|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
1-461 |
0e+00 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 911.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 1 MNLSATHAVSVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGK 80
Cdd:PRK13968 2 TITPATHAISVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 81 PIAQARGEVAKSANLCDWYAEHGPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKH 160
Cdd:PRK13968 82 PINQARAEVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 161 APNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPF 240
Cdd:PRK13968 162 APNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 241 IVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQ 320
Cdd:PRK13968 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 321 QVTATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTD 400
Cdd:PRK13968 322 QVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTD 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1623529901 401 EAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTVWKDRR 461
Cdd:PRK13968 402 ETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVWKDRI 462
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
40-457 |
0e+00 |
|
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: 691.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 40 GYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAKSANLCDWYAEHGPAMLATEATLVENNQA 119
Cdd:cd07100 11 AFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADEPIETDAGKA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 120 VIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQII 199
Cdd:cd07100 91 YVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEAII 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 200 NDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGI 279
Cdd:cd07100 171 ADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 280 AEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMT 359
Cdd:cd07100 251 YDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPTVLTDVTPGMP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 360 GFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFG 439
Cdd:cd07100 331 AYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVKRSGYG 410
|
410
....*....|....*...
gi 1623529901 440 RELSHFGLHEFCNAQTVW 457
Cdd:cd07100 411 RELGRFGIREFVNIKTVW 428
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
10-457 |
0e+00 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 515.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEV 89
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 90 AKSANLCDWYAEHGPAMLATE---ATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMG 166
Cdd:PRK09406 85 LKCAKGFRYYAEHAEALLADEpadAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 167 SARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDA 246
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 247 DLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATL 326
Cdd:PRK09406 245 DLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 327 DEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQR 406
Cdd:PRK09406 325 AAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQER 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1623529901 407 FARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTVW 457
Cdd:PRK09406 405 FIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVW 455
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
10-457 |
1.26e-163 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 470.38 E-value: 1.26e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEV 89
Cdd:COG1012 25 VINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 90 AKSANLCDWYAEHGPAMLA-TEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSA 168
Cdd:COG1012 105 DRAADFLRYYAGEARRLYGeTIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 169 RLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDAD 247
Cdd:COG1012 185 LLLAELLEEAGLPAGVLNVVTGDGSEVGAaLVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 248 LDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATLD 327
Cdd:COG1012 265 LDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 328 EGATLLLGAEKIEGA-GNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQR 406
Cdd:COG1012 345 EGAELLTGGRRPDGEgGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARR 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1623529901 407 FARELECGGVFLNGYCAS-DARVAFGGVKKSGFGRELSHFGLHEFCNAQTVW 457
Cdd:COG1012 425 VARRLEAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKTVT 476
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
10-456 |
5.76e-162 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 465.47 E-value: 5.76e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEV 89
Cdd:pfam00171 11 VINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 90 AKSANLCDWYAEHGPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSAR 169
Cdd:pfam00171 91 DRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 170 LLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADL 248
Cdd:pfam00171 171 LLAELFEEAGLPAGVLNVVTGSGAEVGEaLVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 249 DEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATLDE 328
Cdd:pfam00171 251 DAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 329 GATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFA 408
Cdd:pfam00171 331 GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVA 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1623529901 409 RELECGGVFLNGYCASDARVA-FGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:pfam00171 411 RRLEAGMVWINDYTTGDADGLpFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
11-456 |
5.35e-147 |
|
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: 426.85 E-value: 5.35e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAEHG--------PAmlateatLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAP 162
Cdd:cd07103 82 YAASFLEWFAEEArriygrtiPS-------PAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 163 NVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFI 241
Cdd:cd07103 155 ETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEaLCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 242 VLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQ 321
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 322 VTATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDE 401
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1623529901 402 AQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07103 395 ARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
44-457 |
1.79e-144 |
|
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: 419.69 E-value: 1.79e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 44 WRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAKSANLCDWYAEHGPAMLATEATL-VENNQAVIE 122
Cdd:cd07078 14 WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSpDPGELAIVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 123 YRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IIND 201
Cdd:cd07078 94 REPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAaLASH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 202 DRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAE 281
Cdd:cd07078 174 PRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 282 AFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATLDEGATLLLGAEKIEG-AGNYYAPTVLCNVTAGMTG 360
Cdd:cd07078 254 EFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKGYFVPPTVLTDVDPDMPI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 361 FRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGVFLNGYCAS-DARVAFGGVKKSGFG 439
Cdd:cd07078 334 AQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGaEPSAPFGGVKQSGIG 413
|
410
....*....|....*...
gi 1623529901 440 RELSHFGLHEFCNAQTVW 457
Cdd:cd07078 414 REGGPYGLEEYTEPKTVT 431
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
41-458 |
1.75e-119 |
|
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: 356.07 E-value: 1.75e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 41 YRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAKSANLCdwyaeHGPAMLATEA------TLV 114
Cdd:cd07104 13 QKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAIL-----REAAGLPRRPegeilpSDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 115 ENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPN--VMGSArLLGEIFAAAGLPDGVFGWVNATN 192
Cdd:cd07104 88 PGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRtpVTGGL-LIAEIFEEAGLPKGVLNVVPGGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 193 DGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASK 271
Cdd:cd07104 167 SEIGDaLVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 272 RFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATLDEGATLLLGAekiEGAGNYYAPTVL 351
Cdd:cd07104 247 RILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG---TYEGLFYQPTVL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 352 CNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGVFLNGYCASD-ARVAF 430
Cdd:cd07104 324 SDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDePHVPF 403
|
410 420
....*....|....*....|....*...
gi 1623529901 431 GGVKKSGFGRELSHFGLHEFcnaqTVWK 458
Cdd:cd07104 404 GGVKASGGGRFGGPASLEEF----TEWQ 427
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
12-450 |
2.06e-117 |
|
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: 351.25 E-value: 2.06e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 12 NPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAK 91
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 92 SANLCDWYAehGPAMLATEATLVENNQAVIEY---RPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSA 168
Cdd:cd07150 85 TPELLRAAA--GECRRVRGETLPSDSPGTVSMsvrRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 169 RLLGEIFAAAGLPDGVFGWVNATNDGVS-QIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDAD 247
Cdd:cd07150 163 LKIAEIMEEAGLPKGVFNVVTGGGAEVGdELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 248 LDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATLD 327
Cdd:cd07150 243 LDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 328 EGATLLLGAekiEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRF 407
Cdd:cd07150 323 KGAKLLTGG---KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1623529901 408 ARELECGGVFLNGYCASD-ARVAFGGVKKSGFGRELSHFGLHEF 450
Cdd:cd07150 400 AERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEF 443
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
11-450 |
4.31e-117 |
|
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: 350.78 E-value: 4.31e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAEHGPAMLATEATLVENN-QAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSAR 169
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGfERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 170 LLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLD 249
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 250 EAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATLDEG 329
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 330 ATLLLGAEK---IEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQR 406
Cdd:cd07102 321 ARALIDGALfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1623529901 407 FARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEF 450
Cdd:cd07102 401 LGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQL 444
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
11-457 |
7.76e-116 |
|
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: 348.10 E-value: 7.76e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:cd07088 18 LNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAE-----HGPAMLATEatlvENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVM 165
Cdd:cd07088 98 FTADYIDYMAEwarriEGEIIPSDR----PNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 166 GSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLN 244
Cdd:cd07088 174 LNALEFAELVDEAGLPAGVLNIVTGRGSVVGDaLVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 245 DADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTA 324
Cdd:cd07088 254 DADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVER 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 325 TLDEGATLLLGAEKIEGA-GNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQ 403
Cdd:cd07088 334 AVEAGATLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNT 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1623529901 404 AQRFARELECGGVFLN--------GYCAsdarvafgGVKKSGFGRELSHFGLHEFCNAQTVW 457
Cdd:cd07088 414 AMRATNELEFGETYINrenfeamqGFHA--------GWKKSGLGGADGKHGLEEYLQTKVVY 467
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
11-457 |
9.88e-116 |
|
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: 346.82 E-value: 9.88e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCdwyaeHGPAMLATEATLVENN---QAVIEYRPLGAILAVMPWNFPV----WQVMrgavPILLAGNSYLLKHAPN 163
Cdd:cd07106 82 GAVAWL-----RYTASLDLPDEVIEDDdtrRVELRRKPLGVVAAIVPWNFPLllaaWKIA----PALLAGNTVVLKPSPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 164 VMGSARLLGEIFAAAgLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVL 243
Cdd:cd07106 153 TPLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 244 NDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPM---ARFDLRDELHQ 320
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVqnkMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 321 QVtatLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTD 400
Cdd:cd07106 312 DA---KAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSD 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1623529901 401 EAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTVW 457
Cdd:cd07106 389 LERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVIN 445
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
4-456 |
6.67e-115 |
|
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: 345.64 E-value: 6.67e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 4 SATHAVsVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIA 83
Cdd:cd07138 13 TETIDV-INPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPIT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 84 QARGevaksanlcdWYAEHGPAMLATEATLVEN-------NQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSY 156
Cdd:cd07138 92 LARA----------AQVGLGIGHLRAAADALKDfefeerrGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 157 LLK---HAPnvmGSARLLGEIFAAAGLPDGVFGWVNATNDGV-SQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVL 232
Cdd:cd07138 162 VLKpseVAP---LSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 233 ELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARF 312
Cdd:cd07138 239 ELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 313 DLRDELHQQVTATLDEGATLLLG-AEKIEG--AGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSE 389
Cdd:cd07138 319 AQFDRVQGYIQKGIEEGARLVAGgPGRPEGleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTP 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1623529901 390 FGLSATVYTTDEAQAQRFARELECGGVFLNGyCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07138 399 YGLAGYVWSADPERARAVARRLRAGQVHING-AAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
10-456 |
8.97e-115 |
|
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: 344.93 E-value: 8.97e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQAR-GE 88
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 89 VAKSANLCDWYAEhgpAMLATEATLVENNQAVIEY---RPLGAILAVMPWNFPV----WQVmrgaVPILLAGNSYLLKHA 161
Cdd:cd07093 81 IPRAAANFRFFAD---YILQLDGESYPQDGGALNYvlrQPVGVAGLITPWNLPLmlltWKI----APALAFGNTVVLKPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 162 PNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPF 240
Cdd:cd07093 154 EWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAaLVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 241 IVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQ 320
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 321 QVTATLDEGATLLLGAEKIE----GAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATV 396
Cdd:cd07093 314 YVELARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 397 YTTDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07093 394 WTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
12-441 |
1.34e-114 |
|
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: 344.19 E-value: 1.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 12 NPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAK 91
Cdd:cd07149 5 SPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 92 SANLCDWYAE-----HGpAMLATEATL-VENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVM 165
Cdd:cd07149 85 AIETLRLSAEeakrlAG-ETIPFDASPgGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 166 GSARLLGEIFAAAGLPDGVFGWVNATNDGV-SQIINDDRIAAVTVTGSVRAGKAIGAQAGaaLKKCVLELGGSDPFIVLN 244
Cdd:cd07149 164 LSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 245 DADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTA 324
Cdd:cd07149 242 DADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 325 TLDEGATLLLGAEKIegaGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQA 404
Cdd:cd07149 322 AVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1623529901 405 QRFARELECGGVFLNGycASDARV---AFGGVKKSGFGRE 441
Cdd:cd07149 399 LKAARELEVGGVMIND--SSTFRVdhmPYGGVKESGTGRE 436
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
11-450 |
8.41e-113 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 341.28 E-value: 8.41e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:PLN02278 45 YNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAEHG--------PAMLATEATLVENnqavieyRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAP 162
Cdd:PLN02278 125 YGASFLEYFAEEAkrvygdiiPSPFPDRRLLVLK-------QPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 163 NVMGSARLLGEIFAAAGLPDGVFGWVNATNDGV-SQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFI 241
Cdd:PLN02278 198 LTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 242 VLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQ 321
Cdd:PLN02278 278 VFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESH 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 322 VTATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDE 401
Cdd:PLN02278 358 VQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDL 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1623529901 402 AQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEF 450
Cdd:PLN02278 438 QRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
11-456 |
1.03e-111 |
|
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: 337.01 E-value: 1.03e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:cd07145 4 RNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAEH-----GPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVM 165
Cdd:cd07145 84 RTIRLFKLAAEEakvlrGETIPVDAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 166 GSARLLGEIFAAAGLPDGVFGWVNATNDGV-SQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLN 244
Cdd:cd07145 164 LTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 245 DADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTA 324
Cdd:cd07145 244 DADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVND 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 325 TLDEGATLLLGAEKIEGAgnYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQA 404
Cdd:cd07145 324 AVEKGGKILYGGKRDEGS--FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1623529901 405 QRFARELECGGVFLNGycASDAR---VAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07145 402 LKVARELEAGGVVIND--STRFRwdnLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
44-458 |
1.22e-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: 333.81 E-value: 1.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 44 WRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAKSANLCDWYAEHGPAMLATEATL-VENNQAVIE 122
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSpDPGGEAYVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 123 YRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IIND 201
Cdd:cd06534 90 REPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAaLLSH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 202 DRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAE 281
Cdd:cd06534 170 PRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 282 AFTRKFVdavaalkmgdprdeqnyvgpmarfdlrdelhqqvtatldegatlllgaekiegagnyyapTVLCNVTAGMTGF 361
Cdd:cd06534 250 EFVEKLV------------------------------------------------------------TVLVDVDPDMPIA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 362 RQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGVFLNGYCA-SDARVAFGGVKKSGFGR 440
Cdd:cd06534 270 QEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGVKNSGIGR 349
|
410
....*....|....*...
gi 1623529901 441 ELSHFGLHEFCNAQTVWK 458
Cdd:cd06534 350 EGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
11-456 |
1.23e-110 |
|
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: 334.19 E-value: 1.23e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAEHGPAMLATEAT----LVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLK---HAPn 163
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRKVptglLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKpseVTP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 164 vmGSARLLGEIFAAAGLPDGVFGWVnaTNDG-VSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIV 242
Cdd:cd07099 160 --LVGELLAEAWAAAGPPQGVLQVV--TGDGaTGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 243 LNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQV 322
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 323 TATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEA 402
Cdd:cd07099 316 DDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1623529901 403 QAQRFARELECGGVFLN----GYCASDArvAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07099 396 RAEAIARRLEAGAVSINdvllTAGIPAL--PFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
11-456 |
4.65e-110 |
|
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: 333.39 E-value: 4.65e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGY--RQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQAR-G 87
Cdd:cd07139 19 VSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRrA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 88 EVAKSANLCDWYAEHGPAMLATEA-TLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMG 166
Cdd:cd07139 99 QGPGPAALLRYYAALARDFPFEERrPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 167 SARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDA 246
Cdd:cd07139 179 DAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 247 DLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATL 326
Cdd:cd07139 259 DLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 327 DEGATLLLGAEKIEG--AGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQA 404
Cdd:cd07139 339 AEGARLVTGGGRPAGldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERG 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1623529901 405 QRFARELECGGVFLNGYcASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07139 419 LAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
4-456 |
3.74e-109 |
|
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: 331.14 E-value: 3.74e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 4 SATHAVSVNPT-TGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPI 82
Cdd:cd07097 12 GGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 83 AQARGEVAKSANLCDWYAEHGPAMLATEATLVENNQAVIEYR-PLGAILAVMPWNFPV----WQvmrgAVPILLAGNSYL 157
Cdd:cd07097 92 PEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTRePLGVVGLITPWNFPIaipaWK----IAPALAYGNTVV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 158 LKHAPNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGG 236
Cdd:cd07097 168 FKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQaLVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 237 SDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRD 316
Cdd:cd07097 248 KNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 317 ELHQQVTATLDEGATLLLGAEKIEGA--GNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSA 394
Cdd:cd07097 328 KDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1623529901 395 TVYTTDEAQAQRFARELECGGVFLNGYCAS-DARVAFGGVKKSGFG-RELSHFGLHEFCNAQTV 456
Cdd:cd07097 408 GIVTTSLKHATHFKRRVEAGVVMVNLPTAGvDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
13-456 |
2.54e-107 |
|
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: 325.83 E-value: 2.54e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 13 PTTGEVVSSLPWASEREVDAAIALAAAGYRQ--WRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDwYAEHGPAMLATEA--TLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSA 168
Cdd:cd07118 84 GAADLWR-YAASLARTLHGDSynNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 169 RLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDAD 247
Cdd:cd07118 163 LMLAELLIEAGLPAGVVNIVTGYGATVGQaMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 248 LDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATLD 327
Cdd:cd07118 243 LDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 328 EGATLLLGAEKIE-GAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQR 406
Cdd:cd07118 323 EGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALT 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1623529901 407 FARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07118 403 VARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
10-457 |
2.61e-107 |
|
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: 325.71 E-value: 2.61e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGY--RQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQAR- 86
Cdd:cd07112 6 TINPATGRVLAEVAACDAADVDRAVAAARRAFesGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 87 GEVAKSANLCDWYAEHGPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMG 166
Cdd:cd07112 86 VDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 167 SARLLGEIFAAAGLPDGVFGWVNATNDGVSQII---NDdrIAAVTVTGSVRAGKAIGAQAGAA-LKKCVLELGGSDPFIV 242
Cdd:cd07112 166 TALRLAELALEAGLPAGVLNVVPGFGHTAGEALglhMD--VDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKSPNIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 243 LNDA-DLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQ 321
Cdd:cd07112 244 FADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 322 VTATLDEGATLLLG--AEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTT 399
Cdd:cd07112 324 IESGKAEGARLVAGgkRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTS 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1623529901 400 DEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTVW 457
Cdd:cd07112 404 DLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTW 461
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
11-441 |
1.30e-106 |
|
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: 323.81 E-value: 1.30e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAE-----HGPAM-LATEATlVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNV 164
Cdd:cd07147 84 RAIDTFRIAAEeatriYGEVLpLDISAR-GEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 165 MGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAalKKCVLELGGSDPFIVLN 244
Cdd:cd07147 163 PLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIVDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 245 DADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTA 324
Cdd:cd07147 241 DADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 325 TLDEGATLLLGAEKiegAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQA 404
Cdd:cd07147 321 AVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKA 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1623529901 405 QRFARELECGGVFLNGycASDARV---AFGGVKKSGFGRE 441
Cdd:cd07147 398 LRAWDELEVGGVVIND--VPTFRVdhmPYGGVKDSGIGRE 435
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
11-456 |
3.96e-106 |
|
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: 322.66 E-value: 3.96e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQW-RQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARG-E 88
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAmQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 89 VAKSANLCDWYAEHGPAM-----LATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPN 163
Cdd:cd07089 82 VDGPIGHLRYFADLADSFpwefdLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 164 VMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDD-RIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIV 242
Cdd:cd07089 162 TPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 243 LNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQV 322
Cdd:cd07089 242 LDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 323 TATLDEGATLLLGAEKIEG--AGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTD 400
Cdd:cd07089 322 ARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSAD 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1623529901 401 EAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07089 402 VDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
10-457 |
1.46e-104 |
|
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: 318.73 E-value: 1.46e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQ--WRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARG 87
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 88 EVAKSAnlcDWYAEHGPAMLATEATLV----ENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLK---H 160
Cdd:cd07114 81 QVRYLA---EWYRYYAGLADKIEGAVIpvdkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKpseH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 161 APnvmGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDP 239
Cdd:cd07114 158 TP---ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEaLVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 240 FIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELH 319
Cdd:cd07114 235 NIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 320 QQVTATLDEGATLLLGAEKIEGA----GNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSAT 395
Cdd:cd07114 315 RYVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1623529901 396 VYTTDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTVW 457
Cdd:cd07114 395 IWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVW 456
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
11-450 |
3.10e-104 |
|
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: 318.09 E-value: 3.10e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:cd07151 15 LNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAEHGPAMLATE-ATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPN--VMGS 167
Cdd:cd07151 95 AAMAITREAATFPLRMEGRIlPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDtpITGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 168 ArLLGEIFAAAGLPDGVFGWVnaTNDGvSQIinDDRIAA------VTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFI 241
Cdd:cd07151 175 L-LLAKIFEEAGLPKGVLNVV--VGAG-SEI--GDAFVEhpvprlISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 242 VLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQ 321
Cdd:cd07151 249 VLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 322 VTATLDEGATLLLGAEKiegAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDE 401
Cdd:cd07151 329 IEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDL 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1623529901 402 AQAQRFARELECGGVFLNGYCASD-ARVAFGGVKKSGFGRELSHFGLHEF 450
Cdd:cd07151 406 ERGVQFARRIDAGMTHINDQPVNDePHVPFGGEKNSGLGRFNGEWALEEF 455
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
10-457 |
1.44e-102 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 314.29 E-value: 1.44e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTG-EVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGE 88
Cdd:cd07131 18 SRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 89 VAKSANLCDWYAEHGPAMLA-TEATLVENNQAVIEYRPLGAILAVMPWNFPV----WQVMrgavPILLAGNSYLLKHAPN 163
Cdd:cd07131 98 VQEAIDMAQYAAGEGRRLFGeTVPSELPNKDAMTRRQPIGVVALITPWNFPVaipsWKIF----PALVCGNTVVFKPAED 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 164 VMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIV 242
Cdd:cd07131 174 TPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEaLVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 243 LNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQV 322
Cdd:cd07131 254 MDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 323 TATLDEGATLLLGAEKIEG----AGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYT 398
Cdd:cd07131 334 EIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYT 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 399 TDEAQAQRFARELECGGVFLNGYC-ASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTVW 457
Cdd:cd07131 414 EDVNKAFRARRDLEAGITYVNAPTiGAEVHLPFGGVKKSGNGHREAGTTALDAFTEWKAV 473
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
11-450 |
1.45e-102 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 313.21 E-value: 1.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:TIGR01780 2 YNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAEHGPAML-ATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSAR 169
Cdd:TIGR01780 82 YAASFLEWFAEEAKRVYgDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 170 LLGEIFAAAGLPDGVFGWVnaTNDGVSQIIN----DDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLND 245
Cdd:TIGR01780 162 ALARLAEQAGIPKGVLNVI--TGSRAKEVGNvlttSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 246 ADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTAT 325
Cdd:TIGR01780 240 ADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 326 LDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQ 405
Cdd:TIGR01780 320 VEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIW 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1623529901 406 RFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEF 450
Cdd:TIGR01780 400 RVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEY 444
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
12-441 |
8.37e-101 |
|
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: 308.85 E-value: 8.37e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 12 NPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAK 91
Cdd:cd07090 3 EPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 92 SANLCDWYAEHGPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSARLL 171
Cdd:cd07090 83 SADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 172 GEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEA 251
Cdd:cd07090 163 AEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 252 VKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATLDEGAT 331
Cdd:cd07090 243 VNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGAK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 332 LLLGAE------KIEGaGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQ 405
Cdd:cd07090 323 VLCGGErvvpedGLEN-GFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAH 401
|
410 420 430
....*....|....*....|....*....|....*.
gi 1623529901 406 RFARELECGGVFLNGYCASDARVAFGGVKKSGFGRE 441
Cdd:cd07090 402 RVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRE 437
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
11-450 |
5.09e-99 |
|
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: 304.25 E-value: 5.09e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQAR-GEV 89
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 90 AKSANLCDWYA---EHGPAMLATEatLVENNQAVIEYRPLGAILAVMPWNFP----VWQVmrgaVPILLAGNSYLLKHAP 162
Cdd:cd07092 82 PGAVDNFRFFAgaaRTLEGPAAGE--YLPGHTSMIRREPIGVVAQIAPWNYPlmmaAWKI----APALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 163 NVMGSARLLGEIfAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFI 241
Cdd:cd07092 156 TTPLTTLLLAEL-AAEVLPPGVVNVVCGGGASAGDaLVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 242 VLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDelhqQ 321
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRE----R 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 322 VTATLD---EGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYT 398
Cdd:cd07092 311 VAGFVErapAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWT 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1623529901 399 TDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEF 450
Cdd:cd07092 391 RDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDY 442
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
11-456 |
5.36e-99 |
|
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: 304.28 E-value: 5.36e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAgyrqwRQTPLA--DRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGE 88
Cdd:cd07146 4 RNPYTGEVVGTVPAGTEEALREALALAAS-----YRSTLTryQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 89 VAKSANLCDWYAEH-----GPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPN 163
Cdd:cd07146 79 VGRAADVLRFAAAEalrddGESFSCDLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 164 VMGSARLLGEIFAAAGLPDGVFGWV-NATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGaaLKKCVLELGGSDPFIV 242
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVtGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 243 LNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQV 322
Cdd:cd07146 237 MDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 323 TATLDEGATLLLGAEKiEGAgnYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEA 402
Cdd:cd07146 317 EEAIAQGARVLLGNQR-QGA--LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1623529901 403 QAQRFARELECGGVFLN---GYcaSDARVAFGGVKKSGFG-RELSHFGLHEFCNAQTV 456
Cdd:cd07146 394 TIKRLVERLDVGTVNVNevpGF--RSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
10-441 |
2.83e-98 |
|
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: 303.33 E-value: 2.83e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEV 89
Cdd:cd07086 17 SRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 90 AKSANLCDWYAE-----HGPAMlATEATlvenNQAVIE-YRPLGAILAVMPWNFPV----WQvmrgAVPILLAGNSYLLK 159
Cdd:cd07086 97 QEMIDICDYAVGlsrmlYGLTI-PSERP----GHRLMEqWNPLGVVGVITAFNFPVavpgWN----AAIALVCGNTVVWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 160 HAPNVMGSA----RLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELG 235
Cdd:cd07086 168 PSETTPLTAiavtKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 236 GSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPmarfdLR 315
Cdd:cd07086 248 GNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP-----LI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 316 DELH-QQVTATLD----EGATLLLGAEKIEG--AGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDS 388
Cdd:cd07086 323 NQAAvEKYLNAIEiaksQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDV 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1623529901 389 EFGLSATVYTTDEAQAQRF--ARELECGGVFLNGYCaSDARV--AFGGVKKSGFGRE 441
Cdd:cd07086 403 PQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPT-SGAEIggAFGGEKETGGGRE 458
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
11-456 |
1.49e-97 |
|
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: 300.50 E-value: 1.49e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAE-----HGPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVM 165
Cdd:cd07094 84 RAIDTLRLAAEeaeriRGEEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 166 GSARLLGEIFAAAGLPDGVFGWVN-ATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGaaLKKCVLELGGSDPFIVLN 244
Cdd:cd07094 164 LSALELAKILVEAGVPEGVLQVVTgEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVDR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 245 DADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTA 324
Cdd:cd07094 242 DADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 325 TLDEGATLLLGAEKiegAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQA 404
Cdd:cd07094 322 AVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1623529901 405 QRFARELECGGVFLNGYCASDA-RVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07094 399 FKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
10-456 |
9.10e-97 |
|
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: 299.12 E-value: 9.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQ--WRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPI-AQAR 86
Cdd:cd07091 23 TINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLeESAK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 87 GEVAKSANLCDWYAehGPAMLATEATlVENNQAVIEY---RPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPN 163
Cdd:cd07091 103 GDVALSIKCLRYYA--GWADKIQGKT-IPIDGNFLAYtrrEPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 164 VMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDD-RIAAVTVTGSVRAGKAIgAQAGAA--LKKCVLELGGSDPF 240
Cdd:cd07091 180 TPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHmDVDKIAFTGSTAVGRTI-MEAAAKsnLKKVTLELGGKSPN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 241 IVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQ 320
Cdd:cd07091 259 IVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 321 QVTATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTD 400
Cdd:cd07091 339 YIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKD 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1623529901 401 EAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07091 419 INKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
11-457 |
3.98e-95 |
|
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: 295.37 E-value: 3.98e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQ--WRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGE 88
Cdd:cd07119 18 INPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEID 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 89 VAKSANLCDWYAEhgpamLATEAT--LVENNQAVIEY---RPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPN 163
Cdd:cd07119 98 IDDVANCFRYYAG-----LATKETgeVYDVPPHVISRtvrEPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 164 VMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIV 242
Cdd:cd07119 173 TPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAeLAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 243 LNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQV 322
Cdd:cd07119 253 FADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 323 TATLDEGATLLLGAEKIEGA----GNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYT 398
Cdd:cd07119 333 QLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWT 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1623529901 399 TDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTVW 457
Cdd:cd07119 413 KDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHIN 471
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
40-456 |
4.77e-95 |
|
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: 293.33 E-value: 4.77e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 40 GYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAKSANLCDWYAEHgpAMLATEATL---VEN 116
Cdd:cd07105 12 AFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASL--ITQIIGGSIpsdKPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 117 NQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSARLLGEIFAAAGLPDGVFGWV-NATNDG- 194
Cdd:cd07105 90 TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVtHSPEDAp 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 195 --VSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKR 272
Cdd:cd07105 170 evVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTER 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 273 FILEAGIAEAFTRKFVDAVAALKMGDprdeqNYVGPMARFDLRDELHQQVTATLDEGATLLLGA-EKIEGAGNYYAPTVL 351
Cdd:cd07105 250 IIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlADESPSGTSMPPTIL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 352 CNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGVFLNGYCASD-ARVAF 430
Cdd:cd07105 325 DNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDePTLPH 404
|
410 420
....*....|....*....|....*.
gi 1623529901 431 GGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07105 405 GGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
10-456 |
2.19e-94 |
|
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: 292.22 E-value: 2.19e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQ-WRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGE 88
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 89 VAKSANLCDWYAEHGPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSA 168
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 169 RLLGEIFAAAGLPDGVFGWVNAT-NDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDAD 247
Cdd:cd07109 161 LRLAELAEEAGLPAGALNVVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 248 LDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNyVGPMARFDLRDELHQQVTATLD 327
Cdd:cd07109 241 LEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD-LGPLISAKQLDRVEGFVARARA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 328 EGATLLLGAEKIEGA---GNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQA 404
Cdd:cd07109 320 RGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1623529901 405 QRFARELECGGVFLNGYCASDA-RVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07109 400 LRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
10-457 |
4.32e-94 |
|
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: 291.65 E-value: 4.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARG-E 88
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 89 VAKSANLCDWYAehGPA-MLATEATLVEN---NQAVIEyrPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNV 164
Cdd:cd07115 81 VPRAADTFRYYA--GWAdKIEGEVIPVRGpflNYTVRE--PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 165 MGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVL 243
Cdd:cd07115 157 PLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAaLVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 244 NDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVT 323
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 324 ATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQ 403
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1623529901 404 AQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTVW 457
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVW 450
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
4-441 |
7.54e-94 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 292.17 E-value: 7.54e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 4 SATHAVSVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIA 83
Cdd:PRK13252 20 SGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 84 QAR-GEVAKSANLCDWYAEHGPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAP 162
Cdd:PRK13252 100 ETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 163 NVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIV 242
Cdd:PRK13252 180 VTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 243 LNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQV 322
Cdd:PRK13252 260 FDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 323 TATLDEGATLLLGAEKIEGA----GNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYT 398
Cdd:PRK13252 340 EKGKAEGARLLCGGERLTEGgfanGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFT 419
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1623529901 399 TDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRE 441
Cdd:PRK13252 420 ADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRE 462
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
11-450 |
9.45e-94 |
|
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: 290.79 E-value: 9.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:cd07110 2 INPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAEHGPAMLATEATLV----ENNQAVIEYRPLGAILAVMPWNFP----VWQVmrgaVPILLAGNSYLLKHAP 162
Cdd:cd07110 82 DVAGCFEYYADLAEQLDAKAERAVplpsEDFKARVRREPVGVVGLITPWNFPllmaAWKV----APALAAGCTVVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 163 NVMGSARLLGEIFAAAGLPDGVFGWVNATNDGV-SQIINDDRIAAVTVTGSVRAGKAIgAQAGAALKKCV-LELGGSDPF 240
Cdd:cd07110 158 LTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAgAPLAAHPGIDKISFTGSTATGSQV-MQAAAQDIKPVsLELGGKSPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 241 IVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQ 320
Cdd:cd07110 237 IVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 321 QVTATLDEGATLLLGAEKIE--GAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYT 398
Cdd:cd07110 317 FIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1623529901 399 TDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEF 450
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNY 448
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
5-450 |
5.98e-93 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 289.50 E-value: 5.98e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 5 ATHAVsVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQ 84
Cdd:PRK13473 17 EKQPV-YNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 85 ARG-EVAKSANLCDWYAE-----HGPAmlATEatLVENNQAVIEYRPLGAILAVMPWNFP----VWQVMrgavPILLAGN 154
Cdd:PRK13473 96 ALNdEIPAIVDVFRFFAGaarclEGKA--AGE--YLEGHTSMIRRDPVGVVASIAPWNYPlmmaAWKLA----PALAAGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 155 SYLLKHAPNVMGSARLLGEIfAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLE 233
Cdd:PRK13473 168 TVVLKPSEITPLTALKLAEL-AADILPPGVLNVVTGRGATVGDaLVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 234 LGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFD 313
Cdd:PRK13473 247 LGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 314 LRDELHQQVTATLDEG-ATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGL 392
Cdd:PRK13473 327 HRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGL 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1623529901 393 SATVYTTDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEF 450
Cdd:PRK13473 407 ASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDY 464
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
11-456 |
1.36e-92 |
|
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: 288.57 E-value: 1.36e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYR-QWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARG-E 88
Cdd:cd07113 20 TNPATEQVIASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 89 VAKSANLCDWYAehGPAMLATEATLV--------ENNQAVIEYRPLGAILAVMPWNFPV----WQVMrgavPILLAGNSY 156
Cdd:cd07113 100 VGQSANFLRYFA--GWATKINGETLApsipsmqgERYTAFTRREPVGVVAGIVPWNFSVmiavWKIG----AALATGCTI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 157 LLKhaPNVMGSARLL--GEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLEL 234
Cdd:cd07113 174 VIK--PSEFTPLTLLrvAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 235 GGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMArfdl 314
Cdd:cd07113 252 GGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLA---- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 315 rDELH-QQVTATLD----EGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSE 389
Cdd:cd07113 328 -NQPHfDKVCSYLDdaraEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTP 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1623529901 390 FGLSATVYTTDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07113 407 FGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
12-441 |
1.07e-91 |
|
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: 286.00 E-value: 1.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 12 NPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQT-PLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:cd07082 22 SPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAE-----HGPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVM 165
Cdd:cd07082 102 RTIDYIRDTIEelkrlDGDSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 166 GSARLLGEIFAAAGLPDGVFGWVnaTNDG---VSQIINDDRIAAVTVTGSVRAGKAIGAQAGaaLKKCVLELGGSDPFIV 242
Cdd:cd07082 182 LLGIPLAEAFHDAGFPKGVVNVV--TGRGreiGDPLVTHGRIDVISFTGSTEVGNRLKKQHP--MKRLVLELGGKDPAIV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 243 LNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQV 322
Cdd:cd07082 258 LPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 323 TATLDEGATLLLGAEKIEgaGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEA 402
Cdd:cd07082 338 DDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDIN 415
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1623529901 403 QAQRFARELECGGVFLNGYCASDARV-AFGGVKKSGFGRE 441
Cdd:cd07082 416 KARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQ 455
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
12-443 |
8.79e-91 |
|
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: 283.10 E-value: 8.79e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 12 NPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPI-AQARGEVA 90
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAEhgpamLATEA--TLVENNQAVIEY---RPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVM 165
Cdd:cd07108 83 VLADLFRYFGG-----LAGELkgETLPFGPDVLTYtvrEPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 166 GSARLLGEIFAAAgLPDGVFGWVNATNDGVSQIINDDR-IAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLN 244
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 245 DADLDEAVKAAVTG-RYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMarfdLRDELHQQVT 323
Cdd:cd07108 237 DADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAI----ISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 324 ATLDEG-----ATLLLGA----EKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSA 394
Cdd:cd07108 313 GYIDLGlstsgATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1623529901 395 TVYTTDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELS 443
Cdd:cd07108 393 YVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREAS 441
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
10-456 |
1.07e-90 |
|
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: 283.91 E-value: 1.07e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQ-WRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQ-ARG 87
Cdd:cd07144 27 TVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnALG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 88 EVAKSANLCDWYAehGPAMLATEATLVENN--QAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVM 165
Cdd:cd07144 107 DLDEIIAVIRYYA--GWADKIQGKTIPTSPnkLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 166 GSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLN 244
Cdd:cd07144 185 LSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSaLAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 245 DADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVA-ALKMGDPRDEQNYVGPMARFDLRDELHQQVT 323
Cdd:cd07144 265 DADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 324 ATLDEGATLLLGAEK---IEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTD 400
Cdd:cd07144 345 KGKKEGAKLVYGGEKapeGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKD 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1623529901 401 EAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07144 425 IRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
11-460 |
1.61e-90 |
|
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: 282.65 E-value: 1.61e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQAR-GEV 89
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 90 AKSANLCDWYAEHGPAMLATEA----TLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVM 165
Cdd:cd07098 81 LVTCEKIRWTLKHGEKALRPESrpggLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 166 GSA----RLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFI 241
Cdd:cd07098 161 WSSgfflSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 242 VLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQ 321
Cdd:cd07098 241 VLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 322 VTATLDEGATLLLGAEKIEGA----GNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVY 397
Cdd:cd07098 321 VADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1623529901 398 TTDEAQAQRFARELECGGVFLNGYCASDARVA--FGGVKKSGFGRELSHFGLHEFCNAQTVWKDR 460
Cdd:cd07098 401 GKDIKRARRIASQLETGMVAINDFGVNYYVQQlpFGGVKGSGFGRFAGEEGLRGLCNPKSVTEDR 465
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
16-439 |
2.51e-90 |
|
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: 281.49 E-value: 2.51e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 16 GEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAKSANL 95
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 96 CdwyaeHGPAMLATEA-----TLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPN--VMGSA 168
Cdd:cd07152 81 L-----HEAAGLPTQPqgeilPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRtpVSGGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 169 rLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADL 248
Cdd:cd07152 156 -VIARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 249 DEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATLDE 328
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 329 GATLLLGAEKiegAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFA 408
Cdd:cd07152 315 GARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430
....*....|....*....|....*....|..
gi 1623529901 409 RELECGGVFLNGYCASDARVA-FGGVKKSGFG 439
Cdd:cd07152 392 DRLRTGMLHINDQTVNDEPHNpFGGMGASGNG 423
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
13-456 |
1.46e-88 |
|
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: 277.27 E-value: 1.46e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 13 PTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAKS 92
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 93 ANLCDWYAEHGPAMLATE---ATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSAR 169
Cdd:cd07101 83 AIVARYYARRAERLLKPRrrrGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 170 LLGEIFAAAGLPDGVFGWVNATNDGVSQIINDdRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLD 249
Cdd:cd07101 163 WAVELLIEAGLPRDLWQVVTGPGSEVGGAIVD-NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 250 EAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATLDEG 329
Cdd:cd07101 242 KAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 330 ATLLLGAEKIEGAGNY-YAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFA 408
Cdd:cd07101 322 ATVLAGGRARPDLGPYfYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1623529901 409 RELECGGVFLN-GYCASDARVA--FGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07101 402 ARLRAGTVNVNeGYAAAWASIDapMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
10-457 |
4.67e-87 |
|
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: 273.48 E-value: 4.67e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEV 89
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 90 AKSANLCDWYAEHGPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPV-WQVMRGAVPiLLAGNSYLLKHAPNVMGSA 168
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLmFAAAKIAAP-LAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 169 RLLGEIFAAAgLPDGVFGWVNATNDGVSQIINDDR-IAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDAD 247
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 248 LDEAVKAAVTG-RYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATL 326
Cdd:cd07107 239 PEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 327 DEGATLLLG---AEKIEGAGNYY-APTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEA 402
Cdd:cd07107 319 REGARLVTGggrPEGPALEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1623529901 403 QAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTVW 457
Cdd:cd07107 399 QAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVN 453
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
12-450 |
1.16e-86 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 273.32 E-value: 1.16e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 12 NPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAK 91
Cdd:PRK11241 32 NPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 92 SANLCDWYAEHGPAMLATeatLVENNQA----VIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGS 167
Cdd:PRK11241 112 AASFIEWFAEEGKRIYGD---TIPGHQAdkrlIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 168 ARLLGEIFAAAGLPDGVFGWVNATNDGV-SQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDA 246
Cdd:PRK11241 189 ALALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 247 DLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATL 326
Cdd:PRK11241 269 DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADAL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 327 DEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQR 406
Cdd:PRK11241 349 EKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFR 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1623529901 407 FARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEF 450
Cdd:PRK11241 429 VGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDY 472
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
9-439 |
2.01e-86 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 273.71 E-value: 2.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 9 VSVNP-TTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARG 87
Cdd:cd07124 49 ESRNPaDPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 88 EVAKSANLCDWYAEHgpaMLATEATLV-----ENNQAVieYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAP 162
Cdd:cd07124 129 DVAEAIDFLEYYARE---MLRLRGFPVemvpgEDNRYV--YRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 163 NVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAG------AALKKCVLELG 235
Cdd:cd07124 204 DTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDyLVEHPDVRFIAFTGSREVGLRIYERAAkvqpgqKWLKRVIAEMG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 236 GSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLR 315
Cdd:cd07124 284 GKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGAR 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 316 DELhQQVTATLDEGATLLLGAEKIEGA--GNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLS 393
Cdd:cd07124 364 DRI-RRYIEIGKSEGRLLLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLT 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1623529901 394 ATVYTTDEAQAQRFARELECGGVFLNGYCASdARVA---FGGVKKSGFG 439
Cdd:cd07124 443 GGVFSRSPEHLERARREFEVGNLYANRKITG-ALVGrqpFGGFKMSGTG 490
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
13-456 |
9.48e-86 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 272.14 E-value: 9.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 13 PTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAKS 92
Cdd:PRK09407 39 PFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 93 ANLCDWYAEHGPAMLATE---ATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSAR 169
Cdd:PRK09407 119 ALTARYYARRAPKLLAPRrraGALPVLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTAL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 170 LLGEIFAAAGLPDGVFGWVnaTNDGV---SQIIndDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDA 246
Cdd:PRK09407 199 AAVELLYEAGLPRDLWQVV--TGPGPvvgTALV--DNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 247 DLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATL 326
Cdd:PRK09407 275 DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 327 DEGATLLLGAEKIEGAGNY-YAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQ 405
Cdd:PRK09407 355 AKGATVLAGGKARPDLGPLfYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGR 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1623529901 406 RFARELECGGVFLN-GYCASDARVA--FGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:PRK09407 435 AIAARIRAGTVNVNeGYAAAWGSVDapMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
56-457 |
5.57e-85 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 266.60 E-value: 5.57e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 56 LRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAKSANLCDWYAEHGPAMlatEATLVE----NNQAVIEYRPLGAILA 131
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRY---EGEIIQsdrpGENILLFKRALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 132 VMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVT 210
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQeLAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 211 GSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDA 290
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 291 VAALKMGDPRDEQNY-VGPMARFDLRDELHQQVTATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPV 369
Cdd:PRK10090 238 MQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 370 ATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGVFLNgycasdaRVAF-------GGVKKSGFGREL 442
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN-------RENFeamqgfhAGWRKSGIGGAD 390
|
410
....*....|....*
gi 1623529901 443 SHFGLHEFCNAQTVW 457
Cdd:PRK10090 391 GKHGLHEYLQTQVVY 405
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
11-456 |
3.96e-84 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 267.37 E-value: 3.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGY-----RQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQA 85
Cdd:PLN02467 28 VNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 86 RGEVAKSANLCDWYAEHGPAMLATEATLV----ENNQAVIEYRPLGAILAVMPWNFP----VWQVmrgaVPILLAGNSYL 157
Cdd:PLN02467 108 AWDMDDVAGCFEYYADLAEALDAKQKAPVslpmETFKGYVLKEPLGVVGLITPWNYPllmaTWKV----APALAAGCTAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 158 LKhaPNVMGSARL--LGEIFAAAGLPDGVFGWVNAT-NDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLEL 234
Cdd:PLN02467 184 LK--PSELASVTCleLADICREVGLPPGVLNVVTGLgTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLEL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 235 GGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDL 314
Cdd:PLN02467 262 GGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 315 RDELHQQVTATLDEGATLLLGAEKIEG--AGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGL 392
Cdd:PLN02467 342 YEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGL 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1623529901 393 SATVYTTDEAQAQRFARELECGGVFLNgyCASD--ARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:PLN02467 422 AGAVISNDLERCERVSEAFQAGIVWIN--CSQPcfCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
11-456 |
2.46e-81 |
|
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: 259.38 E-value: 2.46e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYR-QW-RQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPI-AQARG 87
Cdd:cd07143 27 YNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWgLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFgTAKRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 88 EVAKSANLCDWYA-----EHGPAMLATEATLvennqAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAP 162
Cdd:cd07143 107 DVQASADTFRYYGgwadkIHGQVIETDIKKL-----TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 163 NVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDD-RIAAVTVTGSVRAGKAI-GAQAGAALKKCVLELGGSDPF 240
Cdd:cd07143 182 LTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHmDIDKVAFTGSTLVGRKVmEAAAKSNLKKVTLELGGKSPN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 241 IVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQ 320
Cdd:cd07143 262 IVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 321 QVTATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTD 400
Cdd:cd07143 342 YIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNN 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1623529901 401 EAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07143 422 INNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
10-445 |
8.16e-81 |
|
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: 258.04 E-value: 8.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARG-E 88
Cdd:cd07559 20 NYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLAaD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 89 VAKSANLCDWYAEhgpAMLATEATLV---ENNQAVIEYRPLGAILAVMPWNFP----VWQVmrgaVPILLAGNSYLLKHA 161
Cdd:cd07559 100 IPLAIDHFRYFAG---VIRAQEGSLSeidEDTLSYHFHEPLGVVGQIIPWNFPllmaAWKL----APALAAGNTVVLKPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 162 PNVMGSARLLGEIFAAAgLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPF 240
Cdd:cd07559 173 SQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKpLASHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 241 IVLNDA-----DLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLR 315
Cdd:cd07559 252 IFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 316 DELHQQVTATLDEGATLLLGAEKIEG----AGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFG 391
Cdd:cd07559 332 EKILSYVDIGKEEGAEVLTGGERLTLggldKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYG 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1623529901 392 LSATVYTTDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRE-----LSHF 445
Cdd:cd07559 412 LGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGREthkmmLDHY 470
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
11-439 |
5.44e-80 |
|
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: 255.90 E-value: 5.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:cd07085 21 YNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDwYAEHGPAMLATEaTLVENNQAVIEY---RPLGAILAVMPWNFPV----WqvMrgaVPILLA-GNSYLLKHAP 162
Cdd:cd07085 101 RGLEVVE-FACSIPHLLKGE-YLENVARGIDTYsyrQPLGVVAGITPFNFPAmiplW--M---FPMAIAcGNTFVLKPSE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 163 NVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIV 242
Cdd:cd07085 174 RVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 243 LNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQV 322
Cdd:cd07085 254 MPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 323 TATLDEGATLLLGAEKIEGA----GNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYT 398
Cdd:cd07085 334 ESGVEEGAKLVLDGRGVKVPgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFT 413
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1623529901 399 TDEAQAQRFARELECGGVFLN-GYCASDARVAFGGVKKSGFG 439
Cdd:cd07085 414 RSGAAARKFQREVDAGMVGINvPIPVPLAFFSFGGWKGSFFG 455
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
10-456 |
6.47e-80 |
|
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: 254.96 E-value: 6.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYR--QWRQTPlADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARG 87
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 88 EVAKSANLCDWYAEHGPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGS 167
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 168 ARLLGEIFAAA-GLPDGVFGWVN-ATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLND 245
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTeSGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 246 ADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTAT 325
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 326 LDEGATLLLGAEKIEG---AGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEA 402
Cdd:cd07120 320 IAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1623529901 403 QAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
10-450 |
8.78e-79 |
|
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: 252.70 E-value: 8.78e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQAR-GE 88
Cdd:cd07111 41 TINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRdCD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 89 VAKSANLCDWYAehGPAMLATEAtlvennqaVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSA 168
Cdd:cd07111 121 IPLVARHFYHHA--GWAQLLDTE--------LAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 169 RLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADL 248
Cdd:cd07111 191 LLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 249 DEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTATLDE 328
Cdd:cd07111 271 DSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 329 GATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFA 408
Cdd:cd07111 351 GADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVA 430
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1623529901 409 RELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEF 450
Cdd:cd07111 431 LSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
10-457 |
1.93e-76 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 247.12 E-value: 1.93e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQ--WRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQA-R 86
Cdd:PRK09847 39 TVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 87 GEVAKSANLCDWYAEHGPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMG 166
Cdd:PRK09847 119 DDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 167 SARLLGEIFAAAGLPDGVFGWVNATNDGVSQIIN-DDRIAAVTVTGSVRAGKAIGAQAGAA-LKKCVLELGGSDPFIVLN 244
Cdd:PRK09847 199 SAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSrHNDIDAIAFTGSTRTGKQLLKDAGDSnMKRVWLEAGGKSANIVFA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 245 DA-DLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVT 323
Cdd:PRK09847 279 DCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIR 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 324 ATLDEGATLLLGAEkiEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQ 403
Cdd:PRK09847 359 EGESKGQLLLDGRN--AGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSR 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1623529901 404 AQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTVW 457
Cdd:PRK09847 437 AHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIW 490
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
10-456 |
4.44e-76 |
|
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: 245.87 E-value: 4.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQ--WRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQAR- 86
Cdd:cd07142 23 TIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 87 GEVAKSANLCDWYAE-----HGPAMLATEatlveNNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHA 161
Cdd:cd07142 103 AEVPLAARLFRYYAGwadkiHGMTLPADG-----PHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 162 PNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGV-SQIINDDRIAAVTVTGSVRAGKAI-GAQAGAALKKCVLELGGSDP 239
Cdd:cd07142 178 EQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAgAAIASHMDVDKVAFTGSTEVGKIImQLAAKSNLKPVTLELGGKSP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 240 FIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELH 319
Cdd:cd07142 258 FIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKIL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 320 QQVTATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTT 399
Cdd:cd07142 338 SYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSK 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1623529901 400 DEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07142 418 NIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
10-441 |
4.40e-74 |
|
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: 240.43 E-value: 4.40e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARG-E 88
Cdd:cd07117 20 SYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 89 VAKSANLCDWYAEhgpAMLATEATLVENNQ---AVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVM 165
Cdd:cd07117 100 IPLAADHFRYFAG---VIRAEEGSANMIDEdtlSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 166 GSARLLGEIFAAAgLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLN 244
Cdd:cd07117 177 LSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEyLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 245 DADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTA 324
Cdd:cd07117 256 DANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 325 TLDEGATLLLGAEKIEG----AGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTD 400
Cdd:cd07117 336 AKEEGAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKD 415
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1623529901 401 EAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRE 441
Cdd:cd07117 416 INRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRE 456
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
10-441 |
2.03e-71 |
|
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: 233.64 E-value: 2.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEV 89
Cdd:cd07130 16 SISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 90 AKSANLCDwYAE------HGPAMlATEatlvENNQAVIE-YRPLGAILAVMPWNFPV----WQVMRGAVpillAGNSYLL 158
Cdd:cd07130 96 QEMIDICD-FAVglsrqlYGLTI-PSE----RPGHRMMEqWNPLGVVGVITAFNFPVavwgWNAAIALV----CGNVVVW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 159 KHAPNVMGSA----RLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLEL 234
Cdd:cd07130 166 KPSPTTPLTAiavtKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 235 GGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDL 314
Cdd:cd07130 246 GGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 315 RDELHQQVTATLDEGATLLLGAEKIEGAGNYYAPTVLcNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSA 394
Cdd:cd07130 326 VDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSS 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1623529901 395 TVYTTDEAQAQRF--ARELECGGVFLNgYCASDARV--AFGGVKKSGFGRE 441
Cdd:cd07130 405 SIFTTDLRNAFRWlgPKGSDCGIVNVN-IGTSGAEIggAFGGEKETGGGRE 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
10-456 |
3.25e-71 |
|
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: 233.16 E-value: 3.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYR--QWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQA-R 86
Cdd:cd07140 25 TINPTDGSVICKVSLATVEDVDRAVAAAKEAFEngEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLAlK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 87 GEVAKS-------ANLCDwyAEHGPAMLATEATlVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLK 159
Cdd:cd07140 105 THVGMSiqtfryfAGWCD--KIQGKTIPINQAR-PNRNLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 160 HAPNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIIND-DRIAAVTVTGSVRAGKAI-GAQAGAALKKCVLELGGS 237
Cdd:cd07140 182 PAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDhPDVRKLGFTGSTPIGKHImKSCAVSNLKKVSLELGGK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 238 DPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDE 317
Cdd:cd07140 262 SPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 318 LHQQVTATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDAD--HALALANDSEFGLSAT 395
Cdd:cd07140 342 LVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDvdGVLQRANDTEYGLASG 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1623529901 396 VYTTDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07140 422 VFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
9-437 |
2.89e-70 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 231.75 E-value: 2.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 9 VSVNPT-TGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARG 87
Cdd:PRK03137 53 VSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 88 EVAKSANLCDWYAEHgpAMLATEATLV-----ENNQAVieYRPLGAILAVMPWNFPVwQVMRG-AVPILLAGNSYLLKHA 161
Cdd:PRK03137 133 DTAEAIDFLEYYARQ--MLKLADGKPVesrpgEHNRYF--YIPLGVGVVISPWNFPF-AIMAGmTLAAIVAGNTVLLKPA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 162 PNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAA------LKKCVLEL 234
Cdd:PRK03137 208 SDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDyLVDHPKTRFITFTGSREVGLRIYERAAKVqpgqiwLKRVIAEM 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 235 GGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPrDEQNYVGPMARFDL 314
Cdd:PRK03137 288 GGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNAYMGPVINQAS 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 315 RDELHQQVTATLDEGaTLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSA 394
Cdd:PRK03137 367 FDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTG 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1623529901 395 TVYTTDEAQAQRFARELECGGVFLNGYCASdARV---AFGGVKKSG 437
Cdd:PRK03137 446 AVISNNREHLEKARREFHVGNLYFNRGCTG-AIVgyhPFGGFNMSG 490
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
11-456 |
1.84e-67 |
|
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: 223.38 E-value: 1.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQ---WRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIA-QAR 86
Cdd:cd07141 27 INPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSkSYL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 87 GEVAKSANLCDWYAehGPAMLATEATLVENNQAVIEYR--PLGAILAVMPWNFPV----WQVmrgaVPILLAGNSYLLKH 160
Cdd:cd07141 107 VDLPGAIKVLRYYA--GWADKIHGKTIPMDGDFFTYTRhePVGVCGQIIPWNFPLlmaaWKL----APALACGNTVVLKP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 161 APNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAA-LKKCVLELGGSD 238
Cdd:cd07141 181 AEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAaISSHPDIDKVAFTGSTEVGKLIQQAAGKSnLKRVTLELGGKS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 239 PFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDEL 318
Cdd:cd07141 261 PNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 319 HQQVTATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYT 398
Cdd:cd07141 341 LELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFT 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1623529901 399 TDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07141 421 KDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
29-445 |
2.37e-67 |
|
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: 221.76 E-value: 2.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 29 EVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAKSANLCDW----YAEHgp 104
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDIsikaYHER-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 105 amLATEATLVENNQAVIEYRPLGAILAVMPWNFPVwQVMRGA-VPILLAGNSYLLK---HAPNVmgsARLLGEIFAAAGL 180
Cdd:cd07095 79 --TGERATPMAQGRAVLRHRPHGVMAVFGPFNFPG-HLPNGHiVPALLAGNTVVFKpseLTPAV---AELMVELWEEAGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 181 PDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQ-AGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGR 259
Cdd:cd07095 153 PPGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 260 YQNSGQVCAASKRFILEAG-IAEAFTRKFVDAVAALKMGDPRDEQNYVGPM--ARFDLRDELHQQvtATLDEGATLLLGA 336
Cdd:cd07095 233 FLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLiiAAAAARYLLAQQ--DLLALGGEPLLAM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 337 EKIEGAGNYYAPTVLcNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGV 416
Cdd:cd07095 311 ERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIV 389
|
410 420 430
....*....|....*....|....*....|...
gi 1623529901 417 F----LNGycASDARvAFGGVKKSGFGRELSHF 445
Cdd:cd07095 390 NwnrpTTG--ASSTA-PFGGVGLSGNHRPSAYY 419
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
3-439 |
5.40e-64 |
|
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: 213.97 E-value: 5.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 3 LSATHAVSVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPI 82
Cdd:TIGR01722 13 ASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 83 AQARGEVAKSANLCDWYAEHGPAMLATEATLVENNQAVIEYR-PLGAILAVMPWNF----PVWQvmrgaVPILLA-GNSY 156
Cdd:TIGR01722 93 SDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRqPLGVCAGITPFNFpamiPLWM-----FPIAIAcGNTF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 157 LLKHAPNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGG 236
Cdd:TIGR01722 168 VLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 237 SDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILeAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRD 316
Cdd:TIGR01722 248 KNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVL-VGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 317 ELHQQVTATLDEGATLLLGAE--KIEG--AGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGL 392
Cdd:TIGR01722 327 RVASLIAGGAAEGAEVLLDGRgyKVDGyeEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGN 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1623529901 393 SATVYTTDEAQAQRFARELECGGVFLN-------GYcasdarVAFGGVKKSGFG 439
Cdd:TIGR01722 407 GTAIFTRDGAAARRFQHEIEVGQVGVNvpipvplPY------FSFTGWKDSFFG 454
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
10-456 |
1.21e-63 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 213.91 E-value: 1.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQ--WRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARG 87
Cdd:PLN02766 40 TRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 88 -EVAKSANLCDWYAE-----HGPAMLATEA----TLVEnnqavieyrPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYL 157
Cdd:PLN02766 120 vDIPAAAGLLRYYAGaadkiHGETLKMSRQlqgyTLKE---------PIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 158 LKHAPNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDR-IAAVTVTGSVRAGKAI-GAQAGAALKKCVLELG 235
Cdd:PLN02766 191 VKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMdVDKVSFTGSTEVGRKImQAAATSNLKQVSLELG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 236 GSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLR 315
Cdd:PLN02766 271 GKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQF 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 316 DELHQQVTATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSAT 395
Cdd:PLN02766 351 EKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAG 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1623529901 396 VYTTDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:PLN02766 431 IVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
10-445 |
1.36e-62 |
|
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: 210.39 E-value: 1.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIaqaRGEV 89
Cdd:cd07116 20 NITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPV---RETL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 90 AKSANLC-DWYAEHGPAMLATEATLVENNQAVIEY---RPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVM 165
Cdd:cd07116 97 AADIPLAiDHFRYFAGCIRAQEGSISEIDENTVAYhfhEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 166 GSARLLGEIFAAAgLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFI--- 241
Cdd:cd07116 177 ASILVLMELIGDL-LPPGVVNVVNGFGLEAGKpLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIffa 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 242 -VLN--DADLDEAVKAAVTGRYqNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDEL 318
Cdd:cd07116 256 dVMDadDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 319 HQQVTATLDEGATLLLGAEKIEGAGN----YYAPTVLCNvTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSA 394
Cdd:cd07116 335 LSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGA 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1623529901 395 TVYTTDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRE-----LSHF 445
Cdd:cd07116 414 GVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGREnhkmmLDHY 469
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
10-456 |
6.51e-60 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 205.04 E-value: 6.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQ--WRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARG 87
Cdd:PLN02466 77 TLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 88 -EVAKSANLCDWYAE-----HGPAMLATEatlveNNQAVIEYRPLGAILAVMPWNFPV----WQVMrgavPILLAGNSYL 157
Cdd:PLN02466 157 aELPMFARLFRYYAGwadkiHGLTVPADG-----PHHVQTLHEPIGVAGQIIPWNFPLlmfaWKVG----PALACGNTIV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 158 LKHAPNVMGSARLLGEIFAAAGLPDGVFGWVNA----TNDGVSQIINDDRIAavtVTGSVRAGKAI-GAQAGAALKKCVL 232
Cdd:PLN02466 228 LKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfgptAGAALASHMDVDKLA---FTGSTDTGKIVlELAAKSNLKPVTL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 233 ELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKfvdAVA-ALK--MGDPRDEQNYVGPM 309
Cdd:PLN02466 305 ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK---AKArALKrvVGDPFKKGVEQGPQ 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 310 ARFDLRDELHQQVTATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSE 389
Cdd:PLN02466 382 IDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTR 461
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1623529901 390 FGLSATVYTTDEAQAQRFARELECGGVFLNGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:PLN02466 462 YGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
11-459 |
4.08e-58 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 201.51 E-value: 4.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:PLN02419 134 INPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIF 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLcdwyAEH--GPAMLATEATLVENNQAVIEY---RPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVM 165
Cdd:PLN02419 214 RGLEV----VEHacGMATLQMGEYLPNVSNGVDTYsirEPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 166 GSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLND 245
Cdd:PLN02419 290 GASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 246 ADLDEAVKAAVTGRYQNSGQVCAASKRFILeAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVTAT 325
Cdd:PLN02419 370 ANIDATLNALLAAGFGAAGQRCMALSTVVF-VGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSG 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 326 LDEGATLLLGAEKI----EGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDE 401
Cdd:PLN02419 449 VDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSG 528
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1623529901 402 AQAQRFARELECGGVFLN-GYCASDARVAFGGvKKSGFGRELSHF---GLHEFCNAQTV---WKD 459
Cdd:PLN02419 529 AAARKFQMDIEAGQIGINvPIPVPLPFFSFTG-NKASFAGDLNFYgkaGVDFFTQIKLVtqkQKD 592
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
5-456 |
1.05e-57 |
|
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: 198.57 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 5 ATHAVSVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQ 84
Cdd:cd07125 46 EGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 85 ARGEVAKSANLCDWYA---EHGPAMLATEATLVENNQavIEYRPLGAILAVMPWNFPVwqvmrgAVPI------LLAGNS 155
Cdd:cd07125 126 ADAEVREAIDFCRYYAaqaRELFSDPELPGPTGELNG--LELHGRGVFVCISPWNFPL------AIFTgqiaaaLAAGNT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 156 YLLKHAPNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIG---AQAGAALKKCV 231
Cdd:cd07125 198 VIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEaLVAHPRIDGVIFTGSTETAKLINralAERDGPILPLI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 232 LELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMAR 311
Cdd:cd07125 278 AETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLID 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 312 FDLRDELHQQVtaTLDEGATLLLGAEKI-EGAGNYYAPTVLCNVtaGMTGFRQELFGPVATLTTAR--DADHALALANDS 388
Cdd:cd07125 358 KPAGKLLRAHT--ELMRGEAWLIAPAPLdDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKaeDLDEAIEDINAT 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1623529901 389 EFGLSATVYTTDEAQAQRFARELECGGVFLN----GycASDARVAFGGVKKSGFGREL--SHFgLHEFCNAQTV 456
Cdd:cd07125 434 GYGLTLGIHSRDEREIEYWRERVEAGNLYINrnitG--AIVGRQPFGGWGLSGTGPKAggPNY-LLRFGNEKTV 504
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
11-439 |
2.74e-56 |
|
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: 193.02 E-value: 2.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYR---QWrqTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARG 87
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFLdrnNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 88 EVAKSANLCDWYAE-------HGPAMLATEATlvENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKH 160
Cdd:cd07148 82 EVTRAIDGVELAADelgqlggREIPMGLTPAS--AGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 161 APNVMGSARLLGEIFAAAGLPDGvfgWVNAT---NDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAgAALKKCVLELGGS 237
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEG---WCQAVpceNAVAEKLVTDPRVAFFSFIGSARVGWMLRSKL-APGTRCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 238 DPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDE 317
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 318 LHQQVTATLDEGATLLLGAEKIegAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVY 397
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRL--SDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1623529901 398 TTDEAQAQRFARELECGGVFLNGYCAsdARV---AFGGVKKSGFG 439
Cdd:cd07148 394 TKDLDVALKAVRRLDATAVMVNDHTA--FRVdwmPFAGRRQSGYG 436
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
7-439 |
4.58e-55 |
|
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: 191.25 E-value: 4.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 7 HAVSVNP-TTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQA 85
Cdd:cd07083 33 RMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 86 RGEVAKSANLCDWYAEHGPAMLATEATLV----ENNQAVieYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHA 161
Cdd:cd07083 113 IDDVAEAIDFIRYYARAALRLRYPAVEVVpypgEDNESF--YVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 162 PNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGV-SQIINDDRIAAVTVTGSVRAGKAIGAQAG------AALKKCVLEL 234
Cdd:cd07083 191 EDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAArlapgqTWFKRLYVET 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 235 GGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMarfdL 314
Cdd:cd07083 271 GGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPV----I 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 315 RDELHQQVTATLDEG---ATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDAD--HALALANDSE 389
Cdd:cd07083 347 DAEQEAKVLSYIEHGkneGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTP 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1623529901 390 FGLSATVYTTDEAQAQRFARELECGGVFLNGYcASDARVA---FGGVKKSGFG 439
Cdd:cd07083 427 YGLTGGVYSRKREHLEEARREFHVGNLYINRK-ITGALVGvqpFGGFKLSGTN 478
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
9-437 |
4.46e-54 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 188.24 E-value: 4.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 9 VSVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGE 88
Cdd:PRK09457 18 ESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 89 VAKSANLCDW----YAEHGPamlaTEATLVENNQAVIEYRPLGaILAVM-PWNFPVWQVMRGAVPILLAGNSYLLKHAPN 163
Cdd:PRK09457 98 VTAMINKIAIsiqaYHERTG----EKRSEMADGAAVLRHRPHG-VVAVFgPYNFPGHLPNGHIVPALLAGNTVVFKPSEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 164 VMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQ-AGAALKKCVLELGGSDPFIV 242
Cdd:PRK09457 173 TPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQfAGQPEKILALEMGGNNPLVI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 243 LNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGI-AEAFTRKFVDAVAALKMGDPRDE-QNYVGPMARFDLRDELHQ 320
Cdd:PRK09457 253 DEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWDAEpQPFMGAVISEQAAQGLVA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 321 QVTATLDEGATLLLGAEKIEGAGNYYAPTVLcNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTD 400
Cdd:PRK09457 333 AQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDD 411
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1623529901 401 EAQAQRFARELECGGVF----LNGyCASDArvAFGGVKKSG 437
Cdd:PRK09457 412 REDYDQFLLEIRAGIVNwnkpLTG-ASSAA--PFGGVGASG 449
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
10-441 |
1.58e-53 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 186.96 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 10 SVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEV 89
Cdd:PLN02315 38 SVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 90 AKSANLCDwYAEHGPAMLATEATLVEN-NQAVIE-YRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNV--- 164
Cdd:PLN02315 118 QEIIDMCD-FAVGLSRQLNGSIIPSERpNHMMMEvWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTpli 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 165 -MGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVL 243
Cdd:PLN02315 197 tIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVM 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 244 NDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVT 323
Cdd:PLN02315 277 DDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 324 ATLDEGATLLLGAEKIEGAGNYYAPTVLcNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQ 403
Cdd:PLN02315 357 IIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPET 435
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1623529901 404 AQRFAREL--ECGGVFLNgYCASDARV--AFGGVKKSGFGRE 441
Cdd:PLN02315 436 IFKWIGPLgsDCGIVNVN-IPTNGAEIggAFGGEKATGGGRE 476
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
11-439 |
1.94e-49 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 175.71 E-value: 1.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVA 90
Cdd:PLN00412 36 TNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 91 KSANLCDWYAEHGPAMLATEATLV-------ENNQAVIEYR-PLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKhaP 162
Cdd:PLN00412 116 RSGDLISYTAEEGVRILGEGKFLVsdsfpgnERNKYCLTSKiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLK--P 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 163 NVMG--SARLLGEIFAAAGLPDGVFGWVNatndGVSQIIND-----DRIAAVTVTGSvRAGKAIGAQAG-AALKkcvLEL 234
Cdd:PLN00412 194 PTQGavAALHMVHCFHLAGFPKGLISCVT----GKGSEIGDfltmhPGVNCISFTGG-DTGIAISKKAGmVPLQ---MEL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 235 GGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNyVGPMARFDL 314
Cdd:PLN00412 266 GGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCD-ITPVVSESS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 315 RDELHQQVTATLDEGATLLlgaEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSA 394
Cdd:PLN00412 345 ANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQG 421
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1623529901 395 TVYTTDEAQAQRFARELECGGVFLNGYCASDA-RVAFGGVKKSGFG 439
Cdd:PLN00412 422 CVFTRDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIG 467
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
48-456 |
1.77e-45 |
|
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: 163.47 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 48 PLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQA--------RGEV--AKsANLCDWYA-EHGPAMLATEATlven 116
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteiavvLGEIdhAL-KHLKKWMKpRRVSVPLLLQPA---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 117 nQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLK---HAPNVmgsARLLGEIFAAAgLPDGVFGWVNATND 193
Cdd:cd07087 93 -KAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKpseLAPAT---SALLAKLIPKY-FDPEAVAVVEGGVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 194 gVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRF 273
Cdd:cd07087 168 -VATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 274 ILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYvgpmARfdLRDELHQQVTATLDEGATLLLGAEkIEGAGNYYAPTVLCN 353
Cdd:cd07087 247 LVHESIKDELIEELKKAIKEFYGEDPKESPDY----GR--IINERHFDRLASLLDDGKVVIGGQ-VDKEERYIAPTILDD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 354 VTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGVFLNG---YCASDArVAF 430
Cdd:cd07087 320 VSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDvllHAAIPN-LPF 398
|
410 420
....*....|....*....|....*.
gi 1623529901 431 GGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07087 399 GGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
43-458 |
5.75e-43 |
|
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: 157.00 E-value: 5.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 43 QWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAqargEVAKS-------------ANLCDWYAehgPAMLAT 109
Cdd:cd07134 13 ALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAA----EVDLTeilpvlseinhaiKHLKKWMK---PKRVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 110 EATLvENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLK------HAPNVMgsARLLGEIFAaaglPDG 183
Cdd:cd07134 86 PLLL-FGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKpseltpHTSAVI--AKIIREAFD----EDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 184 VF---GWVNatndgVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRY 260
Cdd:cd07134 159 VAvfeGDAE-----VAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 261 QNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNyvGPMARFdLRDELHQQVTATLDE----GATLLLGA 336
Cdd:cd07134 234 LNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKAS--PDLARI-VNDRHFDRLKGLLDDavakGAKVEFGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 337 EkIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGV 416
Cdd:cd07134 311 Q-FDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1623529901 417 FLNGYCA--SDARVAFGGVKKSGFGRELSHFGLHEFCNAQTVWK 458
Cdd:cd07134 390 VVNDVVLhfLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
26-456 |
9.28e-40 |
|
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: 148.14 E-value: 9.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 26 SEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQAR-GEVAKSANLCDWYAEHGP 104
Cdd:cd07135 3 PLDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKNLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 105 AMLATEAtlVENN-------QAVIEYRPLGAILAVMPWNFPVW---QVMRGAvpiLLAGNSYLLK---HAPNvmgSARLL 171
Cdd:cd07135 83 KWAKDEK--VKDGplafmfgKPRIRKEPLGVVLIIGPWNYPVLlalSPLVGA---IAAGCTVVLKpseLTPH---TAALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 172 GEIFAAAgLPDGVFGWVNATNDGVSQIIND--DRIaavTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLD 249
Cdd:cd07135 155 AELVPKY-LDPDAFQVVQGGVPETTALLEQkfDKI---FYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 250 EAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYvgpmARfdLRDELH-QQVTATLDE 328
Cdd:cd07135 231 LAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDY----TR--IVNPRHfNRLKSLLDT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 329 -GATLLLGAEKIEgAGNYYAPTVLCNVTAG---MTGfrqELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQA 404
Cdd:cd07135 305 tKGKVVIGGEMDE-ATRFIPPTIVSDVSWDdslMSE---ELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEI 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1623529901 405 QRFARELECGGVFLNGYC--ASDARVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07135 381 DHILTRTRSGGVVINDTLihVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
16-437 |
1.23e-34 |
|
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: 135.41 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 16 GEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRigAALRARGEEVAQMITLEM---GKPIAQARGEVAks 92
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLK--AADLLSGKYRYELNAATMlgqGKNVWQAEIDAA-- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 93 ANLCDW------YAEHGPAMLATEATLVENNQavIEYRPL-GAILAVMPWNFPVWQVMRGAVPILLaGNSYLLKHAPNVM 165
Cdd:cd07123 133 CELIDFlrfnvkYAEELYAQQPLSSPAGVWNR--LEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 166 GSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDR-IAAVTVTGSVRAGKAIGAQAGAALK------KCVLELGGSD 238
Cdd:cd07123 210 LSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPhLAGLHFTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 239 PFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPM---ARFD-L 314
Cdd:cd07123 290 FHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVideKAFDrI 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 315 RDELHQqvtATLDEGATLLLGAEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHA--LALAND-SEFG 391
Cdd:cd07123 370 KGYIDH---AKSDPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEetLELVDTtSPYA 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1623529901 392 LSATVYTTDEA---QAQ---RFAreleCGGVFLNGYCaSDARVA---FGGVKKSG 437
Cdd:cd07123 447 LTGAIFAQDRKairEATdalRNA----AGNFYINDKP-TGAVVGqqpFGGARASG 496
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
43-456 |
4.08e-32 |
|
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: 126.83 E-value: 4.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 43 QWRQTP---LADRADALRRIGAALRARGEEVAQMITLEMG-KPIAQAR-GEVAKSANLCDWYAEHG-----PAMLATEAT 112
Cdd:cd07133 10 AFLANPppsLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLlAEILPSIAGIKHARKHLkkwmkPSRRHVGLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 113 LVENnQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSARLLGEIFAAAGLPDGVfgwvnatn 192
Cdd:cd07133 90 FLPA-KAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 193 dgvsQIINDDR-IAA---------VTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQN 262
Cdd:cd07133 161 ----AVVTGGAdVAAafsslpfdhLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 263 SGQVCAASKRFILEAGIAEAFTRKFVDAVAALkMGDPRDEQNYVGPMarfdlrDELH-QQVTATLDE----GATL--LLG 335
Cdd:cd07133 237 AGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-YPTLADNPDYTSII------NERHyARLQGLLEDarakGARVieLNP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 336 AEKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGG 415
Cdd:cd07133 310 AGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGG 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1623529901 416 VFLNG----YCASDArvAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:cd07133 390 VTINDtllhVAQDDL--PFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
41-440 |
5.28e-32 |
|
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: 126.76 E-value: 5.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 41 YRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQA-RGEV------AKSA--NLCDWYA-EHGPAMLATE 110
Cdd:cd07137 12 FRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVsvlvssCKLAikELKKWMApEKVKTPLTTF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 111 ATlvennQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKH---APNvmgSARLLGEIFAAAgLPDGVFGW 187
Cdd:cd07137 92 PA-----KAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPselAPA---TSALLAKLIPEY-LDTKAIKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 188 VNATNDGVSQIInDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRY-QNSGQV 266
Cdd:cd07137 163 IEGGVPETTALL-EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 267 CAASKRFILEagiaEAFTRKFVDAVAA--LKM--GDPRDEQNyvgpMARfdLRDELHQQVTATLDEGATLllgAEKIEGA 342
Cdd:cd07137 242 CIAPDYVLVE----ESFAPTLIDALKNtlEKFfgENPKESKD----LSR--IVNSHHFQRLSRLLDDPSV---ADKIVHG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 343 GN------YYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGV 416
Cdd:cd07137 309 GErdeknlYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGV 388
|
410 420 430
....*....|....*....|....*....|.
gi 1623529901 417 FLNgycasDARV-------AFGGVKKSGFGR 440
Cdd:cd07137 389 TFN-----DTVVqyaidtlPFGGVGESGFGA 414
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
121-440 |
3.02e-29 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 119.15 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 121 IEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLK---HAPNVmgsARLLGEIFAAAGLPDGVfgwvnATNDG--- 194
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKpseLTPNT---SKVIAKIIEETFDEEYV-----AVVEGgve 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 195 VSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFI 274
Cdd:cd07136 168 ENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 275 LEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVgpmarfdlR--DELH-QQVTATLDEGATLLLGaeKIEGAGNYYAPTVL 351
Cdd:cd07136 248 VHESVKEKFIKELKEEIKKFYGEDPLESPDYG--------RiiNEKHfDRLAGLLDNGKIVFGG--NTDRETLYIEPTIL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 352 CNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGVflngyCASDA----- 426
Cdd:cd07136 318 DNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGG-----CINDTimhla 392
|
330
....*....|....*.
gi 1623529901 427 --RVAFGGVKKSGFGR 440
Cdd:cd07136 393 npYLPFGGVGNSGMGS 408
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
121-439 |
2.13e-28 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 117.44 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 121 IEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLK---HAPNvmgSARLLGEIFAAAgLPDGVFGWVNAtndGVSQ 197
Cdd:PTZ00381 105 IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKpseLSPH---TSKLMAKLLTKY-LDPSYVRVIEG---GVEV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 198 IIN--DDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFIL 275
Cdd:PTZ00381 178 TTEllKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 276 EAGIAEAFTRKFVDAVAALKMGDPRDEQNYvgpmARfdLRDELHQQVTATL--DEGATLLLGAEkIEGAGNYYAPTVLCN 353
Cdd:PTZ00381 258 HRSIKDKFIEALKEAIKEFFGEDPKKSEDY----SR--IVNEFHTKRLAELikDHGGKVVYGGE-VDIENKYVAPTIIVN 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 354 VTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGVFLNG--YCASDARVAFG 431
Cdd:PTZ00381 331 PDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDcvFHLLNPNLPFG 410
|
....*...
gi 1623529901 432 GVKKSGFG 439
Cdd:PTZ00381 411 GVGNSGMG 418
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
41-421 |
1.62e-27 |
|
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: 114.18 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 41 YRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAKSANlcdwyaehgpaMLATEATLVENN--- 117
Cdd:cd07129 12 FESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTG-----------QLRLFADLVREGswl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 118 QAVIE-----------------YRPLGAILAVMPWNFPV-WQVMRG-AVPILLAGNSYLLKHAPNVMGSARLLGEIFAAA 178
Cdd:cd07129 81 DARIDpadpdrqplprpdlrrmLVPLGPVAVFGASNFPLaFSVAGGdTASALAAGCPVVVKAHPAHPGTSELVARAIRAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 179 ----GLPDGVFGWVNATNDGVSQ-IINDDRIAAVTVTGSVRAGKAIGAQAGA--ALKKCVLELGGSDPFIVLNDA----- 246
Cdd:cd07129 161 lratGLPAGVFSLLQGGGREVGVaLVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGAlaerg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 247 -DLDEAVKAAVTgryQNSGQVC-----------AASKRFIleAGIAEAFTrkfvdAVAALKMGDPRDEQNYVgpmarfdl 314
Cdd:cd07129 241 eAIAQGFVGSLT---LGAGQFCtnpglvlvpagPAGDAFI--AALAEALA-----AAPAQTMLTPGIAEAYR-------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 315 rdelhQQVTATLDEGATLLLGAEKIEGAGNYYAPTVLcnVTAGMT-----GFRQELFGPVATLTTARDADHALALANDSE 389
Cdd:cd07129 303 -----QGVEALAAAPGVRVLAGGAAAEGGNQAAPTLF--KVDAAAfladpALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
410 420 430
....*....|....*....|....*....|....*.
gi 1623529901 390 FGLSATVYTT--DEAQAQRFARELE--CGGVFLNGY 421
Cdd:cd07129 376 GQLTATIHGEedDLALARELLPVLErkAGRLLFNGW 411
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
5-456 |
1.74e-27 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 116.07 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 5 ATHAVSVNPTTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQ 84
Cdd:PRK11904 562 EARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQD 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 85 ARGEVAKSANLCDWYAEHGPAMLATEATLV----ENNQavIEYRPLGAILAVMPWNFP----VWQVmrgaVPILLAGNSY 156
Cdd:PRK11904 642 AIAEVREAVDFCRYYAAQARRLFGAPEKLPgptgESNE--LRLHGRGVFVCISPWNFPlaifLGQV----AAALAAGNTV 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 157 LLKHAPNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGV-SQIINDDRIAAVTVTGSVRAGKAIG---AQAGAALKKCVL 232
Cdd:PRK11904 716 IAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIAGVAFTGSTETARIINrtlAARDGPIVPLIA 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 233 ELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARF 312
Cdd:PRK11904 796 ETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDA 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 313 DLRDELHQQVtATLDEGATLLLGAEKIEGA--GNYYAPTVLcnVTAGMTGFRQELFGPVATLTT--ARDADHALALANDS 388
Cdd:PRK11904 876 EAKANLDAHI-ERMKREARLLAQLPLPAGTenGHFVAPTAF--EIDSISQLEREVFGPILHVIRykASDLDKVIDAINAT 952
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1623529901 389 EFGLSATVYTTDEAQAQRFARELECGGVFLN----GycasdARVA---FGGVKKSGFGREL--SHFgLHEFCNAQTV 456
Cdd:PRK11904 953 GYGLTLGIHSRIEETADRIADRVRVGNVYVNrnqiG-----AVVGvqpFGGQGLSGTGPKAggPHY-LLRFATEKTV 1023
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
5-439 |
3.99e-27 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 115.35 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 5 ATHAVsVNP-TTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIA 83
Cdd:PRK11905 567 GTRPV-LNPaDHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLA 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 84 QARGEVAKSANLCDWYAEHGPAMLATEATlvennqavieyRPLGAILAVMPWNFP----VWQVmrgaVPILLAGNSYLLK 159
Cdd:PRK11905 646 NAIAEVREAVDFLRYYAAQARRLLNGPGH-----------KPLGPVVCISPWNFPlaifTGQI----AAALVAGNTVLAK 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 160 HAPNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGV-SQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVL---ELG 235
Cdd:PRK11905 711 PAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETG 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 236 GSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLR 315
Cdd:PRK11905 791 GQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQ 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 316 DELHQQVTATLDEGATLL-LGAEKIEGAGNYYAPTVLcnVTAGMTGFRQELFGPVATLTT--ARDADHALALANDSEFGL 392
Cdd:PRK11905 871 ANIEAHIEAMRAAGRLVHqLPLPAETEKGTFVAPTLI--EIDSISDLEREVFGPVLHVVRfkADELDRVIDDINATGYGL 948
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1623529901 393 SATVYTTDEAQAQRFARELECGGVFLN----GycasdARV---AFGGVKKSGFG 439
Cdd:PRK11905 949 TFGLHSRIDETIAHVTSRIRAGNIYVNrniiG-----AVVgvqPFGGEGLSGTG 997
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
42-420 |
2.86e-26 |
|
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: 110.41 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 42 RQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQArGEVAKSANLCDWYAEHGPAMLATEATLVENNQAVI 121
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFVIYSYRIPHEPGNHLGQGLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 122 -----EYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSARLLGEIFAAAG-LPDGVFGWVNATNDGV 195
Cdd:cd07084 92 qqshgYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKTM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 196 SQIINDDRIAAVTVTGSVRAGKAIGAQAGAAlkKCVLELGGSDPFIVLNDAD-LDEAVKAAVTGRYQNSGQVCAASKR-F 273
Cdd:cd07084 172 QALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMlF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 274 ILEAGIaeafTRKFVDAVAALkMGDPRDEQNYVGPMARFDLrdeLHQQVTATLDEGATLLLG--AEKIEGAGNYYAPTVL 351
Cdd:cd07084 250 VPENWS----KTPLVEKLKAL-LARRKLEDLLLGPVQTFTT---LAMIAHMENLLGSVLLFSgkELKNHSIPSIYGACVA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1623529901 352 CNV-------TAGMTGFRQELFGPVATLTTARD--ADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGVFLNG 420
Cdd:cd07084 322 SALfvpideiLKTYELVTEEIFGPFAIVVEYKKdqLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAGRTYAI 399
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
17-419 |
4.54e-26 |
|
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: 110.39 E-value: 4.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 17 EVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEVAKSANLC 96
Cdd:TIGR01238 63 DIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFC 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 97 DWYAEHGPAMLATEAtlvennqavieYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSARLLGEIFA 176
Cdd:TIGR01238 143 RYYAKQVRDVLGEFS-----------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 177 AAGLPDGVFGWVNATNDGV-SQIINDDRIAAVTVTGSVRAGKAIG---AQAGAALKKCVLELGGSDPFIVLNDADLDEAV 252
Cdd:TIGR01238 212 EAGFPAGTIQLLPGRGADVgAALTSDPRIAGVAFTGSTEVAQLINqtlAQREDAPVPLIAETGGQNAMIVDSTALPEQVV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 253 KAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELH---QQVTATLDEG 329
Cdd:TIGR01238 292 RDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLahiEHMSQTQKKI 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 330 ATLLLGAEKIEGAGNYYAPTV--LCNVTAgmtgFRQELFGPVATLT--TARDADHALALANDSEFGLSATVYTTDEAQAQ 405
Cdd:TIGR01238 372 AQLTLDDSRACQHGTFVAPTLfeLDDIAE----LSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIETTYR 447
|
410
....*....|....
gi 1623529901 406 RFARELECGGVFLN 419
Cdd:TIGR01238 448 WIEKHARVGNCYVN 461
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
119-440 |
9.25e-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: 108.85 E-value: 9.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 119 AVIEYRPLGAILAVMPWNFPV---WQVMRGAVPillAGNSYLLKH---APNvmgSARLLGEIfaaagLP---DG-----V 184
Cdd:cd07132 94 VYIYKEPLGVVLIIGAWNYPLqltLVPLVGAIA---AGNCVVIKPsevSPA---TAKLLAEL-----IPkylDKecypvV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 185 FGWVNATNDGVSQiinddRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQNSG 264
Cdd:cd07132 163 LGGVEETTELLKQ-----RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 265 QVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYvGPMArfdlRDELHQQVTATLdEGATLLLGAEKIEgAGN 344
Cdd:cd07132 238 QTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDY-GRII----NDRHFQRLKKLL-SGGKVAIGGQTDE-KER 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 345 YYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGVflngyCAS 424
Cdd:cd07132 311 YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGV-----CVN 385
|
330 340
....*....|....*....|...
gi 1623529901 425 D-------ARVAFGGVKKSGFGR 440
Cdd:cd07132 386 DtimhytlDSLPFGGVGNSGMGA 408
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
136-411 |
2.50e-23 |
|
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: 102.35 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 136 NFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSARLLGEIFAAAG-LPDGVFGWV-NATNDGVSQIINDDriaAVTVTGSV 213
Cdd:cd07128 155 NFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLIcGSVGDLLDHLGEQD---VVAFTGSA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 214 RAGKAIGAQAGAA------------LKKCVLelgGSDpfIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAE 281
Cdd:cd07128 232 ATAAKLRAHPNIVarsirfnaeadsLNAAIL---GPD--ATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 282 AFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDELHQQVtATLDEGATLLLGA---EKIEGA----GNYYAPTVL-CN 353
Cdd:cd07128 307 AVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGpdrFEVVGAdaekGAFFPPTLLlCD 385
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1623529901 354 VTAGMTGFRQ-ELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFAREL 411
Cdd:cd07128 386 DPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
119-456 |
3.17e-21 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 95.88 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 119 AVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSARLLGEIFAAAGLPDGVF---GWVNATNDGV 195
Cdd:PLN02174 106 AEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRvveGAVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 196 SQiinddRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQ-NSGQVCaASKRFI 274
Cdd:PLN02174 186 EQ-----KWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQAC-ISPDYI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 275 LeagIAEAFTRKFVDAVAalkmgdpRDEQNYVG--PMARFDLRDELHQ----QVTATLDEGAT---LLLGAEKiEGAGNY 345
Cdd:PLN02174 260 L---TTKEYAPKVIDAMK-------KELETFYGknPMESKDMSRIVNSthfdRLSKLLDEKEVsdkIVYGGEK-DRENLK 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 346 YAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGVFLNGYCASD 425
Cdd:PLN02174 329 IAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHL 408
|
330 340 350
....*....|....*....|....*....|...
gi 1623529901 426 A--RVAFGGVKKSGFGRELSHFGLHEFCNAQTV 456
Cdd:PLN02174 409 AlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
4-419 |
2.00e-18 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 88.46 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 4 SATHAVsVNPT-TGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPI 82
Cdd:COG4230 569 GEARPV-RNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTL 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 83 AQARGEVAKSANLCDWYAEhgpamlatEATLVENNQAVieYRPLGAILAVMPWNFP----VWQVmrgaVPILLAGNSYLL 158
Cdd:COG4230 648 PDAIAEVREAVDFCRYYAA--------QARRLFAAPTV--LRGRGVFVCISPWNFPlaifTGQV----AAALAAGNTVLA 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 159 KHAPNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGV-SQIINDDRIAAVTVTGSVRAGKAIG---AQAGAALKKCVLEL 234
Cdd:COG4230 714 KPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVgAALVADPRIAGVAFTGSTETARLINrtlAARDGPIVPLIAET 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 235 GGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDL 314
Cdd:COG4230 794 GGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEA 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 315 RDELHQQVTATLDEG---ATLLLGAEKIEgaGNYYAPTVlcnvtagmtgFR--------QELFGPVATLTT--ARDADHA 381
Cdd:COG4230 874 RANLEAHIERMRAEGrlvHQLPLPEECAN--GTFVAPTL----------IEidsisdleREVFGPVLHVVRykADELDKV 941
|
410 420 430
....*....|....*....|....*....|....*...
gi 1623529901 382 LALANDSEFGLSATVYTTDEAQAQRFARELECGGVFLN 419
Cdd:COG4230 942 IDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
41-440 |
1.89e-17 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 84.39 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 41 YRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQA-RGEV---AKSAN-----LCDWYA-EHGPAMLATe 110
Cdd:PLN02203 19 YESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyRDEVgvlTKSANlalsnLKKWMApKKAKLPLVA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 111 atLVENNQAVIEyrPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGSARLLgeifaAAGLP---DGVFGW 187
Cdd:PLN02203 98 --FPATAEVVPE--PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFL-----AANIPkylDSKAVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 188 VNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKKCVLELGGSDPFIV---LNDADLDEAVKAAVTGRYQN-S 263
Cdd:PLN02203 169 VIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 264 GQVCAASKRFILEagiaEAFTRKFVDAV-AALK--MGDPRDEQNYvgpMARfdLRDELH-QQVTATLDE---GATLLLGA 336
Cdd:PLN02203 249 GQACIAIDYVLVE----ERFAPILIELLkSTIKkfFGENPRESKS---MAR--ILNKKHfQRLSNLLKDprvAASIVHGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 337 eKIEGAGNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFARELECGGV 416
Cdd:PLN02203 320 -SIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV 398
|
410 420
....*....|....*....|....*..
gi 1623529901 417 FLNGYC---ASDArVAFGGVKKSGFGR 440
Cdd:PLN02203 399 TFNDAIiqyACDS-LPFGGVGESGFGR 424
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
136-411 |
2.26e-17 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 84.37 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 136 NFPVWQVMRGAVPILLAGNSYLLKHA-PNVMGSARLLGEIFAAAGLPDGVFGWV-NATNDGVSQIINDDriaAVTVTGSV 213
Cdd:PRK11903 159 NFPAWGLWEKAAPALLAGVPVIVKPAtATAWLTQRMVKDVVAAGILPAGALSVVcGSSAGLLDHLQPFD---VVSFTGSA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 214 RAGKAIGAQAGAA------------LKKCVLeLGGSDPfivlNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAE 281
Cdd:PRK11903 236 ETAAVLRSHPAVVqrsvrvnveadsLNSALL-GPDAAP----GSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYD 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 282 AFTRKFVDAVAALKMGDPRDEQNYVGPMA-RFDLRD------ELHQQVTATLDEGATLLLGAEkiEGAGNYYAPTVL-CN 353
Cdd:PRK11903 311 AVAEALAARLAKTTVGNPRNDGVRMGPLVsRAQLAAvraglaALRAQAEVLFDGGGFALVDAD--PAVAACVGPTLLgAS 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1623529901 354 VTAGMTGFRQ-ELFGPVATLTTARDADHALALANDSEFGLSATVYTTDEAQAQRFAREL 411
Cdd:PRK11903 389 DPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALEL 447
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
11-405 |
3.60e-17 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 84.64 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 11 VNP-TTGEVVSSLPWASEREVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLEMGKPIAQARGEV 89
Cdd:PRK11809 664 INPaDPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEV 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 90 AKSANLCDWYAEHGPAMLATEAtlvennqavieYRPLGAILAVMPWNFPVwQVMRGAVPILLA-GNSYLLKHA---PNVM 165
Cdd:PRK11809 744 REAVDFLRYYAGQVRDDFDNDT-----------HRPLGPVVCISPWNFPL-AIFTGQVAAALAaGNSVLAKPAeqtPLIA 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 166 GSA-RLLGEifaaAGLPDGVFGWVNATNDGV-SQIINDDRIAAVTVTGSVRAGKAIGAQAGAALKK------CVLELGGS 237
Cdd:PRK11809 812 AQAvRILLE----AGVPAGVVQLLPGRGETVgAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPqgrpipLIAETGGQ 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 238 DPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAVAALKMGDPRDEQNYVGPMARFDLRDE 317
Cdd:PRK11809 888 NAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKAN 967
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 318 LHQQVTATLDEGAT---LLLGAEKIEGAGNYYAPTV--LCNVTAgmtgFRQELFGPVatLTTAR----DADHALALANDS 388
Cdd:PRK11809 968 IERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLieLDSFDE----LKREVFGPV--LHVVRynrnQLDELIEQINAS 1041
|
410
....*....|....*...
gi 1623529901 389 EFGLSATVYT-TDEAQAQ 405
Cdd:PRK11809 1042 GYGLTLGVHTrIDETIAQ 1059
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
28-432 |
7.15e-16 |
|
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: 79.20 E-value: 7.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 28 REVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQMITLE--MGKP---IAQARGEVAKSAnlcdwyaeh 102
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEEtgMGRVedkIAKNHLAAEKTP--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 103 GPAMLATEATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNSylLKHAPNVMGSA------RLLGEIFA 176
Cdd:cd07121 75 GTEDLTTTAWSGDNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNA--VVFNPHPGAKKvsayavELINKAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 177 AAGLPDGVFGWVNA-TNDGVSQIINDDRIAAVTVTGsvraGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAA 255
Cdd:cd07121 153 EAGGPDNLVVTVEEpTIETTNELMAHPDINLLVVTG----GPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 256 VTGRYQNSGQVCAASKRFILEAGIAEAFTRKFVDAvAALKMGDPRDEQnyvgpmarfdlrdelhQQVTATLDEG------ 329
Cdd:cd07121 229 VQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQRN-GAYVLNDEQAEQ----------------LLEVVLLTNKgatpnk 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 330 ------ATLLLGAEKIEGAGNyyAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGL--SATVYTTDE 401
Cdd:cd07121 292 kwvgkdASKILKAAGIEVPAD--IRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNV 369
|
410 420 430
....*....|....*....|....*....|.
gi 1623529901 402 AQAQRFARELECGGVFLNGycASDARVAFGG 432
Cdd:cd07121 370 ENLTKMARAMQTTIFVKNG--PSYAGLGVGG 398
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
41-413 |
6.59e-14 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 73.40 E-value: 6.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 41 YRQWRQTPLADRADALRRIGAALRARGEEVAQMITLE--MGkpiaqargevaksaNLCDWYAEH--------GPAMLATE 110
Cdd:PRK15398 49 QQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEEtgMG--------------RVEDKIAKNvaaaektpGVEDLTTE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 111 ATLVENNQAVIEYRPLGAILAVMPWNFPVWQVMRGAVPILLAGNS-YLLKH--APNVmgSA---RLLGEIFAAAGLPDGV 184
Cdd:PRK15398 115 ALTGDNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSvVFSPHpgAKKV--SLraiELLNEAIVAAGGPENL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 185 FGWV-NATNDGVSQIINDDRIAAVTVTGsvraGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQNS 263
Cdd:PRK15398 193 VVTVaEPTIETAQRLMKHPGIALLVVTG----GPAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKGASFDN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 264 GQVCAASKRFILEAGIAEAFTRKFVDAVAALkmgdprdeqnyvgpmarfdLRDELHQQVT-ATLDEG-----------AT 331
Cdd:PRK15398 269 NLPCIAEKEVIVVDSVADELMRLMEKNGAVL-------------------LTAEQAEKLQkVVLKNGgtvnkkwvgkdAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 332 LLLGAEKIEGAGNyyaPTVL-CNVTAGMTGFRQELFGPVATLTTARDADHALALANDSEFGL--SATVYTTDEAQAQRFA 408
Cdd:PRK15398 330 KILEAAGINVPKD---TRLLiVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNKMA 406
|
....*
gi 1623529901 409 RELEC 413
Cdd:PRK15398 407 RAIQT 411
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
120-419 |
1.38e-10 |
|
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: 62.89 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 120 VIEY-RPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGS----ARLLGEIFAAAGLPDGVFGWV-NATND 193
Cdd:cd07122 89 IVEIaEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCsieaAKIMREAAVAAGAPEGLIQWIeEPSIE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 194 GVSQIINDDRIAAVTVTGS---VRA----GK-AIGAQAGAAlkkcvlelggsdPFIVLNDADLDEAVKAAVTGRYQNSGQ 265
Cdd:cd07122 169 LTQELMKHPDVDLILATGGpgmVKAayssGKpAIGVGPGNV------------PAYIDETADIKRAVKDIILSKTFDNGT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 266 VCAASKRFILEAGIAEAFTRKF------------VDAVAALkMGDPRDEQN--YVGPMARfdlrdELHQQVTATLDEGAT 331
Cdd:cd07122 237 ICASEQSVIVDDEIYDEVRAELkrrgayflneeeKEKLEKA-LFDDGGTLNpdIVGKSAQ-----KIAELAGIEVPEDTK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 332 LLLGAEKIEGAGNYYAptvlcnvtagmtgfrQELFGPVATLTTARDADHALALAND----SEFGLSATVYTTDEAQAQRF 407
Cdd:cd07122 311 VLVAEETGVGPEEPLS---------------REKLSPVLAFYRAEDFEEALEKARElleyGGAGHTAVIHSNDEEVIEEF 375
|
330
....*....|..
gi 1623529901 408 ARELECGGVFLN 419
Cdd:cd07122 376 ALRMPVSRILVN 387
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
29-419 |
1.15e-09 |
|
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: 60.57 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 29 EVDAAIALAAAGYRQWRQTPLADRADALRRIGAALRARGEEVAQ----------MITLEMGKPIAQARG---------EV 89
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHavmhttgqafMMAFQAGGPHAQDRGleavayawrEM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 90 AKSANLCDW---YAEHGPAMLATEATLVennqavieyrPLGAILAVMPWNFPVWQVMRGAVPILLAGNSYLLKHAPN--- 163
Cdd:cd07127 165 SRIPPTAEWekpQGKHDPLAMEKTFTVV----------PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAail 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 164 -VMGSARLLGEIFAAAGL-PDGVFGWVNATNDGVSQIINDD-RIAAVTVTGSVRAGKAIGAQAGAALkkCVLELGGSDPF 240
Cdd:cd07127 235 pLAITVQVAREVLAEAGFdPNLVTLAADTPEEPIAQTLATRpEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 241 IVLNDADLDEAVKAAVTGRYQNSGQVCAASKR-FILEAGIAEAFTRKFVDAVAAL-------KMGDPRDEQNYVGPmarf 312
Cdd:cd07127 313 VVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNiYVPRDGIQTDDGRKSFDEVAADlaaaidgLLADPARAAALLGA---- 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 313 dLRDELHQQVTATLDEGATLLLGAEKIEGA----GNYYAPTVLCNVTAGMTGFRQELFGPVATLTTARDADHALALANDS 388
Cdd:cd07127 389 -IQSPDTLARIAEARQLGEVLLASEAVAHPefpdARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARES 467
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1623529901 389 --EFG-LSATVYTTDEA---QAQRFARE----LEC---GGVFLN 419
Cdd:cd07127 468 vrEHGaMTVGVYSTDPEvveRVQEAALDagvaLSInltGGVFVN 511
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
61-287 |
2.33e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 53.04 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 61 AALRARgEEVAQMITLEMG---------KPIAQARGEVAKSanlCDwyaEHGPAMLATEatlvENNQAVIEYRPLGAILA 131
Cdd:cd07081 33 AAEDAR-IDLAKLAVSETGmgrvedkviKNHFAAEYIYNVY---KD---EKTCGVLTGD----ENGGTLIIAEPIGVVAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 132 VMPWNFPVWQVMRGAVPILLAGNSYLLKHAPNVMGS----ARLLGEIFAAAGLPDGVFGWVNATNDGVSQ-IINDDRIAA 206
Cdd:cd07081 102 ITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVtqraATLLLQAAVAAGAPENLIGWIDNPSIELAQrLMKFPGIGL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 207 VTVTGsvraGKAIGAQAGAALKKCVLELGGSDPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRK 286
Cdd:cd07081 182 LLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRL 257
|
.
gi 1623529901 287 F 287
Cdd:cd07081 258 F 258
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
71-406 |
3.30e-04 |
|
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: 42.87 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 71 AQMITLEMGKPIAQARGEVAKSANLCDWYAEHGPAMLATEATLVENNQAVIE--YR-PLGAILAVMPWNF----PVWQVM 143
Cdd:cd07126 85 ARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLARSFNVPGDHQGQQSsgYRwPYGPVAIITPFNFpleiPALQLM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 144 rGAvpiLLAGNSYLLKHAPNVMGSARLLGEIFAAAGLPDGVFGWVNATNDGVSQIINDDRIAAVTVTGSVRAGKAIGAQA 223
Cdd:cd07126 165 -GA---LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAERLALEL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 224 GAALKkcvLELGGSDPFIVLND-ADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAftrKFVDAVAALkmGDPRDE 302
Cdd:cd07126 241 HGKVK---LEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQA---GILDKLKAL--AEQRKL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 303 QNY-VGPMARFDlrdelHQQVTATLDE-----GATLLLGAEKIEGA------GNY-----YAPTVLCNVTAGMTGFRQEL 365
Cdd:cd07126 313 EDLtIGPVLTWT-----TERILDHVDKllaipGAKVLFGGKPLTNHsipsiyGAYeptavFVPLEEIAIEENFELVTTEV 387
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1623529901 366 FGPVATLTTARDA--DHALALANDSEFGLSATVYTTDEAQAQR 406
Cdd:cd07126 388 FGPFQVVTEYKDEqlPLVLEALERMHAHLTAAVVSNDIRFLQE 430
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
167-419 |
6.93e-04 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 42.09 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 167 SARLLGEIFAAAGLPDGVFGW-----VNATNdgvsQIINDDRIAAVTVTGS---VRA----GK-AIGAQAGAAlkkcvle 233
Cdd:PRK13805 154 AAKIVLDAAVAAGAPKDIIQWieepsVELTN----ALMNHPGIALILATGGpgmVKAayssGKpALGVGAGNV------- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 234 lggsdPFIVLNDADLDEAVKAAVTGRYQNSGQVCAASKRFILEAGIAEAFTRKF------------VDAVAALKMGDPRD 301
Cdd:PRK13805 223 -----PAYIDKTADIKRAVNDILLSKTFDNGMICASEQAVIVDDEIYDEVKEEFashgayflnkkeLKKLEKFIFGKENG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623529901 302 EQN--YVGPMARfdlrdELHQQVTATLDEGATLLLGAekIEGAGNYYAptvlcnvtagmtgFRQELFGPVATLTTARDAD 379
Cdd:PRK13805 298 ALNadIVGQSAY-----KIAEMAGFKVPEDTKILIAE--VKGVGESEP-------------LSHEKLSPVLAMYKAKDFE 357
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1623529901 380 HALALA----NDSEFGLSATVYTTDEAQAQRFARELECGGVFLN 419
Cdd:PRK13805 358 DAVEKAeklvEFGGLGHTAVIYTNDDELIKEFGLRMKACRILVN 401
|
|
| |
