKIGGDYIPGDWTYDTLETEGLVRREPL-----GVVAAITPFNYPLF 172
Cdd:PRK11903 85 DIATANSGTTRNDSAVDIDGGIFTLGyYAKLG-AALGDARLLRDGEAVQLGKDPAFQGQHVlvptrGVALFINAFNFPAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 173 DAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAG-FPPDAIALLnlPGKEAEKIVADDRVAAVSFTGSTEVGERV 251
Cdd:PRK11903 164 GLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVV--CGSSAGLLDHLQPFDVVSFTGSAETAAVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 252 VKVGGVKQ----YVMELGGGDPAIVLEDAD-----LDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLS 322
Cdd:PRK11903 242 RSHPAVVQrsvrVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 323 SLRVGDPRDPTVDVGPLISPSAVDEMMAAIEdAVEKGGRVLAGGRRLGPT--------YVQPTFVEAP----ADRVKDMv 390
Cdd:PRK11903 322 KTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVdadpavaaCVGPTLLGASdpdaATAVHDV- 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
1UXU_A 391 lykrEVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAV 439
Cdd:PRK11903 400 ----EVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
70-490 |
1.81e-28 |
|
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: 117.13 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 70 SARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAA-VGEVKAAVDRLRLAELDLKK-IGGDYIPGDWTydTL 147
Cdd:cd07137 14 SGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCKLAIKELKKwMAPEKVKTPLT--TF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 148 ETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKAL---LDA-------GFPPDAI 217
Cdd:cd07137 92 PAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIpeyLDTkaikvieGGVPETT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 218 ALLNlpgKEAEKIVaddrvaavsFTGSTEVGeRVVKVGGVKQY---VMELGGGDPAIVLEDADLDLAADKIARGIY-SYA 293
Cdd:cd07137 172 ALLE---QKWDKIF---------FTGSPRVG-RIIMAAAAKHLtpvTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 294 GQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDpTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPTY 373
Cdd:cd07137 239 GQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKE-SKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 374 VQPTFVEAPAdrvKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMP 453
Cdd:cd07137 318 IEPTILLDPP---LDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTV 394
|
410 420 430
....*....|....*....|....*....|....*...
1UXU_A 454 RH-GIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVF 490
Cdd:cd07137 395 VQyAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAVLY 432
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
151-489 |
2.07e-28 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 117.22 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 151 GLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMaVKALLDAGFPPDAIALLNlPGKEAEKI 230
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKV-IAKIIEETFDEEYVAVVE-GGVEENQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 231 VADDRVAAVSFTGSTEVGervvKVggvkqyVM------------ELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCD 298
Cdd:cd07136 172 LLDQKFDYIFFTGSVRVG----KI------VMeaaakhltpvtlELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 299 AIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDpTVDVGPLISPSAVDEMMAAIEDA-VEKGGRVLAGGRrlgptYVQPT 377
Cdd:cd07136 242 APDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGLLDNGkIVFGGNTDRETL-----YIEPT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 378 FVEAPADrvkDMVLYKREVFAPVaLAV-EVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHG 456
Cdd:cd07136 316 ILDNVTW---DDPVMQEEIFGPI-LPVlTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHL 391
|
330 340 350
....*....|....*....|....*....|....*....
1UXU_A 457 IG-YYPFGGRKKSgvfreGIG-----YAVEAVTAYKTIV 489
Cdd:cd07136 392 ANpYLPFGGVGNS-----GMGsyhgkYSFDTFSHKKSIL 425
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
79-470 |
1.44e-26 |
|
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: 111.93 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 79 RLAVLRKAADIIERNLDVFAEVLVMNAGKPK-SAAVGEVKAAVDRLRLAELDLKKIGGD-YIPGDWTydTLETEGLVRRE 156
Cdd:cd07132 22 RIQQLEALLRMLEENEDEIVEALAKDLRKPKfEAVLSEILLVKNEIKYAISNLPEWMKPePVKKNLA--TLLDDVYIYKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 157 PLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKAL---LDagfpPDAIALLNLPGKEAEKIVaD 233
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyLD----KECYPVVLGGVEETTELL-K 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 234 DRVAAVSFTGSTEVGERVVKVGGvkQY----VMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPV 309
Cdd:cd07132 175 QRFDYIFYTGSTSVGKIVMQAAA--KHltpvTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 310 YGKLVEEVAKRLSSLRVGDPRDpTVDVGPLISPSAVDEMMAAIEdavekGGRVLAGGR-----RlgptYVQPTFVE--AP 382
Cdd:cd07132 253 QEKFVEALKKTLKEFYGEDPKE-SPDYGRIINDRHFQRLKKLLS-----GGKVAIGGQtdekeR----YIAPTVLTdvKP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 383 ADRVkdMvlyKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGY-YP 461
Cdd:cd07132 323 SDPV--M---QEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDsLP 397
|
....*....
1UXU_A 462 FGGRKKSGV 470
Cdd:cd07132 398 FGGVGNSGM 406
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
20-439 |
7.99e-24 |
|
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: 104.27 E-value: 7.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 20 PSYLAGEW-GGSGQEIEVKSPIDLATIAKVispSREEVERTLDVLFKR--GRWSARDMPGTERLAVLRKAADIIERNLDV 96
Cdd:cd07128 2 QSYVAGQWhAGTGDGRTLHDAVTGEVVARV---SSEGLDFAAAVAYARekGGPALRALTFHERAAMLKALAKYLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 97 FAEVLVMNAGKPKSAAV------GEVKAAVDRLRLaELDLKKIggdYIPGDWtyDTLETEG-------LVRREplGVVAA 163
Cdd:cd07128 79 LYALSAATGATRRDSWIdidggiGTLFAYASLGRR-ELPNAHF---LVEGDV--EPLSKDGtfvgqhiLTPRR--GVAVH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 164 ITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAG-FPPDAIALLNLPgkeaekiVAD--DRVA--- 237
Cdd:cd07128 151 INAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGS-------VGDllDHLGeqd 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 238 AVSFTGSTEVGER-----VVKVGGVKqYVMELGGGDPAIVLEDA-----DLDLAADKIARGIYSYAGQRCDAIKLVLAER 307
Cdd:cd07128 224 VVAFTGSAATAAKlrahpNIVARSIR-FNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFVPE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 308 PVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEdAVEKGGRVLAGGR---------RLGPTYVQPTF 378
Cdd:cd07128 303 ARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVA-TLLAEAEVVFGGPdrfevvgadAEKGAFFPPTL 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
1UXU_A 379 VEA----PADRVKDMvlykrEVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAV 439
Cdd:cd07128 382 LLCddpdAATAVHDV-----EAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
156-490 |
4.54e-22 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 98.96 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 156 EPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKaLLDAGFPPDAIALLNLPGKEAEKIVaDDR 235
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAK-LLEQYLDSSAVRVVEGAVTETTALL-EQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 236 VAAVSFTGSTEVGeRVVKVGGVKQY---VMELGGGDPAIVLEDADLDLAADKIARGIYS-YAGQRCDAIKLVLAERPVYG 311
Cdd:PLN02174 189 WDKIFYTGSSKIG-RVIMAAAAKHLtpvVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYAP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 312 KLVEEVAKRLSSLRVGDPRDpTVDVGPLISPSAVDEmMAAIEDAVEKGGRVLAGGRRLGPTY-VQPTFVeapADRVKDMV 390
Cdd:PLN02174 268 KVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDR-LSKLLDEKEVSDKIVYGGEKDRENLkIAPTIL---LDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 391 LYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRH-GIGYYPFGGRKKSG 469
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHlALHTLPFGGVGESG 422
|
330 340
....*....|....*....|.
1UXU_A 470 VFREGIGYAVEAVTAYKTIVF 490
Cdd:PLN02174 423 MGAYHGKFSFDAFSHKKAVLY 443
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
69-453 |
2.21e-20 |
|
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: 93.76 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 69 WSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKiggdyipGDWTYDTLE 148
Cdd:cd07129 13 ESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVRE-------GSWLDARID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 149 TEGLVR-----------REPLGVVAAITPFNYPL-FDAVNKITYSFI-YGNAVVVKPSISDP----LPAAMAVKALLDAG 211
Cdd:cd07129 86 PADPDRqplprpdlrrmLVPLGPVAVFGASNFPLaFSVAGGDTASALaAGCPVVVKAHPAHPgtseLVARAIRAALRATG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 212 FPPDAIALLNLPGKEA-EKIVADDRVAAVSFTGSTEVG----------ERVVKVGGvkqyvmELGGGDPAIVLEDAdLDL 280
Cdd:cd07129 166 LPAGVFSLLQGGGREVgVALVKHPAIKAVGFTGSRRGGralfdaaaarPEPIPFYA------ELGSVNPVFILPGA-LAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 281 AADKIARGIY-SY---AGQRCDAIKLVLAER-PVYGKLVEEVAKRLSSlrvgdprdptVDVGPLISP---SAVDEMMAAI 352
Cdd:cd07129 239 RGEAIAQGFVgSLtlgAGQFCTNPGLVLVPAgPAGDAFIAALAEALAA----------APAQTMLTPgiaEAYRQGVEAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 353 EDAveKGGRVLAGGRRLGPTY-VQPTFVEAPADRVKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFG-- 429
Cdd:cd07129 309 AAA--PGVRVLAGGAAAEGGNqAAPTLFKVDAAAFLADPALQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGee 386
|
410 420
....*....|....*....|....*.
1UXU_A 430 RDVVKIRRAVRLLE--VGAIYINDMP 453
Cdd:cd07129 387 DDLALARELLPVLErkAGRLLFNGWP 412
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
151-489 |
7.46e-20 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 92.10 E-value: 7.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 151 GLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKAL---LDagfpPDAIALLnLPGKEA 227
Cdd:PLN02203 102 AEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIpkyLD----SKAVKVI-EGGPAV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 228 EKIVADDRVAAVSFTGSTEVGeRVVKVGGVKQYV---MELGGGDPAIV---LEDADLDLAADKIARGIYSY-AGQRCDAI 300
Cdd:PLN02203 177 GEQLLQHKWDKIFFTGSPRVG-RIIMTAAAKHLTpvaLELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 301 KLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTvDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPTYVQPTFVE 380
Cdd:PLN02203 256 DYVLVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKKLFIEPTILL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 381 APAdrvKDMVLYKREVFAPVALAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYIND-MPRHGIGY 459
Cdd:PLN02203 335 NPP---LDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDaIIQYACDS 411
|
330 340 350
....*....|....*....|....*....|
1UXU_A 460 YPFGGRKKSGVFREGIGYAVEAVTAYKTIV 489
Cdd:PLN02203 412 LPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
21-437 |
7.65e-20 |
|
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: 92.17 E-value: 7.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 21 SYLAGEWGGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLF---KRGRWSARDMPgtERLA----VLRKAADIIERN 93
Cdd:cd07126 1 NLVAGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRqcpKSGLHNPLKNP--ERYLlygdVSHRVAHELRKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 94 L--DVFAEVLVMNAGKPKSAAVGEVKA--------AVDRLR-LAEldlkkigGDYIPGDwtYDTLETEGLvrREPLGVVA 162
Cdd:cd07126 79 EveDFFARLIQRVAPKSDAQALGEVVVtrkflenfAGDQVRfLAR-------SFNVPGD--HQGQQSSGY--RWPYGPVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 163 AITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFT 242
Cdd:cd07126 148 IITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 243 GSTEVGERVVKV--GGVKqyvMELGGGDPAIVLED-ADLDLAADKIARGIYSYAGQRCDAIKLVLAER-----PVYGKLV 314
Cdd:cd07126 228 GSSKVAERLALElhGKVK---LEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHEnwvqaGILDKLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 315 EEVAKR-LSSLrvgdprdptvDVGPLISPSAvdemmAAIEDAVEK-----GGRVLAGGRRLG-----PTY--VQPTFVEA 381
Cdd:cd07126 305 ALAEQRkLEDL----------TIGPVLTWTT-----ERILDHVDKllaipGAKVLFGGKPLTnhsipSIYgaYEPTAVFV 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
1UXU_A 382 PADRVKDMVLYK---REVFAPVALAVEVKD--LDQAIELANGRPYGLDAAVFGRDVVKIRR 437
Cdd:cd07126 370 PLEEIAIEENFElvtTEVFGPFQVVTEYKDeqLPLVLEALERMHAHLTAAVVSNDIRFLQE 430
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
157-446 |
1.10e-17 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 85.99 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 157 PLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVK----ALLDAGFPPDAIALL-NLPGKEAEKIV 231
Cdd:cd07127 193 PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPLAITVQvareVLAEAGFDPNLVTLAaDTPEEPIAQTL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 232 ADD-RVAAVSFTGSTEVGERVVKVGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLA----- 305
Cdd:cd07127 273 ATRpEVRIIDFTGSNAFGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgi 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 306 ----ERPVYGKLVEEVAKRLSSLrVGDPRDPTVDVGPLISPSAVdemmAAIEDAvEKGGRVLAGGRRLGptyvQPTFVEA 381
Cdd:cd07127 353 qtddGRKSFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTL----ARIAEA-RQLGEVLLASEAVA----HPEFPDA 422
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1UXU_A 382 padRVKDMVL----------YKREVFAPVALAVEVKDLDQAIELANG--RPYG-LDAAVFGRDVVKIRRAVRL-LEVGA 446
Cdd:cd07127 423 ---RVRTPLLlkldasdeaaYAEERFGPIAFVVATDSTDHSIELAREsvREHGaMTVGVYSTDPEVVERVQEAaLDAGV 498
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
108-366 |
5.79e-16 |
|
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: 79.57 E-value: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 108 PKSAAVGEVKAAVDRLRLAELDLKKIGGdYIPGDWTYDTLETEglVRREPLGVVAAITPFNYPLfDAVNKITYSFIYGNA 187
Cdd:cd07077 54 NWIAMMGCSESKLYKNIDTERGITASVG-HIQDVLLPDNGETY--VRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 188 VVVKPSISDPLPA---AMAVKALLDAGFPPDAIALLNLPGKE-AEKIVADDRVAAVSFTGSTEVGERVVKVGGVKQyVME 263
Cdd:cd07077 130 CIFRPHPSAPFTNralALLFQAADAAHGPKILVLYVPHPSDElAEELLSHPKIDLIVATGGRDAVDAAVKHSPHIP-VIG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 264 LGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDP---TVDVGPLI 340
Cdd:cd07077 209 FGAGNSPVVVDETADEERASGSVHDSKFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETkplSKETTPSF 288
|
250 260 270
....*....|....*....|....*....|....
1UXU_A 341 SPSAVDEMM--------AAIEDAVEKGGRVLAGG 366
Cdd:cd07077 289 DDEALESMTplecqfrvLDVISAVENAWMIIESG 322
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
72-416 |
1.34e-08 |
|
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: 56.86 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 72 RDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGkpksaaVGEVKAAVDRLRLAeldLKKIGG--DYIPGDWTYDTLET 149
Cdd:cd07121 21 RKCTLADREKIIEAIREALLSNAEELAEMAVEETG------MGRVEDKIAKNHLA---AEKTPGteDLTTTAWSGDNGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 150 egLVRREPLGVVAAITPFNYPLFDAVNKiTYSFIY-GNAVVVKPSISDPLPAAMAV----KALLDAGFPPDAIALLNLPG 224
Cdd:cd07121 92 --LVEYAPFGVIGAITPSTNPTETIINN-SISMLAaGNAVVFNPHPGAKKVSAYAVelinKAIAEAGGPDNLVVTVEEPT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 225 KE-AEKIVADDRVAAVSFTGSTEVGERVVKVGgvKQYVMELGGGDPAIVLEDADLDLAADKIARGIySYAGQ-RCDAIKL 302
Cdd:cd07121 169 IEtTNELMAHPDINLLVVTGGPAVVKAALSSG--KKAIGAGAGNPPVVVDETADIEKAARDIVQGA-SFDNNlPCIAEKE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 303 VLAERPVYGKLV-------------EEVAKRLSSLRVGDPrdptvdvGPLISPSAVDEMMAAIEDAVekGGRVLAGGRRL 369
Cdd:cd07121 246 VIAVDSVADYLIaamqrngayvlndEQAEQLLEVVLLTNK-------GATPNKKWVGKDASKILKAA--GIEVPADIRLI 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
1UXU_A 370 gptyvqptFVEAPADRVKDMVlykrEVFAPVALAVEVKDLDQAIELA 416
Cdd:cd07121 317 --------IVETDKDHPFVVE----EQMMPILPVVRVKNFDEAIELA 351
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
156-450 |
8.44e-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: 54.42 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 156 EPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSisdplPAA-----MAVKALLDA----GFPPDAIALLNLPGKE 226
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPH-----PRAkkcsiEAAKIMREAavaaGAPEGLIQWIEEPSIE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 227 A-EKIVADDRVAAVSFTGstevGERVVKVG--------GVkqyvmelGGGD-PAIVLEDADLDLAADKIargIYSYA--- 293
Cdd:cd07122 169 LtQELMKHPDVDLILATG----GPGMVKAAyssgkpaiGV-------GPGNvPAYIDETADIKRAVKDI---ILSKTfdn 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 294 GQRCDAIKLVLAERPVYGKLVEEVAKRlsslrvGdprdptvdvGPLISPSAVDEMMAAIE--------DAVEKGGRVLAg 365
Cdd:cd07122 235 GTICASEQSVIVDDEIYDEVRAELKRR------G---------AYFLNEEEKEKLEKALFddggtlnpDIVGKSAQKIA- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 366 gRRLGPTYVQPT-FVEAPADRVKDMVLYKREVFAPVALAVEVKDLDQAIELAN------GRpyGLDAAVFGRDVVKIRRA 438
Cdd:cd07122 299 -ELAGIEVPEDTkVLVAEETGVGPEEPLSREKLSPVLAFYRAEDFEEALEKARelleygGA--GHTAVIHSNDEEVIEEF 375
|
330
....*....|..
1UXU_A 439 VRLLEVGAIYIN 450
Cdd:cd07122 376 ALRMPVSRILVN 387
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
152-416 |
2.15e-07 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 53.37 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 152 LVRREPLGVVAAITPFNYPLFDAVNKiTYSFIY-GNAVVVKPSisdplPAAMAV---------KALLDAGFPPDAIALLN 221
Cdd:PRK15398 124 LIEYAPFGVIGAVTPSTNPTETIINN-AISMLAaGNSVVFSPH-----PGAKKVslraiellnEAIVAAGGPENLVVTVA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 222 LPGKE-AEKIVADDRVAAVSFTGSTEVGERVVKVGgvKQYVMELGGGDPAIVLEDADLDLAADKIARGIySYAGQ-RCDA 299
Cdd:PRK15398 198 EPTIEtAQRLMKHPGIALLVVTGGPAVVKAAMKSG--KKAIGAGAGNPPVVVDETADIEKAARDIVKGA-SFDNNlPCIA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 300 IKLVLAERPVYGKLVE------------EVAKRLSSLRVGDPRDPTVDvgpLISPSAVdEMMAAIEDAVEKGGRVLaggr 367
Cdd:PRK15398 275 EKEVIVVDSVADELMRlmekngavlltaEQAEKLQKVVLKNGGTVNKK---WVGKDAA-KILEAAGINVPKDTRLL---- 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
1UXU_A 368 rlgptyvqptFVEAPADRVKDMVlykrEVFAPVALAVEVKDLDQAIELA 416
Cdd:PRK15398 347 ----------IVETDANHPFVVT----ELMMPVLPVVRVKDVDEAIALA 381
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
138-416 |
5.84e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 51.88 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 138 IPGDWTYDTLeteglVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDA----GFP 213
Cdd:cd07081 81 LTGDENGGTL-----IIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 214 PDAIALLNLPGKE-AEKIVADDRVAAVSFTGstevGERVVKVG--GVKQYVMELGGGDPAIVLEDADLDLAADKIARGIY 290
Cdd:cd07081 156 ENLIGWIDNPSIElAQRLMKFPGIGLLLATG----GPAVVKAAysSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 291 SYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRD-------PTVDVGPLISPSAVDEMMAAIEDAVEKGGRVL 363
Cdd:cd07081 232 FDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQqvqpvilKNGDVNRDIVGQDAYKIAAAAGLKVPQETRIL 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
1UXU_A 364 aggrrlgptyvqptFVEAPAdrVKDMVLYKREVFAPVALAVEVKDLDQAIELA 416
Cdd:cd07081 312 --------------IGEVTS--LAEHEPFAHEKLSPVLAMYRAANFADADAKA 348
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
150-323 |
6.52e-06 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 48.21 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 150 EGLVRREPLGVVAAITPFNYPLFdAVNKITYSFIYGNAVVVKPSISDP--LPAAMAVKALLDAGFP-PDAIALLNLPG-- 224
Cdd:pfam05893 81 PSYEKAFPPGLVFHVLSGNVPLL-PVMSILMGLLVKNVNLLKVSSSDPftAAALLASFADLDPTHPlADSLSVVYWDGgs 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 225 -KEAEKIV--ADDRVAAVSFTGSTEVGErvvKVGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIK 301
Cdd:pfam05893 160 tQLEDLIVanADVVIAWGGEDAINAIRE---CLKPGKQWIDFGAKISFAVVDREAALDKAAERAADDICVFDQQACLSPQ 236
|
170 180
....*....|....*....|...
1UXU_A 302 LVLAERPvyGKL-VEEVAKRLSS 323
Cdd:pfam05893 237 TVFVESD--DKItPDEFAERLAA 257
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
54-237 |
3.04e-04 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 43.03 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 54 EEVERTLDVLfKRGRWSARDMPGTERLAVLRKAADII----ERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELD 129
Cdd:cd07080 5 PDLDALIEEL-RLNRRALAALPVEEIVDFLDRAGKRLldpdYPLRQQAERLLPTVTGYSEEMLREGLKRLMALFRRENLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UXU_A 130 LK---KIGGDYIPGDWtyDTLETEGLVRREPLGVVAAITPFNYPLFdAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKA 206
Cdd:cd07080 84 RIlerELGSPGILDEW--VPPGRGGYIRAQPRGLVVHIIAGNVPLL-PVWSIVRGLLVKNVNLLKMSSSDPLTATALLRS 160
|
170 180 190
....*....|....*....|....*....|....*....
1UXU_A 207 L--LDAGFP-PDAIALLNLPGKEA---EKIV--ADDRVA 237
Cdd:cd07080 161 LadVDPNHPlTDSISVVYWPGGDAeleERILasADAVVA 199
|
|
| |
