|
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: 897.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 1 MTYSSATHAHSVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMG 80
Cdd:PRK13968 1 MTITPATHAISVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 81 KPIVQARAEVAKSASLCDWYAEHGPAMLHPESTQVEN--AVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLK 158
Cdd:PRK13968 81 KPINQARAEVAKSANLCDWYAEHGPAMLKAEPTLVENqqAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 159 HAPNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 238
Cdd:PRK13968 161 HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 239 FIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELH 318
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 319 QQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTA 398
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737306150 399 NDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVWKDRV 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: 664.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 31 VERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAEHGPAMLHP 110
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 111 ESTQVE--NAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAELIGKVFADAGFPEGVFGWVN 188
Cdd:cd07100 81 EPIETDagKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 189 ATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAA 268
Cdd:cd07100 161 IDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 269 AKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATLAEGATLLLGGEKMSGTGNYYAPT 348
Cdd:cd07100 241 AKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 349 VLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIFINGYSASDARVA 428
Cdd:cd07100 321 VLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLP 400
|
410 420
....*....|....*....|....*...
gi 1737306150 429 FGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07100 401 FGGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
11-456 |
5.75e-171 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 488.09 E-value: 5.75e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDWYAEHGPAMLHPESTQVEN-----AVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:PRK09406 85 LKCAKGFRYYAEHAEALLADEPADAAAvgasrAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 166 SAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA 245
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 246 DLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATL 325
Cdd:PRK09406 245 DLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 326 AEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAET 405
Cdd:PRK09406 325 AAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQER 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1737306150 406 FARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:PRK09406 405 FIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVW 455
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
4-455 |
3.98e-160 |
|
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: 460.46 E-value: 3.98e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 4 SSATHAHSVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPI 83
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 84 VQARAEVAKSASLCDWYAEHGPaMLHPESTQVEN---AVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHA 160
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLAR-RLDGETLPSDPgrlAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 161 PNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 239
Cdd:pfam00171 163 ELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALvEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 240 IVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQ 319
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 320 QVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTAN 399
Cdd:pfam00171 323 YVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSD 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737306150 400 DALAETFARELECGGIFINGYSASDARVA-FGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:pfam00171 403 LERALRVARRLEAGMVWINDYTTGDADGLpFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
11-456 |
1.60e-158 |
|
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: 457.28 E-value: 1.60e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:COG1012 25 VINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDWYAEHGPAML---HPESTQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSA 167
Cdd:COG1012 105 DRAADFLRYYAGEARRLYgetIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 168 ELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDAD 246
Cdd:COG1012 185 LLLAELLEEAGLPAGVLNVVTGDGSEVGAALvAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 247 LDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATLA 326
Cdd:COG1012 265 LDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 327 EGATLLLGGEKMSGT-GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAET 405
Cdd:COG1012 345 EGAELLTGGRRPDGEgGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARR 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1737306150 406 FARELECGGIFINGYSAS-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 |
5.36e-146 |
|
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: 424.15 E-value: 5.36e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYAEHGP---AMLHPESTQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAE 168
Cdd:cd07103 82 YAASFLEWFAEEARriyGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 169 LIGKVFADAGFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 247
Cdd:cd07103 162 ALAELAEEAGLPAGVLNVVTGSPAEIGEAlCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 248 DLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATLAE 327
Cdd:cd07103 242 DKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 328 GATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFA 407
Cdd:cd07103 322 GAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1737306150 408 RELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07103 402 EALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
32-456 |
2.03e-137 |
|
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: 401.59 E-value: 2.03e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 32 ERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAEHGPAMLHPE 111
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 112 STQV---ENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAELIGKVFADAGFPEGVFGWVN 188
Cdd:cd07078 81 IPSPdpgELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 189 ATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCA 267
Cdd:cd07078 161 GDGDEVGAALaSHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 268 AAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATLAEGATLLLGGEKMSGT-GNYYA 346
Cdd:cd07078 241 AASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkGYFVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 347 PTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIFINGYSAS-DA 425
Cdd:cd07078 321 PTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGaEP 400
|
410 420 430
....*....|....*....|....*....|.
gi 1737306150 426 RVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07078 401 SAPFGGVKQSGIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
12-456 |
1.07e-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: 350.03 E-value: 1.07e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07088 18 LNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYAE-----HGPAMlhPESTQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGS 166
Cdd:cd07088 98 FTADYIDYMAEwarriEGEII--PSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 167 AELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA 245
Cdd:cd07088 176 ALEFAELVDEAGLPAGVLNIVTGRGSVVGDALvAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 246 DLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATL 325
Cdd:cd07088 256 DLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 326 AEGATLLLGGEKMSGT-GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAE 404
Cdd:cd07088 336 EAGATLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAM 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 405 TFARELECGGIFIN--------GYSAsdarvafgGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07088 416 RATNELEFGETYINrenfeamqGFHA--------GWKKSGLGGADGKHGLEEYLQTKVVY 467
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
13-449 |
5.86e-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: 345.08 E-value: 5.86e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 13 NPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAK 92
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 93 S-------ASLCdwYAEHGPAMLHPESTQVENAVieYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07150 85 TpellraaAGEC--RRVRGETLPSDSPGTVSMSV--RRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 166 SAELIGKVFADAGFPEGVFGWVNATNDGVS-QAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGdELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 245 ADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 325 LAEGATLLLGGEkmsGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAE 404
Cdd:cd07150 321 VAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAF 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1737306150 405 TFARELECGGIFINGYSASD-ARVAFGGVKKSGFGRELSHFGLHEF 449
Cdd:cd07150 398 KLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEF 443
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
12-455 |
1.03e-113 |
|
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: 341.89 E-value: 1.03e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYAEHGPAMLHPESTQVEN------AVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRKVPTGLlmpnkkATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 166 SAELIGKVFADAGFPEGVFGWVnaTNDG-VSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVV--TGDGaTGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 245 ADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07099 239 ADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 325 LAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAE 404
Cdd:cd07099 319 VAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAE 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1737306150 405 TFARELECGGIFIN--GYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07099 399 AIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
30-457 |
1.05e-113 |
|
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: 341.05 E-value: 1.05e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 30 DVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAE-----HG 104
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGlprrpEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 105 pAMLHPESTQVENAVIEyRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN--VLGSAeLIGKVFADAGFPEG 182
Cdd:cd07104 81 -EILPSDVPGKESMVRR-VPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRtpVTGGL-LIAEIFEEAGLPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 183 VFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQN 261
Cdd:cd07104 158 VLNVVPGGGSEIGDAlVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 262 TGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATLAEGATLLLGGEkmsGT 341
Cdd:cd07104 238 QGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT---YE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 342 GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIFINGYS 421
Cdd:cd07104 315 GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQT 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 1737306150 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 ... |
4-455 |
1.03e-111 |
|
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: 337.17 E-value: 1.03e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 4 SSATHAHSV-NPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKP 82
Cdd:cd07138 10 PAGTETIDViNPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 83 IVQARAEVAKSAslcdwyAEHGPAML-----HPESTQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLL 157
Cdd:cd07138 90 ITLARAAQVGLG------IGHLRAAAdalkdFEFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 158 K---HAPnvlGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAIND-RRIAAVTVTGSVRAGAAIGAQAGAALKKCVLEL 233
Cdd:cd07138 164 KpseVAP---LSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAhPDVDMVSFTGSTRAGKRVAEAAADTVKRVALEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 234 GGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDL 313
Cdd:cd07138 241 GGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 314 RDELHQQVQATLAEGATLLLGG-EKMSG--TGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFG 390
Cdd:cd07138 321 FDRVQGYIQKGIEEGARLVAGGpGRPEGleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYG 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737306150 391 LSATVFTANDALAETFARELECGGIFINGySASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07138 401 LAGYVWSADPERARAVARRLRAGQVHING-AAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
12-455 |
6.82e-110 |
|
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: 332.39 E-value: 6.82e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07145 4 RNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYAEHGPaMLHPESTQVEN--------AVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNV 163
Cdd:cd07145 84 RTIRLFKLAAEEAK-VLRGETIPVDAyeynerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 164 LGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVL 242
Cdd:cd07145 163 PLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIvTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 243 NDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQ 322
Cdd:cd07145 243 KDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 323 ATLAEGATLLLGGEKMSgtGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDAL 402
Cdd:cd07145 323 DAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1737306150 403 AETFARELECGGIFINGYSA--SDArVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07145 401 ALKVARELEAGGVVINDSTRfrWDN-LPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
12-449 |
1.93e-109 |
|
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: 331.13 E-value: 1.93e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYAEHGPAMLHPESTQVENAV---IEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAE 168
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGFeryIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 169 LIGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLD 248
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 249 LAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATLAEG 328
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 329 ATLLLGGEKMS---GTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAET 405
Cdd:cd07102 321 ARALIDGALFPedkAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1737306150 406 FARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEF 449
Cdd:cd07102 401 LGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQL 444
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
12-455 |
3.30e-108 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 329.34 E-value: 3.30e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:PLN02278 45 YNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYAEHGpamLHPESTQVENAVIEYR------PLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:PLN02278 125 YGASFLEYFAEEA---KRVYGDIIPSPFPDRRllvlkqPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 166 SAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIA-AVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:PLN02278 202 TALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVrKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDD 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 245 ADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQAT 324
Cdd:PLN02278 282 ADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 325 LAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAE 404
Cdd:PLN02278 362 VSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAW 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1737306150 405 TFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PLN02278 442 RVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
11-455 |
2.57e-107 |
|
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: 325.67 E-value: 2.57e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARA-E 89
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYAEHGPAMLHpESTQVENAVIEY---RPLGPVLAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHAPN 162
Cdd:cd07093 81 IPRAAANFRFFADYILQLDG-ESYPQDGGALNYvlrQPVGVAGLITPWNLPLmlltWKI----APALAFGNTVVLKPSEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 163 VLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV 241
Cdd:cd07093 156 TPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALvAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 242 LNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQV 321
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 322 QATLAEGATLLLGGEKMS----GTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFT 397
Cdd:cd07093 316 ELARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737306150 398 ANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07093 396 RDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
11-456 |
3.77e-107 |
|
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: 325.27 E-value: 3.77e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQ--WRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARA 88
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 89 EVAKSASLCDWYAehGPAmlhpesTQVENAVI-----------EYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLL 157
Cdd:cd07114 81 QVRYLAEWYRYYA--GLA------DKIEGAVIpvdkgdylnftRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 158 K---HAPnvLGSAELiGKVFADAGFPEGVFGWVNATNDGVSQAIND-RRIAAVTVTGSVRAGAAIGAQAGAALKKCVLEL 233
Cdd:cd07114 153 KpseHTP--ASTLEL-AKLAEEAGFPPGVVNVVTGFGPETGEALVEhPLVAKIAFTGGTETGRHIARAAAENLAPVTLEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 234 GGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDL 313
Cdd:cd07114 230 GGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 314 RDELHQQVQATLAEGATLLLGGEKMSGT----GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDF 389
Cdd:cd07114 310 LEKVERYVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEY 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737306150 390 GLSATVFTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07114 390 GLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVW 456
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
11-455 |
5.85e-107 |
|
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: 325.36 E-value: 5.85e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPA-TGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAE 89
Cdd:cd07097 18 NRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYAehGPAM-LHPESTQV--ENAVIEYR--PLGPVLAVMPWNFPL----WQvlrgAVPILLAGNSYLLKHA 160
Cdd:cd07097 98 VTRAGQIFRYYA--GEALrLSGETLPStrPGVEVETTrePLGVVGLITPWNFPIaipaWK----IAPALAYGNTVVFKPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 161 PNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 239
Cdd:cd07097 172 ELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALvEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 240 IVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQ 319
Cdd:cd07097 252 VVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 320 QVQATLAEGATLLLGGEKMSGT--GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFT 397
Cdd:cd07097 332 YIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVT 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 398 ANDALAETFARELECGGIFINGYSAS-DARVAFGGVKKSGFG-RELSHFGLHEFCNVQTV 455
Cdd:cd07097 412 TSLKHATHFKRRVEAGVVMVNLPTAGvDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
13-455 |
7.44e-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: 7.44e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 13 NPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAK 92
Cdd:cd07149 5 SPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 93 SASLCDWYAE-----HG---PAMLHPEStqvENAV-IEYR-PLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN 162
Cdd:cd07149 85 AIETLRLSAEeakrlAGetiPFDASPGG---EGRIgFTIRePIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 163 VLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGaaLKKCVLELGGSDPFIV 241
Cdd:cd07149 162 TPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALvTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 242 LNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQV 321
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 322 QATLAEGATLLLGGEKMsgtGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDA 401
Cdd:cd07149 320 EEAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQ 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737306150 402 LAETFARELECGGIFINGysASDARV---AFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07149 397 KALKAARELEVGGVMIND--SSTFRVdhmPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
12-456 |
9.88e-106 |
|
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: 321.40 E-value: 9.88e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYAEhgpaMLHPESTQVENA----VIEYRPLGPVLAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHAPN- 162
Cdd:cd07106 82 GAVAWLRYTAS----LDLPDEVIEDDDtrrvELRRKPLGVVAAIVPWNFPLllaaWKI----APALLAGNTVVLKPSPFt 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 163 ---VLGSAELIGKVFadagfPEGVfgwVNATNDG--VSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGS 236
Cdd:cd07106 154 plcTLKLGELAQEVL-----PPGV---LNVVSGGdeLGPALtSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 237 DPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPM---ARFDL 313
Cdd:cd07106 226 DAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVqnkMQYDK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 314 RDELHQQVQatlAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSA 393
Cdd:cd07106 306 VKELVEDAK---AKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737306150 394 TVFTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07106 383 SVWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVIN 445
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
10-456 |
2.40e-105 |
|
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: 320.70 E-value: 2.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 10 HSVNPATGETLAAYPWATSGDVERAIVQADIGF--RQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQAR 87
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFesGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 88 A-EVAKSASLCDWYAE-----------HGPAMLhpestqvenAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSY 155
Cdd:cd07112 85 AvDVPSAANTFRWYAEaidkvygevapTGPDAL---------ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 156 LLKHAPNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI---NDrrIAAVTVTGSVRAGAA-IGAQAGAALKKCVL 231
Cdd:cd07112 156 VLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALglhMD--VDALAFTGSTEVGRRfLEYSGQSNLKRVWL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 232 ELGGSDPFIVLNDA-DLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMAR 310
Cdd:cd07112 234 ECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 311 FDLRDELHQQVQATLAEGATLLLGGEK-MSGTGNYYA-PTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSD 388
Cdd:cd07112 314 EAHFDKVLGYIESGKAEGARLVAGGKRvLTETGGFFVePTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737306150 389 FGLSATVFTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07112 394 YGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTW 461
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
12-455 |
1.93e-102 |
|
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: 313.74 E-value: 1.93e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGF--RQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPI-VQARA 88
Cdd:cd07139 19 VSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPIsWSRRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 89 EVAKSASLCDWYAEHGPAMLHPE---STQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07139 99 QGPGPAALLRYYAALARDFPFEErrpGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 166 SAELIGKVFADAGFPEGVFGWVNATNDgVSQA-INDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07139 179 DAYLLAEAAEEAGLPPGVVNVVPADRE-VGEYlVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 245 ADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07139 258 ADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 325 LAEGATLLLGGEKMSG--TGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDAL 402
Cdd:cd07139 338 RAEGARLVTGGGRPAGldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVER 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1737306150 403 AETFARELECGGIFINGYSaSDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07139 418 GLAVARRIRTGTVGVNGFR-LDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
38-457 |
1.29e-101 |
|
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: 308.00 E-value: 1.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 38 ADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAEHGPAMLHPESTQV-- 115
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPdp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 116 -ENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAELIGKVFADAGFPEGVFGWVNATNDGV 194
Cdd:cd06534 83 gGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 195 SQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFI 273
Cdd:cd06534 163 GAALlSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 274 VEAGVADAFTQRFVdavkalkmgapdeednyigpmarfdlrdelhqqvqatlaegatlllggekmsgtgnyyapTVLGGV 353
Cdd:cd06534 243 VHESIYDEFVEKLV------------------------------------------------------------TVLVDV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 354 TPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIFINGYSA-SDARVAFGGV 432
Cdd:cd06534 263 DPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGV 342
|
410 420
....*....|....*....|....*
gi 1737306150 433 KKSGFGRELSHFGLHEFCNVQTVWK 457
Cdd:cd06534 343 KNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
14-455 |
3.33e-101 |
|
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: 310.04 E-value: 3.33e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 14 PATGETLAAYPWATSGDVERAIVQADIGFRQ--WRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDwYAEHGPAMLHPEStqVEN------AVIEYRPLGPVLAVMPWNFPLWqVLRGAVP-ILLAGNSYLLKHAPNVL 164
Cdd:cd07118 84 GAADLWR-YAASLARTLHGDS--YNNlgddmlGLVLREPIGVVGIITPWNFPFL-ILSQKLPfALAAGCTVVVKPSEFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 165 GSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 243
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMtEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 244 DADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQA 323
Cdd:cd07118 240 DADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 324 TLAEGATLLLGGEKMS-GTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDAL 402
Cdd:cd07118 320 GRAEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1737306150 403 AETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07118 400 ALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
12-440 |
8.14e-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: 306.09 E-value: 8.14e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYAE-----HGPAMLHPESTQVEN--AVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVL 164
Cdd:cd07147 84 RAIDTFRIAAEeatriYGEVLPLDISARGEGrqGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 165 GSAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSvrAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07147 164 LSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGS--PAVGWDLKARAGKKKVVLELGGNAAVIVDSD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 245 ADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07147 242 ADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 325 LAEGATLLLGGEKmsgTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAE 404
Cdd:cd07147 322 VDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKAL 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 1737306150 405 TFARELECGGIFINGYSAsdARV---AFGGVKKSGFGRE 440
Cdd:cd07147 399 RAWDELEVGGVVINDVPT--FRVdhmPYGGVKDSGIGRE 435
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
12-455 |
7.17e-99 |
|
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: 304.23 E-value: 7.17e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07151 15 LNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYAEHGPAM---LHPESTQ-VENAVieYR-PLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN--VL 164
Cdd:cd07151 95 AAMAITREAATFPLRMegrILPSDVPgKENRV--YRePLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDtpIT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 165 GSAeLIGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIAAV-TVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 243
Cdd:cd07151 173 GGL-LLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLiSFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 244 DADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQA 323
Cdd:cd07151 252 DADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 324 TLAEGATLLLGGEKmsgTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALA 403
Cdd:cd07151 332 AVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERG 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1737306150 404 ETFARELECGGIFINGYSASD-ARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07151 409 VQFARRIDAGMTHINDQPVNDePHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
12-459 |
8.83e-99 |
|
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: 304.22 E-value: 8.83e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQAR-AEV 90
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDWYAEHGPAMLHPESTQV------ENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVL 164
Cdd:cd07098 81 LVTCEKIRWTLKHGEKALRPESRPGgllmfyKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 165 GSA----ELIGKVFADAGFPEG----VFGWVNATNDGVSQAINDRriaaVTVTGSVRAGAAIGAQAGAALKKCVLELGGS 236
Cdd:cd07098 161 WSSgfflSIIRECLAACGHDPDlvqlVTCLPETAEALTSHPVIDH----ITFIGSPPVGKKVMAAAAESLTPVVLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 237 DPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDE 316
Cdd:cd07098 237 DPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 317 LHQQVQATLAEGATLLLGGEKMSGT----GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLS 392
Cdd:cd07098 317 LEELVADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737306150 393 ATVFTANDALAETFARELECGGIFINGYSASDARVA--FGGVKKSGFGRELSHFGLHEFCNVQTVWKDR 459
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQlpFGGVKGSGFGRFAGEEGLRGLCNPKSVTEDR 465
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
11-456 |
1.05e-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: 304.27 E-value: 1.05e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAA-YPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAE 89
Cdd:cd07131 18 SRNPADLEEVVGtFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYAEHGpAMLHPESTQVE----NAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07131 98 VQEAIDMAQYAAGEG-RRLFGETVPSElpnkDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 166 SAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDR-RIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07131 177 CALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 245 ADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07131 257 ADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 325 LAEGATLLLGGEKMSG----TGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTAND 400
Cdd:cd07131 337 KEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDV 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737306150 401 ALAETFARELECGGIFINGYS-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 |
1.07e-98 |
|
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: 303.78 E-value: 1.07e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQW-RRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARA-E 89
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAmQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYAEHGPAMLHPES-------TQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN 162
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWEFDlpvpalrGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 163 VLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV 241
Cdd:cd07089 162 TPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALtTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 242 LNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQV 321
Cdd:cd07089 242 LDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 322 QATLAEGATLLLGGEKMSG--TGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTAN 399
Cdd:cd07089 322 ARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSAD 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737306150 400 DALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07089 402 VDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
11-455 |
2.74e-97 |
|
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: 299.92 E-value: 2.74e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQ-WRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAE 89
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYAehGPA-MLHPESTQVENAVIEY---RPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07109 81 VEAAARYFEYYG--GAAdKLHGETIPLGPGYFVYtvrEPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 166 SAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALvAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 245 ADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGaPDEEDNYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 325 LAEGATLLLGGEKMSGT---GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDA 401
Cdd:cd07109 318 RARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1737306150 402 LAETFARELECGGIFINGYSASDA-RVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07109 398 RALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
11-440 |
1.84e-96 |
|
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: 298.32 E-value: 1.84e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:cd07086 17 SRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDWYAEHGpAMLHPE---STQVENAVIE-YRPLGPVLAVMPWNFP----LWQvlrgAVPILLAGNSYLLKHAPN 162
Cdd:cd07086 97 QEMIDICDYAVGLS-RMLYGLtipSERPGHRLMEqWNPLGVVGVITAFNFPvavpGWN----AAIALVCGNTVVWKPSET 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 163 V----LGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 238
Cdd:cd07086 172 TpltaIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 239 FIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPmarfdLRDELH 318
Cdd:cd07086 252 IIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP-----LINQAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 319 -QQVQATLA----EGATLLLGGEKMSGT--GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGL 391
Cdd:cd07086 327 vEKYLNAIEiaksQGGTVLTGGKRIDGGepGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGL 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1737306150 392 SATVFTANDALAETF--ARELECGGIFINGySASDARV--AFGGVKKSGFGRE 440
Cdd:cd07086 407 SSSIFTEDLREAFRWlgPKGSDCGIVNVNI-PTSGAEIggAFGGEKETGGGRE 458
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
13-440 |
1.71e-95 |
|
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: 295.37 E-value: 1.71e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 13 NPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAK 92
Cdd:cd07090 3 EPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 93 SASLCDWYAEHGPAmLHPESTQVENAVIEY---RPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAEL 169
Cdd:cd07090 83 SADCLEYYAGLAPT-LSGEHVPLPGGSFAYtrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 170 IGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDL 249
Cdd:cd07090 162 LAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLEN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 250 AVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATLAEGA 329
Cdd:cd07090 242 AVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 330 TLLLGGEKMSGT-----GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAE 404
Cdd:cd07090 322 KVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAH 401
|
410 420 430
....*....|....*....|....*....|....*.
gi 1737306150 405 TFARELECGGIFINGYSASDARVAFGGVKKSGFGRE 440
Cdd:cd07090 402 RVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRE 437
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
12-449 |
1.08e-94 |
|
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: 293.18 E-value: 1.08e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:TIGR01780 2 YNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYAEHGP----AMLHPESTQVENAVIEyRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSA 167
Cdd:TIGR01780 82 YAASFLEWFAEEAKrvygDTIPSPQSDKRLIVIK-QPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 168 ELIGKVFADAGFPEGVFGWVnaTNDGVSQAIN----DRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 243
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVI--TGSRAKEVGNvlttSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 244 DADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQA 323
Cdd:TIGR01780 239 DADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 324 TLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALA 403
Cdd:TIGR01780 319 AVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRI 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1737306150 404 ETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEF 449
Cdd:TIGR01780 399 WRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEY 444
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
12-456 |
7.33e-94 |
|
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: 291.91 E-value: 7.33e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQ--WRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAE 89
Cdd:cd07119 18 INPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEID 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYA-----EHGPAMLHPESTQvenAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVL 164
Cdd:cd07119 98 IDDVANCFRYYAglatkETGEVYDVPPHVI---SRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 165 GSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 243
Cdd:cd07119 175 LTTIALFELIEEAGLPAGVVNLVTGSGATVGAELaESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 244 DADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQA 323
Cdd:cd07119 255 DADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 324 TLAEGATLLLGGEKMSG----TGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTAN 399
Cdd:cd07119 335 GKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKD 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737306150 400 DALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07119 415 IARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHIN 471
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
11-455 |
1.02e-93 |
|
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: 291.42 E-value: 1.02e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESV--AHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQ-AR 87
Cdd:cd07091 23 TINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIERDRDELAALESLDNGKPLEEsAK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 88 AEVAKSASLCDWYAehGPA-MLHPESTQVENAVIEY---RPLGPVLAVMPWNFPL----WQVlrgaVPILLAGNSYLLKH 159
Cdd:cd07091 103 GDVALSIKCLRYYA--GWAdKIQGKTIPIDGNFLAYtrrEPIGVCGQIIPWNFPLlmlaWKL----APALAAGNTVVLKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 160 APNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAA-IGAQAGAALKKCVLELGGSD 237
Cdd:cd07091 177 AEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAIsSHMDVDKIAFTGSTAVGRTiMEAAAKSNLKKVTLELGGKS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 238 PFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDEL 317
Cdd:cd07091 257 PNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 318 HQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFT 397
Cdd:cd07091 337 LSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFT 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737306150 398 ANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07091 417 KDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
12-455 |
1.23e-93 |
|
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: 290.38 E-value: 1.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARA-EV 90
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDWYAEHGPAMLHPESTQ-VEN--AVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSA 167
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGPAAGEyLPGhtSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 168 ELIGKVFADaGFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDAD 246
Cdd:cd07092 162 LLLAELAAE-VLPPGVVNVVCGGGASAGDAlVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 247 LDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDelhqQVQATLA 326
Cdd:cd07092 241 LDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRE----RVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 327 ---EGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALA 403
Cdd:cd07092 317 rapAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1737306150 404 ETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07092 397 MRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
12-455 |
5.61e-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: 288.56 E-value: 5.61e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KS--------ASLCDWYAEHGPAMLHPESTQvENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNV 163
Cdd:cd07094 84 RAidtlrlaaEEAERIRGEEIPLDATQGSDN-RLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 164 LGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVraGAAIGAQAGAALKKCVLELGGSDPFIVL 242
Cdd:cd07094 163 PLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFaADERVAMLSFTGSA--AVGEALRANAGGKRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 243 NDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQ 322
Cdd:cd07094 241 RDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 323 ATLAEGATLLLGGEKmsgTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDAL 402
Cdd:cd07094 321 EAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1737306150 403 AETFARELECGGIFINGYSASDA-RVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07094 398 AFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
30-455 |
7.86e-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: 287.55 E-value: 7.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 30 DVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAEHGPAM-- 107
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIig 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 108 -LHPESTQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAELIGKVFADAGFPEGVFGW 186
Cdd:cd07105 81 gSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 187 V-NATNDG---VSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQNT 262
Cdd:cd07105 161 VtHSPEDApevVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 263 GQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGapdeeDNYIGPMARFDLRDELHQQVQATLAEGATLLLGG-EKMSGT 341
Cdd:cd07105 241 GQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlADESPS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 342 GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIFINGYS 421
Cdd:cd07105 316 GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMT 395
|
410 420 430
....*....|....*....|....*....|....*
gi 1737306150 422 ASD-ARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07105 396 VHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
11-456 |
2.21e-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: 2.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQAR-AE 89
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYAehGPA-MLHPESTQVENAVIEY---RPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07115 81 VPRAADTFRYYA--GWAdKIEGEVIPVRGPFLNYtvrEPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 166 SAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 244
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALvEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 245 ADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 325 LAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAE 404
Cdd:cd07115 319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1737306150 405 TFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07115 399 RVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVW 450
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
12-455 |
2.26e-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: 287.33 E-value: 2.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07110 2 INPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYAE--HGPAMLHPESTQVEN----AVIEYRPLGPVLAVMPWNFPL----WQVlrgaVPILLAGNSYLLKhaP 161
Cdd:cd07110 82 DVAGCFEYYADlaEQLDAKAERAVPLPSedfkARVRREPVGVVGLITPWNFPLlmaaWKV----APALAAGCTVVLK--P 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 162 NVLGS-AEL-IGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 238
Cdd:cd07110 156 SELTSlTELeLAEIAAEAGLPPGVLNVVTGTGDEAGAPLaAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 239 FIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELH 318
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 319 QQVQATLAEGATLLLGGEKMS--GTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVF 396
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737306150 397 TANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
12-455 |
1.98e-89 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 280.26 E-value: 1.98e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARA-EV 90
Cdd:PRK13473 22 YNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNdEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDWYAE-----HGPAMlhPESTQVENAVIEYRPLGPVLAVMPWNFPL----WQVLrgavPILLAGNSYLLKHAP 161
Cdd:PRK13473 102 PAIVDVFRFFAGaarclEGKAA--GEYLEGHTSMIRRDPVGVVASIAPWNYPLmmaaWKLA----PALAAGNTVVLKPSE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 162 NVLGSAELIGKVFADAgFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 240
Cdd:PRK13473 176 ITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDAlVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 241 VLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQ 320
Cdd:PRK13473 255 VFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGF 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 321 VQATLAEG-ATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTAN 399
Cdd:PRK13473 335 VERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRD 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737306150 400 DALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PRK13473 415 VGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
13-440 |
2.34e-89 |
|
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: 279.84 E-value: 2.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 13 NPATGETLAAYPWATSGDVERAIVQADIGFRQWRR-ESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07082 22 SPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYAE-----HGPAMLHPESTQVEN--AVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKhaPNVL 164
Cdd:cd07082 102 RTIDYIRDTIEelkrlDGDSLPGDWFPGTKGkiAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFK--PATQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 165 GS--AELIGKVFADAGFPEGVFGWVnaTNDG---VSQAINDRRIAAVTVTGSVRAGAAIGAQAGaaLKKCVLELGGSDPF 239
Cdd:cd07082 180 GVllGIPLAEAFHDAGFPKGVVNVV--TGRGreiGDPLVTHGRIDVISFTGSTEVGNRLKKQHP--MKRLVLELGGKDPA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 240 IVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQ 319
Cdd:cd07082 256 IVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 320 QVQATLAEGATLLLGGEKMsgTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTAN 399
Cdd:cd07082 336 LIDDAVAKGATVLNGGGRE--GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKD 413
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1737306150 400 DALAETFARELECGGIFINGYSASDARV-AFGGVKKSGFGRE 440
Cdd:cd07082 414 INKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQ 455
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
11-438 |
7.55e-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: 274.87 E-value: 7.55e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPA-TGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAE 89
Cdd:cd07124 50 SRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADAD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYAEHgpaMLHPESTQVENAVIE-----YRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVL 164
Cdd:cd07124 130 VAEAIDFLEYYARE---MLRLRGFPVEMVPGEdnryvYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 165 GSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVR------AGAAIGAQAGAALKKCVLELGGSD 237
Cdd:cd07124 207 VIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLvEHPDVRFIAFTGSREvglriyERAAKVQPGQKWLKRVIAEMGGKN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 238 PFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDEL 317
Cdd:cd07124 287 AIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 318 HQQVQATLAEGaTLLLGGEKM-SGTGNYY-APTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATV 395
Cdd:cd07124 367 RRYIEIGKSEG-RLLLGGEVLeLAAEGYFvQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGV 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1737306150 396 FTANDALAETFARELECGGIFIN--GYSASDARVAFGGVKKSGFG 438
Cdd:cd07124 446 FSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGTG 490
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
14-455 |
1.31e-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: 272.26 E-value: 1.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 14 PATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAKS 93
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 94 ASLCDWYAEHGPAMLHPESTQ-----VENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAE 168
Cdd:cd07101 83 AIVARYYARRAERLLKPRRRRgaipvLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 169 LIGKVFADAGFPEGVFGWVNATNDGVSQAINDRrIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLD 248
Cdd:cd07101 163 WAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN-ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 249 LAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATLAEG 328
Cdd:cd07101 242 KAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 329 ATLLLGGEKMSGTGNY-YAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFA 407
Cdd:cd07101 322 ATVLAGGRARPDLGPYfYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1737306150 408 RELECGGIFIN-GYSASDARVA--FGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07101 402 ARLRAGTVNVNeGYAAAWASIDapMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
4-440 |
8.26e-86 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 271.37 E-value: 8.26e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 4 SSATHAHSVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPI 83
Cdd:PRK13252 19 TSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 84 VQAR-AEVAKSASLCDWYAEHGPAmLHPESTQVENAVIEY---RPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKH 159
Cdd:PRK13252 99 QETSvVDIVTGADVLEYYAGLAPA-LEGEQIPLRGGSFVYtrrEPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 160 APNVLGSAELIGKVFADAGFPEGVFGWVNATNDgVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 238
Cdd:PRK13252 178 SEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLtEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 239 FIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELH 318
Cdd:PRK13252 257 LIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 319 QQVQATLAEGATLLLGGEKMS----GTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSAT 394
Cdd:PRK13252 337 GYIEKGKAEGARLLCGGERLTeggfANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAG 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1737306150 395 VFTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRE 440
Cdd:PRK13252 417 VFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRE 462
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
12-455 |
2.17e-85 |
|
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: 269.23 E-value: 2.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIvqaDIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVA 91
Cdd:cd07146 4 RNPYTGEVVGTVPAGTEEALREAL---ALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYAEH-----GPAMLHPEST--QVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVL 164
Cdd:cd07146 81 RAADVLRFAAAEalrddGESFSCDLTAngKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 165 GSAELIGKVFADAGFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAAIGAQAGAalKKCVLELGGSDPFIVLN 243
Cdd:cd07146 161 LSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDElITHPDVDLVTFTGGVAVGKAIAATAGY--KRQLLELGGNDPLIVMD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 244 DADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQA 323
Cdd:cd07146 239 DADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 324 TLAEGATLLLGGEKmsgTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALA 403
Cdd:cd07146 319 AIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737306150 404 ETFARELECGGIFIN---GYSASdaRVAFGGVKKSGFG-RELSHFGLHEFCNVQTV 455
Cdd:cd07146 396 KRLVERLDVGTVNVNevpGFRSE--LSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
57-456 |
1.42e-84 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 265.45 E-value: 1.42e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 57 LRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAE-----HGPAMlhPESTQVENAVIEYRPLGPVLAV 131
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEwarryEGEII--QSDRPGENILLFKRALGVTTGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 132 MPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTG 210
Cdd:PRK10090 79 LPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELaGNPKVAMVSMTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 211 SVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAV 290
Cdd:PRK10090 159 SVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 291 KALKMGAPDEEDNY-IGPMARFDLRDELHQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVA 369
Cdd:PRK10090 239 QAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 370 AITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEF 449
Cdd:PRK10090 319 PVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEY 398
|
....*..
gi 1737306150 450 CNVQTVW 456
Cdd:PRK10090 399 LQTQVVY 405
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
11-446 |
1.81e-84 |
|
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: 267.74 E-value: 1.81e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRE-SVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQ-ARA 88
Cdd:cd07144 27 TVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnALG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 89 EVAKSASLCDWYAehGPA-MLHPESTQVENAVIEY---RPLGPVLAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHA 160
Cdd:cd07144 107 DLDEIIAVIRYYA--GWAdKIQGKTIPTSPNKLAYtlhEPYGVCGQIIPWNYPLamaaWKL----APALAAGNTVVIKPA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 161 PNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 239
Cdd:cd07144 181 ENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALaEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 240 IVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVK-ALKMGAPDEEDNYIGPMARFDLRDELH 318
Cdd:cd07144 261 LVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQVSKTQYDRVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 319 QQVQATLAEGATLLLGGEKMS---GTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATV 395
Cdd:cd07144 341 SYIEKGKKEGAKLVYGGEKAPeglGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAV 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1737306150 396 FTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGL 446
Cdd:cd07144 421 FTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGL 471
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
17-438 |
2.37e-84 |
|
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: 266.08 E-value: 2.37e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 17 GETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAKSASL 96
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 97 CdwyaEHGPAM-LHPESTQVENA-----VIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN--VLGSAe 168
Cdd:cd07152 81 L----HEAAGLpTQPQGEILPSApgrlsLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRtpVSGGV- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 169 LIGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLD 248
Cdd:cd07152 156 VIARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 249 LAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATLAEG 328
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 329 ATLLLGGEKmsgTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFAR 408
Cdd:cd07152 316 ARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430
....*....|....*....|....*....|.
gi 1737306150 409 ELECGGIFINGYSASDARVA-FGGVKKSGFG 438
Cdd:cd07152 393 RLRTGMLHINDQTVNDEPHNpFGGMGASGNG 423
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
12-455 |
4.69e-83 |
|
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: 264.01 E-value: 4.69e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFR-QWRRE-SVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQ-ARA 88
Cdd:cd07143 27 YNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWGLKvSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTaKRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 89 EVAKSASLCDWYA-----EHGPAMlhpESTQVENAVIEYRPLGPVLAVMPWNFPL----WQVlrgaVPILLAGNSYLLKH 159
Cdd:cd07143 107 DVQASADTFRYYGgwadkIHGQVI---ETDIKKLTYTRHEPIGVCGQIIPWNFPLlmcaWKI----APALAAGNTIVLKP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 160 APNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDR-RIAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGGSD 237
Cdd:cd07143 180 SELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHmDIDKVAFTGSTLVgRKVMEAAAKSNLKKVTLELGGKS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 238 PFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDEL 317
Cdd:cd07143 260 PNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 318 HQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFT 397
Cdd:cd07143 340 MSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFT 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737306150 398 ANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07143 420 NNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
11-456 |
7.84e-83 |
|
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: 262.70 E-value: 7.84e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDWYAEHGPaMLHPESTQVENAVIEY---RPLGPVLAVMPWNFP-LWQVLRGAVPiLLAGNSYLLKHAPNVLGS 166
Cdd:cd07107 81 MVAAALLDYFAGLVT-ELKGETIPVGGRNLHYtlrEPYGVVARIVAFNHPlMFAAAKIAAP-LAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 167 AELIGKVFADAgFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA 245
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALvRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 246 DLDLAVNAAVAG-RYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQAT 324
Cdd:cd07107 238 DPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 325 LAEGATLLLGGEKMSGT----GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTAND 400
Cdd:cd07107 318 KREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737306150 401 ALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVN 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
4-455 |
3.17e-82 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 262.89 E-value: 3.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 4 SSATHAHSV-NPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKP 82
Cdd:PRK09407 28 GAAGPTREVtAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 83 IVQARAEVAKSASLCDWYAEHGPAMLHPESTQ-----VENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLL 157
Cdd:PRK09407 108 RRHAFEEVLDVALTARYYARRAPKLLAPRRRAgalpvLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 158 K----HAPNVLGSAELIgkvfADAGFPEGVFGWVNATNDGVSQAINDRrIAAVTVTGSVRAGAAIGAQAGAALKKCVLEL 233
Cdd:PRK09407 188 KpdsqTPLTALAAVELL----YEAGLPRDLWQVVTGPGPVVGTALVDN-ADYLMFTGSTATGRVLAEQAGRRLIGFSLEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 234 GGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDL 313
Cdd:PRK09407 263 GGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 314 RDELHQQVQATLAEGATLLLGGEKMSGTGNY-YAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLS 392
Cdd:PRK09407 343 LETVSAHVDDAVAKGATVLAGGKARPDLGPLfYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLN 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737306150 393 ATVFTANDALAETFARELECGGIFIN-GYSASDARVA--FGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PRK09407 423 ASVWTGDTARGRAIAARIRAGTVNVNeGYAAAWGSVDapMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
12-455 |
7.89e-81 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 258.89 E-value: 7.89e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGF-----RQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQA 86
Cdd:PLN02467 28 VNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 87 RAEVAKSASLCDWYAEHGPAMLHPESTQVENAVIEYR------PLGPVLAVMPWNFPL----WQVlrgaVPILLAGNSYL 156
Cdd:PLN02467 108 AWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKgyvlkePLGVVGLITPWNYPLlmatWKV----APALAAGCTAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 157 LKhaPNVLGSA---ELiGKVFADAGFPEGVFGWVNATNDGVSQAINDR-RIAAVTVTGSVRAGAAIGAQAGAALKKCVLE 232
Cdd:PLN02467 184 LK--PSELASVtclEL-ADICREVGLPPGVLNVVTGLGTEAGAPLASHpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 233 LGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFD 312
Cdd:PLN02467 261 LGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 313 LRDELHQQVQATLAEGATLLLGGEKMSG--TGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFG 390
Cdd:PLN02467 341 QYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYG 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737306150 391 LSATVFTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PLN02467 421 LAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
4-438 |
1.96e-80 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 257.06 E-value: 1.96e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 4 SSATHAHSVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQ---KLRDLgaaLRSRAEEMAQTISREMG 80
Cdd:cd07085 13 KTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQvmfKFRQL---LEENLDELARLITLEHG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 81 KPIVQARAEVAKSASLCDwYAEHGPAMLHPEST-QVENAVIEY---RPLGPVLAVMPWNFP----LWQVlrgavPILLA- 151
Cdd:cd07085 90 KTLADARGDVLRGLEVVE-FACSIPHLLKGEYLeNVARGIDTYsyrQPLGVVAGITPFNFPamipLWMF-----PMAIAc 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 152 GNSYLLKHAPNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVL 231
Cdd:cd07085 164 GNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 232 ELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARF 311
Cdd:cd07085 244 LGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 312 DLRDELHQQVQATLAEGATLLLGGE--KMSG--TGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDS 387
Cdd:cd07085 324 AAKERIEGLIESGVEEGAKLVLDGRgvKVPGyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINAN 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1737306150 388 DFGLSATVFTANDALAETFARELECGGIFIN-GYSASDARVAFGGVKKSGFG 438
Cdd:cd07085 404 PYGNGAAIFTRSGAAARKFQREVDAGMVGINvPIPVPLAFFSFGGWKGSFFG 455
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
13-455 |
1.02e-79 |
|
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: 254.59 E-value: 1.02e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 13 NPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPI-VQARAEVA 91
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 92 KSASLCDWYA-----------EHGPAMLHpESTQVenavieyrPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLK-- 158
Cdd:cd07108 83 VLADLFRYFGglagelkgetlPFGPDVLT-YTVRE--------PLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKaa 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 159 -HAP-NVLGSAELIGKVFadagfPEGVFGWVNATNDGVSQAINDRR-IAAVTVTGSVRAGAAIGAQAGAALKKCVLELGG 235
Cdd:cd07108 154 eDAPlAVLLLAEILAQVL-----PAGVLNVITGYGEECGAALVDHPdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 236 SDPFIVLNDADLDLAVNAAVAG-RYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMarfdLR 314
Cdd:cd07108 229 KSPMIVFPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAI----IS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 315 DELHQQVQATLAEG-----ATLLLGG----EKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLAN 385
Cdd:cd07108 305 EKQFAKVCGYIDLGlstsgATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMAN 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737306150 386 DSDFGLSATVFTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFG-LHEFCNVQTV 455
Cdd:cd07108 385 DSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
13-453 |
1.83e-79 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 254.83 E-value: 1.83e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 13 NPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAK 92
Cdd:PRK11241 32 NPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 93 SASLCDWYAEHGPAMLH---PESTQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAEL 169
Cdd:PRK11241 112 AASFIEWFAEEGKRIYGdtiPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 170 IGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIA-AVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLD 248
Cdd:PRK11241 192 LAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVrKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 249 LAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATLAEG 328
Cdd:PRK11241 272 KAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 329 ATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLsATVFTANDaLAETF-- 406
Cdd:PRK11241 352 ARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGL-AAYFYARD-LSRVFrv 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1737306150 407 ARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQ 453
Cdd:PRK11241 430 GEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
12-455 |
4.20e-78 |
|
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: 250.82 E-value: 4.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRE-SVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARA-E 89
Cdd:cd07113 20 TNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKtTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYAEHG------------PAMLHPESTqvenAVIEYRPLGPVLAVMPWNFPL----WQVLrgavPILLAGN 153
Cdd:cd07113 100 VGQSANFLRYFAGWAtkingetlapsiPSMQGERYT----AFTRREPVGVVAGIVPWNFSVmiavWKIG----AALATGC 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 154 SYLLK---HAP-NVLGSAELIgkvfADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKC 229
Cdd:cd07113 172 TIVIKpseFTPlTLLRVAELA----KEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 230 VLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMA 309
Cdd:cd07113 248 TLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 310 RFDLRDELHQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDF 389
Cdd:cd07113 328 NQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPF 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737306150 390 GLSATVFTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07113 408 GLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
11-444 |
6.86e-76 |
|
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: 245.33 E-value: 6.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQAR-AE 89
Cdd:cd07559 20 NYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLaAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYA-----EHGPAMLHPESTQvenAVIEYRPLGPVLAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHA 160
Cdd:cd07559 100 IPLAIDHFRYFAgviraQEGSLSEIDEDTL---SYHFHEPLGVVGQIIPWNFPLlmaaWKL----APALAAGNTVVLKPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 161 P----NVLGSAELIGKVFadagfPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGG 235
Cdd:cd07559 173 SqtplSILVLMELIGDLL-----PKGVVNVVTGFGSEAGKPLaSHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 236 SDPFIVLNDA-----DLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMAR 310
Cdd:cd07559 248 KSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 311 FDLRDELHQQVQATLAEGATLLLGGEKMSGT----GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLAND 386
Cdd:cd07559 328 KDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIAND 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737306150 387 SDFGLSATVFTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRE-----LSHF 444
Cdd:cd07559 408 TEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGREthkmmLDHY 470
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
11-455 |
4.50e-74 |
|
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: 240.47 E-value: 4.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQ--WRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQAR- 87
Cdd:cd07142 23 TIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 88 AEVAKSASLCDWYAE-----HGPAMlhpESTQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN 162
Cdd:cd07142 103 AEVPLAARLFRYYAGwadkiHGMTL---PADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 163 VLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDRR-IAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGGSDPFI 240
Cdd:cd07142 180 TPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMdVDKVAFTGSTEVgKIIMQLAAKSNLKPVTLELGGKSPFI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 241 VLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQ 320
Cdd:cd07142 260 VCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 321 VQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTAND 400
Cdd:cd07142 340 IEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNI 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1737306150 401 ALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07142 420 DTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
11-456 |
4.64e-74 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 240.95 E-value: 4.64e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQ--WRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQA-R 87
Cdd:PRK09847 39 TVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 88 AEVAKSASLCDWYAEHGPAM---LHPESTQvENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVL 164
Cdd:PRK09847 119 DDIPGAARAIRWYAEAIDKVygeVATTSSH-ELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 165 GSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI---NDrrIAAVTVTGSVRAGAAIGAQA-GAALKKCVLELGGSDPFI 240
Cdd:PRK09847 198 LSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALsrhND--IDAIAFTGSTRTGKQLLKDAgDSNMKRVWLEAGGKSANI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 241 VLNDA-DLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQ 319
Cdd:PRK09847 276 VFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 320 QVQATLAEGaTLLLGGEKmSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTAN 399
Cdd:PRK09847 356 FIREGESKG-QLLLDGRN-AGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRD 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737306150 400 DALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVW 456
Cdd:PRK09847 434 LSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIW 490
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
11-455 |
9.74e-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: 238.78 E-value: 9.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFR--QWRRESvAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARA 88
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 89 EVAKSASLCDWYA-----EHGpAMLHPESTQVenAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNV 163
Cdd:cd07120 80 EISGAISELRYYAglartEAG-RMIEPEPGSF--SLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 164 LGSAELIGKVFADA-GFPEGVfgwVNATNDGVSQA----INDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 238
Cdd:cd07120 157 AQINAAIIRILAEIpSLPAGV---VNLFTESGSEGaahlVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 239 FIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELH 318
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 319 QQVQATLAEGATLLLGGEKMSGT---GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATV 395
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 396 FTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07120 394 WTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
10-455 |
1.06e-72 |
|
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: 236.86 E-value: 1.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 10 HSVNPATGETLAAYPWATSGDVERAIVQADIGFRQ---WRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPI-VQ 85
Cdd:cd07141 25 PTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFsKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 86 ARAEVAKSASLCDWYAehGPA-MLHPESTQVENAVIEY---RPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAP 161
Cdd:cd07141 105 YLVDLPGAIKVLRYYA--GWAdKIHGKTIPMDGDFFTYtrhEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 162 NVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDR-RIAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGGSDPF 239
Cdd:cd07141 183 QTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHpDIDKVAFTGSTEVgKLIQQAAGKSNLKRVTLELGGKSPN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 240 IVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQ 319
Cdd:cd07141 263 IVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 320 QVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTAN 399
Cdd:cd07141 343 LIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737306150 400 DALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07141 423 IDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
11-449 |
1.43e-70 |
|
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: 231.52 E-value: 1.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQAR-AE 89
Cdd:cd07111 41 TINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRdCD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYAehGPAMLhpestqVENAVIEYRPLGPVLAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHAPNVLG 165
Cdd:cd07111 121 IPLVARHFYHHA--GWAQL------LDTELAGWKPVGVVGQIVPWNFPLlmlaWKI----CPALAMGNTVVLKPAEYTPL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 166 SAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA 245
Cdd:cd07111 189 TALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 246 DLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATL 325
Cdd:cd07111 269 DLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 326 AEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAET 405
Cdd:cd07111 349 AEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALE 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1737306150 406 FARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEF 449
Cdd:cd07111 429 VALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
11-440 |
2.39e-70 |
|
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: 230.80 E-value: 2.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARA-E 89
Cdd:cd07117 20 SYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYA-----EHGPAMLHPESTQvenAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVL 164
Cdd:cd07117 100 IPLAADHFRYFAgviraEEGSANMIDEDTL---SIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 165 GSAELIGKVFADAgFPEGVFGWVNATNDGVSQAINDRR-IAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 243
Cdd:cd07117 177 LSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 244 DADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQA 323
Cdd:cd07117 256 DANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 324 TLAEGATLLLGGEKMSGT----GNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTAN 399
Cdd:cd07117 336 AKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKD 415
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1737306150 400 DALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRE 440
Cdd:cd07117 416 INRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRE 456
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
30-439 |
2.33e-69 |
|
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: 226.77 E-value: 2.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 30 DVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEV----AKSASLCDWYAEHGP 105
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVaamaGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 106 amLHPESTQVENAVIEYRPLGPVLAVMPWNFPLwQVLRGA-VPILLAGNSYLLK---HAPNVlgsAELIGKVFADAGFPE 181
Cdd:cd07095 81 --ERATPMAQGRAVLRHRPHGVMAVFGPFNFPG-HLPNGHiVPALLAGNTVVFKpseLTPAV---AELMVELWEEAGLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 182 GVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCV-LELGGSDPFIVLNDADLDLAVNAAVAGRYQ 260
Cdd:cd07095 155 GVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLIVQSAFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 261 NTGQVCAAAKRFIVEAG-VADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATLAEGATLLLGGEKMS 339
Cdd:cd07095 235 TAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 340 GTGNYYAPTVLggvtpQMTAFR----QELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGI 415
Cdd:cd07095 315 AGTAFLSPGII-----DVTDAAdvpdEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIV 389
|
410 420
....*....|....*....|....*..
gi 1737306150 416 FIN---GYSASDArvAFGGVKKSGFGR 439
Cdd:cd07095 390 NWNrptTGASSTA--PFGGVGLSGNHR 414
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
11-436 |
1.38e-68 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 227.13 E-value: 1.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPA-TGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAE 89
Cdd:PRK03137 54 SINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYAEHgpaMLH------PESTQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNV 163
Cdd:PRK03137 134 TAEAIDFLEYYARQ---MLKladgkpVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 164 LGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDR-RIAAVTVTGS------VRAGAAIGAQAGAALKKCVLELGGS 236
Cdd:PRK03137 211 PVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHpKTRFITFTGSrevglrIYERAAKVQPGQIWLKRVIAEMGGK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 237 DPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPdEEDNYIGPMARFDLRDE 316
Cdd:PRK03137 291 DAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNAYMGPVINQASFDK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 317 LHQQVQATLAEGaTLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVF 396
Cdd:PRK03137 370 IMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVI 448
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1737306150 397 TANDALAETFARELECGGIFIN--------GYSasdarvAFGGVKKSG 436
Cdd:PRK03137 449 SNNREHLEKARREFHVGNLYFNrgctgaivGYH------PFGGFNMSG 490
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
11-455 |
6.02e-68 |
|
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: 224.68 E-value: 6.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFR--QWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQA-R 87
Cdd:cd07140 25 TINPTDGSVICKVSLATVEDVDRAVAAAKEAFEngEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLAlK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 88 AEVAKS-------ASLCDwyAEHGPAMlhPESTQVENAVIEY---RPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLL 157
Cdd:cd07140 105 THVGMSiqtfryfAGWCD--KIQGKTI--PINQARPNRNLTLtkrEPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 158 KHAP----NVLGSAELIGKvfadAGFPEGVFGWVNATNDGVSQAINDR-RIAAVTVTGSVRA-GAAIGAQAGAALKKCVL 231
Cdd:cd07140 181 KPAQvtplTALKFAELTVK----AGFPKGVINILPGSGSLVGQRLSDHpDVRKLGFTGSTPIgKHIMKSCAVSNLKKVSL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 232 ELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARF 311
Cdd:cd07140 257 ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 312 DLRDELHQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDA--AHALQLANDSDF 389
Cdd:cd07140 337 AHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEY 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737306150 390 GLSATVFTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07140 417 GLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
11-440 |
1.01e-64 |
|
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: 215.92 E-value: 1.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:cd07130 16 SISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDwYAE------HGPAMlhpESTQVENAVIE-YRPLGPVLAVMPWNFPL----WQvlrgAVPILLAGNSYLLKH 159
Cdd:cd07130 96 QEMIDICD-FAVglsrqlYGLTI---PSERPGHRMMEqWNPLGVVGVITAFNFPVavwgWN----AAIALVCGNVVVWKP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 160 APNV----LGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGG 235
Cdd:cd07130 168 SPTTpltaIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 236 SDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRD 315
Cdd:cd07130 248 NNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 316 ELHQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGvTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATV 395
Cdd:cd07130 328 NYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEG-LSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSI 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1737306150 396 FTANDALAETF--ARELECGGIFIN-GYSASDARVAFGGVKKSGFGRE 440
Cdd:cd07130 407 FTTDLRNAFRWlgPKGSDCGIVNVNiGTSGAEIGGAFGGEKETGGGRE 454
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
11-455 |
4.87e-64 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 214.68 E-value: 4.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQ--WRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARA 88
Cdd:PLN02766 40 TRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 89 -EVAKSASLCDWYAehGPA-MLHPESTQVENAVIEY---RPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNV 163
Cdd:PLN02766 120 vDIPAAAGLLRYYA--GAAdKIHGETLKMSRQLQGYtlkEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 164 LGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDRR-IAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGGSDPFIV 241
Cdd:PLN02766 198 PLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMdVDKVSFTGSTEVgRKIMQAAATSNLKQVSLELGGKSPLLI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 242 LNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQV 321
Cdd:PLN02766 278 FDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 322 QATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDA 401
Cdd:PLN02766 358 EHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLD 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1737306150 402 LAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PLN02766 438 VANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
11-455 |
4.82e-59 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 202.35 E-value: 4.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQ--WRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQAR- 87
Cdd:PLN02466 77 TLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAk 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 88 AEVAKSASLCDWYAE-----HGPAMLHPESTQVEnavIEYRPLGPVLAVMPWNFPL----WQVlrgaVPILLAGNSYLLK 158
Cdd:PLN02466 157 AELPMFARLFRYYAGwadkiHGLTVPADGPHHVQ---TLHEPIGVAGQIIPWNFPLlmfaWKV----GPALACGNTIVLK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 159 HAPNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDRR-IAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGGS 236
Cdd:PLN02466 230 TAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMdVDKLAFTGSTDTgKIVLELAAKSNLKPVTLELGGK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 237 DPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRfvDAVKALK--MGAPDEEDNYIGPMARFDLR 314
Cdd:PLN02466 310 SPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKrvVGDPFKKGVEQGPQIDSEQF 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 315 DELHQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSAT 394
Cdd:PLN02466 388 EKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAG 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737306150 395 VFTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PLN02466 468 VFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
8-438 |
2.44e-58 |
|
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: 199.73 E-value: 2.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 8 HAHSVNP-ATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQA 86
Cdd:cd07083 33 RMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 87 RAEVAKSASLCDWYAEH-----GPAMLHPESTQVENAVIeYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAP 161
Cdd:cd07083 113 IDDVAEAIDFIRYYARAalrlrYPAVEVVPYPGEDNESF-YVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 162 NVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRA------GAAIGAQAGAALKKCVLELG 234
Cdd:cd07083 192 DAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLtEHERIRGINFTGSLETgkkiyeAAARLAPGQTWFKRLYVETG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 235 GSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLR 314
Cdd:cd07083 272 GKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 315 DELHQQVQATLAEGaTLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITI--ANDAAHALQLANDSDFGLS 392
Cdd:cd07083 352 AKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRykDDDFAEALEVANSTPYGLT 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1737306150 393 ATVFTANDALAETFARELECGGIFINGYS--ASDARVAFGGVKKSGFG 438
Cdd:cd07083 431 GGVYSRKREHLEEARREFHVGNLYINRKItgALVGVQPFGGFKLSGTN 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
5-438 |
2.32e-57 |
|
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: 196.64 E-value: 2.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 5 SATHAHSVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIV 84
Cdd:TIGR01722 14 SGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 85 QARAEVAKSASLCDWYAEHGPAMLHPESTQVENAVIEY---RPLGPVLAVMPWNF----PLWQvlrgaVPILLA-GNSYL 156
Cdd:TIGR01722 94 DALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYsirQPLGVCAGITPFNFpamiPLWM-----FPIAIAcGNTFV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 157 LKHAPNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGS 236
Cdd:TIGR01722 169 LKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 237 DPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRfIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDE 316
Cdd:TIGR01722 249 NHMVVMPDADKDAAADALVGAAYGAAGQRCMAISA-AVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 317 LHQQVQATLAEGATLLLGGE--KMSG--TGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLS 392
Cdd:TIGR01722 328 VASLIAGGAAEGAEVLLDGRgyKVDGyeEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNG 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1737306150 393 ATVFTANDALAETFARELECGGIFIN-------GYsasdarVAFGGVKKSGFG 438
Cdd:TIGR01722 408 TAIFTRDGAAARRFQHEIEVGQVGVNvpipvplPY------FSFTGWKDSFFG 454
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
5-458 |
4.93e-56 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 195.74 E-value: 4.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 5 SATHAHSVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIV 84
Cdd:PLN02419 127 SSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLK 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 85 QARAEVAKSASLCDWYAEHGPAMLHPESTQVENAVIEY---RPLGPVLAVMPWNFP----LWQVlrgavPILLA-GNSYL 156
Cdd:PLN02419 207 DSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYsirEPLGVCAGICPFNFPamipLWMF-----PVAVTcGNTFI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 157 LKHAPNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGS 236
Cdd:PLN02419 282 LKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 237 DPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRfIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDE 316
Cdd:PLN02419 362 NHGLVLPDANIDATLNALLAAGFGAAGQRCMALST-VVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKER 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 317 LHQQVQATLAEGATLLLGGEKMS----GTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLS 392
Cdd:PLN02419 441 ICRLIQSGVDDGAKLLLDGRDIVvpgyEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNG 520
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737306150 393 ATVFTANDALAETFARELECGGIFIN-GYSASDARVAFGGvKKSGFGRELSHF---GLHEFCNVQTV---WKD 458
Cdd:PLN02419 521 AAIFTSSGAAARKFQMDIEAGQIGINvPIPVPLPFFSFTG-NKASFAGDLNFYgkaGVDFFTQIKLVtqkQKD 592
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
12-455 |
1.33e-55 |
|
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: 192.80 E-value: 1.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGE-TLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:cd07125 51 IDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDWY---AEHGPAMLHPESTQVENAVIEYRPLGPVLAVMPWNFPLwqvlrgAVPI------LLAGNSYLLKHAP 161
Cdd:cd07125 131 REAIDFCRYYaaqARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPL------AIFTgqiaaaLAAGNTVIAKPAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 162 NVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAA---IGAQAGAALKKCVLELGGSD 237
Cdd:cd07125 205 QTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEAlVAHPRIDGVIFTGSTETAKLinrALAERDGPILPLIAETGGKN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 238 PFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDEL 317
Cdd:cd07125 285 AMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 318 HQQVQatLAEGATLLLGGEKMS-GTGNYYAPTVLGGVTPqmTAFRQELFGPVAAITIA--NDAAHALQLANDSDFGLSAT 394
Cdd:cd07125 365 RAHTE--LMRGEAWLIAPAPLDdGNGYFVAPGIIEIVGI--FDLTTEVFGPILHVIRFkaEDLDEAIEDINATGYGLTLG 440
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737306150 395 VFTANDALAETFARELECGGIFIN----GysASDARVAFGGVKKSGFGREL--SHFgLHEFCNVQTV 455
Cdd:cd07125 441 IHSRDEREIEYWRERVEAGNLYINrnitG--AIVGRQPFGGWGLSGTGPKAggPNY-LLRFGNEKTV 504
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
11-444 |
1.51e-55 |
|
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: 191.90 E-value: 1.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIvqaRAEV 90
Cdd:cd07116 20 NITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPV---RETL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLC-DWYAEHGPAMLHPEST--QVENAVIEY---RPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVL 164
Cdd:cd07116 97 AADIPLAiDHFRYFAGCIRAQEGSisEIDENTVAYhfhEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 165 GSAELIGKVFADAgFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI--- 240
Cdd:cd07116 177 ASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLaSSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIffa 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 241 -VLN--DADLDLAVNAAVAGRYqNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDEL 317
Cdd:cd07116 256 dVMDadDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 318 HQQVQATLAEGATLLLGGEKMSGTGN----YYAPTVLGGvTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSA 393
Cdd:cd07116 335 LSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGA 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737306150 394 TVFTANDALAETFARELECGGIFINGYSASDARVAFGGVKKSGFGRE-----LSHF 444
Cdd:cd07116 414 GVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGREnhkmmLDHY 469
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
12-438 |
3.64e-53 |
|
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: 184.93 E-value: 3.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAH-RAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWLPAHeRIAILERLADLMEERADELALLIAREGGKPLVDAKVEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDWYAE-------HGPAMLHPESTQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNV 163
Cdd:cd07148 84 TRAIDGVELAADelgqlggREIPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 164 LGSAELIGKVFADAGFPEGvfgWVNAT---NDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAAlKKCVLELGGSDPFI 240
Cdd:cd07148 164 PLSCLAFVDLLHEAGLPEG---WCQAVpceNAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 241 VLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQ 320
Cdd:cd07148 240 VDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 321 VQATLAEGATLLLGGEKMSGTgnYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTAND 400
Cdd:cd07148 320 VNEAVAAGARLLCGGKRLSDT--TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDL 397
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1737306150 401 ALAETFARELECGGIFINGYSAsdARV---AFGGVKKSGFG 438
Cdd:cd07148 398 DVALKAVRRLDATAVMVNDHTA--FRVdwmPFAGRRQSGYG 436
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
10-436 |
1.37e-51 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 181.31 E-value: 1.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 10 HSVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAE 89
Cdd:PRK09457 18 ESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VA----KSASLCDWYAEH-----GPAmlhPESTqvenAVIEYRPLGpVLAVM-PWNFPlwqvlrG------AVPILLAGN 153
Cdd:PRK09457 98 VTaminKIAISIQAYHERtgekrSEM---ADGA----AVLRHRPHG-VVAVFgPYNFP------GhlpnghIVPALLAGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 154 SYLLK---HAPNVlgsAELIGKVFADAGFPEGVFGWVNATND-GVSQAiNDRRIAAVTVTGSVRAGAAIGAQAGAALKKC 229
Cdd:PRK09457 164 TVVFKpseLTPWV---AELTVKLWQQAGLPAGVLNLVQGGREtGKALA-AHPDIDGLLFTGSANTGYLLHRQFAGQPEKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 230 V-LELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGV-ADAFTQRFVDAVKALKMGAPDEEDN-YIG 306
Cdd:PRK09457 240 LaLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWDAEPQpFMG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 307 PMARFDLRDELHQQVQATLAEGATLLLGGEKMSGTgnyyaptvLGGVTP---QMTAFR----QELFGPVAAITIANDAAH 379
Cdd:PRK09457 320 AVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAG--------TGLLTPgiiDVTGVAelpdEEYFGPLLQVVRYDDFDE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737306150 380 ALQLANDSDFGLSATVFTANDALAETFARELECGGIF----INGySASDArvAFGGVKKSG 436
Cdd:PRK09457 392 AIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNwnkpLTG-ASSAA--PFGGVGASG 449
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
4-438 |
2.10e-47 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 170.32 E-value: 2.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 4 SSATHAHSVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPI 83
Cdd:PLN00412 28 SSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 84 VQARAEVAKSASLCDWYAEHGPAML----------HPESTQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGN 153
Cdd:PLN00412 108 KDAVTEVVRSGDLISYTAEEGVRILgegkflvsdsFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 154 SYLLKhaPNVLG--SAELIGKVFADAGFPEGVFGWVNatndGVSQAIND-----RRIAAVTVTGSVRAGAAIGAQAGAAL 226
Cdd:PLN00412 188 AVVLK--PPTQGavAALHMVHCFHLAGFPKGLISCVT----GKGSEIGDfltmhPGVNCISFTGGDTGIAISKKAGMVPL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 227 KkcvLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPdEEDNYIG 306
Cdd:PLN00412 262 Q---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDIT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 307 PMARFDLRDELHQQVQATLAEGATLLlggEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLAND 386
Cdd:PLN00412 338 PVVSESSANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNA 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1737306150 387 SDFGLSATVFTANDALAETFARELECGGIFINGYSASDA-RVAFGGVKKSGFG 438
Cdd:PLN00412 415 SNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIG 467
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
11-440 |
4.23e-47 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 169.63 E-value: 4.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 11 SVNPATGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:PLN02315 38 SVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDwYAEHGPAMLHPE---STQVENAVIE-YRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNV--- 163
Cdd:PLN02315 118 QEIIDMCD-FAVGLSRQLNGSiipSERPNHMMMEvWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTpli 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 164 -LGSAELIGKVFADAGFPEGVFGWVNATNDgVSQAIN-DRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV 241
Cdd:PLN02315 197 tIAMTKLVAEVLEKNNLPGAIFTSFCGGAE-IGEAIAkDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 242 LNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQV 321
Cdd:PLN02315 276 MDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 322 QATLAEGATLLLGGEKMSGTGNYYAPTVLgGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANda 401
Cdd:PLN02315 356 EIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRN-- 432
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1737306150 402 lAETFAREL-----ECGGIFIN-GYSASDARVAFGGVKKSGFGRE 440
Cdd:PLN02315 433 -PETIFKWIgplgsDCGIVNVNiPTNGAEIGGAFGGEKATGGGRE 476
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
42-455 |
3.91e-44 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 160.00 E-value: 3.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 42 FRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQAR-AEVAKSASLCDWYAEHGPAMLHPES------TQ 114
Cdd:cd07087 11 FLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAVVLGEIDHALKHLKKWMKPRRvsvpllLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 115 VENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLK---HAPNVlgsAELIGKVFADAgFPEGVFGWVNATN 191
Cdd:cd07087 91 PAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKpseLAPAT---SALLAKLIPKY-FDPEAVAVVEGGV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 192 DgVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKR 271
Cdd:cd07087 167 E-VATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 272 FIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYigpmARfdLRDELHQQVQATLAEGATLLLGGEkMSGTGNYYAPTVLG 351
Cdd:cd07087 246 VLVHESIKDELIEELKKAIKEFYGEDPKESPDY----GR--IINERHFDRLASLLDDGKVVIGGQ-VDKEERYIAPTILD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 352 GVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIFING--YSASDARVAF 429
Cdd:cd07087 319 DVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDvlLHAAIPNLPF 398
|
410 420
....*....|....*....|....*.
gi 1737306150 430 GGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07087 399 GGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
30-455 |
1.74e-41 |
|
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: 152.76 E-value: 1.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 30 DVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQAR-AEVAKSASLCDWYAEHGPAML 108
Cdd:cd07135 6 EIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKNLKKWA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 109 HPESTQVE-------NAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLK---HAPNvlgSAELIGKVFADAg 178
Cdd:cd07135 86 KDEKVKDGplafmfgKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKpseLTPH---TAALLAELVPKY- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 179 FPEGVFGWVNAtndGVSQ--AINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVA 256
Cdd:cd07135 162 LDPDAFQVVQG---GVPEttALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 257 GRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYiGPMARFDLRDELHQQVQATlaeGATLLLGGE 336
Cdd:cd07135 239 GKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDY-TRIVNPRHFNRLKSLLDTT---KGKVVIGGE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 337 kMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIF 416
Cdd:cd07135 315 -MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVV 393
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1737306150 417 ING----YSASDArvAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07135 394 INDtlihVGVDNA--PFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
44-457 |
1.81e-41 |
|
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: 152.77 E-value: 1.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 44 QWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPivqaRAEVAKS-------------ASLCDWYAEH--GPAML 108
Cdd:cd07134 13 ALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP----AAEVDLTeilpvlseinhaiKHLKKWMKPKrvRTPLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 109 HPEStqveNAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLK---HAPNvlgSAELIGKVFADAgFPE---G 182
Cdd:cd07134 89 LFGT----KSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKpseLTPH---TSAVIAKIIREA-FDEdevA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 183 VF-GWVNatndgVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQN 261
Cdd:cd07134 161 VFeGDAE-----VAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 262 TGQVCAAAKRFIVEAGVADAFTQRFVDAVKAL--KMGAPDEEDNY---IGPMARFDLRDELHQQVqatlAEGATLLLGGE 336
Cdd:cd07134 236 AGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFygKDAARKASPDLariVNDRHFDRLKGLLDDAV----AKGAKVEFGGQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 337 kMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIF 416
Cdd:cd07134 312 -FDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVV 390
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1737306150 417 INGYSA--SDARVAFGGVKKSGFGRELSHFGLHEFCNVQTVWK 457
Cdd:cd07134 391 VNDVVLhfLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
12-436 |
3.49e-36 |
|
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: 139.64 E-value: 3.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPAT-GETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQ---KLRDLgAALRSRAEEMAQTisreM---GKPIV 84
Cdd:cd07123 51 VMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAiflKAADL-LSGKYRYELNAAT----MlgqGKNVW 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 85 QAraEVAKSASLCDW------YAEHgpaMLH--PESTQ--VENAViEYRPL-GPVLAVMPWNFPLWQVLRGAVPILLaGN 153
Cdd:cd07123 126 QA--EIDAACELIDFlrfnvkYAEE---LYAqqPLSSPagVWNRL-EYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 154 SYLLKHAPNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALK----- 227
Cdd:cd07123 199 VVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVlASPHLAGLHFTGSTPTFKSLWKQIGENLDryrty 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 228 -KCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIG 306
Cdd:cd07123 279 pRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 307 PM---ARFD-LRDELHqqvQATLAEGATLLLGGEKMSGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDA--AHA 380
Cdd:cd07123 359 AVideKAFDrIKGYID---HAKSDPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSdfEET 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737306150 381 LQLAND-SDFGLSATVFTANDALAETFARELE--CGGIFINGYSaSDARVA---FGGVKKSG 436
Cdd:cd07123 436 LELVDTtSPYALTGAIFAQDRKAIREATDALRnaAGNFYINDKP-TGAVVGqqpFGGARASG 496
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
41-438 |
3.04e-31 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 125.53 E-value: 3.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 41 GFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQAR-AEVAKSASLCDWYAEHGPAMLHPESTQVENAV 119
Cdd:PTZ00381 19 SFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmTEVLLTVAEIEHLLKHLDEYLKPEKVDTVGVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 120 ------IEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLK---HAPNvlgSAELIGKVFaDAGFPEGVFGWVNaT 190
Cdd:PTZ00381 99 gpgksyIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKpseLSPH---TSKLMAKLL-TKYLDPSYVRVIE-G 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 191 NDGVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAK 270
Cdd:PTZ00381 174 GVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 271 RFIVEAGVADAFTQRFVDAVKALkMGA-PDEEDNYigpmARFDLRDELHQQVQATLAEGATLLLGGEkMSGTGNYYAPTV 349
Cdd:PTZ00381 254 YVLVHRSIKDKFIEALKEAIKEF-FGEdPKKSEDY----SRIVNEFHTKRLAELIKDHGGKVVYGGE-VDIENKYVAPTI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 350 LGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIFING--YSASDARV 427
Cdd:PTZ00381 328 IVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDcvFHLLNPNL 407
|
410
....*....|.
gi 1737306150 428 AFGGVKKSGFG 438
Cdd:PTZ00381 408 PFGGVGNSGMG 418
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
42-439 |
5.29e-29 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 118.28 E-value: 5.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 42 FRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQA-RAEV------AKSA--SLCDWYA-EHGPAmlhPE 111
Cdd:cd07137 12 FRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVsvlvssCKLAikELKKWMApEKVKT---PL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 112 STQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKH---APNvlgSAELIGKVFA---DAGFPEGVFG 185
Cdd:cd07137 89 TTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPselAPA---TSALLAKLIPeylDTKAIKVIEG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 186 WVNatndgVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRY-QNTGQ 264
Cdd:cd07137 166 GVP-----ETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 265 VCAAAKRFIVEAGvadaFTQRFVDAVKA--LKMGAPDEEDNyiGPMARfdLRDELHQQVQATLAE----GATLLLGGEKm 338
Cdd:cd07137 241 ACIAPDYVLVEES----FAPTLIDALKNtlEKFFGENPKES--KDLSR--IVNSHHFQRLSRLLDdpsvADKIVHGGER- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 339 SGTGNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIFIN 418
Cdd:cd07137 312 DEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFN 391
|
410 420
....*....|....*....|....*...
gi 1737306150 419 gysasDARV-------AFGGVKKSGFGR 439
Cdd:cd07137 392 -----DTVVqyaidtlPFGGVGESGFGA 414
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
12-418 |
3.42e-28 |
|
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: 116.93 E-value: 3.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAY-PWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:TIGR01238 56 TNPADRRDIVGQvFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDWYAEHGPAMLHPEStqvenavieYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAELI 170
Cdd:TIGR01238 136 REAVDFCRYYAKQVRDVLGEFS---------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 171 GKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVL---ELGGSDPFIVLNDAD 246
Cdd:TIGR01238 207 VELMQEAGFPAGTIQLLPGRGADVGAALtSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPliaETGGQNAMIVDSTAL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 247 LDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATLA 326
Cdd:TIGR01238 287 PEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQ 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 327 EGAT---LLLGGEKMSGTGNYYAPTVLGgvTPQMTAFRQELFGPVAAIT--IANDAAHALQLANDSDFGLSATVFTANDA 401
Cdd:TIGR01238 367 TQKKiaqLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIET 444
|
410
....*....|....*..
gi 1737306150 402 LAETFARELECGGIFIN 418
Cdd:TIGR01238 445 TYRWIEKHARVGNCYVN 461
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
32-439 |
3.50e-28 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 116.17 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 32 ERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQA-RAEV------AKSA--SLCDWYA- 101
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAvLSEIllvkneIKYAisNLPEWMKp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 102 EHGPAMLhpeSTQVENAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLK------HAPNVLgsAELIGKVFA 175
Cdd:cd07132 81 EPVKKNL---ATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKpsevspATAKLL--AELIPKYLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 176 DAGFPEgVFGWVNATNDGVSQaindrRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAV 255
Cdd:cd07132 156 KECYPV-VLGGVEETTELLKQ-----RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 256 AGRYQNTGQVCAAAKRFIVEAGVADaftqRFVDAVK-ALK--MGAPDEEDNYIGPMARfdlrDELHQQVQAtLAEGATLL 332
Cdd:cd07132 230 WGKFINAGQTCIAPDYVLCTPEVQE----KFVEALKkTLKefYGEDPKESPDYGRIIN----DRHFQRLKK-LLSGGKVA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 333 LGGEKMSGTgNYYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELEC 412
Cdd:cd07132 301 IGGQTDEKE-RYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSS 379
|
410 420 430
....*....|....*....|....*....|.
gi 1737306150 413 GGIFING----YSASDarVAFGGVKKSGFGR 439
Cdd:cd07132 380 GGVCVNDtimhYTLDS--LPFGGVGNSGMGA 408
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
42-455 |
5.12e-27 |
|
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: 112.58 E-value: 5.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 42 FRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMG-KPIVQAR-AEVAKSASLCDWYAEHGPAMLHPESTQVE--- 116
Cdd:cd07133 11 FLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLlAEILPSIAGIKHARKHLKKWMKPSRRHVGllf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 117 ---NAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLK---HAPNvlgSAELIGKVFADAgFPEGVFGWVNAT 190
Cdd:cd07133 91 lpaKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKpseFTPR---TSALLAELLAEY-FDEDEVAVVTGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 191 NDgVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAK 270
Cdd:cd07133 167 AD-VAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 271 RFIVEAGVADAFTQRFVDAVKALkmgAPDEEDN--YIGPMarfdlrDELH-QQVQATLAE----GATLLL---GGEKMSG 340
Cdd:cd07133 246 YVLVPEDKLEEFVAAAKAAVAKM---YPTLADNpdYTSII------NERHyARLQGLLEDarakGARVIElnpAGEDFAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 341 TGNyYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIFING- 419
Cdd:cd07133 317 TRK-LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDt 395
|
410 420 430
....*....|....*....|....*....|....*....
gi 1737306150 420 ---YSASDArvAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:cd07133 396 llhVAQDDL--PFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
120-439 |
5.39e-27 |
|
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: 112.60 E-value: 5.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 120 IEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLK---HAPNVlgsAELIGKVFADAgFPEGVFGWVNATNDgVSQ 196
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKpseLTPNT---SKVIAKIIEET-FDEEYVAVVEGGVE-ENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 197 AINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEA 276
Cdd:cd07136 171 ELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 277 GVADAFTQRFVDAVKALKMGAPDEEDNY---IgpmarfdlrDELHQQVQATLAEGATLLLGGeKMSGTGNYYAPTVLGGV 353
Cdd:cd07136 251 SVKEKFIKELKEEIKKFYGEDPLESPDYgriI---------NEKHFDRLAGLLDNGKIVFGG-NTDRETLYIEPTILDNV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 354 TPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIFINgysasDA-------R 426
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN-----DTimhlanpY 395
|
330
....*....|...
gi 1737306150 427 VAFGGVKKSGFGR 439
Cdd:cd07136 396 LPFGGVGNSGMGS 408
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
12-438 |
1.37e-24 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 107.26 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPA-TGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:PRK11905 572 LNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEV 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDWYAEHGPAMLHPESTqvenavieyRPLGPVLAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHAPNV-LG 165
Cdd:PRK11905 652 REAVDFLRYYAAQARRLLNGPGH---------KPLGPVVCISPWNFPLaiftGQI----AAALVAGNTVLAKPAEQTpLI 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 166 SAELIgKVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVL---ELGGSDPFIV 241
Cdd:PRK11905 719 AARAV-RLLHEAGVPKDALQLLPGDGRTVGAALvADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAMIV 797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 242 LNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQV 321
Cdd:PRK11905 798 DSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHI 877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 322 QATLAEG---ATLLLGGEKMSGTgnYYAPTVLggvtpQMTAFRQ---ELFGPVAAITI--ANDAAHALQLANDSDFGLSA 393
Cdd:PRK11905 878 EAMRAAGrlvHQLPLPAETEKGT--FVAPTLI-----EIDSISDlerEVFGPVLHVVRfkADELDRVIDDINATGYGLTF 950
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1737306150 394 TVFTANDALAETFARELECGGIFIN----GysasdARV---AFGGVKKSGFG 438
Cdd:PRK11905 951 GLHSRIDETIAHVTSRIRAGNIYVNrniiG-----AVVgvqPFGGEGLSGTG 997
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
31-414 |
2.41e-24 |
|
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: 105.01 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 31 VERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSR-----AEEMAQTISREM-----GKPIVQ--ARAEVAKSASLCD 98
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKsydiaAGAVLVTGKGWMfaeniCGDQVQlrARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 99 WYAEHGPAMLHPESTQVENavieyrPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAELIGKVFADAG 178
Cdd:cd07084 81 EPGNHLGQGLKQQSHGYRW------PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 179 -FPEGVFGWVNAtNDGVSQAINDR-RIAAVTVTGSVRAGAAIGAQAGAAlkKCVLELGGSDPFIVLNDAD-LDLAVNAAV 255
Cdd:cd07084 155 lLPPEDVTLING-DGKTMQALLLHpNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQaVDYVAWQCV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 256 AGRYQNTGQVCAAAKRFIVEAGVAdafTQRFVDAVKALKMGAPDeEDNYIGPMARFDlrdelhqqVQATLAE-----GAT 330
Cdd:cd07084 232 QDMTACSGQKCTAQSMLFVPENWS---KTPLVEKLKALLARRKL-EDLLLGPVQTFT--------TLAMIAHmenllGSV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 331 LLLGG--EKMSGTGNYYAPTVLGGV-------TPQMTAFRQELFGPVAAITIAND--AAHALQLANDSDFGLSATVFTAN 399
Cdd:cd07084 300 LLFSGkeLKNHSIPSIYGACVASALfvpideiLKTYELVTEEIFGPFAIVVEYKKdqLALVLELLERMHGSLTAAIYSND 379
|
410
....*....|....*
gi 1737306150 400 DALAETFARELECGG 414
Cdd:cd07084 380 PIFLQELIGNLWVAG 394
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
117-455 |
3.41e-21 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 95.88 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 117 NAVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAELIGKV---FADAGFPEGVFGWVNATNdg 193
Cdd:PLN02174 105 SAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLleqYLDSSAVRVVEGAVTETT-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 194 vsqAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQ-NTGQVCAAAKRF 272
Cdd:PLN02174 183 ---ALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 273 IveagVADAFTQRFVDAVKAlkmgapdEEDNYIG--PMARFDLRDELHQ----QVQATLAEGAT---LLLGGEKmSGTGN 343
Cdd:PLN02174 260 L----TTKEYAPKVIDAMKK-------ELETFYGknPMESKDMSRIVNSthfdRLSKLLDEKEVsdkIVYGGEK-DRENL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 344 YYAPTVLGGVTPQMTAFRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARELECGGIFINGYSAS 423
Cdd:PLN02174 328 KIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVH 407
|
330 340 350
....*....|....*....|....*....|....
gi 1737306150 424 DA--RVAFGGVKKSGFGRELSHFGLHEFCNVQTV 455
Cdd:PLN02174 408 LAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
13-410 |
1.01e-20 |
|
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: 94.64 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 13 NPATGETLAAypwATSG--DVERAIVQA-DIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQtISREMGKPIVQARAE 89
Cdd:cd07128 21 DAVTGEVVAR---VSSEglDFAAAVAYArEKGGPALRALTFHERAAMLKALAKYLMERKEDLYA-LSAATGATRRDSWID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 90 VAKSASLCDWYAEHGPAMLHPESTQVENAVIE------------YRPLGPVlAVM--PWNFPLWQVLRGAVPILLAGNSY 155
Cdd:cd07128 97 IDGGIGTLFAYASLGRRELPNAHFLVEGDVEPlskdgtfvgqhiLTPRRGV-AVHinAFNFPVWGMLEKFAPALLAGVPV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 156 LLKHAPNVLGSAELIGKVFADAG-FPEGVFGWVNATNDGVSQAINDRRIaaVTVTGS------------VRAGAAIGAQA 222
Cdd:cd07128 176 IVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQDV--VAFTGSaataaklrahpnIVARSIRFNAE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 223 GAALKKCVLelgGSDpfIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEED 302
Cdd:cd07128 254 ADSLNAAIL---GPD--ATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 303 NYIGPMARFDLRDELHQQVqATLAEGATLLLGGEKMS-------GTGNYYAPTVLGGVTP-QMTAFRQ-ELFGPVAAITI 373
Cdd:cd07128 329 VRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRFevvgadaEKGAFFPPTLLLCDDPdAATAVHDvEAFGPVATLMP 407
|
410 420 430
....*....|....*....|....*....|....*..
gi 1737306150 374 ANDAAHALQLANDSDFGLSATVFTANDALAETFAREL 410
Cdd:cd07128 408 YDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
12-455 |
1.22e-20 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 95.27 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPA-TGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:PRK11904 567 VSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEV 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 AKSASLCDWYAEHGPAML-HPES----TQVENAvIEYRPLGPVLAVMPWNFPL----WQVlrgaVPILLAGNSYLLKHAP 161
Cdd:PRK11904 647 REAVDFCRYYAAQARRLFgAPEKlpgpTGESNE-LRLHGRGVFVCISPWNFPLaiflGQV----AAALAAGNTVIAKPAE 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 162 nvlgSAELIG----KVFADAGFPEGVFGWVNATNDGVSQAI-NDRRIAAVTVTGSV---RAGAAIGAQAGAALKKCVLEL 233
Cdd:PRK11904 722 ----QTPLIAaeavKLLHEAGIPKDVLQLLPGDGATVGAALtADPRIAGVAFTGSTetaRIINRTLAARDGPIVPLIAET 797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 234 GGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDL 313
Cdd:PRK11904 798 GGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEA 877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 314 RDELHQQVqATLAEGATLLLGGEKMSGT--GNYYAPTV--LGGVtpqmTAFRQELFGPVAAITI--ANDAAHALQLANDS 387
Cdd:PRK11904 878 KANLDAHI-ERMKREARLLAQLPLPAGTenGHFVAPTAfeIDSI----SQLEREVFGPILHVIRykASDLDKVIDAINAT 952
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737306150 388 DFGLSATVFTANDALAETFARELECGGIFIN----GysasdARVA---FGGVKKSGFGREL--SHFgLHEFCNVQTV 455
Cdd:PRK11904 953 GYGLTLGIHSRIEETADRIADRVRVGNVYVNrnqiG-----AVVGvqpFGGQGLSGTGPKAggPHY-LLRFATEKTV 1023
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
26-368 |
3.31e-19 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 90.80 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 26 ATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAKSASLCDWYAEhgp 105
Cdd:PRK11809 679 ATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAG--- 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 106 amlhpestQVENAVIE--YRPLGPVLAVMPWNFPLwQVLRGAVPILLA-GNSYLLKHAPNV-LGSAELIgKVFADAGFPE 181
Cdd:PRK11809 756 --------QVRDDFDNdtHRPLGPVVCISPWNFPL-AIFTGQVAAALAaGNSVLAKPAEQTpLIAAQAV-RILLEAGVPA 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 182 GVFGWVNATNDGV-SQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKK------CVLELGGSDPFIVLNDADLDLAVNAA 254
Cdd:PRK11809 826 GVVQLLPGRGETVgAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPqgrpipLIAETGGQNAMIVDSSALTEQVVADV 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 255 VAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIGPMARFDLRDELHQQVQATLAEGAT---L 331
Cdd:PRK11809 906 LASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPvfqA 985
|
330 340 350
....*....|....*....|....*....|....*....
gi 1737306150 332 LLGGEKMSGTGNYYAPTV--LGGVtpqmTAFRQELFGPV 368
Cdd:PRK11809 986 ARENSEDWQSGTFVPPTLieLDSF----DELKREVFGPV 1020
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
31-420 |
4.76e-19 |
|
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: 89.14 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 31 VERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEVAKS-------ASLCDWYAEH 103
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTtgqlrlfADLVREGSWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 104 GPAMLH--PESTQVENAVIE--YRPLGPVLAVMPWNFPL-WQVLRG-AVPILLAGNSYLLKHAPNVLGSAELIGKVFADA 177
Cdd:cd07129 81 DARIDPadPDRQPLPRPDLRrmLVPLGPVAVFGASNFPLaFSVAGGdTASALAAGCPVVVKAHPAHPGTSELVARAIRAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 178 ----GFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSVRAGAAigaqagaaLKKCV----------LELGGSDPFIVL 242
Cdd:cd07129 161 lratGLPAGVFSLLQGGGREVGVAlVKHPAIKAVGFTGSRRGGRA--------LFDAAaarpepipfyAELGSVNPVFIL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 243 NDAdldLAVNAA------VAGRYQNTGQVCAAAKRFIVEAGVAdafTQRFVDAVKALKMGAPDeednyiGPMARFDLRDE 316
Cdd:cd07129 233 PGA---LAERGEaiaqgfVGSLTLGAGQFCTNPGLVLVPAGPA---GDAFIAALAEALAAAPA------QTMLTPGIAEA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 317 LHQQVQATLAEGATLLLGGEKMSGTGNYYAPTVLggVTPQMT-----AFRQELFGPVAAITIANDAAHALQLANDSDFGL 391
Cdd:cd07129 301 YRQGVEALAAAPGVRVLAGGAAAEGGNQAAPTLF--KVDAAAfladpALQEEVFGPASLVVRYDDAAELLAVAEALEGQL 378
|
410 420 430
....*....|....*....|....*....|...
gi 1737306150 392 SATVF--TANDALAETFARELE--CGGIFINGY 420
Cdd:cd07129 379 TATIHgeEDDLALARELLPVLErkAGRLLFNGW 411
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
4-418 |
6.17e-19 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 90.00 E-value: 6.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 4 SSATHAHSV-NPA-TGETLAAYPWATSGDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGK 81
Cdd:COG4230 566 AASGEARPVrNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGK 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 82 PIVQARAEVAKSASLCDWYAEhgpamlhpESTQVENAVIEYRPLGPVLAVMPWNFPL----WQVlrgaVPILLAGNSYLL 157
Cdd:COG4230 646 TLPDAIAEVREAVDFCRYYAA--------QARRLFAAPTVLRGRGVFVCISPWNFPLaiftGQV----AAALAAGNTVLA 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 158 KhaPnvlgsAE---LIG----KVFADAGFPEGVFGWVNATNDGVSQA-INDRRIAAVTVTGSV---RAGAAIGAQAGAAL 226
Cdd:COG4230 714 K--P-----AEqtpLIAaravRLLHEAGVPADVLQLLPGDGETVGAAlVADPRIAGVAFTGSTetaRLINRTLAARDGPI 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 227 KKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNYIG 306
Cdd:COG4230 787 VPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVG 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 307 PMARFDLRDELHQQVQATLAEG---ATLLLGGEKMSGTgnYYAPTV--LGGVTpQMTafrQELFGPVAAItI---ANDAA 378
Cdd:COG4230 867 PVIDAEARANLEAHIERMRAEGrlvHQLPLPEECANGT--FVAPTLieIDSIS-DLE---REVFGPVLHV-VrykADELD 939
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1737306150 379 HALQLANDSDFGLSATVFTANDALAETFARELECGGIFIN 418
Cdd:COG4230 940 KVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
42-439 |
2.82e-18 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 87.09 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 42 FRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQA-RAEV---AKSA-----SLCDWYA-EHG--PAMLH 109
Cdd:PLN02203 19 YESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyRDEVgvlTKSAnlalsNLKKWMApKKAklPLVAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 110 PESTQVENavieyRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAELIGKV---FADAGFPEGVFGW 186
Cdd:PLN02203 99 PATAEVVP-----EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANipkYLDSKAVKVIEGG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 187 VNatndgVSQAINDRRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV---LNDADLDLAVNAAVAGRYQN-T 262
Cdd:PLN02203 174 PA-----VGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 263 GQVCAAAKRFIVEAGvadaFTQRFVDAVKA-LK--MGAPDEEDNYigpMARF-------DLRDELHQ-QVQATLAEGATl 331
Cdd:PLN02203 249 GQACIAIDYVLVEER----FAPILIELLKStIKkfFGENPRESKS---MARIlnkkhfqRLSNLLKDpRVAASIVHGGS- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 332 lLGGEKMsgtgnYYAPTVLggVTPQMTA--FRQELFGPVAAITIANDAAHALQLANDSDFGLSATVFTANDALAETFARE 409
Cdd:PLN02203 321 -IDEKKL-----FIEPTIL--LNPPLDSdiMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSE 392
|
410 420 430
....*....|....*....|....*....|...
gi 1737306150 410 LECGGIFING---YSASDArVAFGGVKKSGFGR 439
Cdd:PLN02203 393 TSSGSVTFNDaiiQYACDS-LPFGGVGESGFGR 424
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
12-410 |
9.61e-12 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 67.04 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPwATSGDVERAIVQA-DIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQARAEV 90
Cdd:PRK11903 24 FDPVTGEELVRVS-ATGLDLAAAFAFArEQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 91 ----AKSASLCDWYAEHGPAMLHPESTQVENA---------VIEYRPlGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLL 157
Cdd:PRK11903 103 dggiFTLGYYAKLGAALGDARLLRDGEAVQLGkdpafqgqhVLVPTR-GVALFINAFNFPAWGLWEKAAPALLAGVPVIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 158 KHAPNVLGSAELIGKVFADAG-FPEGVFGWVNATNDGVSQAINDRRIaaVTVTGS------------VRAGAAIGAQAGA 224
Cdd:PRK11903 182 KPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHLQPFDV--VSFTGSaetaavlrshpaVVQRSVRVNVEAD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 225 ALKKCVLeLGGSDPfivlNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAVKALKMGAPDEEDNY 304
Cdd:PRK11903 260 SLNSALL-GPDAAP----GSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 305 IGPMARFDLRDELHQQVQAtLAEGATLLLGGEKM------SGTGNYYAPTVLGGVTPQ--MTAFRQELFGPVAAITIAND 376
Cdd:PRK11903 335 MGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGFalvdadPAVAACVGPTLLGASDPDaaTAVHDVEVFGPVATLLPYRD 413
|
410 420 430
....*....|....*....|....*....|....
gi 1737306150 377 AAHALQLANDSDFGLSATVFTANDALAETFAREL 410
Cdd:PRK11903 414 AAHALALARRGQGSLVASVYSDDAAFLAAAALEL 447
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
29-431 |
2.60e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 55.71 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 29 GDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISRE--MGKP---IVQARAEVAKSAslcdwyaeh 103
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEEtgMGRVedkIAKNHLAAEKTP--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 104 GPAMLHPESTQVEN--AVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPN----VLGSAELIGKVFADA 177
Cdd:cd07121 75 GTEDLTTTAWSGDNglTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGakkvSAYAVELINKAIAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 178 GFPEGVFGWVNA-TNDGVSQAINDRRIAAVTVTGS---VRAGAAIGaqagaalKKCVLELGGSDPFIVLNDADLDLAVNA 253
Cdd:cd07121 155 GGPDNLVVTVEEpTIETTNELMAHPDINLLVVTGGpavVKAALSSG-------KKAIGAGAGNPPVVVDETADIEKAARD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 254 AVAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDAvKALKMGAPDEE---------DNYIGPMARFDLRDelhqqvQAT 324
Cdd:cd07121 228 IVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQRN-GAYVLNDEQAEqllevvlltNKGATPNKKWVGKD------ASK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 325 LAEGATLLLGGEkmsgtgnyyaPTVLGGVTPQMTAFRQ-ELFGPVAAITIANDAAHALQLANDSDFGL--SATVFTANDA 401
Cdd:cd07121 301 ILKAAGIEVPAD----------IRLIIVETDKDHPFVVeEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVE 370
|
410 420 430
....*....|....*....|....*....|.
gi 1737306150 402 LAETFARELECgGIFI-NGysASDARVAFGG 431
Cdd:cd07121 371 NLTKMARAMQT-TIFVkNG--PSYAGLGVGG 398
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
30-289 |
4.08e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 55.29 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 30 DVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISRE--MGKP---IVQARAEVAKSAslcdwyaehG 104
Cdd:PRK15398 37 SVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEEtgMGRVedkIAKNVAAAEKTP---------G 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 105 PAMLHPESTQVEN--AVIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNS-YLLKH--APNV-LGSAELIGKVFADAG 178
Cdd:PRK15398 108 VEDLTTEALTGDNglTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSvVFSPHpgAKKVsLRAIELLNEAIVAAG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 179 FPEGVFGWV-NATNDGVSQAINDRRIAAVTVTGS---VRAGAAIGaqagaalKKCVLELGGSDPFIVLNDADLDLAVNAA 254
Cdd:PRK15398 188 GPENLVVTVaEPTIETAQRLMKHPGIALLVVTGGpavVKAAMKSG-------KKAIGAGAGNPPVVVDETADIEKAARDI 260
|
250 260 270
....*....|....*....|....*....|....*
gi 1737306150 255 VAGRYQNTGQVCAAAKRFIVEAGVADAFTQRFVDA 289
Cdd:PRK15398 261 VKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKN 295
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
119-419 |
1.09e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 50.73 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 119 VIEYRPLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAELIGKVFADA----GFPEGVFGWVNATNDGV 194
Cdd:cd07081 90 LIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGWIDNPSIEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 195 SQAINDR-RIAAVTVTGSvragAAIGAQAGAALKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFI 273
Cdd:cd07081 170 AQRLMKFpGIGLLLATGG----PAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 274 VEAGVADAFTQRFvdavkalkmgapDEEDNYIgpmarfdLRDELHQQVQATLAEGATLllgGEKMSGTGNYYAPTVLGGV 353
Cdd:cd07081 246 VVDSVYDEVMRLF------------EGQGAYK-------LTAEELQQVQPVILKNGDV---NRDIVGQDAYKIAAAAGLK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 354 TPQMTA--------------FRQELFGPVAAITIANDAAHALQLA----NDSDFGLSATVFTANDALAET---FARELEC 412
Cdd:cd07081 304 VPQETRiligevtslaehepFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIENmnqFANAMKT 383
|
....*..
gi 1737306150 413 GGIFING 419
Cdd:cd07081 384 SRFVKNG 390
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
122-372 |
2.65e-05 |
|
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: 46.33 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 122 YR-PLGPVLAVMPWNFPLWQVLRGAVPILLAGNSYLLKHAPNVLGSAELIGKVFADAGFPEGVFGWVNATNDGVSQAIND 200
Cdd:cd07126 139 YRwPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 201 RRIAAVTVTGSVRAGAAIGAQAGAALKkcvLELGGSDPFIVLND-ADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEAGVA 279
Cdd:cd07126 219 ANPRMTLFTGSSKVAERLALELHGKVK---LEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 280 DAftqRFVDAVKALKmGAPDEEDNYIGPMARFDlRDELHQQVQATLA-EGATLLLGGEKMSgtgNYYAPTVLGGVTPqmT 358
Cdd:cd07126 296 QA---GILDKLKALA-EQRKLEDLTIGPVLTWT-TERILDHVDKLLAiPGAKVLFGGKPLT---NHSIPSIYGAYEP--T 365
|
250 260 270
....*....|....*....|....*....|
gi 1737306150 359 AF----------------RQELFGPVAAIT 372
Cdd:cd07126 366 AVfvpleeiaieenfelvTTEVFGPFQVVT 395
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
116-418 |
2.15e-04 |
|
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: 43.63 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 116 ENAVIEY-RPLGPVLAVMPWNFPlwqvlrGAVPI------LLAGNSYLLKHAPNVLGS----AELIGKVFADAGFPEGVF 184
Cdd:cd07122 86 EKGIVEIaEPVGVIAALIPSTNP------TSTAIfkaliaLKTRNAIIFSPHPRAKKCsieaAKIMREAAVAAGAPEGLI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 185 GWV-NATNDGVSQAINDRRIAAVTVTGS---VRAGAAIGaqagaalkKCVLELG-GSDPFIVLNDADLDLAVNAAVAGRY 259
Cdd:cd07122 160 QWIeEPSIELTQELMKHPDVDLILATGGpgmVKAAYSSG--------KPAIGVGpGNVPAYIDETADIKRAVKDIILSKT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 260 QNTGQVCAAAKRFIVEAGVADAFTQRFVdavkalKMGA----PDEEDNyigpMARFDLRDELH-------QQVQ--ATLA 326
Cdd:cd07122 232 FDNGTICASEQSVIVDDEIYDEVRAELK------RRGAyflnEEEKEK----LEKALFDDGGTlnpdivgKSAQkiAELA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 327 -----EGATLLLGGEKMSGTGNyyaptvlggvtpqmtAFRQELFGPVAAITIANDAAHALQLAND----SDFGLSATVFT 397
Cdd:cd07122 302 gievpEDTKVLVAEETGVGPEE---------------PLSREKLSPVLAFYRAEDFEEALEKARElleyGGAGHTAVIHS 366
|
330 340
....*....|....*....|.
gi 1737306150 398 ANDALAETFARELECGGIFIN 418
Cdd:cd07122 367 NDEEVIEEFALRMPVSRILVN 387
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
12-424 |
1.22e-03 |
|
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: 41.31 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 12 VNPATGETLAAYPWAtsgDVERAIVQADIGFRQWRRESVAHRAQKLRDLGAALRSRAEEMAQTISREMGKPIVQA----- 86
Cdd:cd07127 70 VSPYGVELGVTYPQC---DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAfqagg 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 87 -----RA---------EVAKSASLCDW---YAEHGPAMLHPESTQVenavieyrPLGPVLAVMPWNFPLWQVLRGAVPIL 149
Cdd:cd07127 147 phaqdRGleavayawrEMSRIPPTAEWekpQGKHDPLAMEKTFTVV--------PRGVALVIGCSTFPTWNGYPGLFASL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 150 LAGNSYLLKHAPN-VLGSA---ELIGKVFADAGF-PEGVFGWVNATNDGVSQAINDR-RIAAVTVTGSVRAGAAIGAQAG 223
Cdd:cd07127 219 ATGNPVIVKPHPAaILPLAitvQVAREVLAEAGFdPNLVTLAADTPEEPIAQTLATRpEVRIIDFTGSNAFGDWLEANAR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 224 AalKKCVLELGGSDPFIVLNDADLDLAVNAAVAGRYQNTGQVCAAAKRFIVEA-GVA--------DAFTQRFVDAVKALk 294
Cdd:cd07127 299 Q--AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRdGIQtddgrksfDEVAADLAAAIDGL- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737306150 295 MGAPDEEDNYIGPMARFDLRDELhqqvqATLAEGATLLLGGEKMS----GTGNYYAPTVLGGVTPQMTAFRQELFGPVAA 370
Cdd:cd07127 376 LADPARAAALLGAIQSPDTLARI-----AEARQLGEVLLASEAVAhpefPDARVRTPLLLKLDASDEAAYAEERFGPIAF 450
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737306150 371 ITIANDAAHALQLANDSDF---GLSATVFTANDALAETF-------ARELEC---GGIFINGYSA-SD 424
Cdd:cd07127 451 VVATDSTDHSIELARESVRehgAMTVGVYSTDPEVVERVqeaaldaGVALSInltGGVFVNQSAAfSD 518
|
|
| |
