|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
1-462 |
0e+00 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 973.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 1 MTITPATHAISINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMG 80
Cdd:PRK13968 1 MTITPATHAISVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 81 KPINQARAEVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLK 160
Cdd:PRK13968 81 KPINQARAEVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 161 HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 240
Cdd:PRK13968 161 HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 321 HQVEKTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTT 400
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3915524 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVWKDRI 462
Cdd:PRK13968 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVWKDRI 462
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
31-458 |
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: 706.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 31 IENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAMLKA 110
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 111 EPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLN 190
Cdd:cd07100 81 EPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 191 ADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAA 270
Cdd:cd07100 161 IDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 271 AKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLAQGARLLLGGEKMAGAGNYYPPT 350
Cdd:cd07100 241 AKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 351 VLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFINGYCASDARVA 430
Cdd:cd07100 321 VLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLP 400
|
410 420
....*....|....*....|....*...
gi 3915524 431 FGGVKKSGFGRELSHFGLHEFCNIQTVW 458
Cdd:cd07100 401 FGGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
11-458 |
7.05e-171 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 488.09 E-value: 7.05e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDWYAEHGPAMLKAEPT---LVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMG 167
Cdd:PRK09406 85 LKCAKGFRYYAEHAEALLADEPAdaaAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA 247
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 248 DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTL 327
Cdd:PRK09406 245 DLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 328 AQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQ 407
Cdd:PRK09406 325 AAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQER 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 3915524 408 MAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
Cdd:PRK09406 405 FIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVW 455
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
11-458 |
3.62e-164 |
|
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: 471.53 E-value: 3.62e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
Cdd:COG1012 25 VINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDWYAEHGPAML-KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCA 169
Cdd:COG1012 105 DRAADFLRYYAGEARRLYgETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 170 QLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDAD 248
Cdd:COG1012 185 LLLAELLEEAGLPAGVLNVVTGDGSEVGAaLVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 249 LELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLA 328
Cdd:COG1012 265 LDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 329 QGARLLLGGEKMAGA-GNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQ 407
Cdd:COG1012 345 EGAELLTGGRRPDGEgGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARR 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 3915524 408 MAARLECGGVFINGYCAS-DARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
Cdd:COG1012 425 VARRLEAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKTVT 476
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
11-457 |
2.29e-159 |
|
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: 458.53 E-value: 2.29e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
Cdd:pfam00171 11 VINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQ 170
Cdd:pfam00171 91 DRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 171 LIAQVFKDAGIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 249
Cdd:pfam00171 171 LLAELFEEAGLPAGVLNVVTGSGAEVGEaLVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 250 ELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLAQ 329
Cdd:pfam00171 251 DAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 330 GARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMA 409
Cdd:pfam00171 331 GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVA 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 3915524 410 ARLECGGVFINGYCASDARVA-FGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:pfam00171 411 RRLEAGMVWINDYTTGDADGLpFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
12-457 |
3.22e-151 |
|
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: 437.63 E-value: 3.22e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAEHgpamlkAE-------PTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPN 164
Cdd:cd07103 82 YAASFLEWFAEE------ARriygrtiPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 165 VMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV 243
Cdd:cd07103 156 TPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEaLCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 244 LNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQV 323
Cdd:cd07103 236 FDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 324 EKTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDET 403
Cdd:cd07103 316 EDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 3915524 404 QARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
32-458 |
1.08e-148 |
|
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: 430.48 E-value: 1.08e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 32 ENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAMLKAE 111
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 112 -PTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLN 190
Cdd:cd07078 81 iPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 191 ADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCA 269
Cdd:cd07078 161 GDGDEVGAaLASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 270 AAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLAQGARLLLGGEKMAG-AGNYYP 348
Cdd:cd07078 241 AASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKGYFVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 349 PTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFINGYCAS-DA 427
Cdd:cd07078 321 PTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGaEP 400
|
410 420 430
....*....|....*....|....*....|.
gi 3915524 428 RVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
Cdd:cd07078 401 SAPFGGVKQSGIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
30-459 |
5.96e-127 |
|
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: 374.94 E-value: 5.96e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 30 DIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAML- 108
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 109 KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPN--VMGcAQLIAQVFKDAGIPQGVY 186
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRtpVTG-GLLIAEIFEEAGLPKGVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 187 GWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTG 265
Cdd:cd07104 160 NVVPGGGSEIGDaLVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 266 QVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLAQGARLLLGGEkmaGAGN 345
Cdd:cd07104 240 QICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT---YEGL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 346 YYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFINGYCAS 425
Cdd:cd07104 317 FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVN 396
|
410 420 430
....*....|....*....|....*....|....*
gi 3915524 426 D-ARVAFGGVKKSGFGRELSHFGLHEFcniqTVWK 459
Cdd:cd07104 397 DePHVPFGGVKASGGGRFGGPASLEEF----TEWQ 427
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
13-451 |
7.99e-127 |
|
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: 375.51 E-value: 7.99e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 93 SANLCDWYAE-----HGPAMlkaePTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMG 167
Cdd:cd07150 85 TPELLRAAAGecrrvRGETL----PSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVS-QMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 246
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGdELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 247 ADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKT 326
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 327 LAQGARLLLGGEkmaGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQAR 406
Cdd:cd07150 321 VAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAF 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 3915524 407 QMAARLECGGVFINGYCASD-ARVAFGGVKKSGFGRELSHFGLHEF 451
Cdd:cd07150 398 KLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEF 443
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
12-452 |
1.34e-118 |
|
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: 354.61 E-value: 1.34e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAEHGPAMLKAEPT----LVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLK---HAPn 164
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRKVptglLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKpseVTP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 165 vmGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIkDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVL 244
Cdd:cd07099 160 --LVGELLAEAWAAAGPPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 325 KTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQ 404
Cdd:cd07099 317 DAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 3915524 405 ARQMAARLECGGVFIN----GYCASDArvAFGGVKKSGFGRELSHFGLHEFC 452
Cdd:cd07099 397 AEAIARRLEAGAVSINdvllTAGIPAL--PFGGVKDSGGGRRHGAEGLREFC 446
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
12-457 |
3.99e-118 |
|
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: 353.58 E-value: 3.99e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07145 4 RNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAEHGPAMLKAEPTL-----VENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLK---HAP 163
Cdd:cd07145 84 RTIRLFKLAAEEAKVLRGETIPVdayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKpssNTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 164 NVmgcAQLIAQVFKDAGIPQGVYGWLNADNDGV-SQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
Cdd:cd07145 164 LT---AIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 323 VEKTLAQGARLLLGGEKMAGAgnYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDE 402
Cdd:cd07145 321 VNDAVEKGGKILYGGKRDEGS--FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDI 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 3915524 403 TQARQMAARLECGGVFINGycASDAR---VAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07145 399 NRALKVARELEAGGVVIND--STRFRwdnLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
12-458 |
7.05e-116 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 348.10 E-value: 7.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07088 18 LNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAEhgpAMLKAE----PTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMG 167
Cdd:cd07088 98 FTADYIDYMAE---WARRIEgeiiPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 246
Cdd:cd07088 175 NALEFAELVDEAGLPAGVLNIVTGRGSVVGDaLVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 247 ADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKT 326
Cdd:cd07088 255 ADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 327 LAQGARLLLGGEKMAGA-GNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQA 405
Cdd:cd07088 335 VEAGATLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3915524 406 RQMAARLECGGVFIN--------GYCAsdarvafgGVKKSGFGRELSHFGLHEFCNIQTVW 458
Cdd:cd07088 415 MRATNELEFGETYINrenfeamqGFHA--------GWKKSGLGGADGKHGLEEYLQTKVVY 467
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
12-458 |
1.86e-113 |
|
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: 341.05 E-value: 1.86e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCdwyaeHGPAMLKAEPTLV---ENQQAVIEYRPLGTILAIMPWNFPL----WQVMrgavPIILAGNGYLLKHAPN 164
Cdd:cd07106 82 GAVAWL-----RYTASLDLPDEVIeddDTRRVELRRKPLGVVAAIVPWNFPLllaaWKIA----PALLAGNTVVLKPSPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 165 ----VMGCAQLIAQVFkdagiPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 240
Cdd:cd07106 153 tplcTLKLGELAQEVL-----PPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPM---ARFDLRD 317
Cdd:cd07106 228 AIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVqnkMQYDKVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 318 ELhhqVEKTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATI 397
Cdd:cd07106 308 EL---VEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASV 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3915524 398 FTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
Cdd:cd07106 385 WSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVIN 445
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
4-457 |
2.61e-113 |
|
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: 341.40 E-value: 2.61e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 4 TPATHAIsINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPI 83
Cdd:cd07138 12 GTETIDV-INPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 84 NQARAEVAKSAnlcdwyAEHGPAMLKAEPTLVENQQ---AVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLK 160
Cdd:cd07138 91 TLARAAQVGLG------IGHLRAAADALKDFEFEERrgnSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 161 ---HAPnvmGCAQLIAQVFKDAGIPQGVYGWLNADNDGV-SQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELG 236
Cdd:cd07138 165 pseVAP---LSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 237 GSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLR 316
Cdd:cd07138 242 GKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 317 DELHHQVEKTLAQGARLLLGG-EKMAG--AGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGL 393
Cdd:cd07138 322 DRVQGYIQKGIEEGARLVAGGpGRPEGleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGL 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3915524 394 SATIFTTDETQARQMAARLECGGVFINGyCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07138 402 AGYVWSADPERARAVARRLRAGQVHING-AAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
12-457 |
1.10e-112 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 340.90 E-value: 1.10e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:PLN02278 45 YNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAEHGPAML-KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQ 170
Cdd:PLN02278 125 YGASFLEYFAEEAKRVYgDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTAL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 171 LIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIA-AVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 249
Cdd:PLN02278 205 AAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVrKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 250 ELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLAQ 329
Cdd:PLN02278 285 DVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSK 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 330 GARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMA 409
Cdd:PLN02278 365 GAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVS 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 3915524 410 ARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:PLN02278 445 EALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
38-459 |
3.66e-112 |
|
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: 334.97 E-value: 3.66e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 38 AAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAMLKAE-PTLVE 116
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPElPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 117 NQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGV 196
Cdd:cd06534 83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 197 SQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFI 275
Cdd:cd06534 163 GAaLLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 276 IEEGIASAFTERFVaaaaalkmgdprdeenalgpmarfdlrdelhhqvektlaqgarlllggekmagagnyyppTVLANV 355
Cdd:cd06534 243 VHESIYDEFVEKLV------------------------------------------------------------TVLVDV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 356 TPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFINGYCA-SDARVAFGGV 434
Cdd:cd06534 263 DPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGV 342
|
410 420
....*....|....*....|....*
gi 3915524 435 KKSGFGRELSHFGLHEFCNIQTVWK 459
Cdd:cd06534 343 KNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
11-458 |
9.59e-111 |
|
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: 334.52 E-value: 9.59e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARA 88
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 89 EVAKSAnlcDWYAEHGPAMLKAE----PTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLK---H 161
Cdd:cd07114 81 QVRYLA---EWYRYYAGLADKIEgaviPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKpseH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 162 APnvmgCAQL-IAQVFKDAGIPQGVYGWLNADNDGVSQMIKDS-RIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSD 239
Cdd:cd07114 158 TP----ASTLeLAKLAEEAGFPPGVVNVVTGFGPETGEALVEHpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 240 PFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDEL 319
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 320 HHQVEKTLAQGARLLLGGEKMAGA----GNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSA 395
Cdd:cd07114 314 ERYVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3915524 396 TIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
Cdd:cd07114 394 GIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVW 456
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
12-457 |
5.57e-110 |
|
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: 332.64 E-value: 5.57e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAE-----HGPAM-LKAEPTlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNV 165
Cdd:cd07149 84 RAIETLRLSAEeakrlAGETIpFDASPG-GEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGV-SQMIKDSRIAAVTVTGSVRAGAAIGAQAGaaLKKCVLELGGSDPFIVL 244
Cdd:cd07149 163 PLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
Cdd:cd07149 241 ADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 325 KTLAQGARLLLGGEKMagaGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQ 404
Cdd:cd07149 321 EAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQK 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 3915524 405 ARQMAARLECGGVFINGycASDARV---AFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07149 398 ALKAARELEVGGVMIND--SSTFRVdhmPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
11-457 |
4.98e-109 |
|
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: 329.91 E-value: 4.98e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARA-E 89
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYAEhgpAMLKAEPTLVENQQAVIEY---RPLGTILAIMPWNFPL----WQVmrgaVPIILAGNGYLLKHA 162
Cdd:cd07093 81 IPRAAANFRFFAD---YILQLDGESYPQDGGALNYvlrQPVGVAGLITPWNLPLmlltWKI----APALAFGNTVVLKPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 241
Cdd:cd07093 154 EWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAaLVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 322 QVEKTLAQGARLLLGGEKMA----GAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATI 397
Cdd:cd07093 314 YVELARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 398 FTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07093 394 WTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
12-451 |
4.68e-108 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 327.67 E-value: 4.68e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAEHGPAMLKAEPTLVENQ-QAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQ 170
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGfERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 171 LIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLE 250
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 251 LAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLAQG 330
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 331 ARLLLGGEK---MAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQ 407
Cdd:cd07102 321 ARALIDGALfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 3915524 408 MAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEF 451
Cdd:cd07102 401 LGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQL 444
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
11-457 |
9.04e-108 |
|
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: 327.67 E-value: 9.04e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPA-TGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
Cdd:cd07097 18 NRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYAE-----HGPAMLKAEP-TLVENQQavieyRPLGTILAIMPWNFPL----WQvmrgAVPIILAGNGYLL 159
Cdd:cd07097 98 VTRAGQIFRYYAGealrlSGETLPSTRPgVEVETTR-----EPLGVVGLITPWNFPIaipaWK----IAPALAYGNTVVF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 160 KHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGS 238
Cdd:cd07097 169 KPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQaLVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318
Cdd:cd07097 249 NPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 319 LHHQVEKTLAQGARLLLGGEKMAGA--GNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSAT 396
Cdd:cd07097 329 DLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAG 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3915524 397 IFTTDETQARQMAARLECGGVFIN----GYcasDARVAFGGVKKSGFG-RELSHFGLHEFCNIQTV 457
Cdd:cd07097 409 IVTTSLKHATHFKRRVEAGVVMVNlptaGV---DYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
11-458 |
5.36e-106 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 322.63 E-value: 5.36e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARA 88
Cdd:cd07112 6 TINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 89 -EVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMG 167
Cdd:cd07112 86 vDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMI---KDsrIAAVTVTGSVRAGAA-IGAQAGAALKKCVLELGGSDPFIV 243
Cdd:cd07112 166 TALRLAELALEAGLPAGVLNVVPGFGHTAGEALglhMD--VDALAFTGSTEVGRRfLEYSGQSNLKRVWLECGGKSPNIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 244 LNDA-DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
Cdd:cd07112 244 FADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 323 VEKTLAQGARLLLGGEK-MAGAGNYY-PPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTT 400
Cdd:cd07112 324 IESGKAEGARLVAGGKRvLTETGGFFvEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTS 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 3915524 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
Cdd:cd07112 404 DLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTW 461
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
12-451 |
2.79e-105 |
|
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: 320.79 E-value: 2.79e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07151 15 LNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAEHGPAM-LKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPN--VMGc 168
Cdd:cd07151 95 AAMAITREAATFPLRMeGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDtpITG- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 169 AQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAV-TVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA 247
Cdd:cd07151 174 GLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLiSFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 248 DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTL 327
Cdd:cd07151 254 DIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 328 AQGARLLLGGEKmagAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQ 407
Cdd:cd07151 334 EEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQ 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 3915524 408 MAARLECGGVFINGYCASD-ARVAFGGVKKSGFGRELSHFGLHEF 451
Cdd:cd07151 411 FARRIDAGMTHINDQPVNDePHVPFGGEKNSGLGRFNGEWALEEF 455
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
12-457 |
1.29e-104 |
|
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: 319.14 E-value: 1.29e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQAR-A 88
Cdd:cd07139 19 VSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRrA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 89 EVAKSANLCDWYAEHGPAMLKAEP-TLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMG 167
Cdd:cd07139 99 QGPGPAALLRYYAALARDFPFEERrPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA 247
Cdd:cd07139 179 DAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 248 DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTL 327
Cdd:cd07139 259 DLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 328 AQGARLLLGGEKMAG--AGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQA 405
Cdd:cd07139 339 AEGARLVTGGGRPAGldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERG 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 3915524 406 RQMAARLECGGVFINGYcASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07139 419 LAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
11-458 |
1.97e-104 |
|
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: 319.29 E-value: 1.97e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQL-SVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
Cdd:cd07131 18 SRNPADLEEVvGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYAEHGpAMLKAE--PTLVENQQAVIEYRPLGTILAIMPWNFP----LWQVMrgavPIILAGNGYLLKHAP 163
Cdd:cd07131 98 VQEAIDMAQYAAGEG-RRLFGEtvPSELPNKDAMTRRQPIGVVALITPWNFPvaipSWKIF----PALVCGNTVVFKPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 164 NVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
Cdd:cd07131 173 DTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEaLVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPII 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
Cdd:cd07131 253 VMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 323 VEKTLAQGARLLLGGEKMAG----AGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIF 398
Cdd:cd07131 333 NEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIY 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3915524 399 TTDETQARQMAARLECGGVFINGYC-ASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
Cdd:cd07131 413 TEDVNKAFRARRDLEAGITYVNAPTiGAEVHLPFGGVKKSGNGHREAGTTALDAFTEWKAV 473
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
12-457 |
1.22e-103 |
|
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: 316.30 E-value: 1.22e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAE-----HGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVM 166
Cdd:cd07094 84 RAIDTLRLAAEeaeriRGEEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 167 GCAQLIAQVFKDAGIPQGVYGWLNADN-DGVSQMIKDSRIAAVTVTGSVraGAAIGAQAGAALKKCVLELGGSDPFIVLN 245
Cdd:cd07094 164 LSALELAKILVEAGVPEGVLQVVTGEReVLGDAFAADERVAMLSFTGSA--AVGEALRANAGGKRIALELGGNAPVIVDR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEK 325
Cdd:cd07094 242 DADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 326 TLAQGARLLLGGEKmagAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQA 405
Cdd:cd07094 322 AVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 3915524 406 RQMAARLECGGVFINGYCASDA-RVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07094 399 FKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
12-442 |
4.99e-103 |
|
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: 314.63 E-value: 4.99e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQL 171
Cdd:cd07090 82 SSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 172 IAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLEL 251
Cdd:cd07090 162 LAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLEN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 252 AVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLAQGA 331
Cdd:cd07090 242 AVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 332 RLLLGGEKMAG-----AGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQAR 406
Cdd:cd07090 322 KVLCGGERVVPedgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAH 401
|
410 420 430
....*....|....*....|....*....|....*.
gi 3915524 407 QMAARLECGGVFINGYCASDARVAFGGVKKSGFGRE 442
Cdd:cd07090 402 RVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRE 437
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
30-457 |
7.17e-102 |
|
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: 311.05 E-value: 7.17e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 30 DIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAML- 108
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 109 KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVygw 188
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 189 LN------ADN-DGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRY 261
Cdd:cd07105 158 LNvvthspEDApEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 262 QNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDprdeeNALGPMARFDLRDELHHQVEKTLAQGARLLLGG-EKM 340
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlADE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 341 AGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN 420
Cdd:cd07105 313 SPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
410 420 430
....*....|....*....|....*....|....*...
gi 3915524 421 GYCASD-ARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07105 393 GMTVHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
12-457 |
7.28e-102 |
|
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: 311.87 E-value: 7.28e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFR--DWReTNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARA- 88
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDtgDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 89 EVAKSANLCDWYAEHGPAM-----LKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAP 163
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFpwefdLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 164 NVMGCAQLIAQVFKDAGIPQGVygwLN----ADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSD 239
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGV---VNvvtgSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 240 PFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDEL 319
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 320 HHQVEKTLAQGARLLLGGEKMAG--AGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATI 397
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 398 FTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
11-457 |
1.20e-101 |
|
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: 311.81 E-value: 1.20e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
Cdd:cd07086 17 SRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDWYAE-----HGPAMlkaePTLVENQQAVIEYRPLGTILAIMPWNFP----LWQvmrgAVPIILAGNGYLLKH 161
Cdd:cd07086 97 QEMIDICDYAVGlsrmlYGLTI----PSERPGHRLMEQWNPLGVVGVITAFNFPvavpGWN----AAIALVCGNTVVWKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 162 APNV----MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGG 237
Cdd:cd07086 169 SETTpltaIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 238 SDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRD 317
Cdd:cd07086 249 NNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 318 ELHHQVEKTLAQGARLLLGGEKMAG--AGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSA 395
Cdd:cd07086 329 KYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSS 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3915524 396 TIFTTDETQARQM--AARLECGGVFINGYCaSDARV--AFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07086 409 SIFTEDLREAFRWlgPKGSDCGIVNVNIPT-SGAEIggAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
12-442 |
1.42e-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: 308.41 E-value: 1.42e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAE-----HGPAM-LKAEPTlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNV 165
Cdd:cd07147 84 RAIDTFRIAAEeatriYGEVLpLDISAR-GEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSvrAGAAIGAQAGAALKKCVLELGGSDPFIVLN 245
Cdd:cd07147 163 PLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGS--PAVGWDLKARAGKKKVVLELGGNAAVIVDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEK 325
Cdd:cd07147 241 DADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 326 TLAQGARLLLGGEKmagAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQA 405
Cdd:cd07147 321 AVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKA 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 3915524 406 RQMAARLECGGVFINGycASDARV---AFGGVKKSGFGRE 442
Cdd:cd07147 398 LRAWDELEVGGVVIND--VPTFRVdhmPYGGVKDSGIGRE 435
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
12-457 |
1.70e-100 |
|
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: 308.11 E-value: 1.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYAE-----HGpamlKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWqVMRGAVPIIL-AGNGYLLKHAP 163
Cdd:cd07118 82 IEGAADLWRYAASlartlHG----DSYNNLGDDMLGLVLREPIGVVGIITPWNFPFL-ILSQKLPFALaAGCTVVVKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 164 NVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
Cdd:cd07118 157 FTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQaMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
Cdd:cd07118 237 VFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 323 VEKTLAQGARLLLGGEKMA-GAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTD 401
Cdd:cd07118 317 VDAGRAEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 3915524 402 ETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07118 397 IDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
11-458 |
9.38e-100 |
|
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: 306.29 E-value: 9.38e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQAR-AE 89
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYAehGPAMlKAEPTLVENQQAVIEY---RPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVM 166
Cdd:cd07115 81 VPRAADTFRYYA--GWAD-KIEGEVIPVRGPFLNYtvrEPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 167 GCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 245
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAaLVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEK 325
Cdd:cd07115 238 DADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 326 TLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQA 405
Cdd:cd07115 318 GREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 3915524 406 RQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
Cdd:cd07115 398 HRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVW 450
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
11-457 |
1.02e-98 |
|
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: 304.13 E-value: 1.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNID--YRAEKLRDIGKALRARSEEMAQMITREMGKPINQ-AR 87
Cdd:cd07091 23 TINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDprERGRLLNKLADLIERDRDELAALESLDNGKPLEEsAK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 88 AEVAKSANLCDWYAehGPAMlKAEPTLVENQQAVIEY---RPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPN 164
Cdd:cd07091 103 GDVALSIKCLRYYA--GWAD-KIQGKTIPIDGNFLAYtrrEPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 165 VMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDS-RIAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGGSDPFI 242
Cdd:cd07091 180 TPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHmDVDKIAFTGSTAVgRTIMEAAAKSNLKKVTLELGGKSPNI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
Cdd:cd07091 260 VFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 323 VEKTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDE 402
Cdd:cd07091 340 IESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDI 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 3915524 403 TQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07091 420 NKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
13-461 |
2.23e-98 |
|
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: 303.07 E-value: 2.23e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKP-INQARAEVA 91
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAEHGPAMLKAE----PTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMG 167
Cdd:cd07098 82 VTCEKIRWTLKHGEKALRPEsrpgGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 168 CAQ----LIAQVFKDAGIP----QGVYGWLNADNDGVSQMIKDSriaaVTVTGSVRAGAAIGAQAGAALKKCVLELGGSD 239
Cdd:cd07098 162 SSGfflsIIRECLAACGHDpdlvQLVTCLPETAEALTSHPVIDH----ITFIGSPPVGKKVMAAAAESLTPVVLELGGKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 240 PFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDEL 319
Cdd:cd07098 238 PAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 320 HHQVEKTLAQGARLLLGGEKMAGA----GNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSA 395
Cdd:cd07098 318 EELVADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGA 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3915524 396 TIFTTDETQARQMAARLECGGVFINGYCASDARVA--FGGVKKSGFGRELSHFGLHEFCNIQTVWKDR 461
Cdd:cd07098 398 SVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQlpFGGVKGSGFGRFAGEEGLRGLCNPKSVTEDR 465
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
13-457 |
2.35e-97 |
|
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: 300.04 E-value: 2.35e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 13 NPATGEQLSVLPWAGADDIENALQLAAAGfrdwRETNIDY-RAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALAASY----RSTLTRYqRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAEH-----GPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVM 166
Cdd:cd07146 81 RAADVLRFAAAEalrddGESFSCDLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 167 GCAQLIAQVFKDAGIPQGVYGWLNAD-NDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAalKKCVLELGGSDPFIVLN 245
Cdd:cd07146 161 LSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGY--KRQLLELGGNDPLIVMD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEK 325
Cdd:cd07146 239 DADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 326 TLAQGARLLLGGEKmagAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQA 405
Cdd:cd07146 319 AIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 3915524 406 RQMAARLECGGVFIN---GYcaSDARVAFGGVKKSGFG-RELSHFGLHEFCNIQTV 457
Cdd:cd07146 396 KRLVERLDVGTVNVNevpGF--RSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
17-440 |
3.54e-97 |
|
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: 299.21 E-value: 3.54e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 17 GEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANL 96
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 97 CdwyaeHGPAMLKAEP-----TLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPN--VMGCA 169
Cdd:cd07152 81 L-----HEAAGLPTQPqgeilPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRtpVSGGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 170 qLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 249
Cdd:cd07152 156 -VIARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 250 ELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLAQ 329
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 330 GARLLLGGEKmagAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMA 409
Cdd:cd07152 315 GARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430
....*....|....*....|....*....|..
gi 3915524 410 ARLECGGVFINGYCASDARVA-FGGVKKSGFG 440
Cdd:cd07152 392 DRLRTGMLHINDQTVNDEPHNpFGGMGASGNG 423
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
13-451 |
6.41e-97 |
|
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: 298.96 E-value: 6.41e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
Cdd:TIGR01780 3 NPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEILY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 93 SANLCDWYAEHGPAMLKAE-PTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQL 171
Cdd:TIGR01780 83 AASFLEWFAEEAKRVYGDTiPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 172 IAQVFKDAGIPQGVYGWLNADNDGV--SQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 249
Cdd:TIGR01780 163 LARLAEQAGIPKGVLNVITGSRAKEvgNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 250 ELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLAQ 329
Cdd:TIGR01780 243 DQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAVEK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 330 GARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMA 409
Cdd:TIGR01780 323 GAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWRVA 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 3915524 410 ARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEF 451
Cdd:TIGR01780 403 EALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEY 444
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
12-457 |
2.52e-95 |
|
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: 295.03 E-value: 2.52e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07110 2 INPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAEHGPAM-LKAEPTL---VENQQAVIEYRPLGTILAIMPWNFPL----WQVmrgaVPIILAGNGYLLKHAP 163
Cdd:cd07110 82 DVAGCFEYYADLAEQLdAKAERAVplpSEDFKARVRREPVGVVGLITPWNFPLlmaaWKV----APALAAGCTVVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 164 NVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGV-SQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
Cdd:cd07110 158 LTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAgAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
Cdd:cd07110 238 VFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 323 VEKTLAQGARLLLGGEKMA--GAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTT 400
Cdd:cd07110 318 IARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 3915524 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07110 398 DAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
12-457 |
4.97e-95 |
|
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: 293.85 E-value: 4.97e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARA-EV 90
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDWYA---EHGPAMLKAEptLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMG 167
Cdd:cd07092 82 PGAVDNFRFFAgaaRTLEGPAAGE--YLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 168 CAQLIAQVFKDaGIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 246
Cdd:cd07092 160 TTLLLAELAAE-VLPPGVVNVVCGGGASAGDaLVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 247 ADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKt 326
Cdd:cd07092 239 ADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVER- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 327 LAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQAR 406
Cdd:cd07092 318 APAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAM 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 3915524 407 QMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07092 398 RLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
12-458 |
2.71e-93 |
|
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: 290.37 E-value: 2.71e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFR--DWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
Cdd:cd07119 18 INPANGEVIATVPEGTAEDAKRAIAAARRAFDsgEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEID 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCA 169
Cdd:cd07119 98 IDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 170 QLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSR-IAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDAD 248
Cdd:cd07119 178 IALFELIEEAGLPAGVVNLVTGSGATVGAELAESPdVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADAD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 249 LELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLA 328
Cdd:cd07119 258 FETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 329 QGARLLLGGEKMAGA----GNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQ 404
Cdd:cd07119 338 EGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIAR 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 3915524 405 ARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
Cdd:cd07119 418 ANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHIN 471
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
11-457 |
4.85e-93 |
|
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: 289.13 E-value: 4.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFR-DWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFEsGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYAE-----HGPAMlkaepTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPN 164
Cdd:cd07109 81 VEAAARYFEYYGGaadklHGETI-----PLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 165 VMGCAQLIAQVFKDAGIPQGVYGWLNA-DNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV 243
Cdd:cd07109 156 APLTALRLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 244 LNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENaLGPMARFDLRDELHHQV 323
Cdd:cd07109 236 FADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD-LGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 324 EKTLAQGARLLLGGEKMAGA---GNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTT 400
Cdd:cd07109 315 ARARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 3915524 401 DETQARQMAARLECGGVFINGYCASDA-RVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07109 395 DGDRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
11-457 |
1.24e-92 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 289.09 E-value: 1.24e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQAR-AE 89
Cdd:PRK13252 26 VINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSvVD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCA 169
Cdd:PRK13252 106 IVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 170 QLIAQVFKDAGIPQGVYGWLNADNDgVSQMI-KDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDAD 248
Cdd:PRK13252 186 LKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLtEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 249 LELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLA 328
Cdd:PRK13252 265 LDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 329 QGARLLLGGEKM----AGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQ 404
Cdd:PRK13252 345 EGARLLCGGERLteggFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSR 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 3915524 405 ARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:PRK13252 425 AHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
12-442 |
2.35e-92 |
|
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: 287.93 E-value: 2.35e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETN-IDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
Cdd:cd07082 21 YSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMpLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDWYAE-----HGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNV 165
Cdd:cd07082 101 DRTIDYIRDTIEelkrlDGDSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 166 MGCAQLIAQVFKDAGIPQGVYGWLNAD-NDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGaaLKKCVLELGGSDPFIVL 244
Cdd:cd07082 181 VLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP--MKRLVLELGGKDPAIVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
Cdd:cd07082 259 PDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLID 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 325 KTLAQGARLLLGGEKMagAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQ 404
Cdd:cd07082 339 DAVAKGATVLNGGGRE--GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINK 416
|
410 420 430
....*....|....*....|....*....|....*....
gi 3915524 405 ARQMAARLECGGVFINGYCASDARV-AFGGVKKSGFGRE 442
Cdd:cd07082 417 ARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQ 455
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
11-440 |
3.37e-91 |
|
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: 286.04 E-value: 3.37e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPA-TGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
Cdd:cd07124 50 SRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADAD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYAEHgpaMLKAEPTLVEN---QQAVIEYRPLGTILAIMPWNFPLwQVMRG-AVPIILAGNGYLLKHAPNV 165
Cdd:cd07124 130 VAEAIDFLEYYARE---MLRLRGFPVEMvpgEDNRYVYRPLGVGAVISPWNFPL-AILAGmTTAALVTGNTVVLKPAEDT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVR------AGAAIGAQAGAALKKCVLELGGS 238
Cdd:cd07124 206 PVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDyLVEHPDVRFIAFTGSREvglriyERAAKVQPGQKWLKRVIAEMGGK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318
Cdd:cd07124 286 NAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 319 LHHQVEkTLAQGARLLLGGEKMAGA--GNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSAT 396
Cdd:cd07124 366 IRRYIE-IGKSEGRLLLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGG 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 3915524 397 IFTTDETQARQMAARLECGGVFINGYCASdARVA---FGGVKKSGFG 440
Cdd:cd07124 445 VFSRSPEHLERARREFEVGNLYANRKITG-ALVGrqpFGGFKMSGTG 490
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
11-457 |
1.58e-89 |
|
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: 280.83 E-value: 1.58e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRD-WRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQ-ARA 88
Cdd:cd07144 27 TVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnALG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 89 EVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGC 168
Cdd:cd07144 107 DLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 169 AQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDS-RIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA 247
Cdd:cd07144 187 LLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 248 DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAA-ALKMGDPRDEENALGPMARFDLRDELHHQVEKT 326
Cdd:cd07144 267 DLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 327 LAQGARLLLGGEKMA---GAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDET 403
Cdd:cd07144 347 KKEGAKLVYGGEKAPeglGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIR 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 3915524 404 QARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07144 427 RAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
11-442 |
1.04e-88 |
|
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: 277.72 E-value: 1.04e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDWYAEHGPaMLKAE--PTLVENQQaVIEYRPLGTILAIMPWNFP-LWQVMRGAVPIIlAGNGYLLK---HAP- 163
Cdd:cd07107 81 MVAAALLDYFAGLVT-ELKGEtiPVGGRNLH-YTLREPYGVVARIVAFNHPlMFAAAKIAAPLA-AGNTVVVKppeQAPl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 164 NVMGCAQLIAQVFkdagiPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
Cdd:cd07107 158 SALRLAELAREVL-----PPGVFNILPGDGATAGAaLVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 243 VLNDADLELAVKAAVAG-RYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
Cdd:cd07107 233 VFPDADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 322 QVEKTLAQGARLLLGG---EKMAGAGNYY-PPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATI 397
Cdd:cd07107 313 YIDSAKREGARLVTGGgrpEGPALEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAI 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 3915524 398 FTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRE 442
Cdd:cd07107 393 WTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGRE 437
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
12-457 |
3.52e-88 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 276.50 E-value: 3.52e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAEHGPAMLKAE------PTLVenqQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNV 165
Cdd:cd07101 81 DVAIVARYYARRAERLLKPRrrrgaiPVLT---RTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 245
Cdd:cd07101 158 ALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVD-NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEK 325
Cdd:cd07101 237 DADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 326 TLAQGARLLLGGEKMAGAGNY-YPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQ 404
Cdd:cd07101 317 AVAKGATVLAGGRARPDLGPYfYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 3915524 405 ARQMAARLECGGVFIN-GYCASDARVA--FGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07101 397 GRRIAARLRAGTVNVNeGYAAAWASIDapMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
6-457 |
4.76e-88 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 276.79 E-value: 4.76e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 6 ATHAIsINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQ 85
Cdd:PRK13473 17 EKQPV-YNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 86 ARA-EVAKSANLCDWYAE-----HGPAmlKAEptLVENQQAVIEYRPLGTILAIMPWNFPL----WQVMrgavPIILAGN 155
Cdd:PRK13473 96 ALNdEIPAIVDVFRFFAGaarclEGKA--AGE--YLEGHTSMIRRDPVGVVASIAPWNYPLmmaaWKLA----PALAAGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 156 GYLLKHAPNVMGCAQLIAQVFKDAgIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLE 234
Cdd:PRK13473 168 TVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDaLVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 235 LGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFD 314
Cdd:PRK13473 247 LGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 315 LRDELHHQVEKTLAQG-ARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGL 393
Cdd:PRK13473 327 HRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGL 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3915524 394 SATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:PRK13473 407 ASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
57-458 |
7.18e-87 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 271.61 E-value: 7.18e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 57 LRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPamlKAEPTLVE----NQQAVIEYRPLGTILA 132
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWAR---RYEGEIIQsdrpGENILLFKRALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 133 IMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMI-KDSRIAAVTVT 211
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELaGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 212 GSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAA 291
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 292 AAALKMGDPRDEEN-ALGPMARFDLRDELHHQVEKTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPV 370
Cdd:PRK10090 238 MQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 371 AAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFINgycasdaRVAF-------GGVKKSGFGREL 443
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN-------RENFeamqgfhAGWRKSGIGGAD 390
|
410
....*....|....*
gi 3915524 444 SHFGLHEFCNIQTVW 458
Cdd:PRK10090 391 GKHGLHEYLQTQVVY 405
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
5-457 |
4.83e-86 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 272.91 E-value: 4.83e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 5 PATHAIsINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPIN 84
Cdd:PRK09407 31 GPTREV-TAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 85 QARAEVAKSANLCDWYAEHGPAMLKAE------PTLVenqQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYL 158
Cdd:PRK09407 110 HAFEEVLDVALTARYYARRAPKLLAPRrragalPVLT---KTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 159 LKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGS 238
Cdd:PRK09407 187 LKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVD-NADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318
Cdd:PRK09407 266 NPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLET 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 319 LHHQVEKTLAQGARLLLGGEKMAGAGNY-YPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATI 397
Cdd:PRK09407 346 VSAHVDDAVAKGATVLAGGKARPDLGPLfYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASV 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3915524 398 FTTDETQARQMAARLECGGVFIN-GYCASDARVA--FGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:PRK09407 426 WTGDTARGRAIAARIRAGTVNVNeGYAAAWGSVDapMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
13-455 |
6.23e-86 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 271.39 E-value: 6.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
Cdd:PRK11241 32 NPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 93 SANLCDWYAEHGPAML-KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQL 171
Cdd:PRK11241 112 AASFIEWFAEEGKRIYgDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 172 IAQVFKDAGIPQGVYGWLNADNDGV-SQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLE 250
Cdd:PRK11241 192 LAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 251 LAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLAQG 330
Cdd:PRK11241 272 KAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 331 ARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAA 410
Cdd:PRK11241 352 ARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGE 431
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 3915524 411 RLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQ 455
Cdd:PRK11241 432 ALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
12-457 |
9.33e-86 |
|
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: 270.39 E-value: 9.33e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPI-NQARAEV 90
Cdd:cd07108 2 INPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDWYAEHGPAmLKAEpTLVENQQaVIEY---RPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLK---HAP- 163
Cdd:cd07108 82 AVLADLFRYFGGLAGE-LKGE-TLPFGPD-VLTYtvrEPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKaaeDAPl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 164 NVMGCAQLIAQVfkdagIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
Cdd:cd07108 159 AVLLLAEILAQV-----LPAGVLNVITGYGEECGAaLVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 243 VLNDADLELAVKAAVAG-RYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
Cdd:cd07108 234 VFPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 322 QVEKTLA-QGARLLLGG----EKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSAT 396
Cdd:cd07108 314 YIDLGLStSGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAY 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3915524 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFG-LHEFCNIQTV 457
Cdd:cd07108 394 VWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
12-457 |
1.98e-84 |
|
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: 267.39 E-value: 1.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRD-WRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARA-E 89
Cdd:cd07113 20 TNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYAE-----HGPAMLKAEPTLV-ENQQAVIEYRPLGTILAIMPWNFPL----WQVMrgavPIILAGNGYLL 159
Cdd:cd07113 100 VGQSANFLRYFAGwatkiNGETLAPSIPSMQgERYTAFTRREPVGVVAGIVPWNFSVmiavWKIG----AALATGCTIVI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 160 K---HAPNVMgcaQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELG 236
Cdd:cd07113 176 KpseFTPLTL---LRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 237 GSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLR 316
Cdd:cd07113 253 GKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 317 DELHHQVEKTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSAT 396
Cdd:cd07113 333 DKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTAS 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3915524 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07113 413 VWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
13-440 |
1.14e-83 |
|
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: 265.53 E-value: 1.14e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAE---KLRDIgkaLRARSEEMAQMITREMGKPINQARAE 89
Cdd:cd07085 22 NPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQvmfKFRQL---LEENLDELARLITLEHGKTLADARGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDwYAEHGPAMLKAEpTLVENQQAVIEY---RPLGTILAIMPWNFP----LWqvMrgaVPI-ILAGNGYLLKH 161
Cdd:cd07085 99 VLRGLEVVE-FACSIPHLLKGE-YLENVARGIDTYsyrQPLGVVAGITPFNFPamipLW--M---FPMaIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 162 APNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 241
Cdd:cd07085 172 SERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
Cdd:cd07085 252 VVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 322 QVEKTLAQGARLLLGGE--KMAG--AGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATI 397
Cdd:cd07085 332 LIESGVEEGAKLVLDGRgvKVPGyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAI 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 3915524 398 FTTDETQARQMAARLECGGVFIN-GYCASDARVAFGGVKKSGFG 440
Cdd:cd07085 412 FTRSGAAARKFQREVDAGMVGINvPIPVPLAFFSFGGWKGSFFG 455
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
12-457 |
5.63e-83 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 264.67 E-value: 5.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGF-----RDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQA 86
Cdd:PLN02467 28 VNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 87 RAEVAKSANLCDWYAEHGPAMLKAEPTLV----ENQQAVIEYRPLGTILAIMPWNFPL----WQVmrgaVPIILAGNGYL 158
Cdd:PLN02467 108 AWDMDDVAGCFEYYADLAEALDAKQKAPVslpmETFKGYVLKEPLGVVGLITPWNYPLlmatWKV----APALAAGCTAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 159 LKhaPNVMG---CAQLiAQVFKDAGIPQGVYGWLN-ADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLE 234
Cdd:PLN02467 184 LK--PSELAsvtCLEL-ADICREVGLPPGVLNVVTgLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 235 LGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFD 314
Cdd:PLN02467 261 LGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 315 LRDELHHQVEKTLAQGARLLLGGEKMAG--AGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFG 392
Cdd:PLN02467 341 QYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYG 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3915524 393 LSATIFTTDETQARQMAARLECGGVFINgyCASD--ARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:PLN02467 421 LAGAVISNDLERCERVSEAFQAGIVWIN--CSQPcfCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
12-457 |
1.41e-80 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 257.46 E-value: 1.41e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFR-DW-RETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQ-ARA 88
Cdd:cd07143 27 YNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWgLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTaKRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 89 EVAKSANLCDWYA-----EHGPAMLKAEPTLvenqqAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAP 163
Cdd:cd07143 107 DVQASADTFRYYGgwadkIHGQVIETDIKKL-----TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 164 NVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDS-RIAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGGSDPF 241
Cdd:cd07143 182 LTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHmDIDKVAFTGSTLVgRKVMEAAAKSNLKKVTLELGGKSPN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
Cdd:cd07143 262 IVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 322 QVEKTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTD 401
Cdd:cd07143 342 YIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNN 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 3915524 402 ETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07143 422 INNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
11-446 |
1.63e-80 |
|
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: 257.27 E-value: 1.63e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQAR-AE 89
Cdd:cd07559 20 NYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLaAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYAehgpAMLKAEP----TLVENQQAVIEYRPLGTILAIMPWNFPL----WQVmrgaVPIILAGNGYLLKH 161
Cdd:cd07559 100 IPLAIDHFRYFA----GVIRAQEgslsEIDEDTLSYHFHEPLGVVGQIIPWNFPLlmaaWKL----APALAAGNTVVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 162 AP----NVMGCAQLIAQVfkdagIPQGVYGWLNADNDGVSQMIKDS-RIAAVTVTGSVRAGAAIGAQAGAALKKCVLELG 236
Cdd:cd07559 172 ASqtplSILVLMELIGDL-----LPKGVVNVVTGFGSEAGKPLASHpRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 237 GSDPFIVLNDA-----DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMA 311
Cdd:cd07559 247 GKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 312 RFDLRDELHHQVEKTLAQGARLLLGGEKMAG----AGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELAN 387
Cdd:cd07559 327 SKDQLEKILSYVDIGKEEGAEVLTGGERLTLggldKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIAN 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3915524 388 DSEFGLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRE-----LSHF 446
Cdd:cd07559 407 DTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGREthkmmLDHY 470
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
11-457 |
1.13e-76 |
|
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: 246.49 E-value: 1.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFR--DWReTNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARA 88
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 89 EVAKSANLCDWYA-----EHGpAMLKAEPtlveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAP 163
Cdd:cd07120 80 EISGAISELRYYAglartEAG-RMIEPEP----GSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 164 NVMGCAQLIAQVFKDA-GIPQGVYGWLNADNDGVSQMIKDS-RIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 241
Cdd:cd07120 155 QTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASpDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
Cdd:cd07120 235 IVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 322 QVEKTLAQGARLLLGGEKMAG---AGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIF 398
Cdd:cd07120 315 MVERAIAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVW 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 3915524 399 TTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07120 395 TRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
11-458 |
1.74e-76 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 247.50 E-value: 1.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFR--DWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQA-R 87
Cdd:PRK09847 39 TVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 88 AEVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMG 167
Cdd:PRK09847 119 DDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMI-KDSRIAAVTVTGSVRAGAAIGAQA-GAALKKCVLELGGSDPFIVLN 245
Cdd:PRK09847 199 SAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALsRHNDIDAIAFTGSTRTGKQLLKDAgDSNMKRVWLEAGGKSANIVFA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 246 DA-DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
Cdd:PRK09847 279 DCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIR 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 325 KTLAQGaRLLLGGEKMAGAGnYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQ 404
Cdd:PRK09847 359 EGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSR 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 3915524 405 ARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
Cdd:PRK09847 437 AHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIW 490
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
11-451 |
2.75e-76 |
|
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: 246.54 E-value: 2.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQAR-AE 89
Cdd:cd07111 41 TINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRdCD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYAehGPAMLKAEptlvenqqAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCA 169
Cdd:cd07111 121 IPLVARHFYHHA--GWAQLLDT--------ELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 170 QLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 249
Cdd:cd07111 191 LLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 250 ELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLAQ 329
Cdd:cd07111 271 DSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 330 GARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMA 409
Cdd:cd07111 351 GADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVA 430
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 3915524 410 ARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEF 451
Cdd:cd07111 431 LSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
12-457 |
4.93e-75 |
|
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: 243.02 E-value: 4.93e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPI-NQAR 87
Cdd:cd07141 27 INPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFsKSYL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 88 AEVAKSANLCDWYAE-----HGpamlKAEPtLVENQQAVIEYRPLGTILAIMPWNFPL----WQVmrgaVPIILAGNGYL 158
Cdd:cd07141 107 VDLPGAIKVLRYYAGwadkiHG----KTIP-MDGDFFTYTRHEPVGVCGQIIPWNFPLlmaaWKL----APALACGNTVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 159 LKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDS-RIAAVTVTGSVRA-GAAIGAQAGAALKKCVLELG 236
Cdd:cd07141 178 LKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHpDIDKVAFTGSTEVgKLIQQAAGKSNLKRVTLELG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 237 GSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLR 316
Cdd:cd07141 258 GKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQF 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 317 DELHHQVEKTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSAT 396
Cdd:cd07141 338 KKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAA 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3915524 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07141 418 VFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
10-438 |
1.12e-74 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 243.30 E-value: 1.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 10 ISINPA-TGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARA 88
Cdd:PRK03137 53 VSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 89 EVAKSANLCDWYAEHgpaMLK----AEPTLVENQQAVIEYRPLGTILAIMPWNFPLwQVMRG-AVPIILAGNGYLLKHAP 163
Cdd:PRK03137 133 DTAEAIDFLEYYARQ---MLKladgKPVESRPGEHNRYFYIPLGVGVVISPWNFPF-AIMAGmTLAAIVAGNTVLLKPAS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 164 NVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDS-RIAAVTVTGS------VRAGAAIGAQAGAALKKCVLELG 236
Cdd:PRK03137 209 DTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHpKTRFITFTGSrevglrIYERAAKVQPGQIWLKRVIAEMG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 237 GSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPrdEENA-LGPMARFDL 315
Cdd:PRK03137 289 GKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP--EDNAyMGPVINQAS 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 316 RDELHHQVEKTLAQGaRLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSA 395
Cdd:PRK03137 367 FDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTG 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 3915524 396 TIFTTDE---TQARQmaaRLECGGVFINGYCASdARV---AFGGVKKSG 438
Cdd:PRK03137 446 AVISNNRehlEKARR---EFHVGNLYFNRGCTG-AIVgyhPFGGFNMSG 490
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
11-442 |
3.86e-74 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 240.82 E-value: 3.86e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARA-E 89
Cdd:cd07117 20 SYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYA-----EHGPAMLKAEPTLvenqqAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAP- 163
Cdd:cd07117 100 IPLAADHFRYFAgviraEEGSANMIDEDTL-----SIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSt 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 164 ---NVMGCAQLIAQVfkdagIPQGVYGWLNADNDGVSQMIKDSR-IAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSD 239
Cdd:cd07117 175 tslSLLELAKIIQDV-----LPKGVVNIVTGKGSKSGEYLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 240 PFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDEL 319
Cdd:cd07117 250 ANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 320 HHQVEKTLAQGARLLLGGEKMAG----AGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSA 395
Cdd:cd07117 330 LSYVDIAKEEGAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGG 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 3915524 396 TIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRE 442
Cdd:cd07117 410 GVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRE 456
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
11-442 |
1.76e-73 |
|
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: 239.03 E-value: 1.76e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
Cdd:cd07130 16 SISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDwYAE------HGPAMLKAEPTlvenqQAVIE-YRPLGTILAIMPWNFPL----WQVMRGAVpiilAGNGYLL 159
Cdd:cd07130 96 QEMIDICD-FAVglsrqlYGLTIPSERPG-----HRMMEqWNPLGVVGVITAFNFPVavwgWNAAIALV----CGNVVVW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 160 KHAPNV----MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLEL 235
Cdd:cd07130 166 KPSPTTpltaIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 236 GGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDL 315
Cdd:cd07130 246 GGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 316 RDELHHQVEKTLAQGARLLLGGEKMAGAGNYYPPTVlANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSA 395
Cdd:cd07130 326 VDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSS 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 3915524 396 TIFTTDETQA-RQMAAR-LECGGVFINgYCASDARV--AFGGVKKSGFGRE 442
Cdd:cd07130 405 SIFTTDLRNAfRWLGPKgSDCGIVNVN-IGTSGAEIggAFGGEKETGGGRE 454
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
11-457 |
5.90e-72 |
|
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: 235.08 E-value: 5.90e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQAR- 87
Cdd:cd07142 23 TIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 88 AEVAKSANLCDWYAE-----HGPAMLKAEPTLVENQqavieYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHA 162
Cdd:cd07142 103 AEVPLAARLFRYYAGwadkiHGMTLPADGPHHVYTL-----HEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSR-IAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGGSDP 240
Cdd:cd07142 178 EQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMdVDKVAFTGSTEVgKIIMQLAAKSNLKPVTLELGGKSP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
Cdd:cd07142 258 FIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKIL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 321 HQVEKTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTT 400
Cdd:cd07142 338 SYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSK 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 3915524 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07142 418 NIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
11-457 |
1.07e-69 |
|
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: 229.30 E-value: 1.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQA-R 87
Cdd:cd07140 25 TINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLAlK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 88 AEVAKS-------ANLCDWYAEHGPAMLKAEPtlveNQQAVIEYR-PLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLL 159
Cdd:cd07140 105 THVGMSiqtfryfAGWCDKIQGKTIPINQARP----NRNLTLTKRePIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 160 KHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKD-SRIAAVTVTGSVRA-GAAIGAQAGAALKKCVLELGG 237
Cdd:cd07140 181 KPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDhPDVRKLGFTGSTPIgKHIMKSCAVSNLKKVSLELGG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 238 SDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRD 317
Cdd:cd07140 261 KSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 318 ELHHQVEKTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDA--EHALELANDSEFGLSA 395
Cdd:cd07140 341 KLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEYGLAS 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3915524 396 TIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07140 421 GVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
30-446 |
2.86e-65 |
|
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: 216.37 E-value: 2.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 30 DIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWY--AEHGPAM 107
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISikAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 108 LKAEPTlvENQQAVIEYRPLGTILAIMPWNFPLwQVMRGA-VPIILAGNGYLLK---HAPNVmgcAQLIAQVFKDAGIPQ 183
Cdd:cd07095 81 ERATPM--AQGRAVLRHRPHGVMAVFGPFNFPG-HLPNGHiVPALLAGNTVVFKpseLTPAV---AELMVELWEEAGLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 184 GVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCV-LELGGSDPFIVLNDADLELAVKAAVAGRYQ 262
Cdd:cd07095 155 GVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLIVQSAFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 263 NTGQVCAAAKRFIIEEG-IASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLAQGARLLLGGEKMA 341
Cdd:cd07095 235 TAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 342 GAGNYYPPTVLanvtpEMTAFR----EEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGV 417
Cdd:cd07095 315 AGTAFLSPGII-----DVTDAAdvpdEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIV 389
|
410 420 430
....*....|....*....|....*....|...
gi 3915524 418 FIN----GycASDARvAFGGVKKSGFGRELSHF 446
Cdd:cd07095 390 NWNrpttG--ASSTA-PFGGVGLSGNHRPSAYY 419
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
1-457 |
9.80e-65 |
|
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: 217.06 E-value: 9.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 1 MTITPATHAIsINPATGEQ-LSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREM 79
Cdd:cd07125 41 ETETGEGAPV-IDPADHERtIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 80 GKPINQARAEVAKSANLCDWY---AEHGPAMLKAEPTLVENQQavIEYRPLGTILAIMPWNFPLwqvmrgAVPI------ 150
Cdd:cd07125 120 GKTLADADAEVREAIDFCRYYaaqARELFSDPELPGPTGELNG--LELHGRGVFVCISPWNFPL------AIFTgqiaaa 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 151 ILAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAA---IGAQAGA 226
Cdd:cd07125 192 LAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEaLVAHPRIDGVIFTGSTETAKLinrALAERDG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 227 ALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENA 306
Cdd:cd07125 272 PILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 307 LGPMARFDLRDELHHQVEktLAQGARLLLGGEKM-AGAGNYYPPTVLANVTPEmtAFREEMFGPVAAITIAK--DAEHAL 383
Cdd:cd07125 352 VGPLIDKPAGKLLRAHTE--LMRGEAWLIAPAPLdDGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFKaeDLDEAI 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 384 ELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN----GycASDARVAFGGVKKSGFGREL--SHFgLHEFCNIQTV 457
Cdd:cd07125 428 EDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrnitG--AIVGRQPFGGWGLSGTGPKAggPNY-LLRFGNEKTV 504
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
11-457 |
6.72e-63 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 211.99 E-value: 6.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARA 88
Cdd:PLN02766 40 TRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 89 -EVAKSANLCDWYAE-----HGPAMLKAEP----TLVEnqqavieyrPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYL 158
Cdd:PLN02766 120 vDIPAAAGLLRYYAGaadkiHGETLKMSRQlqgyTLKE---------PIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 159 LKHAPNVMGCAQLIAQVFKDAGIPQGV------YGwLNADNDGVSQMIKDSriaaVTVTGSVRA-GAAIGAQAGAALKKC 231
Cdd:PLN02766 191 VKPAEQTPLSALFYAHLAKLAGVPDGVinvvtgFG-PTAGAAIASHMDVDK----VSFTGSTEVgRKIMQAAATSNLKQV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 232 VLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMA 311
Cdd:PLN02766 266 SLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 312 RFDLRDELHHQVEKTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEF 391
Cdd:PLN02766 346 DKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKY 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3915524 392 GLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:PLN02766 426 GLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
11-446 |
3.74e-59 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 201.53 E-value: 3.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQA-RAE 89
Cdd:cd07116 20 NITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETlAAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 90 VAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCA 169
Cdd:cd07116 100 IPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 170 QLIAQVFKDAgIPQGVYGWLNADNDGVSQMIKDS-RIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI----VL 244
Cdd:cd07116 180 LVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSkRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIffadVM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 245 N--DADLELAVKAAVAGRYqNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
Cdd:cd07116 259 DadDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 323 VEKTLAQGARLLLGGEK-----MAGAGNYYPPTVLANvtPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATI 397
Cdd:cd07116 338 IDIGKEEGAEVLTGGERnelggLLGGGYYVPTTFKGG--NKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGV 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 3915524 398 FTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRE-----LSHF 446
Cdd:cd07116 416 WTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGREnhkmmLDHY 469
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
12-440 |
9.76e-58 |
|
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: 196.87 E-value: 9.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDY-RAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWLPAHeRIAILERLADLMEERADELALLIAREGGKPLVDAKVEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDWYAEH-----GPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNV 165
Cdd:cd07148 84 TRAIDGVELAADElgqlgGREIPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAAlKKCVLELGGSDPFIVLN 245
Cdd:cd07148 164 PLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEK 325
Cdd:cd07148 243 SADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 326 TLAQGARLLLGGEKMAGAgnYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQA 405
Cdd:cd07148 323 AVAAGARLLCGGKRLSDT--TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVA 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 3915524 406 RQMAARLECGGVFINGYCAsdARV---AFGGVKKSGFG 440
Cdd:cd07148 401 LKAVRRLDATAVMVNDHTA--FRVdwmPFAGRRQSGYG 436
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
8-440 |
2.96e-56 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 194.33 E-value: 2.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 8 HAISINP-ATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQA 86
Cdd:cd07083 33 RMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 87 RAEVAKSANLCDWYAEH-----GPAMLKAEPTLVENQQAvieYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKH 161
Cdd:cd07083 113 IDDVAEAIDFIRYYARAalrlrYPAVEVVPYPGEDNESF---YVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 162 APNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGV-SQMIKDSRIAAVTVTGSVRA------GAAIGAQAGAALKKCVLE 234
Cdd:cd07083 190 AEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETgkkiyeAAARLAPGQTWFKRLYVE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 235 LGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFD 314
Cdd:cd07083 270 TGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 315 LRDELHHQVEKTLAQGaRLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAE--HALELANDSEFG 392
Cdd:cd07083 350 QEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYG 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 3915524 393 LSATIFTTDETQARQMAARLECGGVFINGYcASDARVA---FGGVKKSGFG 440
Cdd:cd07083 429 LTGGVYSRKREHLEEARREFHVGNLYINRK-ITGALVGvqpFGGFKLSGTN 478
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
11-457 |
4.77e-56 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 194.64 E-value: 4.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQAR- 87
Cdd:PLN02466 77 TLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAk 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 88 AEVAKSANLCDWYAE-----HGPAMLKAEPTLVEnqqavIEYRPLGTILAIMPWNFPL----WQVMrgavPIILAGNGYL 158
Cdd:PLN02466 157 AELPMFARLFRYYAGwadkiHGLTVPADGPHHVQ-----TLHEPIGVAGQIIPWNFPLlmfaWKVG----PALACGNTIV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 159 LKHAPNVMGCAQLIAQVFKDAGIPQGV------YGwLNADNDGVSQMIKDsRIA--AVTVTGSVragaAIGAQAGAALKK 230
Cdd:PLN02466 228 LKTAEQTPLSALYAAKLLHEAGLPPGVlnvvsgFG-PTAGAALASHMDVD-KLAftGSTDTGKI----VLELAAKSNLKP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 231 CVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERfvAAAAALK--MGDPRDEENALG 308
Cdd:PLN02466 302 VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKrvVGDPFKKGVEQG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 309 PMARFDLRDELHHQVEKTLAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELAND 388
Cdd:PLN02466 380 PQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANN 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3915524 389 SEFGLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:PLN02466 460 TRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
13-440 |
6.80e-56 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 192.79 E-value: 6.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
Cdd:TIGR01722 22 NPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 93 SANLCDwYAEHGPAMLKAEP-TLVENQQAVIEYR-PLGTILAIMPWNF----PLWQvmrgaVPIILA-GNGYLLKHAPNV 165
Cdd:TIGR01722 102 GLEVVE-HACGVNSLLKGETsTQVATRVDVYSIRqPLGVCAGITPFNFpamiPLWM-----FPIAIAcGNTFVLKPSEKV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 245
Cdd:TIGR01722 176 PSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIeEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEK 325
Cdd:TIGR01722 256 DADKDAAADALVGAAYGAAGQRCMAISAAVL-VGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 326 TLAQGARLLLGGE--KMAG--AGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTD 401
Cdd:TIGR01722 335 GAAEGAEVLLDGRgyKVDGyeEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRD 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 3915524 402 ETQARQMAARLECGGVFIN-------GYcasdarVAFGGVKKSGFG 440
Cdd:TIGR01722 415 GAAARRFQHEIEVGQVGVNvpipvplPY------FSFTGWKDSFFG 454
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
11-442 |
8.70e-54 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 187.73 E-value: 8.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 11 SINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
Cdd:PLN02315 38 SVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDwYAEHGPAMLKAE--PTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNV--- 165
Cdd:PLN02315 118 QEIIDMCD-FAVGLSRQLNGSiiPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTpli 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 166 -MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVL 244
Cdd:PLN02315 197 tIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVM 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
Cdd:PLN02315 277 DDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 325 KTLAQGARLLLGGEKMAGAGNYYPPTVLaNVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTD-ET 403
Cdd:PLN02315 357 IIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNpET 435
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 3915524 404 QARQMAAR-LECGGVFINgYCASDARV--AFGGVKKSGFGRE 442
Cdd:PLN02315 436 IFKWIGPLgSDCGIVNVN-IPTNGAEIggAFGGEKATGGGRE 476
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
10-438 |
9.01e-51 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 179.38 E-value: 9.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 10 ISINPATGEQLsvlpWAG----ADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQ 85
Cdd:PRK09457 18 ESRNPVSGEVL----WQGndatAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 86 ARAEVAKSANLCDW----YAEHGPAmlKAEPTLveNQQAVIEYRPLGTILAIMPWNFPlwqvmrG------AVPIILAGN 155
Cdd:PRK09457 94 AATEVTAMINKIAIsiqaYHERTGE--KRSEMA--DGAAVLRHRPHGVVAVFGPYNFP------GhlpnghIVPALLAGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 156 GYLLK---HAPNVmgcAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCV 232
Cdd:PRK09457 164 TVVFKpseLTPWV---AELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 233 -LELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGI-ASAFTERFVAAAAALKMGDPrDEENA--LG 308
Cdd:PRK09457 241 aLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRW-DAEPQpfMG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 309 PMARFDLRDELHHQVEKTLAQGARLLLGGEKMAGAgnyypptvLANVTP---EMTAFR----EEMFGPVAAITIAKDAEH 381
Cdd:PRK09457 320 AVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAG--------TGLLTPgiiDVTGVAelpdEEYFGPLLQVVRYDDFDE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3915524 382 ALELANDSEFGLSATIFTTDETQARQMAARLECGGVF----INGyCASDArvAFGGVKKSG 438
Cdd:PRK09457 392 AIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNwnkpLTG-ASSAA--PFGGVGASG 449
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
12-460 |
2.96e-50 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 180.33 E-value: 2.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:PLN02419 134 INPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIF 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLcdwyAEH--GPAMLKAEPTLVENQQAVIEY---RPLGTILAIMPWNFP----LWQVmrgavPI-ILAGNGYLLKH 161
Cdd:PLN02419 214 RGLEV----VEHacGMATLQMGEYLPNVSNGVDTYsirEPLGVCAGICPFNFPamipLWMF-----PVaVTCGNTFILKP 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 162 APNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 241
Cdd:PLN02419 285 SEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRfIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
Cdd:PLN02419 365 LVLPDANIDATLNALLAAGFGAAGQRCMALST-VVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 322 QVEKTLAQGARLLLGGEKMA----GAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATI 397
Cdd:PLN02419 444 LIQSGVDDGAKLLLDGRDIVvpgyEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAI 523
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 398 FTTDETQARQMAARLECGGVFIN-GYCASDARVAFGGvKKSGFGRELSHF---GLHEFCNIQTV---WKD 460
Cdd:PLN02419 524 FTSSGAAARKFQMDIEAGQIGINvPIPVPLPFFSFTG-NKASFAGDLNFYgkaGVDFFTQIKLVtqkQKD 592
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
12-440 |
1.33e-49 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 176.49 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
Cdd:PLN00412 36 TNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 92 KSANLCDWYAEHGPAMLKAEPTLV--------ENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKhaP 163
Cdd:PLN00412 116 RSGDLISYTAEEGVRILGEGKFLVsdsfpgneRNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLK--P 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 164 NVMGC--AQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSR-IAAVTVTGSVRAGAAIGAQAGAALKkcvLELGGSDP 240
Cdd:PLN00412 194 PTQGAvaALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPgVNCISFTGGDTGIAISKKAGMVPLQ---MELGGKDA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENaLGPMARFDLRDELH 320
Cdd:PLN00412 271 CIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCD-ITPVVSESSANFIE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 321 HQVEKTLAQGARLLlggEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTT 400
Cdd:PLN00412 350 GLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTR 426
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 3915524 401 DETQARQMAARLECGGVFINGYCASDA-RVAFGGVKKSGFG 440
Cdd:PLN00412 427 DINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIG 467
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
29-457 |
5.71e-48 |
|
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: 170.48 E-value: 5.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 29 DDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVAKSANLCDWYAEHGPAM 107
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKNLKKW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 108 LKAEP---TLVENQ--QAVIEYRPLGTILAIMPWNFPLW---QVMRGAvpiILAGNGYLLK---HAPNvmgCAQLIAQVF 176
Cdd:cd07135 85 AKDEKvkdGPLAFMfgKPRIRKEPLGVVLIIGPWNYPVLlalSPLVGA---IAAGCTVVLKpseLTPH---TAALLAELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 177 K---DAGIPQGVYGwlnadndGVSQMIK--DSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLEL 251
Cdd:cd07135 159 PkylDPDAFQVVQG-------GVPETTAllEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 252 AVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPrDEENALGPMARFDLRDELHHQVEKTlaqGA 331
Cdd:cd07135 232 AAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLLDTT---KG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 332 RLLLGGEkMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAAR 411
Cdd:cd07135 308 KVVIGGE-MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTR 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 3915524 412 LECGGVFINGYC--ASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07135 387 TRSGGVVINDTLihVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
34-453 |
4.75e-45 |
|
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: 162.40 E-value: 4.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 34 ALQLAAAGfrDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPinqaRAEVAKS-------------ANLCDWY 100
Cdd:cd07134 5 AAQQAHAL--ALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP----AAEVDLTeilpvlseinhaiKHLKKWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 101 AehgPAMLKAePTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLK------HAPNVMgcAQLIAQ 174
Cdd:cd07134 79 K---PKRVRT-PLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKpseltpHTSAVI--AKIIRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 175 VF--KDAGIPQGvygwlNADndgVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELA 252
Cdd:cd07134 153 AFdeDEVAVFEG-----DAE---VAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 253 VKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENAlgPMARfdLRDELHHQ-----VEKTL 327
Cdd:cd07134 225 AKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASP--DLAR--IVNDRHFDrlkglLDDAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 328 AQGARLLLGGEKMAgAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQ 407
Cdd:cd07134 301 AKGAKVEFGGQFDA-AQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNK 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 3915524 408 MAARLECGGVFINGYCA--SDARVAFGGVKKSGFGRELSHFGLHEFCN 453
Cdd:cd07134 380 VLARTSSGGVVVNDVVLhfLNPNLPFGGVNNSGIGSYHGVYGFKAFSH 427
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
49-457 |
2.25e-43 |
|
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: 157.69 E-value: 2.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 49 NIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVAKS--------ANLCDWYA-EHGPAMLKAEPTlvenq 118
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAVVlgeidhalKHLKKWMKpRRVSVPLLLQPA----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 119 QAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLK---HAPNvmgCAQLIAQVFKDAgIPQGVYGWLNADNDg 195
Cdd:cd07087 93 KAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKpseLAPA---TSALLAKLIPKY-FDPEAVAVVEGGVE- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 196 VSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFI 275
Cdd:cd07087 168 VATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 276 IEEGIASAFTERFVAAAAALKMGDPRDEENaLGPMArfdlrDELHHQVEKTLAQGARLLLGGEkMAGAGNYYPPTVLANV 355
Cdd:cd07087 248 VHESIKDELIEELKKAIKEFYGEDPKESPD-YGRII-----NERHFDRLASLLDDGKVVIGGQ-VDKEERYIAPTILDDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 356 TPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFING---YCASDArVAFG 432
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDvllHAAIPN-LPFG 399
|
410 420
....*....|....*....|....*
gi 3915524 433 GVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07087 400 GVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
29-440 |
1.05e-35 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 138.24 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 29 DDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVAKSANLCDWYAEHGPAM 107
Cdd:PTZ00381 7 EIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmTEVLLTVAEIEHLLKHLDEY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 108 LKAEPTLVENQQAV----IEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLK---HAPNvmgCAQLIAQVFkDAG 180
Cdd:PTZ00381 87 LKPEKVDTVGVFGPgksyIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKpseLSPH---TSKLMAKLL-TKY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 181 IPQGVYGWLNADNDgVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGR 260
Cdd:PTZ00381 163 LDPSYVRVIEGGVE-VTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 261 YQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENalgpMARFDLRDELHHQVEKTLAQGARLLLGGEkM 340
Cdd:PTZ00381 242 FLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSED----YSRIVNEFHTKRLAELIKDHGGKVVYGGE-V 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 341 AGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN 420
Cdd:PTZ00381 317 DIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN 396
|
410 420
....*....|....*....|..
gi 3915524 421 G--YCASDARVAFGGVKKSGFG 440
Cdd:PTZ00381 397 DcvFHLLNPNLPFGGVGNSGMG 418
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
26-438 |
9.81e-34 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 133.10 E-value: 9.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 26 AGADDIENALQLAAAGFRDWRETNIDYRAEKLrdigkaLRA--------RSEEMAQ-MITRemGKPINQAraEVAKSANL 96
Cdd:cd07123 66 ADAALVEKAIEAALEARKEWARMPFEDRAAIF------LKAadllsgkyRYELNAAtMLGQ--GKNVWQA--EIDAACEL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 97 CDW------YAEHgpaMLKAEPtlVENQQAV---IEYRPL-GTILAIMPWNFPLWQVMRGAVPIILaGNGYLLKHAPNVM 166
Cdd:cd07123 136 IDFlrfnvkYAEE---LYAQQP--LSSPAGVwnrLEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 167 GCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSR-IAAVTVTGSVRAGAAIGAQAGAALK------KCVLELGGSD 239
Cdd:cd07123 210 LSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPhLAGLHFTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 240 PFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPM---ARFD-L 315
Cdd:cd07123 290 FHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVideKAFDrI 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 316 RDELHHQVEktlAQGARLLLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHA--LELAND-SEFG 392
Cdd:cd07123 370 KGYIDHAKS---DPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEetLELVDTtSPYA 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 3915524 393 LSATIFTTDETQARQMAARLE--CGGVFINGYCaSDARVA---FGGVKKSG 438
Cdd:cd07123 447 LTGAIFAQDRKAIREATDALRnaAGNFYINDKP-TGAVVGqqpFGGARASG 496
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
12-420 |
1.02e-32 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 131.86 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPA-TGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
Cdd:PRK11904 567 VSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEV 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDWYAEHGPAMLKAE-----PTLVENQqavIEYRPLGTILAIMPWNFPL----WQVMRGAVpiilAGNGYLLKH 161
Cdd:PRK11904 647 REAVDFCRYYAAQARRLFGAPeklpgPTGESNE---LRLHGRGVFVCISPWNFPLaiflGQVAAALA----AGNTVIAKP 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 162 APnvmgcaQ--LIA----QVFKDAGIPQGVYGWLNADNDGV-SQMIKDSRIAAVTVTGSV---RAGAAIGAQAGAALKKC 231
Cdd:PRK11904 720 AE------QtpLIAaeavKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIAGVAFTGSTetaRIINRTLAARDGPIVPL 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 232 VLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPM- 310
Cdd:PRK11904 794 IAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVi 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 311 ---ARFDLRDelHHQvekTLAQGARLLLGGEKMAGA--GNYYPPTVLAnvTPEMTAFREEMFGPVAAITI--AKDAEHAL 383
Cdd:PRK11904 874 daeAKANLDA--HIE---RMKREARLLAQLPLPAGTenGHFVAPTAFE--IDSISQLEREVFGPILHVIRykASDLDKVI 946
|
410 420 430
....*....|....*....|....*....|....*..
gi 3915524 384 ELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN 420
Cdd:PRK11904 947 DAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
32-441 |
1.61e-31 |
|
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: 125.41 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 32 ENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQA-RAEV------AKSA--NLCDWyae 102
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAvLSEIllvkneIKYAisNLPEW--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 103 hgpamlkAEPTLVE----NQQ--AVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKH---APNvmgCAQLIA 173
Cdd:cd07132 78 -------MKPEPVKknlaTLLddVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPsevSPA---TAKLLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 174 QVfkdagIPQgvygWLnaDND-------GVSQMIK--DSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVL 244
Cdd:cd07132 148 EL-----IPK----YL--DKEcypvvlgGVEETTEllKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTErfvAAAAALKM---GDPRDEENaLGPMArfdlrDELHH 321
Cdd:cd07132 217 KSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVE---ALKKTLKEfygEDPKESPD-YGRII-----NDRHF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 322 QVEKTLAQGARLLLGGEkMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTD 401
Cdd:cd07132 288 QRLKKLLSGGKVAIGGQ-TDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 3915524 402 ETQARQMAARLECGGVfingyCASD-------ARVAFGGVKKSGFGR 441
Cdd:cd07132 367 KKVINKILSNTSSGGV-----CVNDtimhytlDSLPFGGVGNSGMGA 408
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
26-420 |
3.43e-31 |
|
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: 125.41 E-value: 3.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 26 AGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEhgp 105
Cdd:TIGR01238 71 ANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAK--- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 106 amlKAEPTLVENQqavieYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGV 185
Cdd:TIGR01238 148 ---QVRDVLGEFS-----VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 186 YGWL-NADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVL---ELGGSDPFIVLNDADLELAVKAAVAGRY 261
Cdd:TIGR01238 220 IQLLpGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPliaETGGQNAMIVDSTALPEQVVRDVLRSAF 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 262 QNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEKTLAQG---ARLLLGGE 338
Cdd:TIGR01238 300 DSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDS 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 339 KMAGAGNYYPPTVLAnvTPEMTAFREEMFGPVAAIT--IAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGG 416
Cdd:TIGR01238 380 RACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGN 457
|
....
gi 3915524 417 VFIN 420
Cdd:TIGR01238 458 CYVN 461
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
40-441 |
4.03e-31 |
|
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: 124.06 E-value: 4.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 40 AGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQA-RAEV------AKSA--NLCDWYA-EHGPAMLK 109
Cdd:cd07137 10 ETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVsvlvssCKLAikELKKWMApEKVKTPLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 110 AEPTlvenqQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKH---APNVmgcAQLIAQVfkdagIPQGVy 186
Cdd:cd07137 90 TFPA-----KAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPselAPAT---SALLAKL-----IPEYL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 187 gwlnaDNDGVsQMIKDSrIAAVTV-----------TGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKA 255
Cdd:cd07137 156 -----DTKAI-KVIEGG-VPETTAlleqkwdkiffTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 256 AVAGRY-QNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENalgpMARFDlrdELHHQV-------EKTL 327
Cdd:cd07137 229 IAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKD----LSRIV---NSHHFQrlsrlldDPSV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 328 AqgARLLLGGEKMAGAgNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQ 407
Cdd:cd07137 302 A--DKIVHGGERDEKN-LYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRR 378
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 3915524 408 MAARLECGGVFINgycasDARV-------AFGGVKKSGFGR 441
Cdd:cd07137 379 IVAETSSGGVTFN-----DTVVqyaidtlPFGGVGESGFGA 414
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
50-441 |
1.51e-30 |
|
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: 123.00 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 50 IDYRAEKLRDIGKALRARSEEMAQMITREMGKP---------------INQARAEVAKsanlcdWyaehgpAMLKAEPTL 114
Cdd:cd07136 19 VEFRIEQLKKLKQAIKKYENEILEALKKDLGKSefeaymteigfvlseINYAIKHLKK------W------MKPKRVKTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 115 VENQ--QAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLK---HAPNVmgcAQLIAQVFKDAGIPQGVYgWL 189
Cdd:cd07136 87 LLNFpsKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKpseLTPNT---SKVIAKIIEETFDEEYVA-VV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 190 NADNDgVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCA 269
Cdd:cd07136 163 EGGVE-ENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 270 AAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENalgpMARfdLRDELHHQVEKTLAQGARLLLGGeKMAGAGNYYPP 349
Cdd:cd07136 242 APDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPD----YGR--IINEKHFDRLAGLLDNGKIVFGG-NTDRETLYIEP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 350 TVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFINgycasDA-- 427
Cdd:cd07136 315 TILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN-----DTim 389
|
410
....*....|....*....
gi 3915524 428 -----RVAFGGVKKSGFGR 441
Cdd:cd07136 390 hlanpYLPFGGVGNSGMGS 408
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
12-440 |
3.21e-29 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 121.51 E-value: 3.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPA-TGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
Cdd:PRK11905 572 LNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEV 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDWYAEHGPAMLKAEPTlvenqqavieyRPLGTILAIMPWNFPL----WQVmrgaVPIILAGNGYLLKHAPnvm 166
Cdd:PRK11905 652 REAVDFLRYYAAQARRLLNGPGH-----------KPLGPVVCISPWNFPLaiftGQI----AAALVAGNTVLAKPAE--- 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 167 gcaQ--LIA----QVFKDAGIPQGVYGWLNADNDGV-SQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVL---ELG 236
Cdd:PRK11905 714 ---QtpLIAaravRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETG 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 237 GSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLR 316
Cdd:PRK11905 791 GQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQ 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 317 DELHHQVEKTLAQGARLL-LGGEKMAGAGNYYPPTVLanvtpEMTAFRE---EMFGPVAAITI--AKDAEHALELANDSE 390
Cdd:PRK11905 871 ANIEAHIEAMRAAGRLVHqLPLPAETEKGTFVAPTLI-----EIDSISDlerEVFGPVLHVVRfkADELDRVIDDINATG 945
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 3915524 391 FGLSATIFT-TDETqARQMAARLECGGVFIN----GycasdARV---AFGGVKKSGFG 440
Cdd:PRK11905 946 YGLTFGLHSrIDET-IAHVTSRIRAGNIYVNrniiG-----AVVgvqPFGGEGLSGTG 997
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
32-417 |
6.17e-29 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 118.11 E-value: 6.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 32 ENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMA----------QMITREMGKPINQ--ARAEVAKSANLCDW 99
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAagavlvtgkgWMFAENICGDQVQlrARAFVIYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 100 YAEHGPAMLKaeptlvenQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQLIAQVFKDA 179
Cdd:cd07084 82 PGNHLGQGLK--------QQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 180 GI-PQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAAlkKCVLELGGSDPFIVLNDAD-LELAVKAAV 257
Cdd:cd07084 154 GLlPPEDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQaVDYVAWQCV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 258 AGRYQNTGQVCAAAKRFIIEEGIAsafTERFVAAAAALkMGDPRDEENALGPMARFDLRDELHHQVEKTlaqGARLLLGG 337
Cdd:cd07084 232 QDMTACSGQKCTAQSMLFVPENWS---KTPLVEKLKAL-LARRKLEDLLLGPVQTFTTLAMIAHMENLL---GSVLLFSG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 338 --EKMAGAGNYY----PPTVLANVTPEMT---AFREEMFGPVAAITIAKD--AEHALELANDSEFGLSATIFTTDETQAR 406
Cdd:cd07084 305 keLKNHSIPSIYgacvASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKKdqLALVLELLERMHGSLTAAIYSNDPIFLQ 384
|
410
....*....|.
gi 3915524 407 QMAARLECGGV 417
Cdd:cd07084 385 ELIGNLWVAGR 395
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
1-420 |
9.85e-27 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 113.88 E-value: 9.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 1 MTITPATHAIsINPA-TGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREM 79
Cdd:COG4230 565 EAASGEARPV-RNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREA 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 80 GKPINQARAEVAKSANLCDWYAEhgpamlKAEPTLVENQQavieYRPLGTILAIMPWNFPL----WQVMRGAVpiilAGN 155
Cdd:COG4230 644 GKTLPDAIAEVREAVDFCRYYAA------QARRLFAAPTV----LRGRGVFVCISPWNFPLaiftGQVAAALA----AGN 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 156 GYLLKHAPnvmgcaQ--LIA----QVFKDAGIPQGVYGWLNADNDGV-SQMIKDSRIAAVTVTGSV---RAGAAIGAQAG 225
Cdd:COG4230 710 TVLAKPAE------QtpLIAaravRLLHEAGVPADVLQLLPGDGETVgAALVADPRIAGVAFTGSTetaRLINRTLAARD 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 226 AALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEEN 305
Cdd:COG4230 784 GPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLST 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 306 ALGPM----ARFDLRD--ELHHQVEKTLAQGARLllggeKMAGAGNYYPPTV--LANVTpEMTafrEEMFGPVAAItI-- 375
Cdd:COG4230 864 DVGPVidaeARANLEAhiERMRAEGRLVHQLPLP-----EECANGTFVAPTLieIDSIS-DLE---REVFGPVLHV-Vry 933
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 3915524 376 -AKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN 420
Cdd:COG4230 934 kADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
39-457 |
1.35e-25 |
|
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: 108.34 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 39 AAGFRDWREtnidyRAEKLRDIGKALRARSEEMAQMITREMGkpiNQAR-----AEVAKSANLCDWYAEHGPAMLKAEPT 113
Cdd:cd07133 13 ANPPPSLEE-----RRDRLDRLKALLLDNQDALAEAISADFG---HRSRhetllAEILPSIAGIKHARKHLKKWMKPSRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 114 LVENQ----QAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQLIAQVFKDAGipqgvygwl 189
Cdd:cd07133 85 HVGLLflpaKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYF--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 190 naDNDGVSQMIKDSRIAA---------VTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGR 260
Cdd:cd07133 156 --DEDEVAVVTGGADVAAafsslpfdhLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 261 YQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKmgdPRDEENAlgpmarfDL--------RDELHHQVEKTLAQGAR 332
Cdd:cd07133 234 LLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMY---PTLADNP-------DYtsiinerhYARLQGLLEDARAKGAR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 333 L--LLGGEKMAGAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAA 410
Cdd:cd07133 304 VieLNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLR 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 3915524 411 RLECGGVFING----YCASDArvAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:cd07133 384 RTHSGGVTINDtllhVAQDDL--PFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
42-441 |
4.87e-23 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 101.34 E-value: 4.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 42 FRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGK-PINQARAEV---AKSAN-----LCDWYA-EHGPAMLKAE 111
Cdd:PLN02203 19 YESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKhRVEAYRDEVgvlTKSANlalsnLKKWMApKKAKLPLVAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 112 PTlvenqQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQLIAQV---FKDAGIPQGVYGW 188
Cdd:PLN02203 99 PA-----TAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANipkYLDSKAVKVIEGG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 189 LNadndgVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV---LNDADLELAVKAAVAGRYQN-T 264
Cdd:PLN02203 174 PA-----VGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 265 GQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENalgpMARfdLRDELHHQVEKTLAQGARL---LLGGEKMA 341
Cdd:PLN02203 249 GQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS----MAR--ILNKKHFQRLSNLLKDPRVaasIVHGGSID 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 342 GAGNYYPPTVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFING 421
Cdd:PLN02203 323 EKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFND 402
|
410 420
....*....|....*....|...
gi 3915524 422 YC---ASDArVAFGGVKKSGFGR 441
Cdd:PLN02203 403 AIiqyACDS-LPFGGVGESGFGR 424
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
12-420 |
1.44e-22 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 101.20 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPAtgEQLSVLPW---AGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARA 88
Cdd:PRK11809 664 INPA--DPRDIVGYvreATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIA 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 89 EVAKSANLCDWYAEHgpamlkaeptlVENQQAVIEYRPLGTILAIMPWNFPLwQVMRGAVPIILA-GNGYLLKHA---PN 164
Cdd:PRK11809 742 EVREAVDFLRYYAGQ-----------VRDDFDNDTHRPLGPVVCISPWNFPL-AIFTGQVAAALAaGNSVLAKPAeqtPL 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 165 VmgCAQLIAqVFKDAGIPQGVYGWLNADNDGV-SQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKK------CVLELGG 237
Cdd:PRK11809 810 I--AAQAVR-ILLEAGVPAGVVQLLPGRGETVgAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPqgrpipLIAETGG 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 238 SDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRD 317
Cdd:PRK11809 887 QNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKA 966
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 318 ELHHQVEKTLAQG---ARLLLGGEKMAGAGNYYPPTVLanvtpEMTAFRE---EMFGPVAAITIAK--DAEHALELANDS 389
Cdd:PRK11809 967 NIERHIQAMRAKGrpvFQAARENSEDWQSGTFVPPTLI-----ELDSFDElkrEVFGPVLHVVRYNrnQLDELIEQINAS 1041
|
410 420 430
....*....|....*....|....*....|..
gi 3915524 390 EFGLSATIFT-TDETQArQMAARLECGGVFIN 420
Cdd:PRK11809 1042 GYGLTLGVHTrIDETIA-QVTGSAHVGNLYVN 1072
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
12-409 |
2.22e-21 |
|
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: 96.57 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 12 INPATGEQLSVLPWAGADdIENALQLA-AAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITremgkpinqaraev 90
Cdd:cd07128 20 HDAVTGEVVARVSSEGLD-FAAAVAYArEKGGPALRALTFHERAAMLKALAKYLMERKEDLYALSA-------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCD-W------------YAEHGPAMLKAEPTLVENqqAVIEYRPLGTILA-------------IMPWNFPLWQVM 144
Cdd:cd07128 85 ATGATRRDsWididggigtlfaYASLGRRELPNAHFLVEG--DVEPLSKDGTFVGqhiltprrgvavhINAFNFPVWGML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 145 RGAVPIILAGNGYLLKHAPNVMGCAQLIAQVFKDAGI-PQGVYGWLNADNDGVSQMIKDSRIaaVTVTGS---------- 213
Cdd:cd07128 163 EKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHLGEQDV--VAFTGSaataaklrah 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 214 --VRAGAAIGAQAGAALKKCVLelgGSDpfIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAA 291
Cdd:cd07128 241 pnIVARSIRFNAEADSLNAAIL---GPD--ATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKAR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 292 AAALKMGDPRDEENALGPMARFDLRDELHHQVEkTLAQGARLLLGG-EKM------AGAGNYYPPTVLANVTP-EMTAFR 363
Cdd:cd07128 316 LAKVVVGDPRLEGVRMGPLVSREQREDVRAAVA-TLLAEAEVVFGGpDRFevvgadAEKGAFFPPTLLLCDDPdAATAVH 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 3915524 364 E-EMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMA 409
Cdd:cd07128 395 DvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
31-422 |
6.44e-21 |
|
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: 94.92 E-value: 6.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 31 IENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANlcdwyaehgpaMLKA 110
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTG-----------QLRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 111 EPTLVEN---QQAVIE-----------------YRPLGTILAIMPWNFPL-WQVMRG-AVPIILAGNGYLLKHAPNVMG- 167
Cdd:cd07129 70 FADLVREgswLDARIDpadpdrqplprpdlrrmLVPLGPVAVFGASNFPLaFSVAGGdTASALAAGCPVVVKAHPAHPGt 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 168 ---CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MIKDSRIAAVTVTGSVRAGAAigaqagaaLKKCV----------L 233
Cdd:cd07129 150 selVARAIRAALRATGLPAGVFSLLQGGGREVGVaLVKHPAIKAVGFTGSRRGGRA--------LFDAAaarpepipfyA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 234 ELGGSDPFIVLNDADLELAVKAA---VAGRYQNTGQVCAAAKRFIIeegIASAFTERFVAAAAALKmgdprdEENALGPM 310
Cdd:cd07129 222 ELGSVNPVFILPGALAERGEAIAqgfVGSLTLGAGQFCTNPGLVLV---PAGPAGDAFIAALAEAL------AAAPAQTM 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 311 ARFDLRDELHHQVEKTLAQGARLLLGGEKMAGAGNYYPPTVL-----ANVTPEmtAFREEMFGPVAAITIAKDAEHALEL 385
Cdd:cd07129 293 LTPGIAEAYRQGVEALAAAPGVRVLAGGAAAEGGNQAAPTLFkvdaaAFLADP--ALQEEVFGPASLVVRYDDAAELLAV 370
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 3915524 386 ANDSEFGLSATIFTT--DETQARQMAARLE--CGGVFINGY 422
Cdd:cd07129 371 AEALEGQLTATIHGEedDLALARELLPVLErkAGRLLFNGW 411
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
120-457 |
4.56e-19 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 89.33 E-value: 4.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 120 AVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQLIAQVFK---DAGIPQGVYGWLNAdndgv 196
Cdd:PLN02174 106 AEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEqylDSSAVRVVEGAVTE----- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 197 SQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQ-NTGQVCAAAKRFI 275
Cdd:PLN02174 181 TTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYIL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 276 IEEGIASAFTERFVAAAAALKMGDPRDEENalgpMAR------FDLRDELHHQVEKTlaqgARLLLGGEKmAGAGNYYPP 349
Cdd:PLN02174 261 TTKEYAPKVIDAMKKELETFYGKNPMESKD----MSRivnsthFDRLSKLLDEKEVS----DKIVYGGEK-DRENLKIAP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 350 TVLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFINGYCASDA-- 427
Cdd:PLN02174 332 TILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlh 411
|
330 340 350
....*....|....*....|....*....|
gi 3915524 428 RVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
Cdd:PLN02174 412 TLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
13-409 |
3.47e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 77.82 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 13 NPATGEQLSVLPWAGADdienalqlAAAGFRDWRETN------IDY--RAEKLRDIGKALRARSEEMAQMITREMGKPIN 84
Cdd:PRK11903 25 DPVTGEELVRVSATGLD--------LAAAFAFAREQGgaalraLTYaqRAALLAAIVKVLQANRDAYYDIATANSGTTRN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 85 QARAEVAKSANLCDWYAEHGPA------MLKAEPT------LVENQQAVIEYRplGTILAIMPWNFPLWQVMRGAVPIIL 152
Cdd:PRK11903 97 DSAVDIDGGIFTLGYYAKLGAAlgdarlLRDGEAVqlgkdpAFQGQHVLVPTR--GVALFINAFNFPAWGLWEKAAPALL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 153 AGNGYLLKHAPNVMGCAQLIAQVFKDAGI-PQGVYGWLNADNDGVSQMIKDSRIaaVTVTGS------------VRAGAA 219
Cdd:PRK11903 175 AGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFDV--VSFTGSaetaavlrshpaVVQRSV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 220 IGAQAGAALKKCVLeLGGSDPfivlNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGD 299
Cdd:PRK11903 253 RVNVEADSLNSALL-GPDAAP----GSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 300 PRDEENALGPMARFDLRDELHHQVEKtLAQGARLLLGGEKMA------GAGNYYPPTVLANVTPE-MTAFRE-EMFGPVA 371
Cdd:PRK11903 328 PRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGFAlvdadpAVAACVGPTLLGASDPDaATAVHDvEVFGPVA 406
|
410 420 430
....*....|....*....|....*....|....*...
gi 3915524 372 AITIAKDAEHALELANDSEFGLSATIFTTDETQARQMA 409
Cdd:PRK11903 407 TLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
29-433 |
2.95e-11 |
|
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: 64.95 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 29 DDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGkpINQARAEVAKsaNLCDWYAEHGPAML 108
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETG--MGRVEDKIAK--NHLAAEKTPGTEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 109 KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQ----LIAQVFKDAGIPQG 184
Cdd:cd07121 80 TTTAWSGDNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAyaveLINKAIAEAGGPDN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 185 VYGWLNADN-DGVSQMIKDSRIAAVTVTGS---VRAGAAIGaqagaalKKCVLELGGSDPFIVLNDADLELAVKAAVAGR 260
Cdd:cd07121 160 LVVTVEEPTiETTNELMAHPDINLLVVTGGpavVKAALSSG-------KKAIGAGAGNPPVVVDETADIEKAARDIVQGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 261 YQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAaLKMGDPrdEENALGPMARFDlrDELHHQVEKTLAQGARLLLggekm 340
Cdd:cd07121 233 SFDNNLPCIAEKEVIAVDSVADYLIAAMQRNGA-YVLNDE--QAEQLLEVVLLT--NKGATPNKKWVGKDASKIL----- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 341 AGAGNYYPPT---VLANVTPEMTAFREEMFGPVAAITIAKDAEHALELANDSEFGL--SATIFTTDETQARQMAARLECg 415
Cdd:cd07121 303 KAAGIEVPADirlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTKMARAMQT- 381
|
410
....*....|....*....
gi 3915524 416 GVFI-NGycASDARVAFGG 433
Cdd:cd07121 382 TIFVkNG--PSYAGLGVGG 398
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
72-402 |
6.21e-10 |
|
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: 60.97 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 72 AQMITREMGKPINQARAEVAKSANLCDWYAEHGPAMLK---AEPTLVENQQAViEYR-PLGTILAIMPWNFPL----WQV 143
Cdd:cd07126 85 ARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLArsfNVPGDHQGQQSS-GYRwPYGPVAIITPFNFPLeipaLQL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 144 MrGAvpiILAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQ 223
Cdd:cd07126 164 M-GA---LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAERLALE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 224 AGAALKkcvLELGGSDPFIVLND-ADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASA-FTERFVAAAAALKMgdpr 301
Cdd:cd07126 240 LHGKVK---LEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAgILDKLKALAEQRKL---- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 302 dEENALGPMARFDLRDELHHqVEKTLA-QGARLLLGGEKMAGA------GNYYPPTVLanvTPEMTAFRE--------EM 366
Cdd:cd07126 313 -EDLTIGPVLTWTTERILDH-VDKLLAiPGAKVLFGGKPLTNHsipsiyGAYEPTAVF---VPLEEIAIEenfelvttEV 387
|
330 340 350
....*....|....*....|....*....|....*...
gi 3915524 367 FGPVAAITIAKDAE--HALELANDSEFGLSATIFTTDE 402
Cdd:cd07126 388 FGPFQVVTEYKDEQlpLVLEALERMHAHLTAAVVSNDI 425
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
29-433 |
1.12e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 57.22 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 29 DDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITRE--MGkpinqaraevaksaNLCDWYAEH--- 103
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEEtgMG--------------RVEDKIAKNvaa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 104 -----GPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNG-YLLKH--APNV-MGCAQLIAQ 174
Cdd:PRK15398 102 aektpGVEDLTTEALTGDNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSvVFSPHpgAKKVsLRAIELLNE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 175 VFKDAGIPQGVYGWL-NADNDGVSQMIKDSRIAAVTVTGS---VRAGAAIGaqagaalKKCVLELGGSDPFIVLNDADLE 250
Cdd:PRK15398 182 AIVAAGGPENLVVTVaEPTIETAQRLMKHPGIALLVVTGGpavVKAAMKSG-------KKAIGAGAGNPPVVVDETADIE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 251 LAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKmgDPRDEEnALGPMArfdLRDElHHQVEKTLAQG 330
Cdd:PRK15398 255 KAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKNGAVLL--TAEQAE-KLQKVV---LKNG-GTVNKKWVGKD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 331 ARLLLggeKMAGAGNYYPPTVLANVTPEMTAF-REEMFGPVAAITIAKDAEHALELANDSEFGL--SATIFTTDETQARQ 407
Cdd:PRK15398 328 AAKIL---EAAGINVPKDTRLLIVETDANHPFvVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNK 404
|
410 420
....*....|....*....|....*..
gi 3915524 408 MAARLECgGVFI-NGycASDARVAFGG 433
Cdd:PRK15398 405 MARAIQT-SIFVkNG--PSYAGLGLGG 428
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
50-424 |
1.12e-08 |
|
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: 56.89 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 50 IDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANL-------------CDWYAEHGPAMLKAEPT--- 113
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSetgmgrvedkvikNHFAAEYIYNVYKDEKTcgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 114 LVENQQ--AVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQLIAQVFKDA----GIPQGVYG 187
Cdd:cd07081 81 LTGDENggTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 188 WL-NADNDGVSQMIKDSRIAAVTVTGSvragAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQ 266
Cdd:cd07081 161 WIdNPSIELAQRLMKFPGIGLLLATGG----PAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 267 VCAAAKRFIIEEGIASAFTERFVAAAAALKMGdprDEENALGP--MARFDLRDELHHQVEKTLA--------QGARLLLG 336
Cdd:cd07081 237 ICASEQSVIVVDSVYDEVMRLFEGQGAYKLTA---EELQQVQPviLKNGDVNRDIVGQDAYKIAaaaglkvpQETRILIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 337 gekmagagnyyPPTVLANVTPemtaFREEMFGPVAAITIAKDAEHALELA----NDSEFGLSATIFtTDETQAR----QM 408
Cdd:cd07081 314 -----------EVTSLAEHEP----FAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMY-SDNIKAIenmnQF 377
|
410
....*....|....*.
gi 3915524 409 AARLECGGVFINGYCA 424
Cdd:cd07081 378 ANAMKTSRFVKNGPCS 393
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
30-420 |
3.40e-07 |
|
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: 52.48 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 30 DIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQ----------MITREMGKPINQARA---------EV 90
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHavmhttgqafMMAFQAGGPHAQDRGleavayawrEM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 91 AKSANLCDWYAEHGpamlKAEPTLVENQQAVIeyrPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQ 170
Cdd:cd07127 165 SRIPPTAEWEKPQG----KHDPLAMEKTFTVV---PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPLA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 171 LIAQ----VFKDAGI-PQGVYgwLNADN--DGVSQ-MIKDSRIAAVTVTGSVRAGAAIGAQAGAalKKCVLELGGSDPFI 242
Cdd:cd07127 238 ITVQvareVLAEAGFdPNLVT--LAADTpeEPIAQtLATRPEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKR-FIIEEGIASA-----FTERFVAAAAALK--MGDPRDEENALGPMarfd 314
Cdd:cd07127 314 VDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNiYVPRDGIQTDdgrksFDEVAADLAAAIDglLADPARAAALLGAI---- 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915524 315 lrdelhhQVEKTLA------QGARLLLGGEKMAGAGnyYP------PTVLANVTPEMTAFREEMFGPVAAITIAKDAEHA 382
Cdd:cd07127 390 -------QSPDTLAriaearQLGEVLLASEAVAHPE--FPdarvrtPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHS 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 3915524 383 LELANDS--EFG-LSATIFTTDETQARQM-------AARLEC---GGVFIN 420
Cdd:cd07127 461 IELARESvrEHGaMTVGVYSTDPEVVERVqeaaldaGVALSInltGGVFVN 511
|
|
| NhaP2 |
COG3263 |
NhaP-type Na+/H+ and K+/H+ antiporter with C-terminal TrkAC and CorC domains [Energy ... |
125-153 |
8.25e-03 |
|
NhaP-type Na+/H+ and K+/H+ antiporter with C-terminal TrkAC and CorC domains [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 442494 [Multi-domain] Cd Length: 502 Bit Score: 38.55 E-value: 8.25e-03
10 20 30
....*....|....*....|....*....|....*.
gi 3915524 125 RPLGTILAIMPWNFPL-------WQVMRGAVPIILA 153
Cdd:COG3263 314 RPLAVFLSLLPFRFSWreklfisWVGLRGAVPIVLA 349
|
|
| |
