|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
1-460 |
0e+00 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 900.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 1 MTYSSATHALSVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMG 80
Cdd:PRK13968 1 MTITPATHAISVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 81 KPIVQARAEVAKSASLCDWYAEHGPAMLRAESTQVEN--AVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLK 158
Cdd:PRK13968 81 KPINQARAEVAKSANLCDWYAEHGPAMLKAEPTLVENqqAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 159 HAPNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 238
Cdd:PRK13968 161 HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 239 FIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELH 318
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 319 QQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTA 398
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1022700636 399 DDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVWKDRV 460
Cdd:PRK13968 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVWKDRI 462
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
31-456 |
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: 664.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 31 VERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAEHGPAMLRA 110
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 111 ESTQVE--NAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSADLIGQAFADAGFPEGVFGWVN 188
Cdd:cd07100 81 EPIETDagKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 189 ATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAA 268
Cdd:cd07100 161 IDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 269 AKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLAEGATLLLGGEKMSGTGNYYAPT 348
Cdd:cd07100 241 AKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 349 VLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECGGVFINGYSASDARVA 428
Cdd:cd07100 321 VLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLP 400
|
410 420
....*....|....*....|....*...
gi 1022700636 429 FGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07100 401 FGGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
11-456 |
1.67e-169 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 484.24 E-value: 1.67e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDWYAEHGPAMLRAESTQVEN-----AVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:PRK09406 85 LKCAKGFRYYAEHAEALLADEPADAAAvgasrAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 166 SADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA 245
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 246 DLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATL 325
Cdd:PRK09406 245 DLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 326 AEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAET 405
Cdd:PRK09406 325 AAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQER 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1022700636 406 FCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:PRK09406 405 FIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVW 455
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
11-455 |
1.51e-157 |
|
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: 453.91 E-value: 1.51e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:pfam00171 11 VINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDWYAEHGPAM--LRAESTQVENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAD 168
Cdd:pfam00171 91 DRAIDVLRYYAGLARRLdgETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 169 LIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 247
Cdd:pfam00171 171 LLAELFEEAGLPAGVLNVVTGSGAEVGEALvEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 248 DLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLAE 327
Cdd:pfam00171 251 DAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 328 GATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFC 407
Cdd:pfam00171 331 GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVA 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1022700636 408 RELECGGVFINGYSASDARVA-FGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:pfam00171 411 RRLEAGMVWINDYTTGDADGLpFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
11-456 |
2.55e-155 |
|
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: 449.19 E-value: 2.55e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:COG1012 25 VINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDWYAEHGPAML---RAESTQVENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSA 167
Cdd:COG1012 105 DRAADFLRYYAGEARRLYgetIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 168 DLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDAD 246
Cdd:COG1012 185 LLLAELLEEAGLPAGVLNVVTGDGSEVGAALvAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 247 LDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLA 326
Cdd:COG1012 265 LDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 327 EGATLLLGGEKMSGT-GNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAET 405
Cdd:COG1012 345 EGAELLTGGRRPDGEgGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARR 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1022700636 406 FCRELECGGVFINGYSAS-DARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:COG1012 425 VARRLEAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKTVT 476
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
12-455 |
6.09e-144 |
|
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: 419.14 E-value: 6.09e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAEHGPamlRAESTQVENA------VIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07103 82 YAASFLEWFAEEAR---RIYGRTIPSPapgkriLVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 166 SADLIGQAFADAGFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEAlCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 245 ADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07103 239 ADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 325 LAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAE 404
Cdd:cd07103 319 VAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1022700636 405 TFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07103 399 RVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
32-456 |
2.50e-136 |
|
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: 398.89 E-value: 2.50e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 32 ERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAEHGPAMLRAE 111
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 112 STQV---ENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSADLIGQAFADAGFPEGVFGWVN 188
Cdd:cd07078 81 IPSPdpgELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 189 ATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCA 267
Cdd:cd07078 161 GDGDEVGAALaSHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 268 AAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLAEGATLLLGGEKMSGT-GNYYA 346
Cdd:cd07078 241 AASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkGYFVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 347 PTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECGGVFINGYSAS-DA 425
Cdd:cd07078 321 PTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGaEP 400
|
410 420 430
....*....|....*....|....*....|.
gi 1022700636 426 RVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07078 401 SAPFGGVKQSGIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
12-456 |
2.19e-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: 349.26 E-value: 2.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07088 18 LNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAEhgpAMLRAE------STQVENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07088 98 FTADYIDYMAE---WARRIEgeiipsDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 166 SADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07088 175 NALEFAELVDEAGLPAGVLNIVTGRGSVVGDALvAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 245 ADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07088 255 ADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 325 LAEGATLLLGGEKMSGT-GNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARA 403
Cdd:cd07088 335 VEAGATLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1022700636 404 ETFCRELECGGVFIN--------GYSAsdarvafgGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07088 415 MRATNELEFGETYINrenfeamqGFHA--------GWKKSGLGGADGKHGLEEYLQTKVVY 467
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
13-449 |
4.01e-115 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 345.47 E-value: 4.01e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 13 NPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAK 92
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 93 S-------ASLCdwYAEHGPAMLRAESTQVENAVieYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07150 85 TpellraaAGEC--RRVRGETLPSDSPGTVSMSV--RRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 166 SADLIGQAFADAGFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDElVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 245 ADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 325 LAEGATLLLGGEkmsGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAE 404
Cdd:cd07150 321 VAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAF 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1022700636 405 TFCRELECGGVFINGYSASD-ARVAFGGVKKSGFGRELSHFGLHEF 449
Cdd:cd07150 398 KLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEF 443
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
30-457 |
2.75e-114 |
|
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: 342.59 E-value: 2.75e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 30 DVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAE-----HG 104
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGlprrpEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 105 pAMLRAESTQVENAVIEyRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN--VLGsADLIGQAFADAGFPEG 182
Cdd:cd07104 81 -EILPSDVPGKESMVRR-VPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRtpVTG-GLLIAEIFEEAGLPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 183 VFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAVAGRYQN 261
Cdd:cd07104 158 VLNVVPGGGSEIGDAlVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 262 TGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLAEGATLLLGGEkmsGT 341
Cdd:cd07104 238 QGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT---YE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 342 GNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECGGVFINGYS 421
Cdd:cd07104 315 GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQT 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 1022700636 422 ASD-ARVAFGGVKKSGFGRELSHFGLHEFcnvqTVWK 457
Cdd:cd07104 395 VNDePHVPFGGVKASGGGRFGGPASLEEF----TEWQ 427
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-455 |
8.57e-112 |
|
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: 337.55 E-value: 8.57e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07138 19 INPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAAQV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSAslcdwyAEHGPAMLRA-----ESTQVENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLK---HAPnv 163
Cdd:cd07138 99 GLG------IGHLRAAADAlkdfeFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKpseVAP-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 164 lGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAIND-RRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVL 242
Cdd:cd07138 171 -LSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAhPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIIL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 243 NDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQ 322
Cdd:cd07138 250 DDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 323 ATLAEGATLLLGG-EKMSG--TGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTAD 399
Cdd:cd07138 330 KGIEEGARLVAGGpGRPEGleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSAD 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1022700636 400 DARAETFCRELECGGVFINGySASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07138 410 PERARAVARRLRAGQVHING-AAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
12-455 |
1.24e-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: 1.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAEHGPAMLRAESTQVEN------AVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRKVPTGLlmpnkkATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 166 SADLIGQAFADAGFPEGVFGWVnaTNDG-VSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVV--TGDGaTGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 245 ADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07099 239 ADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 325 LAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAE 404
Cdd:cd07099 319 VAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAE 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1022700636 405 TFCRELECGGVFIN--GYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07099 399 AIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
12-455 |
5.03e-109 |
|
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: 330.08 E-value: 5.03e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07145 4 RNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAEHGPaMLRAESTQVEN--------AVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNV 163
Cdd:cd07145 84 RTIRLFKLAAEEAK-VLRGETIPVDAyeynerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 164 LGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVL 242
Cdd:cd07145 163 PLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIvTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 243 NDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQ 322
Cdd:cd07145 243 KDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 323 ATLAEGATLLLGGEKMSgtGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDAR 402
Cdd:cd07145 323 DAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1022700636 403 AETFCRELECGGVFINGYSA--SDArVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07145 401 ALKVARELEAGGVVINDSTRfrWDN-LPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
12-449 |
5.26e-108 |
|
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: 327.28 E-value: 5.26e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAEHGPAMLrAESTQVENA----VIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSA 167
Cdd:cd07102 81 GMLERARYMISIAEEAL-ADIRVPEKDgferYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 168 DLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 247
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 248 DLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLAE 327
Cdd:cd07102 240 DAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 328 GATLLLGGEKMS---GTGNYYAPTVLGGVTPEMTAFRQELFGPVAAI-TVANDaAHALQLANDSDFGLSATVFTADDARA 403
Cdd:cd07102 320 GARALIDGALFPedkAGGAYLAPTVLTNVDHSMRVMREETFGPVVGImKVKSD-AEAIALMNDSEYGLTASVWTKDIARA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1022700636 404 ETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEF 449
Cdd:cd07102 399 EALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQL 444
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
13-455 |
6.75e-107 |
|
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: 324.55 E-value: 6.75e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 13 NPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAK 92
Cdd:cd07149 5 SPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 93 SASLCDWYAE-----HG---P--AMLRAESTQvenAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN 162
Cdd:cd07149 85 AIETLRLSAEeakrlAGetiPfdASPGGEGRI---GFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 163 VLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGaaLKKCVLELGGSDPFIV 241
Cdd:cd07149 162 TPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALvTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 242 LNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQV 321
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 322 QATLAEGATLLLGGEKMsgtGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDA 401
Cdd:cd07149 320 EEAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQ 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1022700636 402 RAETFCRELECGGVFINGysASDARV---AFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07149 397 KALKAARELEVGGVMIND--SSTFRVdhmPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
11-456 |
1.45e-106 |
|
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: 323.78 E-value: 1.45e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGF--RQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARA 88
Cdd:cd07112 6 TINPATGRVLAEVAACDAADVDRAVAAARRAFesGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 89 -EVAKSASLCDWYAE-----------HGPAMLraestqvenAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYL 156
Cdd:cd07112 86 vDVPSAANTFRWYAEaidkvygevapTGPDAL---------ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 157 LKHAPNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI---NDrrIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLE 232
Cdd:cd07112 157 LKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALglhMD--VDALAFTGSTEVGRRFLEYSGQSnLKRVWLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 233 LGGSDPFIVLNDA-DLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARF 311
Cdd:cd07112 235 CGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 312 DLRDELHQQVQATLAEGATLLLGGEK-MSGTGNYYA-PTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDF 389
Cdd:cd07112 315 AHFDKVLGYIESGKAEGARLVAGGKRvLTETGGFFVePTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVY 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1022700636 390 GLSATVFTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07112 395 GLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTW 461
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
11-455 |
2.92e-106 |
|
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: 322.98 E-value: 2.92e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARA-E 89
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 90 VAKSASLCDWYAEHGPaMLRAESTQVENAVIEY---RPLGPILAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHAPN 162
Cdd:cd07093 81 IPRAAANFRFFADYIL-QLDGESYPQDGGALNYvlrQPVGVAGLITPWNLPLmlltWKI----APALAFGNTVVLKPSEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 163 VLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV 241
Cdd:cd07093 156 TPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALvAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 242 LNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQV 321
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 322 QATLAEGATLLLGGEKMS----GTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFT 397
Cdd:cd07093 316 ELARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1022700636 398 ADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07093 396 RDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
12-455 |
3.92e-106 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 323.95 E-value: 3.92e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:PLN02278 45 YNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAEHGpamLRAESTQVENAVIEYR------PLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:PLN02278 125 YGASFLEYFAEEA---KRVYGDIIPSPFPDRRllvlkqPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 166 SADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIA-AVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:PLN02278 202 TALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVrKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDD 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 245 ADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQAT 324
Cdd:PLN02278 282 ADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 325 LAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAE 404
Cdd:PLN02278 362 VSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAW 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1022700636 405 TFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PLN02278 442 RVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
11-455 |
9.27e-106 |
|
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: 322.28 E-value: 9.27e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPA-TGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAE 89
Cdd:cd07097 18 NRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 90 VAKSASLCDWYAEHGpamLR-----AESTQVENAVIEYR-PLGPILAVMPWNFPL----WQvlrgAVPILLAGNSYLLKH 159
Cdd:cd07097 98 VTRAGQIFRYYAGEA---LRlsgetLPSTRPGVEVETTRePLGVVGLITPWNFPIaipaWK----IAPALAYGNTVVFKP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 160 APNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 238
Cdd:cd07097 171 AELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALvEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 239 FIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELH 318
Cdd:cd07097 251 LVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 319 QQVQATLAEGATLLLGGEKMSGT--GNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVF 396
Cdd:cd07097 331 RYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIV 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1022700636 397 TADDARAETFCRELECGGVFINGYSAS-DARVAFGGVKKSGFG-RELSHFGLHEFCNVQTV 455
Cdd:cd07097 411 TTSLKHATHFKRRVEAGVVMVNLPTAGvDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
11-456 |
2.03e-105 |
|
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: 320.65 E-value: 2.03e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQ--WRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARA 88
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 89 EVAKSASLCDWYAehgpAMLRAestqVENAVI-----------EYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLL 157
Cdd:cd07114 81 QVRYLAEWYRYYA----GLADK----IEGAVIpvdkgdylnftRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 158 K---HAPnvlGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAIND-RRIAAVTVTGSVRAGAAIGAQAGAALKKCVLEL 233
Cdd:cd07114 153 KpseHTP---ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEhPLVAKIAFTGGTETGRHIARAAAENLAPVTLEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 234 GGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDL 313
Cdd:cd07114 230 GGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 314 RDELHQQVQATLAEGATLLLGGEKMSGT----GNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDF 389
Cdd:cd07114 310 LEKVERYVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEY 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1022700636 390 GLSATVFTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07114 390 GLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVW 456
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
12-456 |
4.82e-104 |
|
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: 316.78 E-value: 4.82e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAEhgpaMLRAESTQVENA----VIEYRPLGPILAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHAPNV 163
Cdd:cd07106 82 GAVAWLRYTAS----LDLPDEVIEDDDtrrvELRRKPLGVVAAIVPWNFPLllaaWKI----APALLAGNTVVLKPSPFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 164 LGSADLIGQAFADAgFPEGVfgwVNATNDG--VSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 240
Cdd:cd07106 154 PLCTLKLGELAQEV-LPPGV---LNVVSGGdeLGPALtSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 241 VLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPM---ARFDLRDEL 317
Cdd:cd07106 230 VLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVqnkMQYDKVKEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 318 HQQVQatlAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFT 397
Cdd:cd07106 310 VEDAK---AKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWS 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1022700636 398 ADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07106 387 SDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVIN 445
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
12-455 |
1.77e-101 |
|
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: 311.05 E-value: 1.77e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGF--RQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPI-VQARA 88
Cdd:cd07139 19 VSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPIsWSRRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 89 EVAKSASLCDWYAEHGPAML---RAESTQVENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07139 99 QGPGPAALLRYYAALARDFPfeeRRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 166 SADLIGQAFADAGFPEGVFGWVNATNDgVSQA-INDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07139 179 DAYLLAEAAEEAGLPPGVVNVVPADRE-VGEYlVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 245 ADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07139 258 ADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 325 LAEGATLLLGGEKMSG--TGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDAR 402
Cdd:cd07139 338 RAEGARLVTGGGRPAGldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVER 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1022700636 403 AETFCRELECGGVFINGYSaSDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07139 418 GLAVARRIRTGTVGVNGFR-LDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
38-457 |
4.45e-100 |
|
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: 304.15 E-value: 4.45e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 38 ADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAEHGPAMLRAESTQV-- 115
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPdp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 116 -ENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSADLIGQAFADAGFPEGVFGWVNATNDGV 194
Cdd:cd06534 83 gGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 195 SQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFI 273
Cdd:cd06534 163 GAALlSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 274 VEAGVAEAFTQRFVdavaalkmgapdeeenyigpmarfdlrdelhqqvqatlaegatlllggekmsgtgnyyapTVLGGV 353
Cdd:cd06534 243 VHESIYDEFVEKLV------------------------------------------------------------TVLVDV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 354 TPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECGGVFINGYSA-SDARVAFGGV 432
Cdd:cd06534 263 DPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGV 342
|
410 420
....*....|....*....|....*
gi 1022700636 433 KKSGFGRELSHFGLHEFCNVQTVWK 457
Cdd:cd06534 343 KNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
12-440 |
7.55e-100 |
|
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: 306.48 E-value: 7.55e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAE-----HGPAMLRAESTQVEN--AVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVL 164
Cdd:cd07147 84 RAIDTFRIAAEeatriYGEVLPLDISARGEGrqGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 165 GSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSvrAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07147 164 LSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGS--PAVGWDLKARAGKKKVVLELGGNAAVIVDSD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 245 ADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07147 242 ADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 325 LAEGATLLLGGEKmsgTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAE 404
Cdd:cd07147 322 VDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKAL 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 1022700636 405 TFCRELECGGVFINGYSAsdARV---AFGGVKKSGFGRE 440
Cdd:cd07147 399 RAWDELEVGGVVINDVPT--FRVdhmPYGGVKDSGIGRE 435
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
11-456 |
6.56e-98 |
|
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: 302.34 E-value: 6.56e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSA-WPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAE 89
Cdd:cd07131 18 SRNPADLEEVVGtFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 90 VAKSASLCDWYAEHGpAMLRAESTQVE----NAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07131 98 VQEAIDMAQYAAGEG-RRLFGETVPSElpnkDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 166 SADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDR-RIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07131 177 CALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 245 ADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07131 257 ADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 325 LAEGATLLLGGEKMSG----TGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADD 400
Cdd:cd07131 337 KEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDV 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1022700636 401 ARAETFCRELECGGVFINGYS-ASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07131 417 NKAFRARRDLEAGITYVNAPTiGAEVHLPFGGVKKSGNGHREAGTTALDAFTEWKAV 473
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
12-455 |
1.38e-97 |
|
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: 300.70 E-value: 1.38e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQ--WRREGiVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARA- 88
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTgdWSTDA-EERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 89 EVAKSASLCDWYAEH----------GPAMLRAESTQvenAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLK 158
Cdd:cd07089 81 QVDGPIGHLRYFADLadsfpwefdlPVPALRGGPGR---RVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 159 HAPNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSD 237
Cdd:cd07089 158 PAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALtTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 238 PFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDEL 317
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 318 HQQVQATLAEGATLLLGGEKMSG--TGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATV 395
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 396 FTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
14-455 |
4.29e-96 |
|
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: 296.94 E-value: 4.29e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 14 PATGETLSAWPWATSQDVERAIALADAGFRQ--WRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDW------------YAEHGPAMLraestqvenAVIEYRPLGPILAVMPWNFPLWqVLRGAVP-ILLAGNSYLLK 158
Cdd:cd07118 84 GAADLWRYaaslartlhgdsYNNLGDDML---------GLVLREPIGVVGIITPWNFPFL-ILSQKLPfALAAGCTVVVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 159 HAPNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSD 237
Cdd:cd07118 154 PSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMtEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 238 PFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDEL 317
Cdd:cd07118 234 PQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 318 HQQVQATLAEGATLLLGGEKMS-GTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVF 396
Cdd:cd07118 314 TDYVDAGRAEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVW 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1022700636 397 TADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07118 394 SKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
12-455 |
4.53e-96 |
|
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: 296.91 E-value: 4.53e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07151 15 LNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAEHGPAM----LRAESTQVENAVieYR-PLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN--VL 164
Cdd:cd07151 95 AAMAITREAATFPLRMegriLPSDVPGKENRV--YRePLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDtpIT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 165 GSAdLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAV-TVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 243
Cdd:cd07151 173 GGL-LLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLiSFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 244 DADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQA 323
Cdd:cd07151 252 DADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 324 TLAEGATLLLGGEKmsgTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARA 403
Cdd:cd07151 332 AVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERG 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1022700636 404 ETFCRELECGGVFINGYSASD-ARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07151 409 VQFARRIDAGMTHINDQPVNDePHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
12-459 |
5.64e-96 |
|
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: 296.90 E-value: 5.64e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQAR-AEV 90
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDWYAEHGPAMLRAESTQV------ENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVL 164
Cdd:cd07098 81 LVTCEKIRWTLKHGEKALRPESRPGgllmfyKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 165 GSA----DLIGQAFADAGFPEG----VFGWVNATNDGVSQAINDRriaaVTVTGSVRAGAAIGAQAGAALKKCVLELGGS 236
Cdd:cd07098 161 WSSgfflSIIRECLAACGHDPDlvqlVTCLPETAEALTSHPVIDH----ITFIGSPPVGKKVMAAAAESLTPVVLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 237 DPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDE 316
Cdd:cd07098 237 DPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 317 LHQQVQATLAEGATLLLGGEKMSGT----GNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLS 392
Cdd:cd07098 317 LEELVADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1022700636 393 ATVFTADDARAETFCRELECGGVFINGYSASDARVA--FGGVKKSGFGRELSHFGLHEFCNVQTVWKDR 459
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQlpFGGVKGSGFGRFAGEEGLRGLCNPKSVTEDR 465
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
11-455 |
4.76e-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: 291.45 E-value: 4.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQ-WRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAE 89
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 90 VAKSASLCDWYAehGPA-MLRAESTQVENAVIEY---RPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07109 81 VEAAARYFEYYG--GAAdKLHGETIPLGPGYFVYtvrEPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 166 SADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALvAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 245 ADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYiGPMARFDLRDELHQQVQAT 324
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDL-GPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 325 LAEGATLLLGGEKMSGT---GNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDA 401
Cdd:cd07109 318 RARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1022700636 402 RAETFCRELECGGVFINGYSASDA-RVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07109 398 RALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
13-440 |
1.13e-93 |
|
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: 290.74 E-value: 1.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 13 NPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAK 92
Cdd:cd07090 3 EPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 93 SASLCDWYAEHGPAmLRAESTQVENAVIEY---RPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSADL 169
Cdd:cd07090 83 SADCLEYYAGLAPT-LSGEHVPLPGGSFAYtrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 170 IGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDL 249
Cdd:cd07090 162 LAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLEN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 250 AVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLAEGA 329
Cdd:cd07090 242 AVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 330 TLLLGGEKMSGT-----GNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAE 404
Cdd:cd07090 322 KVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAH 401
|
410 420 430
....*....|....*....|....*....|....*.
gi 1022700636 405 TFCRELECGGVFINGYSASDARVAFGGVKKSGFGRE 440
Cdd:cd07090 402 RVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRE 437
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
12-455 |
2.88e-93 |
|
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: 289.33 E-value: 2.88e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KS--------ASLCDWYAEHGPAMLRAESTQvENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNV 163
Cdd:cd07094 84 RAidtlrlaaEEAERIRGEEIPLDATQGSDN-RLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 164 LGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVraGAAIGAQAGAALKKCVLELGGSDPFIVL 242
Cdd:cd07094 163 PLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFaADERVAMLSFTGSA--AVGEALRANAGGKRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 243 NDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQ 322
Cdd:cd07094 241 RDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 323 ATLAEGATLLLGGEKmsgTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDAR 402
Cdd:cd07094 321 EAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1022700636 403 AETFCRELECGGVFINGYSASDA-RVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07094 398 AFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
30-455 |
3.29e-93 |
|
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: 288.71 E-value: 3.29e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 30 DVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAEHGPAmLR 109
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQ-II 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 110 AESTQVEN----AVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSADLIGQAFADAGFPEGVFG 185
Cdd:cd07105 80 GGSIPSDKpgtlAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 186 WV-NATNDG---VSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAVAGRYQN 261
Cdd:cd07105 160 VVtHSPEDApevVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 262 TGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGApdeeeNYIGPMARFDLRDELHQQVQATLAEGATLLLGG-EKMSG 340
Cdd:cd07105 240 SGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlADESP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 341 TGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECGGVFINGY 420
Cdd:cd07105 315 SGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGM 394
|
410 420 430
....*....|....*....|....*....|....*.
gi 1022700636 421 SASD-ARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07105 395 TVHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
11-440 |
1.02e-92 |
|
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: 288.69 E-value: 1.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:cd07086 17 SRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDWYAE-----HGPAMlraESTQVENAVIE-YRPLGPILAVMPWNFP----LWQvlrgAVPILLAGNSYLLKHA 160
Cdd:cd07086 97 QEMIDICDYAVGlsrmlYGLTI---PSERPGHRLMEqWNPLGVVGVITAFNFPvavpGWN----AAIALVCGNTVVWKPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 161 PNV----LGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGS 236
Cdd:cd07086 170 ETTpltaIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 237 DPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPmarfdLRDE 316
Cdd:cd07086 250 NAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP-----LINQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 317 LH-QQVQATLA----EGATLLLGGEKMSGT--GNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDF 389
Cdd:cd07086 325 AAvEKYLNAIEiaksQGGTVLTGGKRIDGGepGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQ 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1022700636 390 GLSATVFTADDARAETFCR--ELECGGVFINGySASDARV--AFGGVKKSGFGRE 440
Cdd:cd07086 405 GLSSSIFTEDLREAFRWLGpkGSDCGIVNVNI-PTSGAEIggAFGGEKETGGGRE 458
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
11-456 |
3.02e-92 |
|
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: 287.03 E-value: 3.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQAR-AE 89
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 90 VAKSASLCDWYAehGPA-MLRAESTQVENAVIEY---RPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07115 81 VPRAADTFRYYA--GWAdKIEGEVIPVRGPFLNYtvrEPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 166 SADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALvEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 245 ADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 325 LAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAE 404
Cdd:cd07115 319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1022700636 405 TFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07115 399 RVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVW 450
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
12-455 |
3.71e-92 |
|
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: 286.53 E-value: 3.71e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARA-EV 90
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDWYA---EHGPAMLRAESTQVENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSA 167
Cdd:cd07092 82 PGAVDNFRFFAgaaRTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 168 DLIGQAFADaGFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDAD 246
Cdd:cd07092 162 LLLAELAAE-VLPPGVVNVVCGGGASAGDAlVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 247 LDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDelhqQVQATLA 326
Cdd:cd07092 241 LDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRE----RVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 327 ---EGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARA 403
Cdd:cd07092 317 rapAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1022700636 404 ETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07092 397 MRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
12-449 |
5.58e-92 |
|
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: 285.86 E-value: 5.58e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:TIGR01780 2 YNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAEHGPAML--RAESTQVENAVIEYR-PLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAD 168
Cdd:TIGR01780 82 YAASFLEWFAEEAKRVYgdTIPSPQSDKRLIVIKqPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 169 LIGQAFADAGFPEGVFGWVnaTNDGVSQAIN----DRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:TIGR01780 162 ALARLAEQAGIPKGVLNVI--TGSRAKEVGNvlttSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 245 ADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQAT 324
Cdd:TIGR01780 240 ADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 325 LAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAE 404
Cdd:TIGR01780 320 VEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIW 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1022700636 405 TFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEF 449
Cdd:TIGR01780 400 RVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEY 444
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
12-455 |
7.52e-92 |
|
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: 285.78 E-value: 7.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07110 2 INPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAEHGPAMLRAESTQVE------NAVIEYRPLGPILAVMPWNFPL----WQVlrgaVPILLAGNSYLLKhaP 161
Cdd:cd07110 82 DVAGCFEYYADLAEQLDAKAERAVPlpsedfKARVRREPVGVVGLITPWNFPLlmaaWKV----APALAAGCTVVLK--P 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 162 NVLGSadLIGQAFAD----AGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGS 236
Cdd:cd07110 156 SELTS--LTELELAEiaaeAGLPPGVLNVVTGTGDEAGAPLaAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 237 DPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDE 316
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 317 LHQQVQATLAEGATLLLGGEKMS--GTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSAT 394
Cdd:cd07110 314 VLSFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1022700636 395 VFTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07110 394 VISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
11-455 |
2.51e-91 |
|
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: 285.26 E-value: 2.51e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGI--VHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQ-AR 87
Cdd:cd07091 23 TINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIERDRDELAALESLDNGKPLEEsAK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 88 AEVAKSASLCDWYAehGPA-MLRAESTQVENAVIEY---RPLGPILAVMPWNFPL----WQVlrgaVPILLAGNSYLLKH 159
Cdd:cd07091 103 GDVALSIKCLRYYA--GWAdKIQGKTIPIDGNFLAYtrrEPIGVCGQIIPWNFPLlmlaWKL----APALAAGNTVVLKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 160 APNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAA-IGAQAGAALKKCVLELGGSD 237
Cdd:cd07091 177 AEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAIsSHMDVDKIAFTGSTAVGRTiMEAAAKSNLKKVTLELGGKS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 238 PFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDEL 317
Cdd:cd07091 257 PNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 318 HQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFT 397
Cdd:cd07091 337 LSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFT 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1022700636 398 ADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07091 417 KDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
12-456 |
6.00e-91 |
|
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: 284.59 E-value: 6.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQ--WRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAE 89
Cdd:cd07119 18 INPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEID 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 90 VAKSASLCDWYA-----EHGPAMLRAESTQvenAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVL 164
Cdd:cd07119 98 IDDVANCFRYYAglatkETGEVYDVPPHVI---SRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 165 GSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 243
Cdd:cd07119 175 LTTIALFELIEEAGLPAGVVNLVTGSGATVGAELaESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 244 DADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQA 323
Cdd:cd07119 255 DADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 324 TLAEGATLLLGGEKMSG----TGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTAD 399
Cdd:cd07119 335 GKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKD 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1022700636 400 DARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07119 415 IARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHIN 471
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
12-455 |
5.40e-90 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 281.80 E-value: 5.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARA-EV 90
Cdd:PRK13473 22 YNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNdEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDWYAE-----HGPA----------MLRAEstqvenavieyrPLGPILAVMPWNFPL----WQVLrgavPILLA 151
Cdd:PRK13473 102 PAIVDVFRFFAGaarclEGKAageyleghtsMIRRD------------PVGVVASIAPWNYPLmmaaWKLA----PALAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 152 GNSYLLKHAPNVLGSADLIGQAFADAgFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAAIGAQAGAALKKCV 230
Cdd:PRK13473 166 GNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDAlVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 231 LELGGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMAR 310
Cdd:PRK13473 245 LELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLIS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 311 FDLRDELHQQVQATLAEG-ATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDF 389
Cdd:PRK13473 325 AAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDY 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1022700636 390 GLSATVFTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PRK13473 405 GLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
11-438 |
1.03e-87 |
|
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: 276.80 E-value: 1.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPA-TGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAE 89
Cdd:cd07124 50 SRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADAD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 90 VAKSASLCDWYAEHgpaMLRAESTQVENAVIE-----YRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVL 164
Cdd:cd07124 130 VAEAIDFLEYYARE---MLRLRGFPVEMVPGEdnryvYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 165 GSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVR------AGAAIGAQAGAALKKCVLELGGSD 237
Cdd:cd07124 207 VIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLvEHPDVRFIAFTGSREvglriyERAAKVQPGQKWLKRVIAEMGGKN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 238 PFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDEL 317
Cdd:cd07124 287 AIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 318 HQQVQATLAEGaTLLLGGEKM-SGTGNYY-APTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATV 395
Cdd:cd07124 367 RRYIEIGKSEG-RLLLGGEVLeLAAEGYFvQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGV 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1022700636 396 FTADDARAETFCRELECGGVFIN--GYSASDARVAFGGVKKSGFG 438
Cdd:cd07124 446 FSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGTG 490
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
4-440 |
3.12e-87 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 274.84 E-value: 3.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 4 SSATHALSVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPI 83
Cdd:PRK13252 19 TSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 84 VQAR-AEVAKSASLCDWYAEHGPAmLRAESTQVENAVIEY---RPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKH 159
Cdd:PRK13252 99 QETSvVDIVTGADVLEYYAGLAPA-LEGEQIPLRGGSFVYtrrEPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 160 APNVLGSADLIGQAFADAGFPEGVFGWVNATNDgVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 238
Cdd:PRK13252 178 SEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLtEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 239 FIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELH 318
Cdd:PRK13252 257 LIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 319 QQVQATLAEGATLLLGGEKMS----GTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSAT 394
Cdd:PRK13252 337 GYIEKGKAEGARLLCGGERLTeggfANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAG 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1022700636 395 VFTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRE 440
Cdd:PRK13252 417 VFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRE 462
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
13-440 |
1.96e-86 |
|
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: 272.52 E-value: 1.96e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 13 NPATGETLSAWPWATSQDVERAIALA-DAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07082 22 SPIDGEVIGSVPALSALEILEAAETAyDAGRGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAE-----HGPAMLRAESTQVEN--AVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKhaPNVL 164
Cdd:cd07082 102 RTIDYIRDTIEelkrlDGDSLPGDWFPGTKGkiAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFK--PATQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 165 GS--ADLIGQAFADAGFPEGVFGWVnaTNDG---VSQAINDRRIAAVTVTGSVRAGAAIGAQAGaaLKKCVLELGGSDPF 239
Cdd:cd07082 180 GVllGIPLAEAFHDAGFPKGVVNVV--TGRGreiGDPLVTHGRIDVISFTGSTEVGNRLKKQHP--MKRLVLELGGKDPA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 240 IVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQ 319
Cdd:cd07082 256 IVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 320 QVQATLAEGATLLLGGEKMsgTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTAD 399
Cdd:cd07082 336 LIDDAVAKGATVLNGGGRE--GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKD 413
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1022700636 400 DARAETFCRELECGGVFINGYSASDARV-AFGGVKKSGFGRE 440
Cdd:cd07082 414 INKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQ 455
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
14-455 |
7.77e-86 |
|
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: 270.33 E-value: 7.77e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 14 PATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAKS 93
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 94 ASLCDWYAEHGPAMLRAESTQ-----VENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAD 168
Cdd:cd07101 83 AIVARYYARRAERLLKPRRRRgaipvLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 169 LIGQAFADAGFPEGVFGWVNATNDGVSQAINDRrIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLD 248
Cdd:cd07101 163 WAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN-ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 249 LAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLAEG 328
Cdd:cd07101 242 KAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 329 ATLLLGGEKMSGTGNY-YAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFC 407
Cdd:cd07101 322 ATVLAGGRARPDLGPYfYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1022700636 408 RELECGGVFIN-GYSASDARVA--FGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07101 402 ARLRAGTVNVNeGYAAAWASIDapMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
17-438 |
3.03e-85 |
|
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: 268.39 E-value: 3.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 17 GETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAKSASL 96
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 97 CDWYAE-----HGpAMLRAESTQVENAviEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN--VLGSAdL 169
Cdd:cd07152 81 LHEAAGlptqpQG-EILPSAPGRLSLA--RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRtpVSGGV-V 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 170 IGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDL 249
Cdd:cd07152 157 IARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 250 AVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLAEGA 329
Cdd:cd07152 237 AASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 330 TLLLGGEKmsgTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRE 409
Cdd:cd07152 317 RLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADR 393
|
410 420 430
....*....|....*....|....*....|
gi 1022700636 410 LECGGVFINGYSASDARVA-FGGVKKSGFG 438
Cdd:cd07152 394 LRTGMLHINDQTVNDEPHNpFGGMGASGNG 423
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
12-455 |
5.70e-84 |
|
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: 265.38 E-value: 5.70e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALAdAGFR----QWRREGIVHRAQKLrdlgtaLRSRAEEMAQTISREMGKPIVQAR 87
Cdd:cd07146 4 RNPYTGEVVGTVPAGTEEALREALALA-ASYRstltRYQRSAILNKAAAL------LEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 88 AEVAKSASLCDWYAEHGpamLR----------AESTQVENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLL 157
Cdd:cd07146 77 YEVGRAADVLRFAAAEA---LRddgesfscdlTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 158 KHAPNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAAIGAQAGaaLKKCVLELGGS 236
Cdd:cd07146 154 KPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDElITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 237 DPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDE 316
Cdd:cd07146 232 DPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 317 LHQQVQATLAEGATLLLGGEKmsgTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVF 396
Cdd:cd07146 312 IENRVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVC 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1022700636 397 TADDARAETFCRELECGGVFIN---GYSASdaRVAFGGVKKSGFG-RELSHFGLHEFCNVQTV 455
Cdd:cd07146 389 TNDLDTIKRLVERLDVGTVNVNevpGFRSE--LSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
57-456 |
4.09e-83 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 261.98 E-value: 4.09e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 57 LRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAEHGPamlRAESTQV------ENAVIEYRPLGPILA 130
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWAR---RYEGEIIqsdrpgENILLFKRALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 131 VMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVT 209
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELaGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 210 GSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDA 289
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 290 VAALKMGAPDEEENY-IGPMARFDLRDELHQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPV 368
Cdd:PRK10090 238 MQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 369 AAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHE 448
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHE 397
|
....*...
gi 1022700636 449 FCNVQTVW 456
Cdd:PRK10090 398 YLQTQVVY 405
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
11-446 |
6.80e-82 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 261.19 E-value: 6.80e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRRE-GIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQ-ARA 88
Cdd:cd07144 27 TVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnALG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 89 EVAKSASLCDWYAehGPA-MLRAESTQVENAVIEY---RPLGPILAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHA 160
Cdd:cd07144 107 DLDEIIAVIRYYA--GWAdKIQGKTIPTSPNKLAYtlhEPYGVCGQIIPWNYPLamaaWKL----APALAAGNTVVIKPA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 161 PNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 239
Cdd:cd07144 181 ENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALaEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 240 IVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVA-ALKMGAPDEEENYIGPMARFDLRDELH 318
Cdd:cd07144 261 LVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQVSKTQYDRVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 319 QQVQATLAEGATLLLGGEKMS---GTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATV 395
Cdd:cd07144 341 SYIEKGKKEGAKLVYGGEKAPeglGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAV 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1022700636 396 FTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGL 446
Cdd:cd07144 421 FTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGL 471
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
11-456 |
2.48e-81 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 258.84 E-value: 2.48e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDWYAEHGPaMLRAESTQVENAVIEY---RPLGPILAVMPWNFP-LWQVLRGAVPiLLAGNSYLLKHAPNVLGS 166
Cdd:cd07107 81 MVAAALLDYFAGLVT-ELKGETIPVGGRNLHYtlrEPYGVVARIVAFNHPlMFAAAKIAAP-LAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 167 ADLIGQAFADAgFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA 245
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALvRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 246 DLDLAVSAAVAG-RYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07107 238 DPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 325 LAEGATLLLGGEKMSGT----GNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADD 400
Cdd:cd07107 318 KREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1022700636 401 ARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVN 453
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
12-455 |
9.66e-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: 257.84 E-value: 9.66e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFR-QWRRE-GIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQ-ARA 88
Cdd:cd07143 27 YNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWGLKvSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTaKRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 89 EVAKSASLCDWYA-----EHGPAMlraESTQVENAVIEYRPLGPILAVMPWNFPL----WQVlrgaVPILLAGNSYLLKH 159
Cdd:cd07143 107 DVQASADTFRYYGgwadkIHGQVI---ETDIKKLTYTRHEPIGVCGQIIPWNFPLlmcaWKI----APALAAGNTIVLKP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 160 APNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDR-RIAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGGSD 237
Cdd:cd07143 180 SELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHmDIDKVAFTGSTLVgRKVMEAAAKSNLKKVTLELGGKS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 238 PFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDEL 317
Cdd:cd07143 260 PNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 318 HQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFT 397
Cdd:cd07143 340 MSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFT 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1022700636 398 ADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07143 420 NNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
14-455 |
1.61e-80 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 258.65 E-value: 1.61e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 14 PATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAKS 93
Cdd:PRK09407 39 PFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 94 ASLCDWYAEHGPAMLRAESTQ-----VENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLK----HAPNVL 164
Cdd:PRK09407 119 ALTARYYARRAPKLLAPRRRAgalpvLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKpdsqTPLTAL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 165 GSADLIgqafADAGFPEGVFGWVNATNDGVSQAINDRrIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:PRK09407 199 AAVELL----YEAGLPRDLWQVVTGPGPVVGTALVDN-ADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 245 ADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQAT 324
Cdd:PRK09407 274 ADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 325 LAEGATLLLGGEKMSGTGNY-YAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARA 403
Cdd:PRK09407 354 VAKGATVLAGGKARPDLGPLfYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARG 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1022700636 404 ETFCRELECGGVFIN-GYSASDARVA--FGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PRK09407 434 RAIAARIRAGTVNVNeGYAAAWGSVDapMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
12-455 |
1.83e-79 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 255.43 E-value: 1.83e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGF-----RQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQA 86
Cdd:PLN02467 28 VNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 87 RAEVAKSASLCDWYAEHGPAMLRAESTQVENAVIEYR------PLGPILAVMPWNFPL----WQVlrgaVPILLAGNSYL 156
Cdd:PLN02467 108 AWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKgyvlkePLGVVGLITPWNYPLlmatWKV----APALAAGCTAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 157 LKhaPNVLGSADL--IGQAFADAGFPEGVFGWVNATNDGVSQAINDR-RIAAVTVTGSVRAGAAIGAQAGAALKKCVLEL 233
Cdd:PLN02467 184 LK--PSELASVTCleLADICREVGLPPGVLNVVTGLGTEAGAPLASHpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLEL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 234 GGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDL 313
Cdd:PLN02467 262 GGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 314 RDELHQQVQATLAEGATLLLGGEKMSG--TGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGL 391
Cdd:PLN02467 342 YEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGL 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1022700636 392 SATVFTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PLN02467 422 AGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
4-438 |
3.56e-79 |
|
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: 253.59 E-value: 3.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 4 SSATHALSV-NPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQ---KLRDLgtaLRSRAEEMAQTISREM 79
Cdd:cd07085 12 SKTTEWLDVyNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQvmfKFRQL---LEENLDELARLITLEH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 80 GKPIVQARAEVAKSASLCDwYAEHGPAMLRAEST-QVENAVIEY---RPLGPILAVMPWNFP----LWQVlrgavPILLA 151
Cdd:cd07085 89 GKTLADARGDVLRGLEVVE-FACSIPHLLKGEYLeNVARGIDTYsyrQPLGVVAGITPFNFPamipLWMF-----PMAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 152 -GNSYLLKHAPNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCV 230
Cdd:cd07085 163 cGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 231 LELGGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMAR 310
Cdd:cd07085 243 ALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVIS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 311 FDLRDELHQQVQATLAEGATLLLGGE--KMSG--TGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLAND 386
Cdd:cd07085 323 PAAKERIEGLIESGVEEGAKLVLDGRgvKVPGyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINA 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1022700636 387 SDFGLSATVFTADDARAETFCRELECGGVFIN-GYSASDARVAFGGVKKSGFG 438
Cdd:cd07085 403 NPYGNGAAIFTRSGAAARKFQREVDAGMVGINvPIPVPLAFFSFGGWKGSFFG 455
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
13-453 |
4.20e-78 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 251.36 E-value: 4.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 13 NPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAK 92
Cdd:PRK11241 32 NPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 93 SASLCDWYAEHGPAM----LRAESTQVENAVIEyRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAD 168
Cdd:PRK11241 112 AASFIEWFAEEGKRIygdtIPGHQADKRLIVIK-QPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSAL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 169 LIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIA-AVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 247
Cdd:PRK11241 191 ALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVrKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 248 DLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLAE 327
Cdd:PRK11241 271 DKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 328 GATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFC 407
Cdd:PRK11241 351 GARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVG 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1022700636 408 RELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQ 453
Cdd:PRK11241 431 EALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
13-455 |
7.66e-78 |
|
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: 249.59 E-value: 7.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 13 NPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPI-VQARAEVA 91
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAEHGPAmLRAESTQVENAVIEY---RPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAD 168
Cdd:cd07108 83 VLADLFRYFGGLAGE-LKGETLPFGPDVLTYtvrEPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 169 LIGQAFADAgFPEGVFGWVNATNDGVSQAINDRR-IAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 247
Cdd:cd07108 162 LLAEILAQV-LPAGVLNVITGYGEECGAALVDHPdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 248 DLAVSAAVAG-RYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMarfdLRDELHQQVQATLA 326
Cdd:cd07108 241 DDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAI----ISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 327 EG-----ATLLLGG----EKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFT 397
Cdd:cd07108 317 LGlstsgATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWT 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1022700636 398 ADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFG-LHEFCNVQTV 455
Cdd:cd07108 397 RDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
12-455 |
1.03e-75 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 244.66 E-value: 1.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGI-VHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARA-E 89
Cdd:cd07113 20 TNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTpAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 90 VAKSASLCDWYAEHG------------PAMLRAESTqvenAVIEYRPLGPILAVMPWNFPL----WQVLrgavPILLAGN 153
Cdd:cd07113 100 VGQSANFLRYFAGWAtkingetlapsiPSMQGERYT----AFTRREPVGVVAGIVPWNFSVmiavWKIG----AALATGC 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 154 SYLLKhaPNVLGSADL--IGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVL 231
Cdd:cd07113 172 TIVIK--PSEFTPLTLlrVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 232 ELGGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARF 311
Cdd:cd07113 250 ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 312 DLRDELHQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGL 391
Cdd:cd07113 330 PHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGL 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1022700636 392 SATVFTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07113 410 TASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
11-444 |
2.95e-75 |
|
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: 243.79 E-value: 2.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQAR-AE 89
Cdd:cd07559 20 NYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLaAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 90 VAKSASLCDWYAehgpAMLRAESTQV----EN--AVIEYRPLGPILAVMPWNFPL----WQVlrgaVPILLAGNSYLLKH 159
Cdd:cd07559 100 IPLAIDHFRYFA----GVIRAQEGSLseidEDtlSYHFHEPLGVVGQIIPWNFPLlmaaWKL----APALAAGNTVVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 160 AP----NVLGSADLIGQAFadagfPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELG 234
Cdd:cd07559 172 ASqtplSILVLMELIGDLL-----PKGVVNVVTGFGSEAGKPLaSHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 235 GSDPFIVLNDA-----DLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMA 309
Cdd:cd07559 247 GKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 310 RFDLRDELHQQVQATLAEGATLLLGGEKMSGT----GNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLAN 385
Cdd:cd07559 327 SKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIAN 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1022700636 386 DSDFGLSATVFTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRE-----LSHF 444
Cdd:cd07559 407 DTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGREthkmmLDHY 470
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
11-455 |
2.50e-74 |
|
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: 240.32 E-value: 2.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFR--QWRREGIVhRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARA 88
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 89 EVAKSASLCDWYAehgpAMLRAE---STQVEN---AVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN 162
Cdd:cd07120 80 EISGAISELRYYA----GLARTEagrMIEPEPgsfSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 163 VLGSADLIGQAFADA-GFPEGVfgwVNATNDGVSQA----INDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSD 237
Cdd:cd07120 156 TAQINAAIIRILAEIpSLPAGV---VNLFTESGSEGaahlVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 238 PFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDEL 317
Cdd:cd07120 233 PCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 318 HQQVQATLAEGATLLLGGEKMSGT---GNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSAT 394
Cdd:cd07120 313 DRMVERAIAAGAEVVLRGGPVTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1022700636 395 VFTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07120 393 VWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
11-456 |
4.99e-73 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 238.26 E-value: 4.99e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQ--WRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQA-R 87
Cdd:PRK09847 39 TVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 88 AEVAKSASLCDWYAE-----HGPAmlrAESTQVENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN 162
Cdd:PRK09847 119 DDIPGAARAIRWYAEaidkvYGEV---ATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 163 VLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI---NDrrIAAVTVTGSVRAGAAIGAQA-GAALKKCVLELGGSDP 238
Cdd:PRK09847 196 SPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALsrhND--IDAIAFTGSTRTGKQLLKDAgDSNMKRVWLEAGGKSA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 239 FIVLNDA-DLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDEL 317
Cdd:PRK09847 274 NIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 318 HQQVQATLAEGaTLLLGGEKmSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFT 397
Cdd:PRK09847 354 HSFIREGESKG-QLLLDGRN-AGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWT 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1022700636 398 ADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:PRK09847 432 RDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIW 490
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
11-455 |
9.07e-71 |
|
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: 232.00 E-value: 9.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQ--WRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQAR- 87
Cdd:cd07142 23 TIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 88 AEVAKSASLCDWYAE-----HGPAMlraESTQVENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN 162
Cdd:cd07142 103 AEVPLAARLFRYYAGwadkiHGMTL---PADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 163 VLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRR-IAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGGSDPFI 240
Cdd:cd07142 180 TPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMdVDKVAFTGSTEVgKIIMQLAAKSNLKPVTLELGGKSPFI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 241 VLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQ 320
Cdd:cd07142 260 VCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 321 VQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADD 400
Cdd:cd07142 340 IEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNI 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1022700636 401 ARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07142 420 DTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
12-455 |
9.20e-71 |
|
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: 231.85 E-value: 9.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQ---WRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARA 88
Cdd:cd07141 27 INPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 89 ----EVAKSASLCDWYAE--HGpamlraESTQVENAVIEY---RPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKH 159
Cdd:cd07141 107 vdlpGAIKVLRYYAGWADkiHG------KTIPMDGDFFTYtrhEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 160 APNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDR-RIAAVTVTGSVRAGAA-IGAQAGAALKKCVLELGGSD 237
Cdd:cd07141 181 AEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHpDIDKVAFTGSTEVGKLiQQAAGKSNLKRVTLELGGKS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 238 PFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDEL 317
Cdd:cd07141 261 PNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 318 HQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFT 397
Cdd:cd07141 341 LELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFT 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1022700636 398 ADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07141 421 KDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
11-449 |
1.67e-68 |
|
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: 226.12 E-value: 1.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQAR-AE 89
Cdd:cd07111 41 TINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRdCD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 90 VAKSASLCDWYAehGPAMLRaestqvENAVIEYRPLGPILAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07111 121 IPLVARHFYHHA--GWAQLL------DTELAGWKPVGVVGQIVPWNFPLlmlaWKI----CPALAMGNTVVLKPAEYTPL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 166 SADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA 245
Cdd:cd07111 189 TALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 246 DLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATL 325
Cdd:cd07111 269 DLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 326 AEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAET 405
Cdd:cd07111 349 AEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALE 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1022700636 406 FCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEF 449
Cdd:cd07111 429 VALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
11-440 |
3.53e-68 |
|
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: 225.03 E-value: 3.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARA-E 89
Cdd:cd07117 20 SYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 90 VAKSASLCDWYAehgpAMLRAESTQV------ENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKhaPNV 163
Cdd:cd07117 100 IPLAADHFRYFA----GVIRAEEGSAnmidedTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIK--PSS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 164 LGSADL--IGQAFADAgFPEGVFGWVNATNDGVSQAINDRR-IAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 240
Cdd:cd07117 174 TTSLSLleLAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 241 VLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQ 320
Cdd:cd07117 253 IFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 321 VQATLAEGATLLLGGEKMSGT----GNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVF 396
Cdd:cd07117 333 VDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVF 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1022700636 397 TADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRE 440
Cdd:cd07117 413 TKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRE 456
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
30-444 |
1.87e-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: 1.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 30 DVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEV----AKSASLCDWYAEHGP 105
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVaamaGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 106 amLRAESTQVENAVIEYRPLGPILAVMPWNFPLwQVLRGA-VPILLAGNSYLLK---HAPNVlgsADLIGQAFADAGFPE 181
Cdd:cd07095 81 --ERATPMAQGRAVLRHRPHGVMAVFGPFNFPG-HLPNGHiVPALLAGNTVVFKpseLTPAV---AELMVELWEEAGLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 182 GVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCV-LELGGSDPFIVLNDADLDLAVSAAVAGRYQ 260
Cdd:cd07095 155 GVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLIVQSAFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 261 NTGQVCAAAKRFIVEAG-VAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLAEGATLLLGGEKMS 339
Cdd:cd07095 235 TAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 340 GTGNYYAPTVLggvtpEMTAFR----QELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECGGV 415
Cdd:cd07095 315 AGTAFLSPGII-----DVTDAAdvpdEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIV 389
|
410 420 430
....*....|....*....|....*....|..
gi 1022700636 416 FIN---GYSASDArvAFGGVKKSGFGRELSHF 444
Cdd:cd07095 390 NWNrptTGASSTA--PFGGVGLSGNHRPSAYY 419
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
11-455 |
2.30e-66 |
|
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: 220.44 E-value: 2.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFR--QWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQA-R 87
Cdd:cd07140 25 TINPTDGSVICKVSLATVEDVDRAVAAAKEAFEngEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLAlK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 88 AEVAKS-------ASLCDwyAEHGPAMLRAESTQVENAVIEYR-PLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKH 159
Cdd:cd07140 105 THVGMSiqtfryfAGWCD--KIQGKTIPINQARPNRNLTLTKRePIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 160 APNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDR-RIAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGGSD 237
Cdd:cd07140 183 AQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHpDVRKLGFTGSTPIgKHIMKSCAVSNLKKVSLELGGKS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 238 PFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDEL 317
Cdd:cd07140 263 PLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 318 HQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDA--AHALQLANDSDFGLSATV 395
Cdd:cd07140 343 VEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEYGLASGV 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 396 FTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07140 423 FTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
11-436 |
8.32e-65 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 217.11 E-value: 8.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPA-TGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAE 89
Cdd:PRK03137 54 SINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 90 VAKSASLCDWYAEHgpaMLR-AESTQVENAVIE-----YRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNV 163
Cdd:PRK03137 134 TAEAIDFLEYYARQ---MLKlADGKPVESRPGEhnryfYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 164 LGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDR-RIAAVTVTGS------VRAGAAIGAQAGAALKKCVLELGGS 236
Cdd:PRK03137 211 PVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHpKTRFITFTGSrevglrIYERAAKVQPGQIWLKRVIAEMGGK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 237 DPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPdEEENYIGPMARFDLRDE 316
Cdd:PRK03137 291 DAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNAYMGPVINQASFDK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 317 LHQQVQATLAEGaTLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVF 396
Cdd:PRK03137 370 IMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVI 448
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1022700636 397 TADDARAETFCRELECGGVFIN--------GYSasdarvAFGGVKKSG 436
Cdd:PRK03137 449 SNNREHLEKARREFHVGNLYFNrgctgaivGYH------PFGGFNMSG 490
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
11-440 |
7.96e-61 |
|
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: 205.52 E-value: 7.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:cd07130 16 SISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDwYAE------HGPAMlraESTQVENAVIE-YRPLGPILAVMPWNFPL----WQvlrgAVPILLAGNSYLLKH 159
Cdd:cd07130 96 QEMIDICD-FAVglsrqlYGLTI---PSERPGHRMMEqWNPLGVVGVITAFNFPVavwgWN----AAIALVCGNVVVWKP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 160 APNV----LGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGG 235
Cdd:cd07130 168 SPTTpltaIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 236 SDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRD 315
Cdd:cd07130 248 NNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 316 ELHQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGvTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATV 395
Cdd:cd07130 328 NYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEG-LSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSI 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1022700636 396 FTADDARAETFCREL--ECGGVFIN-GYSASDARVAFGGVKKSGFGRE 440
Cdd:cd07130 407 FTTDLRNAFRWLGPKgsDCGIVNVNiGTSGAEIGGAFGGEKETGGGRE 454
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
11-444 |
7.70e-58 |
|
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: 198.06 E-value: 7.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIvqaRAEV 90
Cdd:cd07116 20 NITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPV---RETL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDWYAEHGPAMLRAES---TQVENAVIEY---RPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVL 164
Cdd:cd07116 97 AADIPLAIDHFRYFAGCIRAQEgsiSEIDENTVAYhfhEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 165 GSADLIGQAFADAgFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI--- 240
Cdd:cd07116 177 ASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLaSSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIffa 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 241 -VLN--DADLDLAVSAAVAGRYqNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDEL 317
Cdd:cd07116 256 dVMDadDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 318 HQQVQATLAEGATLLLGGEKMSGTGN----YYAPTVLGGvTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSA 393
Cdd:cd07116 335 LSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGA 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1022700636 394 TVFTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRE-----LSHF 444
Cdd:cd07116 414 GVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGREnhkmmLDHY 469
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
11-455 |
9.90e-58 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 198.12 E-value: 9.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQ--WRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARA 88
Cdd:PLN02766 40 TRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 89 -EVAKSASLCDWYAehGPA-MLRAESTQVENAVIEY---RPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNV 163
Cdd:PLN02766 120 vDIPAAAGLLRYYA--GAAdKIHGETLKMSRQLQGYtlkEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 164 LGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRR-IAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGGSDPFIV 241
Cdd:PLN02766 198 PLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMdVDKVSFTGSTEVgRKIMQAAATSNLKQVSLELGGKSPLLI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 242 LNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQV 321
Cdd:PLN02766 278 FDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 322 QATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDA 401
Cdd:PLN02766 358 EHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLD 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1022700636 402 RAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PLN02766 438 VANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
12-455 |
4.77e-56 |
|
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: 193.95 E-value: 4.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGE-TLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:cd07125 51 IDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDWY---AEHGPAMLRAESTQVENAVIEYRPLGPILAVMPWNFPLwqvlrgAVPI------LLAGNSYLLKHAP 161
Cdd:cd07125 131 REAIDFCRYYaaqARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPL------AIFTgqiaaaLAAGNTVIAKPAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 162 NVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAA---IGAQAGAALKKCVLELGGSD 237
Cdd:cd07125 205 QTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEAlVAHPRIDGVIFTGSTETAKLinrALAERDGPILPLIAETGGKN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 238 PFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDEL 317
Cdd:cd07125 285 AMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 318 HQQVQatLAEGATLLLGGEKMS-GTGNYYAPTVLGGVTPEmtAFRQELFGPVAAITVA--NDAAHALQLANDSDFGLSAT 394
Cdd:cd07125 365 RAHTE--LMRGEAWLIAPAPLDdGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFkaEDLDEAIEDINATGYGLTLG 440
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1022700636 395 VFTADDARAETFCRELECGGVFIN----GysASDARVAFGGVKKSGFGREL--SHFgLHEFCNVQTV 455
Cdd:cd07125 441 IHSRDEREIEYWRERVEAGNLYINrnitG--AIVGRQPFGGWGLSGTGPKAggPNY-LLRFGNEKTV 504
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
11-455 |
2.21e-55 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 192.72 E-value: 2.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQ--WRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQAR- 87
Cdd:PLN02466 77 TLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAk 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 88 AEVAKSASLCDWYAE-----HGPAMLRAESTQVEnavIEYRPLGPILAVMPWNFPL----WQVlrgaVPILLAGNSYLLK 158
Cdd:PLN02466 157 AELPMFARLFRYYAGwadkiHGLTVPADGPHHVQ---TLHEPIGVAGQIIPWNFPLlmfaWKV----GPALACGNTIVLK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 159 HAPNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRR-IAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGGS 236
Cdd:PLN02466 230 TAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMdVDKLAFTGSTDTgKIVLELAAKSNLKPVTLELGGK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 237 DPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRfvdAVA-ALK--MGAPDEEENYIGPMARFDL 313
Cdd:PLN02466 310 SPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK---AKArALKrvVGDPFKKGVEQGPQIDSEQ 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 314 RDELHQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSA 393
Cdd:PLN02466 387 FEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAA 466
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1022700636 394 TVFTADDARAETFCRELECGGVFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PLN02466 467 GVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
12-458 |
6.87e-55 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 192.65 E-value: 6.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:PLN02419 134 INPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIF 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLcdwyAEHGPAMLRAESTQ----VENAVIEY---RPLGPILAVMPWNFP----LWQVlrgavPILLA-GNSYLLKH 159
Cdd:PLN02419 214 RGLEV----VEHACGMATLQMGEylpnVSNGVDTYsirEPLGVCAGICPFNFPamipLWMF-----PVAVTcGNTFILKP 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 160 APNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 239
Cdd:PLN02419 285 SEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 240 IVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRfIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQ 319
Cdd:PLN02419 365 LVLPDANIDATLNALLAAGFGAAGQRCMALST-VVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 320 QVQATLAEGATLLLGGEKMS----GTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATV 395
Cdd:PLN02419 444 LIQSGVDDGAKLLLDGRDIVvpgyEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAI 523
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 396 FTADDARAETFCRELECGGVFIN-GYSASDARVAFGGvKKSGFGRELSHF---GLHEFCNVQTV---WKD 458
Cdd:PLN02419 524 FTSSGAAARKFQMDIEAGQIGINvPIPVPLPFFSFTG-NKASFAGDLNFYgkaGVDFFTQIKLVtqkQKD 592
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
8-438 |
1.40e-54 |
|
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: 189.71 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 8 HALSVNP-ATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQA 86
Cdd:cd07083 33 RMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 87 RAEVAKSASLCDWYAEH-----GPAMLRAESTQVENAVIeYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAP 161
Cdd:cd07083 113 IDDVAEAIDFIRYYARAalrlrYPAVEVVPYPGEDNESF-YVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 162 NVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRA------GAAIGAQAGAALKKCVLELG 234
Cdd:cd07083 192 DAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLtEHERIRGINFTGSLETgkkiyeAAARLAPGQTWFKRLYVETG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 235 GSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLR 314
Cdd:cd07083 272 GKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 315 DELHQQVQATLAEGaTLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITV--ANDAAHALQLANDSDFGLS 392
Cdd:cd07083 352 AKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRykDDDFAEALEVANSTPYGLT 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1022700636 393 ATVFTADDARAETFCRELECGGVFINGYS--ASDARVAFGGVKKSGFG 438
Cdd:cd07083 431 GGVYSRKREHLEEARREFHVGNLYINRKItgALVGVQPFGGFKLSGTN 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
13-438 |
1.89e-54 |
|
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: 188.94 E-value: 1.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 13 NPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAK 92
Cdd:TIGR01722 22 NPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 93 SASLCDwYAEHGPAMLRAE-STQVENAVIEY---RPLGPILAVMPWNF----PLWQvlrgaVPILLA-GNSYLLKHAPNV 163
Cdd:TIGR01722 102 GLEVVE-HACGVNSLLKGEtSTQVATRVDVYsirQPLGVCAGITPFNFpamiPLWM-----FPIAIAcGNTFVLKPSEKV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 164 LGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 243
Cdd:TIGR01722 176 PSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 244 DADLDLAVSAAVAGRYQNTGQVCAAAKRfIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQA 323
Cdd:TIGR01722 256 DADKDAAADALVGAAYGAAGQRCMAISA-AVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 324 TLAEGATLLLGGE--KMSG--TGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTAD 399
Cdd:TIGR01722 335 GAAEGAEVLLDGRgyKVDGyeEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRD 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1022700636 400 DARAETFCRELECGGVFIN-------GYsasdarVAFGGVKKSGFG 438
Cdd:TIGR01722 415 GAAARRFQHEIEVGQVGVNvpipvplPY------FSFTGWKDSFFG 454
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
11-436 |
6.58e-51 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 179.38 E-value: 6.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:PRK09457 19 SRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 A----KSASLCDWYAEHGPAmlRAESTQVENAVIEYRPLGpILAVM-PWNFPlwqvlrG------AVPILLAGNSYLLK- 158
Cdd:PRK09457 99 TaminKIAISIQAYHERTGE--KRSEMADGAAVLRHRPHG-VVAVFgPYNFP------GhlpnghIVPALLAGNTVVFKp 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 159 --HAPNVlgsADLIGQAFADAGFPEGVFGWVNATND-GVSQAiNDRRIAAVTVTGSVRAGAAIGAQAGAALKKCV-LELG 234
Cdd:PRK09457 170 seLTPWV---AELTVKLWQQAGLPAGVLNLVQGGREtGKALA-AHPDIDGLLFTGSANTGYLLHRQFAGQPEKILaLEMG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 235 GSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGV-AEAFTQRFVDAVAALKMGAPDEE-ENYIGPMARFD 312
Cdd:PRK09457 246 GNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWDAEpQPFMGAVISEQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 313 LRDELHQQVQATLAEGATLLLGGEKMSGTgnyyaptvLGGVTP---EMTAFR----QELFGPVAAITVANDAAHALQLAN 385
Cdd:PRK09457 326 AAQGLVAAQAQLLALGGKSLLEMTQLQAG--------TGLLTPgiiDVTGVAelpdEEYFGPLLQVVRYDDFDEAIRLAN 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1022700636 386 DSDFGLSATVFTADDARAETFCRELECGGVF----INGySASDArvAFGGVKKSG 436
Cdd:PRK09457 398 NTRFGLSAGLLSDDREDYDQFLLEIRAGIVNwnkpLTG-ASSAA--PFGGVGASG 449
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
12-438 |
1.71e-50 |
|
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: 177.61 E-value: 1.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVH-RAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWLPAHeRIAILERLADLMEERADELALLIAREGGKPLVDAKVEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDWYAE-------HGPAMLRAESTQVENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNV 163
Cdd:cd07148 84 TRAIDGVELAADelgqlggREIPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 164 LGSAdligQAFAD----AGFPEGvfgWVNAT---NDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAAlKKCVLELGGS 236
Cdd:cd07148 164 PLSC----LAFVDllheAGLPEG---WCQAVpceNAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 237 DPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDE 316
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 317 LHQQVQATLAEGATLLLGGEKMSGTgnYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVF 396
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRLSDT--TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1022700636 397 TADDARAETFCRELECGGVFINGYSAsdARV---AFGGVKKSGFG 438
Cdd:cd07148 394 TKDLDVALKAVRRLDATAVMVNDHTA--FRVdwmPFAGRRQSGYG 436
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
12-438 |
5.79e-48 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 171.86 E-value: 5.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:PLN00412 36 TNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 92 KSASLCDWYAEHGPAMLRAESTQVENA----------VIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKhaP 161
Cdd:PLN00412 116 RSGDLISYTAEEGVRILGEGKFLVSDSfpgnernkycLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLK--P 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 162 NVLG--SADLIGQAFADAGFPEGVFGWVNatndGVSQAIND-----RRIAAVTVTGSVRAGAAIGAQAGAALKkcvLELG 234
Cdd:PLN00412 194 PTQGavAALHMVHCFHLAGFPKGLISCVT----GKGSEIGDfltmhPGVNCISFTGGDTGIAISKKAGMVPLQ---MELG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 235 GSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPdEEENYIGPMARFDLR 314
Cdd:PLN00412 267 GKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDITPVVSESSA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 315 DELHQQVQATLAEGATLLlggEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSAT 394
Cdd:PLN00412 346 NFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGC 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1022700636 395 VFTADDARAETFCRELECGGVFINGYSASDA-RVAFGGVKKSGFG 438
Cdd:PLN00412 423 VFTRDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIG 467
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
11-440 |
1.73e-44 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 162.70 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 11 SVNPATGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:PLN02315 38 SVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDwYAEHGPAMLRAE---STQVENAVIE-YRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNV--- 163
Cdd:PLN02315 118 QEIIDMCD-FAVGLSRQLNGSiipSERPNHMMMEvWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTpli 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 164 -LGSADLIGQAFADAGFPEGVFGWVNATNDgVSQAIN-DRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV 241
Cdd:PLN02315 197 tIAMTKLVAEVLEKNNLPGAIFTSFCGGAE-IGEAIAkDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 242 LNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQV 321
Cdd:PLN02315 276 MDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 322 QATLAEGATLLLGGEKMSGTGNYYAPTVLgGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTaddA 401
Cdd:PLN02315 356 EIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFT---R 431
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1022700636 402 RAETFCREL-----ECGGVFIN-GYSASDARVAFGGVKKSGFGRE 440
Cdd:PLN02315 432 NPETIFKWIgplgsDCGIVNVNiPTNGAEIGGAFGGEKATGGGRE 476
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
32-457 |
9.14e-42 |
|
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: 153.54 E-value: 9.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 32 ERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPivqaRAEVAKS-------------ASLCD 98
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP----AAEVDLTeilpvlseinhaiKHLKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 99 WYAEH--GPAMLRAEStqveNAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLK------HAPNVLgsADLI 170
Cdd:cd07134 77 WMKPKrvRTPLLLFGT----KSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKpseltpHTSAVI--AKII 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 171 GQAFAdagfPEGVF---GWVNatndgVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 247
Cdd:cd07134 151 REAFD----EDEVAvfeGDAE-----VAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 248 DLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAAL--KMGAPDEEENY---IGPMARFDLRDELHQQVq 322
Cdd:cd07134 222 KKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFygKDAARKASPDLariVNDRHFDRLKGLLDDAV- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 323 atlAEGATLLLGGEkMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDAR 402
Cdd:cd07134 301 ---AKGAKVEFGGQ-FDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKAN 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1022700636 403 AETFCRELECGGVFINGYSA--SDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVWK 457
Cdd:cd07134 377 VNKVLARTSSGGVVVNDVVLhfLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
42-455 |
8.73e-40 |
|
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: 148.06 E-value: 8.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 42 FRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQAR-AEVAKSASLCDWYAEHGPAMLRAES------TQ 114
Cdd:cd07087 11 FLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAVVLGEIDHALKHLKKWMKPRRvsvpllLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 115 VENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLK---HAPNVlgsADLIGQAFADAgFPEGVFGWVNATN 191
Cdd:cd07087 91 PAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKpseLAPAT---SALLAKLIPKY-FDPEAVAVVEGGV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 192 DgVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKR 271
Cdd:cd07087 167 E-VATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 272 FIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYigpmARfdLRDELHQQVQATLAEGATLLLGGEkMSGTGNYYAPTVLG 351
Cdd:cd07087 246 VLVHESIKDELIEELKKAIKEFYGEDPKESPDY----GR--IINERHFDRLASLLDDGKVVIGGQ-VDKEERYIAPTILD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 352 GVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECGGVFING--YSASDARVAF 429
Cdd:cd07087 319 DVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDvlLHAAIPNLPF 398
|
410 420
....*....|....*....|....*.
gi 1022700636 430 GGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07087 399 GGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
30-455 |
5.09e-39 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 146.21 E-value: 5.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 30 DVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQAR-AEVAKSASLCDWYAEHGPAML 108
Cdd:cd07135 6 EIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKNLKKWA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 109 RAESTQVE-------NAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLK---HAPN---VLgsADLIGQAFA 175
Cdd:cd07135 86 KDEKVKDGplafmfgKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKpseLTPHtaaLL--AELVPKYLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 176 DAGFpEGVFGWVNATNdgvsqAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAV 255
Cdd:cd07135 164 PDAF-QVVQGGVPETT-----ALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 256 AGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYiGPMARFDLRDELHQQVQATlaeGATLLLGG 335
Cdd:cd07135 238 WGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDY-TRIVNPRHFNRLKSLLDTT---KGKVVIGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 336 EkMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECGGV 415
Cdd:cd07135 314 E-MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1022700636 416 FING----YSASDArvAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07135 393 VINDtlihVGVDNA--PFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
12-436 |
1.72e-31 |
|
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: 126.55 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPAT-GETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQ---KLRDLgTALRSRAEEMAQTisreM---GKPIV 84
Cdd:cd07123 51 VMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAiflKAADL-LSGKYRYELNAAT----MlgqGKNVW 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 85 QAraEVAKSASLCDW------YAE--------HGPAmlraestQVENAViEYRPL-GPILAVMPWNFPLWQVLRGAVPIL 149
Cdd:cd07123 126 QA--EIDAACELIDFlrfnvkYAEelyaqqplSSPA-------GVWNRL-EYRPLeGFVYAVSPFNFTAIGGNLAGAPAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 150 LaGNSYLLKHAPNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALK- 227
Cdd:cd07123 196 M-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVlASPHLAGLHFTGSTPTFKSLWKQIGENLDr 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 228 -----KCVLELGGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEE 302
Cdd:cd07123 275 yrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 303 NYIGPM---ARFD-LRDELHqqvQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDA- 377
Cdd:cd07123 355 NFMGAVideKAFDrIKGYID---HAKSDPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSd 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1022700636 378 -AHALQLAND-SDFGLSATVFTADDARAETFCRELE--CGGVFINGYSaSDARVA---FGGVKKSG 436
Cdd:cd07123 432 fEETLELVDTtSPYALTGAIFAQDRKAIREATDALRnaAGNFYINDKP-TGAVVGqqpFGGARASG 496
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
53-438 |
8.00e-28 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 115.51 E-value: 8.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 53 RAQKLRDLGTALRSRAEEMAQTISREMGKPIVQAR-AEVAKSASLCDWYAEHGPAMLRAESTQVENAV------IEYRPL 125
Cdd:PTZ00381 31 RKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmTEVLLTVAEIEHLLKHLDEYLKPEKVDTVGVFgpgksyIIPEPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 126 GPILAVMPWNFPLWQVLRGAVPILLAGNSYLLK---HAPNvlgSADLIGQAFaDAGFPEGVFGWVNaTNDGVSQAINDRR 202
Cdd:PTZ00381 111 GVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKpseLSPH---TSKLMAKLL-TKYLDPSYVRVIE-GGVEVTTELLKEP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 203 IAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAF 282
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 283 TQRFVDAVAALkMGA-PDEEENYigpmARFDLRDELHQQVQATLAEGATLLLGGEkMSGTGNYYAPTVLGGVTPEMTAFR 361
Cdd:PTZ00381 266 IEALKEAIKEF-FGEdPKKSEDY----SRIVNEFHTKRLAELIKDHGGKVVYGGE-VDIENKYVAPTIIVNPDLDSPLMQ 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1022700636 362 QELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECGGVFING--YSASDARVAFGGVKKSGFG 438
Cdd:PTZ00381 340 EEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDcvFHLLNPNLPFGGVGNSGMG 418
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
26-418 |
1.45e-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: 111.93 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 26 ATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAEHGP 105
Cdd:TIGR01238 71 ANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 106 AMLRAEStqvenavieYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNvlgSADLIGQAFA---DAGFPEG 182
Cdd:TIGR01238 151 DVLGEFS---------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQ---TSLIAYRAVElmqEAGFPAG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 183 VFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVL---ELGGSDPFIVLNDADLDLAVSAAVAGR 258
Cdd:TIGR01238 219 TIQLLPGRGADVGAALtSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPliaETGGQNAMIVDSTALPEQVVRDVLRSA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 259 YQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLAEGAT---LLLGG 335
Cdd:TIGR01238 299 FDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKiaqLTLDD 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 336 EKMSGTGNYYAPTVLGgvTPEMTAFRQELFGPVAAITV--ANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECG 413
Cdd:TIGR01238 379 SRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRykARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVG 456
|
....*
gi 1022700636 414 GVFIN 418
Cdd:TIGR01238 457 NCYVN 461
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
44-455 |
1.80e-26 |
|
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: 111.04 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 44 QWRREGIV---HRAQKLRDLGTALRSRAEEMAQTISREMG-KPIVQAR-AEVAKSASLCDWYAEHGPAMLRAESTQVE-- 116
Cdd:cd07133 10 AFLANPPPsleERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLlAEILPSIAGIKHARKHLKKWMKPSRRHVGll 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 117 ----NAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLK---HAPN--------------------VLGSADl 169
Cdd:cd07133 90 flpaKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKpseFTPRtsallaellaeyfdedevavVTGGAD- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 170 IGQAFADAGFPEGVF-GwvnATNDG--VSQAindrriAA---VTVTgsvragaaigaqagaalkkcvLELGGSDPFIVLN 243
Cdd:cd07133 169 VAAAFSSLPFDHLLFtG---STAVGrhVMRA------AAenlTPVT---------------------LELGGKSPAIIAP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 244 DADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALkmgAPDEEEN--YIGPMarfdlrDELH-QQ 320
Cdd:cd07133 219 DADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM---YPTLADNpdYTSII------NERHyAR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 321 VQATLAE----GATLLL---GGEKMSGTGNyYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSA 393
Cdd:cd07133 290 LQGLLEDarakGARVIElnpAGEDFAATRK-LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLAL 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1022700636 394 TVFTADDARAETFCRELECGGVFING----YSASDArvAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07133 369 YYFGEDKAEQDRVLRRTHSGGVTINDtllhVAQDDL--PFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
31-439 |
5.70e-26 |
|
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: 109.42 E-value: 5.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 31 VERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQA-RAEV------AKSA--SLCDWYA 101
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVsvlvssCKLAikELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 102 -EHGPAMLraeSTQVENAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKH---APNVLGS-ADLIGQaFAD 176
Cdd:cd07137 81 pEKVKTPL---TTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPselAPATSALlAKLIPE-YLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 177 AGFPEGVFGWVNatndgVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAVA 256
Cdd:cd07137 157 TKAIKVIEGGVP-----ETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 257 GRY-QNTGQVCAAAKRFIVEagvaEAFTQRFVDAV--AALKMGAPDEEENyiGPMARfdLRDELHQQVQATLAE----GA 329
Cdd:cd07137 232 GKWgCNNGQACIAPDYVLVE----ESFAPTLIDALknTLEKFFGENPKES--KDLSR--IVNSHHFQRLSRLLDdpsvAD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 330 TLLLGGEKmSGTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRE 409
Cdd:cd07137 304 KIVHGGER-DEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAE 382
|
410 420 430
....*....|....*....|....*....|....*..
gi 1022700636 410 LECGGVFINgysasDARV-------AFGGVKKSGFGR 439
Cdd:cd07137 383 TSSGGVTFN-----DTVVqyaidtlPFGGVGESGFGA 414
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
120-439 |
5.72e-26 |
|
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: 109.52 E-value: 5.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 120 IEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLK---HAPNVlgsADLIGQAFADAgFPEGVFGWVNATNDgVSQ 196
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKpseLTPNT---SKVIAKIIEET-FDEEYVAVVEGGVE-ENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 197 AINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEA 276
Cdd:cd07136 171 ELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 277 GVAEAFTQRFVDAVAALKMGAPDEEENY---IgpmarfdlrDELHQQVQATLAEGATLLLGGeKMSGTGNYYAPTVLGGV 353
Cdd:cd07136 251 SVKEKFIKELKEEIKKFYGEDPLESPDYgriI---------NEKHFDRLAGLLDNGKIVFGG-NTDRETLYIEPTILDNV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 354 TPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECGGVFINgysasDA-------R 426
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN-----DTimhlanpY 395
|
330
....*....|...
gi 1022700636 427 VAFGGVKKSGFGR 439
Cdd:cd07136 396 LPFGGVGNSGMGS 408
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
53-439 |
1.18e-23 |
|
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: 102.68 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 53 RAQKLRDLGTALRSRAEEMAQTISREMGKPIVQA-RAEV------AKSA--SLCDWYA-EHGPAMLraeSTQVENAVIEY 122
Cdd:cd07132 22 RIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAvLSEIllvkneIKYAisNLPEWMKpEPVKKNL---ATLLDDVYIYK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 123 RPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLK------HAPNVLgsADLIGQAFADAGFPEgVFGWVNATNDGVSQ 196
Cdd:cd07132 99 EPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKpsevspATAKLL--AELIPKYLDKECYPV-VLGGVEETTELLKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 197 aindrRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEA 276
Cdd:cd07132 176 -----RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 277 GVAEaftqRFVDAV-AALK--MGAPDEEENYIGPMARfdlrDELHQQVQAtLAEGATLLLGGEKMSGTgNYYAPTVLGGV 353
Cdd:cd07132 251 EVQE----KFVEALkKTLKefYGEDPKESPDYGRIIN----DRHFQRLKK-LLSGGKVAIGGQTDEKE-RYIAPTVLTDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 354 TPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECGGVFING----YSASDarVAF 429
Cdd:cd07132 321 KPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDtimhYTLDS--LPF 398
|
410
....*....|
gi 1022700636 430 GGVKKSGFGR 439
Cdd:cd07132 399 GGVGNSGMGA 408
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
25-438 |
2.90e-23 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 103.41 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 25 WATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAEHG 104
Cdd:PRK11905 586 EASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQA 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 105 PAMLRAESTqvenavieyRPLGPILAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHA---PnvlgsadLIGqAFA-- 175
Cdd:PRK11905 666 RRLLNGPGH---------KPLGPVVCISPWNFPLaiftGQI----AAALVAGNTVLAKPAeqtP-------LIA-ARAvr 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 176 ---DAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVL---ELGGSDPFIVLNDADLD 248
Cdd:PRK11905 725 llhEAGVPKDALQLLPGDGRTVGAALvADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAMIVDSSALPE 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 249 LAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLAEG 328
Cdd:PRK11905 805 QVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAG 884
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 329 ---ATLLLGGEKMSGTgnYYAPTVLggvtpEMTAFRQ---ELFGPVAAITV--ANDAAHALQLANDSDFGLSATVFTADD 400
Cdd:PRK11905 885 rlvHQLPLPAETEKGT--FVAPTLI-----EIDSISDlerEVFGPVLHVVRfkADELDRVIDDINATGYGLTFGLHSRID 957
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1022700636 401 ARAETFCRELECGGVFIN----GysasdARV---AFGGVKKSGFG 438
Cdd:PRK11905 958 ETIAHVTSRIRAGNIYVNrniiG-----AVVgvqPFGGEGLSGTG 997
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
31-415 |
1.02e-21 |
|
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: 97.31 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 31 VERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSR-----AEEMAQTISREM-----GKPIVQ--ARAEVAKSASLCD 98
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKsydiaAGAVLVTGKGWMfaeniCGDQVQlrARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 99 WYAEHGPAMLRAESTQVENavieyrPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSADLIGQAFADAG 178
Cdd:cd07084 81 EPGNHLGQGLKQQSHGYRW------PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 179 -FPEGVFGWVNAtNDGVSQAINDR-RIAAVTVTGSVRAGAAIGAQAGAAlkKCVLELGGSDPFIVLNDAD-LDLAVSAAV 255
Cdd:cd07084 155 lLPPEDVTLING-DGKTMQALLLHpNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQaVDYVAWQCV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 256 AGRYQNTGQVCAAAKRFIVEAGVAeafTQRFVDAVAALKMGAPDeEENYIGPMARFDlrdelhqqVQATLAE-----GAT 330
Cdd:cd07084 232 QDMTACSGQKCTAQSMLFVPENWS---KTPLVEKLKALLARRKL-EDLLLGPVQTFT--------TLAMIAHmenllGSV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 331 LLLGG--EKMSGTGNYYAPTVLGGV-------TPEMTAFRQELFGPVAAITVAND--AAHALQLANDSDFGLSATVFTAD 399
Cdd:cd07084 300 LLFSGkeLKNHSIPSIYGACVASALfvpideiLKTYELVTEEIFGPFAIVVEYKKdqLALVLELLERMHGSLTAAIYSND 379
|
410
....*....|....*.
gi 1022700636 400 DARAETFCRELECGGV 415
Cdd:cd07084 380 PIFLQELIGNLWVAGR 395
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
12-455 |
1.44e-20 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 94.88 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPA-TGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:PRK11904 567 VSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEV 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDWYAEHGPAMLrAESTQV-----ENAVIEYRPLGPILAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHAP 161
Cdd:PRK11904 647 REAVDFCRYYAAQARRLF-GAPEKLpgptgESNELRLHGRGVFVCISPWNFPLaiflGQV----AAALAAGNTVIAKPAE 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 162 NVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSV---RAGAAIGAQAGAALKKCVLELGGSD 237
Cdd:PRK11904 722 QTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALtADPRIAGVAFTGSTetaRIINRTLAARDGPIVPLIAETGGQN 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 238 PFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDEL 317
Cdd:PRK11904 802 AMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANL 881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 318 HQQVqATLAEGATLLLGGEKMSGT--GNYYAPTV--LGGVtpemTAFRQELFGPVAAITV--ANDAAHALQLANDSDFGL 391
Cdd:PRK11904 882 DAHI-ERMKREARLLAQLPLPAGTenGHFVAPTAfeIDSI----SQLEREVFGPILHVIRykASDLDKVIDAINATGYGL 956
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1022700636 392 SATVFTADDARAETFCRELECGGVFIN----GysasdARVA---FGGVKKSGFGREL--SHFgLHEFCNVQTV 455
Cdd:PRK11904 957 TLGIHSRIEETADRIADRVRVGNVYVNrnqiG-----AVVGvqpFGGQGLSGTGPKAggPHY-LLRFATEKTV 1023
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
12-418 |
1.37e-19 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 91.92 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 12 VNPA-TGETLSAWPWATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:COG4230 575 RNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEV 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDWYAehgpamlrAESTQVENAVIEYRPLGPILAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHAPnvlgS 166
Cdd:COG4230 655 REAVDFCRYYA--------AQARRLFAAPTVLRGRGVFVCISPWNFPLaiftGQV----AAALAAGNTVLAKPAE----Q 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 167 ADLIG-QAFA---DAGFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSV---RAGAAIGAQAGAALKKCVLELGGSDP 238
Cdd:COG4230 719 TPLIAaRAVRllhEAGVPADVLQLLPGDGETVGAAlVADPRIAGVAFTGSTetaRLINRTLAARDGPIVPLIAETGGQNA 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 239 FIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELH 318
Cdd:COG4230 799 MIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLE 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 319 QQVQATLAEG---ATLLLGGEKMSGTgnYYAPTV--LGGVTpEMTafrQELFGPVAAItV---ANDAAHALQLANDSDFG 390
Cdd:COG4230 879 AHIERMRAEGrlvHQLPLPEECANGT--FVAPTLieIDSIS-DLE---REVFGPVLHV-VrykADELDKVIDAINATGYG 951
|
410 420
....*....|....*....|....*...
gi 1022700636 391 LSATVFTADDARAETFCRELECGGVFIN 418
Cdd:COG4230 952 LTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
26-368 |
2.35e-19 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 91.57 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 26 ATSQDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAehgp 105
Cdd:PRK11809 679 ATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYA---- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 106 AMLRAEstqVENAVieYRPLGPILAVMPWNFPLwQVLRGAVPILLA-GNSYLLKHAPNvlgsADLI-GQAFA---DAGFP 180
Cdd:PRK11809 755 GQVRDD---FDNDT--HRPLGPVVCISPWNFPL-AIFTGQVAAALAaGNSVLAKPAEQ----TPLIaAQAVRillEAGVP 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 181 EGVFGWVNATNDGV-SQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKK------CVLELGGSDPFIVLNDADLDLAVSA 253
Cdd:PRK11809 825 AGVVQLLPGRGETVgAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPqgrpipLIAETGGQNAMIVDSSALTEQVVAD 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 254 AVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEENYIGPMARFDLRDELHQQVQATLAEGAT--- 330
Cdd:PRK11809 905 VLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPvfq 984
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1022700636 331 LLLGGEKMSGTGNYYAPTVLggvtpEMTAF---RQELFGPV 368
Cdd:PRK11809 985 AARENSEDWQSGTFVPPTLI-----ELDSFdelKREVFGPV 1020
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
31-420 |
1.94e-18 |
|
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: 87.21 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 31 VERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYA----EHGPA 106
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFAdlvrEGSWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 107 MLRAESTQVENAVIE-------YRPLGPILAVMPWNFPL-WQVLRG-AVPILLAGNSYLLKHAPNVLGSADLIGQAFADA 177
Cdd:cd07129 81 DARIDPADPDRQPLPrpdlrrmLVPLGPVAVFGASNFPLaFSVAGGdTASALAAGCPVVVKAHPAHPGTSELVARAIRAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 178 ----GFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAAigaqagaaLKKCV----------LELGGSDPFIVL 242
Cdd:cd07129 161 lratGLPAGVFSLLQGGGREVGVAlVKHPAIKAVGFTGSRRGGRA--------LFDAAaarpepipfyAELGSVNPVFIL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 243 NDAdldLAV-SAAVAGRY-----QNTGQVCAAAKRFIVEAGVAeafTQRFVDAVAALKMGAPDeeenyiGPMARFDLRDE 316
Cdd:cd07129 233 PGA---LAErGEAIAQGFvgsltLGAGQFCTNPGLVLVPAGPA---GDAFIAALAEALAAAPA------QTMLTPGIAEA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 317 LHQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLggVTPEMT-----AFRQELFGPVAAITVANDAAHALQLANDSDFGL 391
Cdd:cd07129 301 YRQGVEALAAAPGVRVLAGGAAAEGGNQAAPTLF--KVDAAAfladpALQEEVFGPASLVVRYDDAAELLAVAEALEGQL 378
|
410 420 430
....*....|....*....|....*....|...
gi 1022700636 392 SATVF--TADDARAETFCRELE--CGGVFINGY 420
Cdd:cd07129 379 TATIHgeEDDLALARELLPVLErkAGRLLFNGW 411
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
13-410 |
2.46e-18 |
|
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: 87.33 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 13 NPATGETLSAwpwATSQ--DVERAIALA-DAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQtISREMGKPIVQARAE 89
Cdd:cd07128 21 DAVTGEVVAR---VSSEglDFAAAVAYArEKGGPALRALTFHERAAMLKALAKYLMERKEDLYA-LSAATGATRRDSWID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 90 VAKSASLCDWYAEHGPAMLRAESTQVENAVIEYRPLGPILA---VMP----------WNFPLWQVLRGAVPILLAGNSYL 156
Cdd:cd07128 97 IDGGIGTLFAYASLGRRELPNAHFLVEGDVEPLSKDGTFVGqhiLTPrrgvavhinaFNFPVWGMLEKFAPALLAGVPVI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 157 LKHAPNVLGSADLIGQAFADAG-FPEGVFGWVNATNDGVSQAINDRRIaaVTVTGS------------VRAGAAIGAQAG 223
Cdd:cd07128 177 VKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQDV--VAFTGSaataaklrahpnIVARSIRFNAEA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 224 AALKKCVLelgGSDpfIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMGAPDEEEN 303
Cdd:cd07128 255 DSLNAAIL---GPD--ATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 304 YIGPMARFDLRDELHQQVqATLAEGATLLLGGEKMS-------GTGNYYAPTVLGGVTP-EMTAFRQ-ELFGPVAAITVA 374
Cdd:cd07128 330 RMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRFevvgadaEKGAFFPPTLLLCDDPdAATAVHDvEAFGPVATLMPY 408
|
410 420 430
....*....|....*....|....*....|....*.
gi 1022700636 375 NDAAHALQLANDSDFGLSATVFTADDARAETFCREL 410
Cdd:cd07128 409 DSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
117-455 |
3.75e-18 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 86.64 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 117 NAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSADLIG---QAFADAGFPEGVFGWVNATNdg 193
Cdd:PLN02174 105 SAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAkllEQYLDSSAVRVVEGAVTETT-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 194 vsqAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAVAGRYQ-NTGQVCAAAKRF 272
Cdd:PLN02174 183 ---ALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 273 IveagVAEAFTQRFVDAVAAlkmgapdEEENYIG--PMARFDLRDELHQ----QVQATLAEGAT---LLLGGEKmSGTGN 343
Cdd:PLN02174 260 L----TTKEYAPKVIDAMKK-------ELETFYGknPMESKDMSRIVNSthfdRLSKLLDEKEVsdkIVYGGEK-DRENL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 344 YYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELECGGVFINGYSAS 423
Cdd:PLN02174 328 KIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVH 407
|
330 340 350
....*....|....*....|....*....|....
gi 1022700636 424 DA--RVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PLN02174 408 LAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
42-439 |
1.21e-13 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 72.84 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 42 FRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQA-RAEV---AKSA-----SLCDWYA-EHGPAMLRAE 111
Cdd:PLN02203 19 YESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyRDEVgvlTKSAnlalsNLKKWMApKKAKLPLVAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 112 STqveNAVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSADLIGQ---AFADAGFPEGVFGWVN 188
Cdd:PLN02203 99 PA---TAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAAnipKYLDSKAVKVIEGGPA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 189 atndgVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV---LNDADLDLAVSAAVAGRYQN-TGQ 264
Cdd:PLN02203 176 -----VGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 265 VCAAAKRFIVEagvaEAFTQRFVDAV-AALK--MGAPDEEENYigpMARF-------DLRDELHQ-QVQATLAEGATllL 333
Cdd:PLN02203 251 ACIAIDYVLVE----ERFAPILIELLkSTIKkfFGENPRESKS---MARIlnkkhfqRLSNLLKDpRVAASIVHGGS--I 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 334 GGEKMsgtgnYYAPTVLggVTPEMTA--FRQELFGPVAAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCRELE 411
Cdd:PLN02203 322 DEKKL-----FIEPTIL--LNPPLDSdiMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETS 394
|
410 420 430
....*....|....*....|....*....|.
gi 1022700636 412 CGGVFING---YSASDArVAFGGVKKSGFGR 439
Cdd:PLN02203 395 SGSVTFNDaiiQYACDS-LPFGGVGESGFGR 424
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
4-410 |
3.91e-11 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 65.11 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 4 SSATHALsVNPATGETLsAWPWATSQDVERAIALA-DAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKP 82
Cdd:PRK11903 17 SGAGTPL-FDPVTGEEL-VRVSATGLDLAAAFAFArEQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 83 IVQARAEV----AKSASLCDWYAEHGPAMLRAESTQVENA---------VIEYRPlGPILAVMPWNFPLWQVLRGAVPIL 149
Cdd:PRK11903 95 RNDSAVDIdggiFTLGYYAKLGAALGDARLLRDGEAVQLGkdpafqgqhVLVPTR-GVALFINAFNFPAWGLWEKAAPAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 150 LAGNSYLLKHAPNVLGSADLIGQAFADAG-FPEGVFGWVNATNDGVSQAINDRRIaaVTVTGS------------VRAGA 216
Cdd:PRK11903 174 LAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHLQPFDV--VSFTGSaetaavlrshpaVVQRS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 217 AIGAQAGAALKKCVLeLGGSDPfivlNDADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALKMG 296
Cdd:PRK11903 252 VRVNVEADSLNSALL-GPDAAP----GSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 297 APDEEENYIGPMARFDLRDELHQQVQAtLAEGATLLLGGEKM------SGTGNYYAPTVLGGVTPE--MTAFRQELFGPV 368
Cdd:PRK11903 327 NPRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGFalvdadPAVAACVGPTLLGASDPDaaTAVHDVEVFGPV 405
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1022700636 369 AAITVANDAAHALQLANDSDFGLSATVFTADDARAETFCREL 410
Cdd:PRK11903 406 ATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALEL 447
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
29-293 |
8.99e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 54.14 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 29 QDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISRE--MGKP---IVQARAEVAKSAslcdwyaeh 103
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEEtgMGRVedkIAKNVAAAEKTP--------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 104 GPAMLRAESTQVEN--AVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNS-YLLKH--APNV-LGSADLIGQAFADA 177
Cdd:PRK15398 107 GVEDLTTEALTGDNglTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSvVFSPHpgAKKVsLRAIELLNEAIVAA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 178 GFPEGVFGWV-NATNDGVSQAINDRRIAAVTVTGS---VRAGAAIGaqagaalKKCVLELGGSDPFIVLNDADLDLAVSA 253
Cdd:PRK15398 187 GGPENLVVTVaEPTIETAQRLMKHPGIALLVVTGGpavVKAAMKSG-------KKAIGAGAGNPPVVVDETADIEKAARD 259
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1022700636 254 AVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAAL 293
Cdd:PRK15398 260 IVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKNGAVL 299
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
119-419 |
2.22e-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: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 119 VIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGS----ADLIGQAFADAGFPEGVFGWVNATNDGV 194
Cdd:cd07081 90 LIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVtqraATLLLQAAVAAGAPENLIGWIDNPSIEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 195 SQAINDR-RIAAVTVTGSvragAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVSAAVAGRYQNTGQVCAAAKRFI 273
Cdd:cd07081 170 AQRLMKFpGIGLLLATGG----PAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 274 VEAGVAEAFTQRFVDAVAALKMGapdEEENYIGP--MARFDLRDELHQQVQATLAEGA-------TLLLGGEKmsgtgny 344
Cdd:cd07081 246 VVDSVYDEVMRLFEGQGAYKLTA---EELQQVQPviLKNGDVNRDIVGQDAYKIAAAAglkvpqeTRILIGEV------- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 345 yapTVLGgvtpEMTAFRQELFGPVAAITVANDAAHALQLA----NDSDFGLSATVFTADD---ARAETFCRELECGGVFI 417
Cdd:cd07081 316 ---TSLA----EHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIkaiENMNQFANAMKTSRFVK 388
|
..
gi 1022700636 418 NG 419
Cdd:cd07081 389 NG 390
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
29-291 |
4.80e-07 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 51.85 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 29 QDVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISRE--MGKP---IVQARAEVAKSAslcdwyaeh 103
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEEtgMGRVedkIAKNHLAAEKTP--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 104 GPAMLRAESTQVEN--AVIEYRPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN----VLGSADLIGQAFADA 177
Cdd:cd07121 75 GTEDLTTTAWSGDNglTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGakkvSAYAVELINKAIAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 178 GFPEGVFGWVNA-TNDGVSQAINDRRIAAVTVTGS---VRAGAAIGaqagaalKKCVLELGGSDPFIVLNDADLDLAVSA 253
Cdd:cd07121 155 GGPDNLVVTVEEpTIETTNELMAHPDINLLVVTGGpavVKAALSSG-------KKAIGAGAGNPPVVVDETADIEKAARD 227
|
250 260 270
....*....|....*....|....*....|....*...
gi 1022700636 254 AVAGRYQNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVA 291
Cdd:cd07121 228 IVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQRNGA 265
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
116-418 |
8.73e-05 |
|
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: 44.79 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 116 ENAVIEY-RPLGPILAVMPWNFPlwqvlrGAVPI------LLAGNSYLLKHAPNVLGS----ADLIGQAFADAGFPEGVF 184
Cdd:cd07122 86 EKGIVEIaEPVGVIAALIPSTNP------TSTAIfkaliaLKTRNAIIFSPHPRAKKCsieaAKIMREAAVAAGAPEGLI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 185 GWV-NATNDGVSQAINDRRIAAVTVTGS---VRAGAAIGaqagaalkKCVLELG-GSDPFIVLNDADLDLAVSAAVAGRY 259
Cdd:cd07122 160 QWIeEPSIELTQELMKHPDVDLILATGGpgmVKAAYSSG--------KPAIGVGpGNVPAYIDETADIKRAVKDIILSKT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 260 QNTGQVCAAAKRFIVEAGVAEAFTQRFVDAVAALkmgAPDEEENYigpMARFDLRDELH-------QQVQ--ATLA---- 326
Cdd:cd07122 232 FDNGTICASEQSVIVDDEIYDEVRAELKRRGAYF---LNEEEKEK---LEKALFDDGGTlnpdivgKSAQkiAELAgiev 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 327 -EGATLLLGGEKmsgtgnyyaptvlgGVTPEmTAFRQELFGPVAAITVANDAAHALQLAND----SDFGLSATVFTADDA 401
Cdd:cd07122 306 pEDTKVLVAEET--------------GVGPE-EPLSREKLSPVLAFYRAEDFEEALEKARElleyGGAGHTAVIHSNDEE 370
|
330
....*....|....*..
gi 1022700636 402 RAETFCRELECGGVFIN 418
Cdd:cd07122 371 VIEEFALRMPVSRILVN 387
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
30-424 |
5.98e-04 |
|
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: 42.08 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 30 DVERAIALADAGFRQWRREGIVHRAQKLRDLGTALRSRAEEMAQTISREMGKPIVQA----------RA---------EV 90
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAfqaggphaqdRGleavayawrEM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 91 AKSASLCDW---YAEHGPAMLRAESTQVenavieyrPLGPILAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSA 167
Cdd:cd07127 165 SRIPPTAEWekpQGKHDPLAMEKTFTVV--------PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 168 DLIGQ----AFADAGF-PEGVFGWVNATNDGVSQAINDR-RIAAVTVTGSVRAGAAIGAQAGAalKKCVLELGGSDPFIV 241
Cdd:cd07127 237 AITVQvareVLAEAGFdPNLVTLAADTPEEPIAQTLATRpEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 242 LNDADL-----DLAVSAAVAgryqnTGQVCAAAKRFIVEA-GVAEAFTQRFVDAVAALKMGAPDeeenyiGPMARFDLRD 315
Cdd:cd07127 315 DSTDDLkamlrNLAFSLSLY-----SGQMCTTPQNIYVPRdGIQTDDGRKSFDEVAADLAAAID------GLLADPARAA 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 316 ELHQQVQ-----ATLAEGATL---LLGGEKMS----GTGNYYAPTVLGGVTPEMTAFRQELFGPVAAITVANDAAHALQL 383
Cdd:cd07127 384 ALLGAIQspdtlARIAEARQLgevLLASEAVAhpefPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIEL 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1022700636 384 ANDSDF---GLSATVFTADDA---RAETFCRE----LEC---GGVFINGYSA-SD 424
Cdd:cd07127 464 ARESVRehgAMTVGVYSTDPEvveRVQEAALDagvaLSInltGGVFVNQSAAfSD 518
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
72-399 |
2.53e-03 |
|
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: 40.17 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 72 AQTISREMGKPIVQARAEVAKSASLCDWYAEHGPAMLrAESTQVENAVIE-----YR-PLGPILAVMPWNFPLWQVLRGA 145
Cdd:cd07126 85 ARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFL-ARSFNVPGDHQGqqssgYRwPYGPVAIITPFNFPLEIPALQL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 146 VPILLAGNSYLLKHAPNVLGSADLIGQAFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAA 225
Cdd:cd07126 164 MGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAERLALELHGK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 226 LKkcvLELGGSDPFIVLND-ADLDLAVSAAVAGRYQNTGQVCAAAKRFIVEAGVAEAftqRFVDAVAALKmGAPDEEENY 304
Cdd:cd07126 244 VK---LEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQA---GILDKLKALA-EQRKLEDLT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022700636 305 IGPMARFDlRDELHQQVQATLA-EGATLLLGGEKMSgtgNYYAPTVLGGVTPemTAF----------------RQELFGP 367
Cdd:cd07126 317 IGPVLTWT-TERILDHVDKLLAiPGAKVLFGGKPLT---NHSIPSIYGAYEP--TAVfvpleeiaieenfelvTTEVFGP 390
|
330 340 350
....*....|....*....|....*....|....
gi 1022700636 368 VAAITVANDAA--HALQLANDSDFGLSATVFTAD 399
Cdd:cd07126 391 FQVVTEYKDEQlpLVLEALERMHAHLTAAVVSND 424
|
|
| |
