|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
25-452 |
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: 698.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 25 LESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDLSADILDYYAEHGPRFLEP 104
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 105 KQLHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCALAFEKLLLDAGAPKGLYTNVF 184
Cdd:cd07100 81 EPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 185 LTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVA 264
Cdd:cd07100 161 IDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 265 AKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVKHGAKLVHGGKRLDRKGWFLEPT 344
Cdd:cd07100 241 AKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 345 ILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVNSATWTAPDLP 424
Cdd:cd07100 321 VLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLP 400
|
410 420
....*....|....*....|....*...
gi 737003225 425 FGGIKNSGYGRELSSLGIDEFVNHKLIH 452
Cdd:cd07100 401 FGGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
4-453 |
1.53e-159 |
|
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: 459.59 E-value: 1.53e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 4 ETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGE 83
Cdd:COG1012 24 DVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 84 VDLSADILDYYAEHGPRFL-EPKQLHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQC 162
Cdd:COG1012 104 VDRAADFLRYYAGEARRLYgETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 163 ALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDA 241
Cdd:COG1012 184 ALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 242 DMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAV 321
Cdd:COG1012 264 DLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 322 KHGAKLVHGGKRLDR-KGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGK 400
Cdd:COG1012 344 AEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARAR 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 737003225 401 RVAAEIETGMVFVNSATWTA-PDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:COG1012 424 RVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
2-451 |
2.31e-156 |
|
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: 450.83 E-value: 2.31e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 2 KYETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEAL 81
Cdd:pfam00171 8 TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 82 GEVDLSADILDYYAEHGPRfLEPKQLHAQSGK-AMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVP 160
Cdd:pfam00171 88 GEVDRAIDVLRYYAGLARR-LDGETLPSDPGRlAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 161 QCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLD 239
Cdd:pfam00171 167 LTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 240 DADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIET 319
Cdd:pfam00171 247 DADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVED 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 320 AVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERG 399
Cdd:pfam00171 327 AKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERA 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 737003225 400 KRVAAEIETGMVFVNSATWTAPD-LPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:pfam00171 407 LRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
6-453 |
3.04e-150 |
|
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: 434.94 E-value: 3.04e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVD 85
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 86 LSADILDYYAEHGPRFL-EPKQLHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCAL 164
Cdd:cd07103 82 YAASFLEWFAEEARRIYgRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 165 AFEKLLLDAGAPKGLYtNVFLTNEQ--SAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDAD 242
Cdd:cd07103 162 ALAELAEEAGLPAGVL-NVVTGSPAeiGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 243 METALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVK 322
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 323 HGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRV 402
Cdd:cd07103 321 KGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 737003225 403 AAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07103 401 AEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
1-449 |
5.24e-148 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 429.54 E-value: 5.24e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 1 MKYETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEA 80
Cdd:PRK09406 1 MPIATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 81 LGEVDLSADILDYYAEHGPRFLEPKQLHAQS---GKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAP 157
Cdd:PRK09406 81 KAEALKCAKGFRYYAEHAEALLADEPADAAAvgaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 158 NVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIV 237
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 238 LDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQI 317
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 318 ETAVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVE 397
Cdd:PRK09406 321 DDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 737003225 398 RGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHK 449
Cdd:PRK09406 401 EQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIK 452
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
29-453 |
1.63e-140 |
|
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: 409.29 E-value: 1.63e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 29 LAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDLSADILDYYAEHGPRFLEPKQLH 108
Cdd:cd07078 4 VAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 109 AQSG-KAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTN 187
Cdd:cd07078 84 PDPGeLAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 188 EQSAKAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAK 266
Cdd:cd07078 164 DEVGAALASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 267 RFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVKHGAKLVHGGKRLDR-KGWFLEPTI 345
Cdd:cd07078 244 RLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKGYFVPPTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 346 LENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVN-SATWTAPDLP 424
Cdd:cd07078 324 LTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINdYSVGAEPSAP 403
|
410 420
....*....|....*....|....*....
gi 737003225 425 FGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07078 404 FGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
5-447 |
2.28e-129 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 382.29 E-value: 2.28e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 5 TINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEV 84
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 85 DLSADILDYYAEHGPRFLEPKQLHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCAL 164
Cdd:PRK13968 91 AKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 165 AFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADME 244
Cdd:PRK13968 171 LIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 245 TALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVKHG 324
Cdd:PRK13968 251 LAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 325 AKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAA 404
Cdd:PRK13968 331 ARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAA 410
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 737003225 405 EIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVN 447
Cdd:PRK13968 411 RLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCN 453
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
6-453 |
5.10e-121 |
|
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: 360.41 E-value: 5.10e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVD 85
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 86 LSADILDYYAEHGPRFLEPKQLHAQSG-KAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCAL 164
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGfERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 165 AFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADME 244
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 245 TALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVKHG 324
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 325 AKLVHGGKRLDR---KGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKR 401
Cdd:cd07102 321 ARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 737003225 402 VAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07102 401 LGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYHL 452
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
4-453 |
5.38e-117 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 351.69 E-value: 5.38e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 4 ETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGE 83
Cdd:PLN02278 43 PVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 84 VDLSADILDYYAEHGPR---FLEPKqlHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVP 160
Cdd:PLN02278 123 VAYGASFLEYFAEEAKRvygDIIPS--PFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 161 QCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSR-VKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLD 239
Cdd:PLN02278 201 LTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPkVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 240 DADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIET 319
Cdd:PLN02278 281 DADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQD 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 320 AVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERG 399
Cdd:PLN02278 361 AVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRA 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 737003225 400 KRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:PLN02278 441 WRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
6-453 |
7.22e-115 |
|
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: 345.00 E-value: 7.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPYTEEKLKTFPLHSDAELESFLAAAEdqyRAWRKTSW----AERKAVLTKAAALLRQNREDYARPITIEMGK-LFDEA 80
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAAR---RAFDTGDWstdaEERARCLRQLHEALEARKEELRALLVAEVGApVMTAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 81 LGEVDLSADILDYYAEHGPRFLEPKQLHAQSGKAM-----IVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKH 155
Cdd:cd07089 79 AMQVDGPIGHLRYFADLADSFPWEFDLPVPALRGGpgrrvVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 156 APNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAI-ADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDA 234
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALtTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 235 FIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVL 314
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 315 GQIETAVKHGAKLVHGGKRLDR--KGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVI 392
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737003225 393 TADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
4-453 |
2.36e-114 |
|
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: 343.86 E-value: 2.36e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 4 ETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGE 83
Cdd:cd07088 16 DVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 84 VDLSADILDYYAEhGPRFLEPKQLHAQSG--KAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQ 161
Cdd:cd07088 96 VEFTADYIDYMAE-WARRIEGEIIPSDRPneNIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 162 CALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDD 240
Cdd:cd07088 175 NALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHpKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 241 ADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETA 320
Cdd:cd07088 255 ADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 321 VKHGAKLVHGGKRLD-RKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERG 399
Cdd:cd07088 335 VEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTA 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 737003225 400 KRVAAEIETGMVFVNSatwTAPDLPFG---GIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07088 415 MRATNELEFGETYINR---ENFEAMQGfhaGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
6-453 |
2.15e-110 |
|
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: 332.96 E-value: 2.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVD 85
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 86 LSADILDYYAEhgprfLEPKQLHAQ---SGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQC 162
Cdd:cd07106 82 GAVAWLRYTAS-----LDLPDEVIEdddTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 163 ALAFEKLLLDAgAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDAD 242
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 243 METALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVK 322
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 323 HGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRV 402
Cdd:cd07106 316 KGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAV 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 737003225 403 AAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07106 396 ARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
30-445 |
3.46e-108 |
|
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: 326.79 E-value: 3.46e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 30 AAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDLSADILDYYAEhgprflEPKQLH- 108
Cdd:cd07104 7 AAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAG------LPRRPEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 109 -----AQSGK-AMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQC-ALAFEKLLLDAGAPKGLYt 181
Cdd:cd07104 81 eilpsDVPGKeSMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 182 NVFLTN--EQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMNNTG 259
Cdd:cd07104 160 NVVPGGgsEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 260 QCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVKHGAKLVHGGKrldRKGW 339
Cdd:cd07104 240 QICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT---YEGL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 340 FLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVNSATWT 419
Cdd:cd07104 317 FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVN 396
|
410 420
....*....|....*....|....*..
gi 737003225 420 -APDLPFGGIKNSGYGRELSSLGIDEF 445
Cdd:cd07104 397 dEPHVPFGGVKASGGGRFGGPASLEEF 423
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
4-453 |
9.48e-107 |
|
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: 324.46 E-value: 9.48e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 4 ETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMG---KLFDEA 80
Cdd:cd07138 17 DVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGapiTLARAA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 81 lgEVDLSADILDYYAEHGPRFlepkQLHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVP 160
Cdd:cd07138 97 --QVGLGIGHLRAAADALKDF----EFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 161 QCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLD 239
Cdd:cd07138 171 LSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 240 DADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIET 319
Cdd:cd07138 251 DADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 320 AVKHGAKLVHGG----KRLDRkGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITAD 395
Cdd:cd07138 331 GIEEGARLVAGGpgrpEGLER-GYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSAD 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 737003225 396 VERGKRVAAEIETGMVFVNSATWtAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07138 410 PERARAVARRLRAGQVHINGAAF-NPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQG 466
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
6-451 |
1.99e-106 |
|
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: 323.02 E-value: 1.99e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVD 85
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 86 LSADILDYYAEHGPRFLEPKQLHAQSG----KAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQ 161
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRKVPTGLLmpnkKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 162 CALAFEKLLLDAGAPKGLYTNVFLTNEQSAkAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDA 241
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGATGA-ALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 242 DMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAV 321
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 322 KHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKR 401
Cdd:cd07099 320 AKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 737003225 402 VAAEIETGMVFVNSATWTA--PDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07099 400 IARRLEAGAVSINDVLLTAgiPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
3-439 |
3.30e-106 |
|
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: 323.36 E-value: 3.30e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG 82
Cdd:cd07086 15 FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDLSADILDYYAehGprflEPKQLHAQ------SGKAMI-VKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKH 155
Cdd:cd07086 95 EVQEMIDICDYAV--G----LSRMLYGLtipserPGHRLMeQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 156 APNVPQCALAFEKLLLDA----GAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGG 231
Cdd:cd07086 169 SETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 232 SDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALK 311
Cdd:cd07086 249 NNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 312 LVLGQIETAVKHGAKLVHGGKRLDR--KGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGG 389
Cdd:cd07086 329 KYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSS 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 737003225 390 SVITADVERGKRV--AAEIETGMVFVNSATWTAP-DLPFGGIKNSGYGRELSS 439
Cdd:cd07086 409 SIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAEiGGAFGGEKETGGGRESGS 461
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
3-449 |
3.89e-106 |
|
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: 323.15 E-value: 3.89e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINP-YTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEAL 81
Cdd:cd07131 16 FDSRNPaDLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 82 GEVDLSADILDYYAEHGPRF--------LEPKQlhaqsgkAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIV 153
Cdd:cd07131 96 GDVQEAIDMAQYAAGEGRRLfgetvpseLPNKD-------AMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 154 KHAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIAD-SRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGS 232
Cdd:cd07131 169 KPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEhPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 233 DAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKL 312
Cdd:cd07131 249 NPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 313 VLGQIETAVKHGAKLVHGGKRLDR----KGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLG 388
Cdd:cd07131 329 VLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLS 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737003225 389 GSVITADVERGKRVAAEIETGMVFVNSATWTAP-DLPFGGIKNSGYGRELSSLGIDEFVNHK 449
Cdd:cd07131 409 SAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEvHLPFGGVKKSGNGHREAGTTALDAFTEW 470
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
3-453 |
7.56e-106 |
|
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: 322.22 E-value: 7.56e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQY--RAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMG---KLF 77
Cdd:cd07139 16 IDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGmpiSWS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 78 deALGEVDLSADILDYYAEHGPRF-LEPKQLHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHA 156
Cdd:cd07139 96 --RRAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 157 PNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFI 236
Cdd:cd07139 174 PETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 237 VLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQ 316
Cdd:cd07139 254 VLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 317 IETAVKHGAKLVHGGKR---LDRkGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVIT 393
Cdd:cd07139 334 IAKGRAEGARLVTGGGRpagLDR-GWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWT 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 394 ADVERGKRVAAEIETGMVFVNSAtWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07139 413 ADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
4-451 |
1.21e-105 |
|
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: 321.22 E-value: 1.21e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 4 ETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGE 83
Cdd:cd07145 2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 84 VDLSADILDYYAEHGPRfLEPKQLHAQSGK------AMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAP 157
Cdd:cd07145 82 VERTIRLFKLAAEEAKV-LRGETIPVDAYEynerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 158 NVPQCALAFEKLLLDAGAPKGLYtNVfLTNEQS---AKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDA 234
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVI-NV-VTGYGSevgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 235 FIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVL 314
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 315 GQIETAVKHGAKLVHGGKRLDrkGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITA 394
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTN 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 737003225 395 DVERGKRVAAEIETGMVFVNSATWTAPD-LPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07145 397 DINRALKVARELEAGGVVINDSTRFRWDnLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
3-451 |
1.74e-104 |
|
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: 318.00 E-value: 1.74e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG 82
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDLSADILDYYAEhgprflEPKQLHAQS----------GK-AMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVI 151
Cdd:cd07149 81 EVDRAIETLRLSAE------EAKRLAGETipfdaspggeGRiGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 152 IVKHAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAI-ADSRVKGVALTGSERAGSAVAAEAGaaLKKSTMELG 230
Cdd:cd07149 155 VLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALvTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 231 GSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGAL 310
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 311 KLVLGQIETAVKHGAKLVHGGKrldRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGS 390
Cdd:cd07149 313 ERIEEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737003225 391 VITADVERGKRVAAEIETGMVFVN-SATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07149 390 VFTNDLQKALKAARELEVGGVMINdSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
5-449 |
2.58e-103 |
|
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: 315.26 E-value: 2.58e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 5 TINPYTEEKLKTFPLHSDAELESFLAAAEDQYR--AWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG 82
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDLSADILDYYA-------------EHGPRFlepkqlhaqsgkAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGN 149
Cdd:cd07114 81 QVRYLAEWYRYYAgladkiegavipvDKGDYL------------NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 150 VIIVKHAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTME 228
Cdd:cd07114 149 TVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHpLVAKIAFTGGTETGRHIARAAAENLAPVTLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 229 LGGSDAFIVLDDADMETALK---WGIWArmnNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLC 305
Cdd:cd07114 229 LGGKSPNIVFDDADLDAAVNgvvAGIFA---AAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 306 TEGALKLVLGQIETAVKHGAKLVHGGKRLD----RKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLAN 381
Cdd:cd07114 306 TERQLEKVERYVARAREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALAN 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 737003225 382 DSPFGLGGSVITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHK 449
Cdd:cd07114 386 DSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
4-453 |
7.51e-103 |
|
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: 314.57 E-value: 7.51e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 4 ETINPY-TEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG 82
Cdd:cd07097 17 ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDLSADILDYYAEHGPRFlePKQLHAQSGKAMIV---KEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNV 159
Cdd:cd07097 97 EVTRAGQIFRYYAGEALRL--SGETLPSTRPGVEVettREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 160 PQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVL 238
Cdd:cd07097 175 PASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHpDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 239 DDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIE 318
Cdd:cd07097 255 DDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 319 TAVKHGAKLVHGGKRLDR--KGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADV 396
Cdd:cd07097 335 IARSEGAKLVYGGERLKRpdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSL 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 737003225 397 ERGKRVAAEIETGMVFVNSAT-WTAPDLPFGGIKNSGYG-RELSSLGIDEFVNHKLIHL 453
Cdd:cd07097 415 KHATHFKRRVEAGVVMVNLPTaGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTVYV 473
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
2-452 |
7.58e-103 |
|
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: 314.53 E-value: 7.58e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 2 KYETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRA--WRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDE 79
Cdd:cd07091 20 TFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 80 AL-GEVDLSADILDYYAE-----HGPRFLEPKQLHAQSgkamiVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIV 153
Cdd:cd07091 100 SAkGDVALSIKCLRYYAGwadkiQGKTIPIDGNFLAYT-----RREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 154 KHAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADS-RVKGVALTGS-ERAGSAVAAEAGAALKKSTMELGG 231
Cdd:cd07091 175 KPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHmDVDKIAFTGStAVGRTIMEAAAKSNLKKVTLELGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 232 SDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALK 311
Cdd:cd07091 255 KSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 312 LVLGQIETAVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSV 391
Cdd:cd07091 335 KILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGV 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737003225 392 ITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIH 452
Cdd:cd07091 415 FTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
3-451 |
8.31e-103 |
|
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: 314.24 E-value: 8.31e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG 82
Cdd:cd07151 12 IDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDLSADILDYYAEHGPRfLEPKQLHAQS-GKA-MIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVP 160
Cdd:cd07151 92 EWGAAMAITREAATFPLR-MEGRILPSDVpGKEnRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 161 QCA-LAFEKLLLDAGAPKGLYtNVFLTNeqsAKAIADSRV-----KGVALTGSERAGSAVAAEAGAALKKSTMELGGSDA 234
Cdd:cd07151 171 ITGgLLLAKIFEEAGLPKGVL-NVVVGA---GSEIGDAFVehpvpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 235 FIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVL 314
Cdd:cd07151 247 FVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 315 GQIETAVKHGAKLVHGGkrlDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITA 394
Cdd:cd07151 327 DKIEQAVEEGATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTS 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 737003225 395 DVERGKRVAAEIETGMVFVNSATWT-APDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07151 404 DLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
3-451 |
1.14e-101 |
|
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: 310.80 E-value: 1.14e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG 82
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDLSADILDYYAEHGPRFL-EPKQLHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQ 161
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRgETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 162 CALAFEKLLLDAGAPKGLYtNVFLTN--EQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLD 239
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVF-NVVTGGgaEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 240 DADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIET 319
Cdd:cd07150 240 DADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 320 AVKHGAKLVHGGKrldRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERG 399
Cdd:cd07150 320 AVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 737003225 400 KRVAAEIETGMVFVNSAT-WTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07150 397 FKLAERLESGMVHINDPTiLDEAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
5-451 |
1.47e-100 |
|
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: 308.13 E-value: 1.47e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 5 TINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEV 84
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 85 DLSADILDYYAEHGPRfLEPKQ-----LHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNV 159
Cdd:cd07110 81 DDVAGCFEYYADLAEQ-LDAKAeravpLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 160 PQCALAFEKLLLDAGAPKGLYtNVF--LTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIV 237
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVL-NVVtgTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 238 LDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQI 317
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 318 ETAVKHGAKLVHGGKRLD--RKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITAD 395
Cdd:cd07110 319 ARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 737003225 396 VERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07110 399 AERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
5-451 |
2.13e-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: 307.83 E-value: 2.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 5 TINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG-E 83
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 84 VDLSADILDYYAEHGPRF------LEPKQLHaqsgkaMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAP 157
Cdd:cd07115 81 VPRAADTFRYYAGWADKIegevipVRGPFLN------YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 158 NVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIAD-SRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFI 236
Cdd:cd07115 155 LTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEhPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 237 VLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQ 316
Cdd:cd07115 235 VFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 317 IETAVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADV 396
Cdd:cd07115 315 VDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 737003225 397 ERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07115 395 GRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
4-451 |
3.62e-100 |
|
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: 307.05 E-value: 3.62e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 4 ETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGE 83
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 84 VDLSADILDYYAEHGPRFLE---PKQLHAQSG--KAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPN 158
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGeeiPLDATQGSDnrLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 159 VPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIA-DSRVKGVALTGSerAGSAVAAEAGAALKKSTMELGGSDAFIV 237
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAaDERVAMLSFTGS--AAVGEALRANAGGKRIALELGGNAPVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 238 LDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQI 317
Cdd:cd07094 240 DRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 318 ETAVKHGAKLVHGGKrldRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVE 397
Cdd:cd07094 320 EEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLN 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 737003225 398 RGKRVAAEIETGMVFVN-SATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07094 397 VAFKAAEKLEVGGVMVNdSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
30-451 |
4.20e-100 |
|
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: 306.04 E-value: 4.20e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 30 AAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGklFDEALGE--VDLSADILDYYAEHGPRFLE---P 104
Cdd:cd07105 7 EAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG--ATAAWAGfnVDLAAGMLREAASLITQIIGgsiP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 105 KQLHAQSgkAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCALAFEKLLLDAGAPKGLYTNVF 184
Cdd:cd07105 85 SDKPGTL--AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 185 LTNEQSAKA----IADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMNNTGQ 260
Cdd:cd07105 163 HSPEDAPEVvealIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 261 CCVAAKRFILHESKADAFVEAFKKSLEDLTPGDplekaTTLGPLCTEGALKLVLGQIETAVKHGAKLVHGGK-RLDRKGW 339
Cdd:cd07105 243 ICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLaDESPSGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 340 FLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVNSAT-W 418
Cdd:cd07105 318 SMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTvH 397
|
410 420 430
....*....|....*....|....*....|...
gi 737003225 419 TAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07105 398 DEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
2-453 |
8.17e-100 |
|
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: 307.03 E-value: 8.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 2 KYETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRA-WRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDE- 79
Cdd:cd07144 24 TIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 80 ALGEVDLSADILDYYAE-----HGPRF-LEPKQLhaqsgkAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIV 153
Cdd:cd07144 104 ALGDLDEIIAVIRYYAGwadkiQGKTIpTSPNKL------AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 154 KHAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTMELGGS 232
Cdd:cd07144 178 KPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 233 DAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSL-EDLTPGDPLEKATTLGPLCTEGALK 311
Cdd:cd07144 258 SPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVGPQVSKTQYD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 312 LVLGQIETAVKHGAKLVHGG---KRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLG 388
Cdd:cd07144 338 RVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLA 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737003225 389 GSVITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07144 418 AAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
4-436 |
9.13e-100 |
|
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: 306.81 E-value: 9.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 4 ETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKT-SWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG 82
Cdd:cd07082 19 EVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDLSADILDYYAEHGPRfLEPKQL------HAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHA 156
Cdd:cd07082 99 EVDRTIDYIRDTIEELKR-LDGDSLpgdwfpGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 157 PNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAI-ADSRVKGVALTGSERAGSAVAAEAGaaLKKSTMELGGSDAF 235
Cdd:cd07082 178 TQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLvTHGRIDVISFTGSTEVGNRLKKQHP--MKRLVLELGGKDPA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 236 IVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLG 315
Cdd:cd07082 256 IVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 316 QIETAVKHGAKLVHGGKRldRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITAD 395
Cdd:cd07082 336 LIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKD 413
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 737003225 396 VERGKRVAAEIETGMVFVNSATWTAPD-LPFGGIKNSGYGRE 436
Cdd:cd07082 414 INKARKLADALEVGTVNINSKCQRGPDhFPFLGRKDSGIGTQ 455
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
39-453 |
1.69e-99 |
|
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: 305.42 E-value: 1.69e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 39 WRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDLSADILDYYAEHGprflepKQLHAQSGK----- 113
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLA------RTLHGDSYNnlgdd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 114 --AMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSA 191
Cdd:cd07118 111 mlGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 192 KAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFIL 270
Cdd:cd07118 191 QAMTEHpDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 271 HESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVKHGAKLVHGGKRLD-RKGWFLEPTILENI 349
Cdd:cd07118 271 HESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLAsAAGLFYQPTIFTDV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 350 EKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIK 429
Cdd:cd07118 351 TPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFK 430
|
410 420
....*....|....*....|....
gi 737003225 430 NSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07118 431 QSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
4-453 |
6.44e-99 |
|
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: 304.62 E-value: 6.44e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 4 ETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRA--WRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEAL 81
Cdd:cd07119 16 DIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 82 GEVDLSADILDYYA-----EHGPRFLEPKQLHAqsgkaMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHA 156
Cdd:cd07119 96 IDIDDVANCFRYYAglatkETGEVYDVPPHVIS-----RTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 157 PNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSR-VKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAF 235
Cdd:cd07119 171 EVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPdVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 236 IVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLG 315
Cdd:cd07119 251 IVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 316 QIETAVKHGAKLVHGGKRLD----RKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSV 391
Cdd:cd07119 331 YIQLGKEEGARLVCGGKRPTgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAV 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737003225 392 ITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07119 411 WTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
5-436 |
8.14e-99 |
|
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: 303.72 E-value: 8.14e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 5 TINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEA-LGE 83
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLArTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 84 VDLSADILDYYAEHGPRflEPKQLHAQSGKAM--IVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQ 161
Cdd:cd07093 81 IPRAAANFRFFADYILQ--LDGESYPQDGGALnyVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 162 CALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAI-ADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDD 240
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALvAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 241 ADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETA 320
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 321 VKHGAKLVHGGKRLD----RKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADV 396
Cdd:cd07093 319 RAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 737003225 397 ERGKRVAAEIETGMVFVNsaTWTAPDL--PFGGIKNSGYGRE 436
Cdd:cd07093 399 GRAHRVARRLEAGTVWVN--CWLVRDLrtPFGGVKASGIGRE 438
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
30-453 |
9.62e-99 |
|
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: 300.30 E-value: 9.62e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 30 AAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDLSADILDYYAEHGPRFLEPKQLHA 109
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 110 QSG-KAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNE 188
Cdd:cd06534 81 DPGgEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 189 QSAKAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKR 267
Cdd:cd06534 161 EVGAALLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 268 FILHESKADAFVEAFKksledltpgdplekattlgplctegalklvlgqietavkhgaklvhggkrldrkgwflepTILE 347
Cdd:cd06534 241 LLVHESIYDEFVEKLV------------------------------------------------------------TVLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 348 NIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVN-SATWTAPDLPFG 426
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINdSSIGVGPEAPFG 340
|
410 420
....*....|....*....|....*..
gi 737003225 427 GIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd06534 341 GVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
2-451 |
1.84e-98 |
|
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: 302.98 E-value: 1.84e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 2 KYETINPYTEEKLKTFPLHSDAELESFLAAA----EDqyRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLF 77
Cdd:cd07112 3 TFATINPATGRVLAEVAACDAADVDRAVAAArrafES--GVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 78 DEAL-GEVDLSADILDYYAEhgprfLEPKQLH--AQSGK---AMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVI 151
Cdd:cd07112 81 SDALaVDVPSAANTFRWYAE-----AIDKVYGevAPTGPdalALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 152 IVKHAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSR-VKGVALTGSERAGSAVAAEAGAA-LKKSTMEL 229
Cdd:cd07112 156 VLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMdVDALAFTGSTEVGRRFLEYSGQSnLKRVWLEC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 230 GGSDAFIVLDDA-DMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEG 308
Cdd:cd07112 236 GGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 309 ALKLVLGQIETAVKHGAKLVHGGKRL--DRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFG 386
Cdd:cd07112 316 HFDKVLGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 737003225 387 LGGSVITADVERGKRVAAEIETGMVFVNsaTWTAPDL--PFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07112 396 LAASVWTSDLSRAHRVARRLRAGTVWVN--CFDEGDIttPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
3-450 |
1.87e-96 |
|
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: 297.62 E-value: 1.87e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG 82
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDLSADILDYYAEHGPRF---LEPKQLHAQSG--KAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAP 157
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIygeVLPLDISARGEgrQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 158 NVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAalKKSTMELGGSDAFIV 237
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 238 LDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQI 317
Cdd:cd07147 239 DSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 318 ETAVKHGAKLVHGGKRldrKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVE 397
Cdd:cd07147 319 NEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLE 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 737003225 398 RGKRVAAEIETGMVFVN-SATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKL 450
Cdd:cd07147 396 KALRAWDELEVGGVVINdVPTFRVDHMPYGGVKDSGIGREGVRYAIEEMTEPRL 449
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
5-451 |
3.60e-96 |
|
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: 296.91 E-value: 3.60e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 5 TINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEV 84
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 85 DLSADILDYYAEHGPRfLEPKQLHAQSGK-AMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCA 163
Cdd:cd07090 81 DSSADCLEYYAGLAPT-LSGEHVPLPGGSfAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 164 LAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADM 243
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 244 ETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVKH 323
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 324 GAKLVHGGKRLD-----RKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVER 398
Cdd:cd07090 320 GAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 737003225 399 GKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07090 400 AHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
6-449 |
9.45e-95 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 294.72 E-value: 9.45e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPYTEEKLKTFPLHSDAELESFLAAAEDQY-----RAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEA 80
Cdd:PLN02467 28 VNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 81 LGEVDLSADILDYYAEHG----PRFLEPKQLHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHA 156
Cdd:PLN02467 108 AWDMDDVAGCFEYYADLAealdAKQKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 157 PNVPQCALAFEKLLLDAGAPKGLYtNVF--LTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDA 234
Cdd:PLN02467 188 ELASVTCLELADICREVGLPPGVL-NVVtgLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 235 FIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVL 314
Cdd:PLN02467 267 IIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 315 GQIETAVKHGAKLVHGGKRLD--RKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVI 392
Cdd:PLN02467 347 KFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVI 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 737003225 393 TADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHK 449
Cdd:PLN02467 427 SNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
6-445 |
5.45e-94 |
|
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: 291.15 E-value: 5.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEAL-GEV 84
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 85 DLSADILDYYA-----EHGPRFLEpkqlHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNV 159
Cdd:cd07092 82 PGAVDNFRFFAgaartLEGPAAGE----YLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 160 PQCALAFEKLLLDaGAPKGLYTNVFLTNEQSAKA-IADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVL 238
Cdd:cd07092 158 PLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDAlVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 239 DDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIE 318
Cdd:cd07092 237 DDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 319 TAVKHgAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVER 398
Cdd:cd07092 317 RAPAH-ARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 737003225 399 GKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEF 445
Cdd:cd07092 396 AMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDY 442
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
3-453 |
5.67e-94 |
|
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: 291.18 E-value: 5.67e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPlhsdAELESFLAAAEDQYRAWRK-TSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEAL 81
Cdd:cd07146 1 LEVRNPYTGEVVGTVP----AGTEEALREALALAASYRStLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 82 GEVDLSADILDYYAEHGPR-----FLEPKQLHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHA 156
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRddgesFSCDLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 157 PNVPQCALAFEKLLLDAGAPKGLYTNVF-LTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGaaLKKSTMELGGSDAF 235
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTgEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 236 IVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLG 315
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 316 QIETAVKHGAKLVHGGKrldRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITAD 395
Cdd:cd07146 315 RVEEAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 396 VERGKRVAAEIETGMVFVNSAT-WTAPDLPFGGIKNSGYG-RELSSLGIDEFVNHKLIHL 453
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNEVPgFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
7-449 |
5.90e-94 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 292.20 E-value: 5.90e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 7 NPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDL 86
Cdd:PRK11241 32 NPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 87 SADILDYYAEHGPRFLEPKQLHAQSGKAMIV-KEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCALA 165
Cdd:PRK11241 112 AASFIEWFAEEGKRIYGDTIPGHQADKRLIViKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 166 FEKLLLDAGAPKGLYTNVfltnEQSAKAI-----ADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDD 240
Cdd:PRK11241 192 LAELAIRAGIPAGVFNVV----TGSAGAVggeltSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 241 ADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETA 320
Cdd:PRK11241 268 ADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 321 VKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGK 400
Cdd:PRK11241 348 LEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVF 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 737003225 401 RVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHK 449
Cdd:PRK11241 428 RVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
6-449 |
5.87e-93 |
|
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: 289.34 E-value: 5.87e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPYTEEKLKTFPLHSDAELESFLAAAEDQYR-AWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG-E 83
Cdd:cd07113 20 TNPATEQVIASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 84 VDLSADILDYYAEHGPRF----LEPKQLHAQSGK--AMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAP 157
Cdd:cd07113 100 VGQSANFLRYFAGWATKIngetLAPSIPSMQGERytAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 158 NVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIV 237
Cdd:cd07113 180 FTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 238 LDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQI 317
Cdd:cd07113 260 LKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 318 ETAVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVE 397
Cdd:cd07113 340 DDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLS 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 737003225 398 RGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHK 449
Cdd:cd07113 420 KALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELK 471
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
6-446 |
1.33e-88 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 277.27 E-value: 1.33e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVD 85
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 86 LSADILDYYAEHGPRFLEPKQlhAQSG-----KAMIVKEPLGILFCIEPWNFPyyqLARVVG---PNFIAGNVIIVKHAP 157
Cdd:cd07101 81 DVAIVARYYARRAERLLKPRR--RRGAipvltRTTVNRRPKGVVGVISPWNYP---LTLAVSdaiPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 158 NVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADsRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIV 237
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVD-NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 238 LDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQI 317
Cdd:cd07101 235 LEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 318 ETAVKHGAKLVHGGK-RLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADV 396
Cdd:cd07101 315 DDAVAKGATVLAGGRaRPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 737003225 397 ERGKRVAAEIETGMVFVN---SATWTAPDLPFGGIKNSGYGRELSSLGIDEFV 446
Cdd:cd07101 395 ARGRRIAARLRAGTVNVNegyAAAWASIDAPMGGMKDSGLGRRHGAEGLLKYT 447
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
7-435 |
1.41e-88 |
|
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: 277.64 E-value: 1.41e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 7 NPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGK-LFDEALGEVD 85
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKtMVDASLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 86 LSADILDYYAEHGPRFLEPKqlhAQSG-------KAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPN 158
Cdd:cd07098 82 VTCEKIRWTLKHGEKALRPE---SRPGgllmfykRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 159 VPQCALAF----EKLLLDAGAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDA 234
Cdd:cd07098 159 VAWSSGFFlsiiRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 235 FIVLDDADMETALKwgIWAR--MNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKL 312
Cdd:cd07098 239 AIVLDDADLDQIAS--IIMRgtFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 313 VLGQIETAVKHGAKLVHGGKR----LDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLG 388
Cdd:cd07098 317 LEELVADAVEKGARLLAGGKRyphpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 737003225 389 GSVITADVERGKRVAAEIETGMVFVN--SATWTAPDLPFGGIKNSGYGR 435
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAINdfGVNYYVQQLPFGGVKGSGFGR 445
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
4-453 |
3.36e-88 |
|
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: 277.03 E-value: 3.36e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 4 ETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG- 82
Cdd:cd07117 19 DSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDLSADILDYYA-----EHGprflEPKQLHAQSgKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAP 157
Cdd:cd07117 99 DIPLAADHFRYFAgviraEEG----SANMIDEDT-LSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 158 NVPQCALAFEKLLLDAgAPKGLYTNVFLTNEQSAKAIADSR-VKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFI 236
Cdd:cd07117 174 TTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 237 VLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQ 316
Cdd:cd07117 253 IFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 317 IETAVKHGAKLVHGGKRLDR----KGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVI 392
Cdd:cd07117 333 VDIAKEEGAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVF 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737003225 393 TADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07117 413 TKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
6-451 |
6.25e-86 |
|
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: 270.26 E-value: 6.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPYTEEKLKTFPLHSDAELESFLAAAEDQYRA-WRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEV 84
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 85 DLSADILDYYAeHGPRFLEPKQLHAQSG-KAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCA 163
Cdd:cd07109 82 EAAARYFEYYG-GAADKLHGETIPLGPGyFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 164 LAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSR-VKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDAD 242
Cdd:cd07109 161 LRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 243 METALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATtLGPLCTEGALKLVLGQIETAVK 322
Cdd:cd07109 241 LEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD-LGPLISAKQLDRVEGFVARARA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 323 HGAKLVHGGKRLD---RKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERG 399
Cdd:cd07109 320 RGARIVAGGRIAEgapAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 737003225 400 KRVAAEIETGMVFVNsaTWTAP---DLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07109 400 LRVARRLRAGQVFVN--NYGAGggiELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
3-435 |
1.69e-85 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 271.37 E-value: 1.69e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG 82
Cdd:PRK09407 34 REVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDLSADILDYYAEHGPRFLEPKQlHAQS----GKAMIVKEPLGILFCIEPWNFPyyqLARVVG---PNFIAGNVIIVKH 155
Cdd:PRK09407 114 EVLDVALTARYYARRAPKLLAPRR-RAGAlpvlTKTTELRQPKGVVGVISPWNYP---LTLAVSdaiPALLAGNAVVLKP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 156 APNVPQCALAFEKLLLDAGAPKGLYTNVflTNEQS--AKAIADsRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSD 233
Cdd:PRK09407 190 DSQTPLTALAAVELLYEAGLPRDLWQVV--TGPGPvvGTALVD-NADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKN 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 234 AFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLV 313
Cdd:PRK09407 267 PMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 314 LGQIETAVKHGAKLVHGGK-RLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVI 392
Cdd:PRK09407 347 SAHVDDAVAKGATVLAGGKaRPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVW 426
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 737003225 393 TADVERGKRVAAEIETGMVFVN---SATWTAPDLPFGGIKNSGYGR 435
Cdd:PRK09407 427 TGDTARGRAIAARIRAGTVNVNegyAAAWGSVDAPMGGMKDSGLGR 472
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
5-451 |
2.79e-85 |
|
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: 268.85 E-value: 2.79e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 5 TINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGK-LFDEALGE 83
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNaLRTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 84 VDLSADILDYYAEHGPRF------LEPKQLHaqsgkaMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAP 157
Cdd:cd07108 81 AAVLADLFRYFGGLAGELkgetlpFGPDVLT------YTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 158 NVPQCALAFEKLLLDAgAPKGLYTNVFLTNEQSAKAIADSR-VKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFI 236
Cdd:cd07108 155 DAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 237 VLDDADMETALKwGIWARMNNT--GQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVL 314
Cdd:cd07108 234 VFPDADLDDAVD-GAIAGMRFTrqGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 315 GQIETAVKH-GAKLVHGGKR----LDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGG 389
Cdd:cd07108 313 GYIDLGLSTsGATVLRGGPLpgegPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737003225 390 SVITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLG-IDEFVNHKLI 451
Cdd:cd07108 393 YVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
5-454 |
1.24e-84 |
|
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: 266.93 E-value: 1.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 5 TINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEV 84
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 85 DLSADILDYYAEHGPRF------LEPKQLHaqsgkaMIVKEPLGILFCIEPWNFPY-YQLARVVGPnFIAGNVIIVKHAP 157
Cdd:cd07107 81 MVAAALLDYFAGLVTELkgetipVGGRNLH------YTLREPYGVVARIVAFNHPLmFAAAKIAAP-LAAGNTVVVKPPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 158 NVPQCALAFEKLLLDAgAPKGLYTNVFLTNEQSAKAIADSR-VKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFI 236
Cdd:cd07107 154 QAPLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 237 VLDDADMETALKwGIWARMNNT--GQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVL 314
Cdd:cd07107 233 VFPDADPEAAAD-AAVAGMNFTwcGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 315 GQIETAVKHGAKLVHGGKRLD----RKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGS 390
Cdd:cd07107 312 HYIDSAKREGARLVTGGGRPEgpalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737003225 391 VITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHLP 454
Cdd:cd07107 392 IWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVR 455
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
51-453 |
2.46e-84 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 264.68 E-value: 2.46e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 51 LTKAAALLRQNREDYARPITIEMGKLFDEALGEVDLSADILDYYAEHGPRFlEPKQLhaQSGKA----MIVKEPLGILFC 126
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRY-EGEII--QSDRPgeniLLFKRALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 127 IEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIA-DSRVKGVALT 205
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAgNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 206 GSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKS 285
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 286 LEDLTPGDPLEKAT-TLGPLCTEGALKLVLGQIETAVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPV 364
Cdd:PRK10090 238 MQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 365 AMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDE 444
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHE 397
|
....*....
gi 737003225 445 FVNHKLIHL 453
Cdd:PRK10090 398 YLQTQVVYL 406
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
6-453 |
3.76e-84 |
|
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: 266.70 E-value: 3.76e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPYTEEKLKTFPLHSDAELESFLAAAEDQYR-AW-RKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG- 82
Cdd:cd07143 27 YNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWgLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDLSADILDYYA-----EHGPRF-LEPKQLhaqsgkAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHA 156
Cdd:cd07143 107 DVQASADTFRYYGgwadkIHGQVIeTDIKKL------TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 157 PNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADS-RVKGVALTGSERA-GSAVAAEAGAALKKSTMELGGSDA 234
Cdd:cd07143 181 ELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHmDIDKVAFTGSTLVgRKVMEAAAKSNLKKVTLELGGKSP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 235 FIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVL 314
Cdd:cd07143 261 NIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIM 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 315 GQIETAVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITA 394
Cdd:cd07143 341 SYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTN 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 737003225 395 DVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07143 421 NINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
5-453 |
9.77e-84 |
|
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: 264.59 E-value: 9.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 5 TINPYTEEKLKTFPLHSDAELESFLAAAEdqyRAWRKTSWAE----RKAVLTKAAALLRQNREDYARPITIEMGKLFDEA 80
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAAR---RAFDETDWAHdprlRARVLLELADAFEANAERLARLLALENGKILGEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 81 LGEVDLSADILDYYA-----EHGPRF-LEPKQLhaqsgkAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVK 154
Cdd:cd07120 78 RFEISGAISELRYYAglartEAGRMIePEPGSF------SLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 155 HAPNVPQCALAFEKLLLDA-GAPKGLyTNVFLTN-EQSAKAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTMELGG 231
Cdd:cd07120 152 PAGQTAQINAAIIRILAEIpSLPAGV-VNLFTESgSEGAAHLVASpDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 232 SDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALK 311
Cdd:cd07120 231 KTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 312 LVLGQIETAVKHGAKLVHGGKRLDR---KGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLG 388
Cdd:cd07120 311 RVDRMVERAIAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737003225 389 GSVITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHL 453
Cdd:cd07120 391 ASVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
30-445 |
2.62e-83 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 263.39 E-value: 2.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 30 AAAEDQyRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDLSADILDYYAEHGprfLEPKQ--L 107
Cdd:cd07152 21 RAAAAQ-RAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLP---TQPQGeiL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 108 HAQSGKAMIVKE-PLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCA-LAFEKLLLDAGAPKGLYTNVFL 185
Cdd:cd07152 97 PSAPGRLSLARRvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 186 TNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAA 265
Cdd:cd07152 177 GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 266 KRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVKHGAKLVHGGKrldRKGWFLEPTI 345
Cdd:cd07152 257 GRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGT---YDGLFYRPTV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 346 LENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVNSATWT-APDLP 424
Cdd:cd07152 334 LSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNdEPHNP 413
|
410 420
....*....|....*....|....*
gi 737003225 425 FGGIKNSGYGrelSSLG----IDEF 445
Cdd:cd07152 414 FGGMGASGNG---SRFGgpanWEEF 435
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
2-451 |
1.06e-82 |
|
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: 263.05 E-value: 1.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 2 KYETINPYTEEKLKTFPLHSDAELESFLAAAEDQYR---AWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFD 78
Cdd:cd07141 23 TFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 79 EA-LGEVDLSADILDYYAEHGPRflepkqLHAQS----GKAMIV--KEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVI 151
Cdd:cd07141 103 KSyLVDLPGAIKVLRYYAGWADK------IHGKTipmdGDFFTYtrHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 152 IVKHAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADS-RVKGVALTGS-ERAGSAVAAEAGAALKKSTMEL 229
Cdd:cd07141 177 VLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHpDIDKVAFTGStEVGKLIQQAAGKSNLKRVTLEL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 230 GGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGA 309
Cdd:cd07141 257 GGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 310 LKLVLGQIETAVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGG 389
Cdd:cd07141 337 FKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAA 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737003225 390 SVITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07141 417 AVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
3-436 |
3.41e-82 |
|
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: 261.27 E-value: 3.41e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYR--AWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEA 80
Cdd:cd07142 21 FPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 81 -LGEVDLSADILDYYAE-----HGPRFLEPKQLHAQSgkamiVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVK 154
Cdd:cd07142 101 rYAEVPLAARLFRYYAGwadkiHGMTLPADGPHHVYT-----LHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 155 HAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSR-VKGVALTGS-ERAGSAVAAEAGAALKKSTMELGGS 232
Cdd:cd07142 176 PAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMdVDKVAFTGStEVGKIIMQLAAKSNLKPVTLELGGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 233 DAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKL 312
Cdd:cd07142 256 SPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 313 VLGQIETAVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVI 392
Cdd:cd07142 336 ILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVF 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 737003225 393 TADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRE 436
Cdd:cd07142 416 SKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGRE 459
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
3-451 |
4.21e-82 |
|
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: 261.12 E-value: 4.21e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG 82
Cdd:cd07559 18 FDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 -EVDLSADILDYYAehgprflepKQLHAQSGK---------AMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVII 152
Cdd:cd07559 98 aDIPLAIDHFRYFA---------GVIRAQEGSlseidedtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 153 VKHAPNVPQCALAFEKLLLDAgAPKGLYTNVFLTNEQSAKAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTMELGG 231
Cdd:cd07559 169 LKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHpRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 232 SDAFIVLDDA-----DMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCT 306
Cdd:cd07559 248 KSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 307 EGALKLVLGQIETAVKHGAKLVHGGKRL----DRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLAND 382
Cdd:cd07559 328 KDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIAND 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 737003225 383 SPFGLGGSVITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRElsslgidefvNHKLI 451
Cdd:cd07559 408 TEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRE----------THKMM 466
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
2-434 |
6.80e-81 |
|
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: 259.08 E-value: 6.80e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 2 KYETINPY-TEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEA 80
Cdd:cd07124 47 KIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 81 LGEVDLSADILDYYAEHGPRfLEPKQLHAQSG-KAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNV 159
Cdd:cd07124 127 DADVAEAIDFLEYYAREMLR-LRGFPVEMVPGeDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 160 PQCALAFEKLLLDAGAPKGLYTnvFLT---NEQSAKAIADSRVKGVALTGS--------ERagSAVAAEAGAALKKSTME 228
Cdd:cd07124 206 PVIAAKLVEILEEAGLPPGVVN--FLPgpgEEVGDYLVEHPDVRFIAFTGSrevglriyER--AAKVQPGQKWLKRVIAE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 229 LGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEG 308
Cdd:cd07124 282 MGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 309 ALKLVLGQIETAvKHGAKLVHGGKRLD--RKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFG 386
Cdd:cd07124 362 ARDRIRRYIEIG-KSEGRLLLGGEVLElaAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYG 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 737003225 387 LGGSVITADVERGKRVAAEIETGMVFVNSATWTA-PDL-PFGGIKNSGYG 434
Cdd:cd07124 441 LTGGVFSRSPEHLERARREFEVGNLYANRKITGAlVGRqPFGGFKMSGTG 490
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
6-448 |
1.10e-80 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 257.53 E-value: 1.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG-EV 84
Cdd:PRK13473 22 YNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNdEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 85 DLSADILDYYAehGP-RFLEpkqlhaqsGKA----------MIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIV 153
Cdd:PRK13473 102 PAIVDVFRFFA--GAaRCLE--------GKAageyleghtsMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 154 KHAPNVPQCALAFEKLLLDAgAPKGLYTNVFLTNEQSAKAIADSR-VKGVALTGSERAGSAVAAEAGAALKKSTMELGGS 232
Cdd:PRK13473 172 KPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPkVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 233 DAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKL 312
Cdd:PRK13473 251 APVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 313 VLGQIETAVKHG-AKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSV 391
Cdd:PRK13473 331 VAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSV 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 737003225 392 ITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEF--VNH 448
Cdd:PRK13473 411 WTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYtvVRH 469
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
3-436 |
1.41e-80 |
|
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: 257.14 E-value: 1.41e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG 82
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDLSADILDYyAEHGPRFLEPKQLHAQ-SGKAMI-VKEPLGILFCIEPWNFPyyqlARVVGPN----FIAGNVIIVKHA 156
Cdd:cd07130 94 EVQEMIDICDF-AVGLSRQLYGLTIPSErPGHRMMeQWNPLGVVGVITAFNFP----VAVWGWNaaiaLVCGNVVVWKPS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 157 PNVPQCALAFEKLLLDA----GAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGS 232
Cdd:cd07130 169 PTTPLTAIAVTKIVARVleknGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 233 DAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKL 312
Cdd:cd07130 249 NAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 313 VLGQIETAVKHGAKLVHGGKRLDRKGWFLEPTILEnIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVI 392
Cdd:cd07130 329 YLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIF 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 737003225 393 TADVERGKRV--AAEIETGMVFVNSATWTAP-DLPFGGIKNSGYGRE 436
Cdd:cd07130 408 TTDLRNAFRWlgPKGSDCGIVNVNIGTSGAEiGGAFGGEKETGGGRE 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
3-436 |
7.14e-78 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 250.57 E-value: 7.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALg 82
Cdd:PRK13252 24 FEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETS- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDL--SADILDYYAEHGPRfLEPKQLHAQSGK-AMIVKEPLGILFCIEPWNFPYyQLAR-VVGPNFIAGNVIIVKHAPN 158
Cdd:PRK13252 103 VVDIvtGADVLEYYAGLAPA-LEGEQIPLRGGSfVYTRREPLGVCAGIGAWNYPI-QIACwKSAPALAAGNAMIFKPSEV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 159 VPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVL 238
Cdd:PRK13252 181 TPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 239 DDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIE 318
Cdd:PRK13252 261 DDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 319 TAVKHGAKLVHGGKRLDR----KGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITA 394
Cdd:PRK13252 341 KGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTA 420
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 737003225 395 DVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRE 436
Cdd:PRK13252 421 DLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRE 462
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
3-451 |
3.13e-76 |
|
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: 246.25 E-value: 3.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRA--WRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEA 80
Cdd:cd07140 23 YNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 81 LG-EVDLSADILDYYAE-----HGpRFLEPKQLHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVK 154
Cdd:cd07140 103 LKtHVGMSIQTFRYFAGwcdkiQG-KTIPINQARPNRNLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 155 HAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIAD-SRVKGVALTGS-ERAGSAVAAEAGAALKKSTMELGGS 232
Cdd:cd07140 182 PAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDhPDVRKLGFTGStPIGKHIMKSCAVSNLKKVSLELGGK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 233 DAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKL 312
Cdd:cd07140 262 SPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 313 VLGQIETAVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSE--QEAIDLANDSPFGLGGS 390
Cdd:cd07140 342 LVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEYGLASG 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737003225 391 VITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07140 422 VFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
3-454 |
3.99e-74 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 241.26 E-value: 3.99e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYR--AWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFdeA 80
Cdd:PLN02766 38 FETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLF--A 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 81 LGE-VDL--SADILDYYAE-----HGPRFLEPKQLHAQSgkamiVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVII 152
Cdd:PLN02766 116 LGKaVDIpaAAGLLRYYAGaadkiHGETLKMSRQLQGYT-----LKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 153 VKHAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSR-VKGVALTGS-ERAGSAVAAEAGAALKKSTMELG 230
Cdd:PLN02766 191 VKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMdVDKVSFTGStEVGRKIMQAAATSNLKQVSLELG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 231 GSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGAL 310
Cdd:PLN02766 271 GKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQF 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 311 KLVLGQIETAVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGS 390
Cdd:PLN02766 351 EKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAG 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737003225 391 VITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLIHLP 454
Cdd:PLN02766 431 IVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTP 494
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
3-451 |
2.48e-69 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 228.63 E-value: 2.48e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRA--WRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEA 80
Cdd:PRK09847 37 FETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 81 L-GEVDLSADILDYYAEHGPRFLEPKQLHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNV 159
Cdd:PRK09847 117 LrDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 160 PQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIA-DSRVKGVALTGSERAGSAVAAEA-GAALKKSTMELGGSDAFIV 237
Cdd:PRK09847 197 PLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSrHNDIDAIAFTGSTRTGKQLLKDAgDSNMKRVWLEAGGKSANIV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 238 LDDA-DMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQ 316
Cdd:PRK09847 277 FADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSF 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 317 IETAVKHGAKLVHGGKrldrKGW--FLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITA 394
Cdd:PRK09847 357 IREGESKGQLLLDGRN----AGLaaAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTR 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 737003225 395 DVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:PRK09847 433 DLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
2-432 |
2.89e-69 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 228.67 E-value: 2.89e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 2 KYETINPY-TEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEA 80
Cdd:PRK03137 51 KIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 81 LGEVDLSADILDYYAEHGPRFLEPKQLHAQSG-KAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNV 159
Cdd:PRK03137 131 DADTAEAIDFLEYYARQMLKLADGKPVESRPGeHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 160 PQCALAFEKLLLDAGAPKGLYTnvFLTNeqSAKAIAD-----SRVKGVALTGS--------ERAGSAVAAEAGaaLKKST 226
Cdd:PRK03137 211 PVIAAKFVEVLEEAGLPAGVVN--FVPG--SGSEVGDylvdhPKTRFITFTGSrevglriyERAAKVQPGQIW--LKRVI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 227 MELGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPlEKATTLGPLCT 306
Cdd:PRK03137 285 AEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNAYMGPVIN 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 307 EGALKLVLGQIETAVKHGaKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFG 386
Cdd:PRK03137 364 QASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYG 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 737003225 387 LGGSVITADVERGKRVAAEIETGMVFVNSATWTApdL----PFGGIKNSG 432
Cdd:PRK03137 443 LTGAVISNNREHLEKARREFHVGNLYFNRGCTGA--IvgyhPFGGFNMSG 490
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
15-436 |
5.15e-68 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 226.23 E-value: 5.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 15 KTFPLHsDAELESFLAA-----AEDQYRA------------WRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLF 77
Cdd:PLN02466 73 KTFPTL-DPRTGEVIAHvaegdAEDVNRAvaaarkafdegpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 78 DEALG-EVDLSADILDYYAE-----HGPRFLEPKQLHAQsgkamIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVI 151
Cdd:PLN02466 152 EQSAKaELPMFARLFRYYAGwadkiHGLTVPADGPHHVQ-----TLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 152 IVKHAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSR-VKGVALTGS-ERAGSAVAAEAGAALKKSTMEL 229
Cdd:PLN02466 227 VLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMdVDKLAFTGStDTGKIVLELAAKSNLKPVTLEL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 230 GGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGA 309
Cdd:PLN02466 307 GGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQ 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 310 LKLVLGQIETAVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGG 389
Cdd:PLN02466 387 FEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAA 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 737003225 390 SVITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRE 436
Cdd:PLN02466 467 GVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGRE 513
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
3-446 |
5.36e-67 |
|
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: 221.89 E-value: 5.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEAL- 81
Cdd:cd07111 39 FPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 82 GEVDLSADILDYYAehgprflepKQLHAQSgKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQ 161
Cdd:cd07111 119 CDIPLVARHFYHHA---------GWAQLLD-TELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 162 CALAFEKLLLDAGAPKGLYtNVFLTNEQSAKAIAD-SRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDD 240
Cdd:cd07111 189 TALLFAEICAEAGLPPGVL-NIVTGNGSFGSALANhPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 241 ADMETALKW---GIWArmnNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQI 317
Cdd:cd07111 268 ADLDSAVEGivdAIWF---NQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 318 ETAVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPV--AMIFRvkSEQEAIDLANDSPFGLGGSVITAD 395
Cdd:cd07111 345 EEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVlvVLTFR--TAKEAVALANNTPYGLAASVWSEN 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 737003225 396 VERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRELSSLGIDEFV 446
Cdd:cd07111 423 LSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYL 473
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
6-447 |
2.56e-63 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 212.69 E-value: 2.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVD 85
Cdd:PLN00412 36 TNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 86 LSADILDYYAEHGPRFL-EPKQLHAQSGKA-------MIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAP 157
Cdd:PLN00412 116 RSGDLISYTAEEGVRILgEGKFLVSDSFPGnernkycLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 158 NVPQCALAFEKLLLDAGAPKGLYTNV---------FLTNEQSAKAIAdsrvkgvaLTGSERAGSAVAAEAGAALKkstME 228
Cdd:PLN00412 196 QGAVAALHMVHCFHLAGFPKGLISCVtgkgseigdFLTMHPGVNCIS--------FTGGDTGIAISKKAGMVPLQ---ME 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 229 LGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPlEKATTLGPLCTEG 308
Cdd:PLN00412 265 LGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDITPVVSES 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 309 ALKLVLGQIETAVKHGAKLVHGGKRLDRKGWflePTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLG 388
Cdd:PLN00412 344 SANFIEGLVMDAKEKGATFCQEWKREGNLIW---PLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQ 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 389 GSVITADVERGKRVAAEIETGMVFVNSATWTAPD-LPFGGIKNSGYGrelsSLGIDEFVN 447
Cdd:PLN00412 421 GCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIG----SQGITNSIN 476
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
7-434 |
8.81e-63 |
|
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: 210.84 E-value: 8.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 7 NPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDL 86
Cdd:cd07085 22 NPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 87 SADILDYyAEHGPRFLEPKQLHaQSGKAMIV---KEPLGILFCIEPWNFPyyqlARVVG---PNFIA-GNVIIVKHAPNV 159
Cdd:cd07085 102 GLEVVEF-ACSIPHLLKGEYLE-NVARGIDTysyRQPLGVVAGITPFNFP----AMIPLwmfPMAIAcGNTFVLKPSERV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 160 PQCALAFEKLLLDAGAPKGLYtNVFLTNEQSAKAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVL 238
Cdd:cd07085 176 PGAAMRLAELLQEAGLPDGVL-NVVHGGKEAVNALLDHpDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 239 DDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIE 318
Cdd:cd07085 255 PDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 319 TAVKHGAKLVHGGKRLDRKGW----FLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITA 394
Cdd:cd07085 335 SGVEEGAKLVLDGRGVKVPGYengnFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTR 414
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 737003225 395 DVERGKRVAAEIETGMVFVNS--ATWTAPdLPFGGIKNSGYG 434
Cdd:cd07085 415 SGAAARKFQREVDAGMVGINVpiPVPLAF-FSFGGWKGSFFG 455
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
30-435 |
2.58e-62 |
|
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: 208.28 E-value: 2.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 30 AAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDLSA---DI-LDYYAEHGPrflePK 105
Cdd:cd07095 7 AAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAgkiDIsIKAYHERTG----ER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 106 QLHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCALAFEKLLLDAGAPKGLYTNVFL 185
Cdd:cd07095 83 ATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 186 TNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKS-TMELGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVA 264
Cdd:cd07095 163 GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKIlALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 265 AKRFILHES-KADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVKHGAKLVHGGKRLDRKGWFLEP 343
Cdd:cd07095 243 ARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLSP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 344 TILENIEKSNPVfHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVNSATWTAP-D 422
Cdd:cd07095 323 GIIDVTDAADVP-DEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGASsT 401
|
410
....*....|...
gi 737003225 423 LPFGGIKNSGYGR 435
Cdd:cd07095 402 APFGGVGLSGNHR 414
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
4-434 |
7.40e-57 |
|
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: 194.56 E-value: 7.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 4 ETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRawRKTSWA---ERKAVLTKAAALLRQNREDYARPITIEMGKLFDEA 80
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFL--DRNNWLpahERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 81 LGEVDLSADILDYYAEHgPRFLEPKQL-----HAQSGK-AMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVK 154
Cdd:cd07148 80 KVEVTRAIDGVELAADE-LGQLGGREIpmgltPASAGRiAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 155 HAPNVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAAlKKSTMELGGSDA 234
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 235 FIVLDDADMETA----LKWGIWarmnNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGAL 310
Cdd:cd07148 238 VIVDRSADLDAMipplVKGGFY----HAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 311 KLVLGQIETAVKHGAKLVHGGKRLDRKgwFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGS 390
Cdd:cd07148 314 DRVEEWVNEAVAAGARLLCGGKRLSDT--TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAA 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 737003225 391 VITADVERGKRVAAEIETGMVFVNSATWTAPD-LPFGGIKNSGYG 434
Cdd:cd07148 392 VFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
3-434 |
1.61e-56 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 195.11 E-value: 1.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINP-YTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEAL 81
Cdd:cd07125 48 APVIDPaDHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 82 GEVDLSADILDYYAEHGPRFLEPKQLHAQSGK-AMIVKEPLGILFCIEPWNFPyyqLARVVGPNF---IAGNVIIVKHAP 157
Cdd:cd07125 128 AEVREAIDFCRYYAAQARELFSDPELPGPTGElNGLELHGRGVFVCISPWNFP---LAIFTGQIAaalAAGNTVIAKPAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 158 NVPQCALAFEKLLLDAGAPKGLYTNVFLTNEQSAKA-IADSRVKGVALTGSERAGSAVAAEAGAALKKST---MELGGSD 233
Cdd:cd07125 205 QTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEAlVAHPRIDGVIFTGSTETAKLINRALAERDGPILpliAETGGKN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 234 AFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLV 313
Cdd:cd07125 285 AMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 314 LGQIETAVKHgAKLVHGGKRLDRKGWFLEPTILENieKSNPVFHQEFFAPVAMIFRVKSEQ--EAIDLANDSPFGLGGSV 391
Cdd:cd07125 365 RAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEI--VGIFDLTTEVFGPILHVIRFKAEDldEAIEDINATGYGLTLGI 441
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 737003225 392 ITADVERGKRVAAEIETGMVFVNSATWTAPDL--PFGGIKNSGYG 434
Cdd:cd07125 442 HSRDEREIEYWRERVEAGNLYINRNITGAIVGrqPFGGWGLSGTG 486
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
5-439 |
2.02e-55 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 191.97 E-value: 2.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 5 TINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEV 84
Cdd:PLN02315 38 SVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 85 DLSADILDYyAEHGPRFLEPKQLHAQSGKAMI--VKEPLGILFCIEPWNFPyyqlARVVGPN----FIAGNVIIVKHAPN 158
Cdd:PLN02315 118 QEIIDMCDF-AVGLSRQLNGSIIPSERPNHMMmeVWNPLGIVGVITAFNFP----CAVLGWNaciaLVCGNCVVWKGAPT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 159 VPQCALAFEKLLLDA----GAPKGLYTNvFLTNEQSAKAIA-DSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSD 233
Cdd:PLN02315 193 TPLITIAMTKLVAEVleknNLPGAIFTS-FCGGAEIGEAIAkDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNN 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 234 AFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLV 313
Cdd:PLN02315 272 AIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 314 LGQIETAVKHGAKLVHGGKRLDRKGWFLEPTILEnIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVIT 393
Cdd:PLN02315 352 EKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFT 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 737003225 394 ADVERGKRVAAEI--ETGMVFVNSATWTAP-DLPFGGIKNSGYGRELSS 439
Cdd:PLN02315 431 RNPETIFKWIGPLgsDCGIVNVNIPTNGAEiGGAFGGEKATGGGREAGS 479
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
7-434 |
1.63e-53 |
|
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: 186.24 E-value: 1.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 7 NPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDL 86
Cdd:TIGR01722 22 NPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 87 SADILDYYAehGPRFLEPKQLHAQSGKAMIV---KEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCA 163
Cdd:TIGR01722 102 GLEVVEHAC--GVNSLLKGETSTQVATRVDVysiRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 164 LAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADM 243
Cdd:TIGR01722 180 VKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 244 ETALKWGIWARMNNTGQCCVAAKRFILhESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVKH 323
Cdd:TIGR01722 260 DAAADALVGAAYGAAGQRCMAISAAVL-VGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 324 GAKLVHGGKRLDRKGW----FLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERG 399
Cdd:TIGR01722 339 GAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAA 418
|
410 420 430
....*....|....*....|....*....|....*.
gi 737003225 400 KRVAAEIETGMVFVNSATWTA-PDLPFGGIKNSGYG 434
Cdd:TIGR01722 419 RRFQHEIEVGQVGVNVPIPVPlPYFSFTGWKDSFFG 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
6-434 |
1.78e-53 |
|
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: 186.63 E-value: 1.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 6 INPY-TEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEV 84
Cdd:cd07083 37 VSPFaPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 85 DLSADILDYYAEHGPRFLEPKQLHAQSGKAM--IVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQC 162
Cdd:cd07083 117 AEAIDFIRYYARAALRLRYPAVEVVPYPGEDneSFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 163 ALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAI-ADSRVKGVALTGSERA------GSAVAAEAGAALKKSTMELGGSDAF 235
Cdd:cd07083 197 GYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLtEHERIRGINFTGSLETgkkiyeAAARLAPGQTWFKRLYVETGGKNAI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 236 IVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLG 315
Cdd:cd07083 277 IVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 316 QIETAvKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQ--EAIDLANDSPFGLGGSVIT 393
Cdd:cd07083 357 YIEHG-KNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYS 435
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 737003225 394 ADVERGKRVAAEIETGMVFVNSATWTA--PDLPFGGIKNSGYG 434
Cdd:cd07083 436 RKREHLEEARREFHVGNLYINRKITGAlvGVQPFGGFKLSGTN 478
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
3-436 |
2.63e-52 |
|
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: 183.04 E-value: 2.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 3 YETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG 82
Cdd:cd07116 18 FDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 -EVDLSADILDYYAehgprflepKQLHAQSGK---------AMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVII 152
Cdd:cd07116 98 aDIPLAIDHFRYFA---------GCIRAQEGSiseidentvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 153 VKHAPNVPQCALAFEKLLLDAgAPKGLYTNVFLTNEQSAKAIADS-RVKGVALTGSERAGSAVAAEAGAALKKSTMELGG 231
Cdd:cd07116 169 LKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSkRIAKVAFTGETTTGRLIMQYASENIIPVTLELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 232 SDAFIVL------DDADMETALKwGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLC 305
Cdd:cd07116 248 KSPNIFFadvmdaDDAFFDKALE-GFVMFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 306 TEGALKLVLGQIETAVKHGAKLVHGGKR----LDRKGWFLEPTILENIEKSNpVFHQEFFAPVAMIFRVKSEQEAIDLAN 381
Cdd:cd07116 327 SLEQLEKILSYIDIGKEEGAEVLTGGERnelgGLLGGGYYVPTTFKGGNKMR-IFQEEIFGPVLAVTTFKDEEEALEIAN 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 737003225 382 DSPFGLGGSVITADVERGKRVAAEIETGMVFVNSATWTAPDLPFGGIKNSGYGRE 436
Cdd:cd07116 406 DTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRE 460
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
47-452 |
8.11e-51 |
|
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: 177.72 E-value: 8.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 47 RKAVLTKAAALLRQNREDYARPITIEMGK-LFDEALGEVDLSADILDYYAEHGPRFLEPKQ----LHAQSGKAMIVKEPL 121
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKpPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRvsvpLLLQPAKAYVIPEPL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 122 GILFCIEPWNFP-YYQLARVVGPnFIAGNVIIVK---HAPNvpqCALAFEKLLLDAgAPKGLYTNVFLTNEQSaKAIADS 197
Cdd:cd07087 102 GVVLIIGPWNYPlQLALAPLIGA-IAAGNTVVLKpseLAPA---TSALLAKLIPKY-FDPEAVAVVEGGVEVA-TALLAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 198 RVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADA 277
Cdd:cd07087 176 PFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 278 FVEAFKKSLEDLTPGDPLEkATTLGPLCTEGALKLVLGQIEtavkhGAKLVHGGKRlDRKGWFLEPTILENIEKSNPVFH 357
Cdd:cd07087 256 LIEELKKAIKEFYGEDPKE-SPDYGRIINERHFDRLASLLD-----DGKVVIGGQV-DKEERYIAPTILDDVSPDSPLMQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 358 QEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVNSATW--TAPDLPFGGIKNSGYGR 435
Cdd:cd07087 329 EEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLhaAIPNLPFGGVGNSGMGA 408
|
410
....*....|....*..
gi 737003225 436 ELSSLGIDEFVNHKLIH 452
Cdd:cd07087 409 YHGKAGFDTFSHLKSVL 425
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
21-449 |
7.45e-49 |
|
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: 172.79 E-value: 7.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 21 SDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGK-LFDEALGEV-DLSADILdYYAEHG 98
Cdd:cd07135 3 PLDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRpPFETLLTEVsGVKNDIL-HMLKNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 99 PRFLEPKQLHA-----QSGKAMIVKEPLGILFCIEPWNFPYY-QLARVVGPnFIAGNVIIVKHAPNVPQCALAFEKLL-- 170
Cdd:cd07135 82 KKWAKDEKVKDgplafMFGKPRIRKEPLGVVLIIGPWNYPVLlALSPLVGA-IAAGCTVVLKPSELTPHTAALLAELVpk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 171 -LDAGApkglyTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKW 249
Cdd:cd07135 161 yLDPDA-----FQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 250 GIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKaTTLGPLCTEGALKLVLGQIETAvkhGAKLVH 329
Cdd:cd07135 236 ILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANAS-PDYTRIVNPRHFNRLKSLLDTT---KGKVVI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 330 GGKRlDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETG 409
Cdd:cd07135 312 GGEM-DEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSG 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 737003225 410 MVFVNSATWTA--PDLPFGGIKNSGYGRELSSLGIDEFVNHK 449
Cdd:cd07135 391 GVVINDTLIHVgvDNAPFGGVGDSGYGAYHGKYGFDTFTHER 432
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
47-449 |
8.96e-46 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 165.59 E-value: 8.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 47 RKAVLTKAAALLRQNREDYARPITIEMGKLFDEA-LGEVDLSADILDYYAEHGPRFLEPKQ----LHAQSGKAMIVKEPL 121
Cdd:PTZ00381 31 RKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETkMTEVLLTVAEIEHLLKHLDEYLKPEKvdtvGVFGPGKSYIIPEPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 122 GILFCIEPWNFPYY----QLARVVGpnfiAGNVIIVKHAPNVPQCALAFEKLLldagaPKGL---YTNVFLTNEQSAKAI 194
Cdd:PTZ00381 111 GVVLVIGAWNYPLNltliPLAGAIA----AGNTVVLKPSELSPHTSKLMAKLL-----TKYLdpsYVRVIEGGVEVTTEL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 195 ADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESK 274
Cdd:PTZ00381 182 LKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 275 ADAFVEAFKKSLEDLTPGDPlEKATTLGPLCTEGALKLVLGQIETavkHGAKLVHGGKrLDRKGWFLEPTILENIEKSNP 354
Cdd:PTZ00381 262 KDKFIEALKEAIKEFFGEDP-KKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE-VDIENKYVAPTIIVNPDLDSP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 355 VFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVNSATW--TAPDLPFGGIKNSG 432
Cdd:PTZ00381 337 LMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFhlLNPNLPFGGVGNSG 416
|
410
....*....|....*..
gi 737003225 433 YGRELSSLGIDEFVNHK 449
Cdd:PTZ00381 417 MGAYHGKYGFDTFSHPK 433
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
30-435 |
1.66e-40 |
|
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: 150.07 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 30 AAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKlfdeALGEVDLSaDILDYYAE------HGPRFLE 103
Cdd:cd07134 5 AAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRK----PAAEVDLT-EILPVLSEinhaikHLKKWMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 104 PKQLHAQSG----KAMIVKEPLGILFCIEPWNFPYyQLArvVGP---NFIAGNVIIVKHAPNVPQCALAFEKLLLDAGAP 176
Cdd:cd07134 80 PKRVRTPLLlfgtKSKIRYEPKGVCLIISPWNYPF-NLA--FGPlvsAIAAGNTAILKPSELTPHTSAVIAKIIREAFDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 177 KglYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMN 256
Cdd:cd07134 157 D--EVAVFEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 257 NTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATT-LGPLCTEGALKLVLGQIETAVKHGAKLVHGGKrLD 335
Cdd:cd07134 235 NAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPdLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQ-FD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 336 RKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVNS 415
Cdd:cd07134 314 AAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVND 393
|
410 420
....*....|....*....|..
gi 737003225 416 --ATWTAPDLPFGGIKNSGYGR 435
Cdd:cd07134 394 vvLHFLNPNLPFGGVNNSGIGS 415
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
4-451 |
1.80e-40 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 152.98 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 4 ETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGE 83
Cdd:PLN02419 132 DVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 84 VDLSADILDYYAEHGPRFLEPKQLHAQSG-KAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQC 162
Cdd:PLN02419 212 IFRGLEVVEHACGMATLQMGEYLPNVSNGvDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 163 ALAFEKLLLDAGAPKGLYTNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDAD 242
Cdd:PLN02419 292 SVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDAN 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 243 METALKWGIWARMNNTGQCCVAAKRFIL---HESKADAFVEAfKKSLEdLTPGDplEKATTLGPLCTEGALKLVLGQIET 319
Cdd:PLN02419 372 IDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVER-AKALK-VTCGS--EPDADLGPVISKQAKERICRLIQS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 320 AVKHGAKLVHGGKRL----DRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITAD 395
Cdd:PLN02419 448 GVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSS 527
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737003225 396 VERGKRVAAEIETGMVFVNSA--------TWTAPDLPFGGIKNSgYGRElsslGIDEFVNHKLI 451
Cdd:PLN02419 528 GAAARKFQMDIEAGQIGINVPipvplpffSFTGNKASFAGDLNF-YGKA----GVDFFTQIKLV 586
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
4-432 |
9.35e-38 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 143.56 E-value: 9.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 4 ETINPYTEEKLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGE 83
Cdd:PRK09457 18 ESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 84 V-------DLSadILDYYAEHGPrflepKQLHAQSGKAMIVKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHA 156
Cdd:PRK09457 98 VtaminkiAIS--IQAYHERTGE-----KRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 157 PNVPQCALAFEKLLLDAGAPKGLyTNVFLTNEQSAKAIADSR-VKGVALTGSERAGSAVAAEAGAALKKS-TMELGGSDA 234
Cdd:PRK09457 171 ELTPWVAELTVKLWQQAGLPAGV-LNLVQGGRETGKALAAHPdIDGLLFTGSANTGYLLHRQFAGQPEKIlALEMGGNNP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 235 FIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESK-ADAFVEAFKKSLEDLTPGDPL-EKATTLGPLCTEGALKL 312
Cdd:PRK09457 250 LVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWDaEPQPFMGAVISEQAAQG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 313 VLGQIETAVKHGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVfHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVI 392
Cdd:PRK09457 330 LVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIIDVTGVAELP-DEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLL 408
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 737003225 393 TADVERGKRVAAEIETGMVFVNSATWTAP-DLPFGGIKNSG 432
Cdd:PRK09457 409 SDDREDYDQFLLEIRAGIVNWNKPLTGASsAAPFGGVGASG 449
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
35-435 |
1.74e-37 |
|
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: 141.85 E-value: 1.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 35 QYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGK--LFDEALGEVDLSADILDYYAEHGPRFLEPKQLHA--- 109
Cdd:cd07133 10 AFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGHrsRHETLLAEILPSIAGIKHARKHLKKWMKPSRRHVgll 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 110 -QSGKAMIVKEPLGILFCIEPWNFPYYqLArvVGP---NFIAGNVIIVKHAPNVPQCALAFEKLLLDAGAPKGLytNVFL 185
Cdd:cd07133 90 fLPAKAEVEYQPLGVVGIIVPWNYPLY-LA--LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV--AVVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 186 TNEQSAKAIAdsrvkgvAL-------TGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMNNT 258
Cdd:cd07133 165 GGADVAAAFS-------SLpfdhllfTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 259 GQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTlgPLCTEGALKLVLGQIETAVKHGAKLV--HGGKRLDR 336
Cdd:cd07133 238 GQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPDYT--SIINERHYARLQGLLEDARAKGARVIelNPAGEDFA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 337 KGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVNSA 416
Cdd:cd07133 316 ATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDT 395
|
410 420
....*....|....*....|.
gi 737003225 417 TW--TAPDLPFGGIKNSGYGR 435
Cdd:cd07133 396 LLhvAQDDLPFGGVGASGMGA 416
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
47-449 |
5.61e-37 |
|
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: 140.43 E-value: 5.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 47 RKAVLTKAAALLRQNREDYARPITIEMGK-LFDEALGEVDLSADILDYYAEHGPRFLEP----KQLHAQSGKAMIVKEPL 121
Cdd:cd07132 22 RIQQLEALLRMLEENEDEIVEALAKDLRKpKFEAVLSEILLVKNEIKYAISNLPEWMKPepvkKNLATLLDDVYIYKEPL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 122 GILFCIEPWNFPYY-QLARVVGPnFIAGNVIIVKHAPNVPQCALAFEKLL---LDagapKGLYTnVFLTNEQSAKAIADS 197
Cdd:cd07132 102 GVVLIIGAWNYPLQlTLVPLVGA-IAAGNCVVIKPSEVSPATAKLLAELIpkyLD----KECYP-VVLGGVEETTELLKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 198 RVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADA 277
Cdd:cd07132 176 RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 278 FVEAFKKSLEDLTPGDPlEKATTLGPLCTEGALKLVLGQIEtavkhGAKLVHGGkRLDRKGWFLEPTILENIEKSNPVFH 357
Cdd:cd07132 256 FVEALKKTLKEFYGEDP-KESPDYGRIINDRHFQRLKKLLS-----GGKVAIGG-QTDEKERYIAPTVLTDVKPSDPVMQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 358 QEFFAPVAMIFRVKSEQEAIDLAN--DSPFGLggSVITADVERGKRVAAEIETGMVFVNSAT--WTAPDLPFGGIKNSGY 433
Cdd:cd07132 329 EEIFGPILPIVTVNNLDEAIEFINsrEKPLAL--YVFSNNKKVINKILSNTSSGGVCVNDTImhYTLDSLPFGGVGNSGM 406
|
410
....*....|....*.
gi 737003225 434 GRELSSLGIDEFVNHK 449
Cdd:cd07132 407 GAYHGKYSFDTFSHKR 422
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
36-451 |
5.88e-35 |
|
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: 134.85 E-value: 5.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 36 YRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEA-LGEVDLSADILDYYAEHGPRFLEPKQ----LHAQ 110
Cdd:cd07137 12 FRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCKLAIKELKKWMAPEKvktpLTTF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 111 SGKAMIVKEPLGILFCIEPWNFPY-YQLARVVGPnFIAGNVIIVKHAPNVPQCALAFEKLL---LDAGAPKglytnVFLT 186
Cdd:cd07137 92 PAKAEIVSEPLGVVLVISAWNFPFlLSLEPVIGA-IAAGNAVVLKPSELAPATSALLAKLIpeyLDTKAIK-----VIEG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 187 NEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETAL------KWGiwarmNNTGQ 260
Cdd:cd07137 166 GVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVrriaggKWG-----CNNGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 261 CCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEkattlgplcTEGALKLV-------LGQIETAVKHGAKLVHGGKR 333
Cdd:cd07137 241 ACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKE---------SKDLSRIVnshhfqrLSRLLDDPSVADKIVHGGER 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 334 lDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFV 413
Cdd:cd07137 312 -DEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTF 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 737003225 414 NSAT--WTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:cd07137 391 NDTVvqYAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
43-435 |
6.83e-35 |
|
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: 134.94 E-value: 6.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 43 SWAERKAVLTKAAALLRQNREDYARPITIEMGK-LFDEALGEVDLSADILDYYAEHGPRFLEPKQ----LHAQSGKAMIV 117
Cdd:cd07136 18 DVEFRIEQLKKLKQAIKKYENEILEALKKDLGKsEFEAYMTEIGFVLSEINYAIKHLKKWMKPKRvktpLLNFPSKSYIY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 118 KEPLGILFCIEPWNFPYyQLA--RVVGPnfI-AGNVIIVKHAPNVPQCALAFEKLLLDAGAPKglYTNVFLTNEQSAKAI 194
Cdd:cd07136 98 YEPYGVVLIIAPWNYPF-QLAlaPLIGA--IaAGNTAVLKPSELTPNTSKVIAKIIEETFDEE--YVAVVEGGVEENQEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 195 ADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESK 274
Cdd:cd07136 173 LDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 275 ADAFVEAFKKSLEDLTPGDPLEKAtTLGPLCTEGALKLVLGQIEtavkhGAKLVHGGKRlDRKGWFLEPTILENIEKSNP 354
Cdd:cd07136 253 KEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLD-----NGKIVFGGNT-DRETLYIEPTILDNVTWDDP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 355 VFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVNS-----ATwtaPDLPFGGIK 429
Cdd:cd07136 326 VMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDtimhlAN---PYLPFGGVG 402
|
....*.
gi 737003225 430 NSGYGR 435
Cdd:cd07136 403 NSGMGS 408
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
20-414 |
3.89e-34 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 136.15 E-value: 3.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 20 HSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDLSADILDYYAEHGP 99
Cdd:PRK11905 587 ASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQAR 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 100 RFLEPKQLhaqsgkamivkEPLGILFCIEPWNFPyyqLARVVG---PNFIAGNVIIVKHAPNVPQCALAFEKLLLDAGAP 176
Cdd:PRK11905 667 RLLNGPGH-----------KPLGPVVCISPWNFP---LAIFTGqiaAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVP 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 177 KGLYTnvFLTNEQS---AKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTM---ELGGSDAFIVLDDADMETALKWG 250
Cdd:PRK11905 733 KDALQ--LLPGDGRtvgAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAMIVDSSALPEQVVADV 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 251 IWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVKHGaKLVHg 330
Cdd:PRK11905 811 IASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAG-RLVH- 888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 331 gkRLDR-----KGWFLEPTILE--NIEksnpVFHQEFFAPVAMIFRVKSEQ--EAIDLANDSPFGLGGSVITADVERGKR 401
Cdd:PRK11905 889 --QLPLpaeteKGTFVAPTLIEidSIS----DLEREVFGPVLHVVRFKADEldRVIDDINATGYGLTFGLHSRIDETIAH 962
|
410
....*....|...
gi 737003225 402 VAAEIETGMVFVN 414
Cdd:PRK11905 963 VTSRIRAGNIYVN 975
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
21-434 |
7.35e-34 |
|
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: 133.11 E-value: 7.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 21 SDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDLSADILDYYAEHGPR 100
Cdd:TIGR01238 72 NLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 101 FLePKQLHaqsgkamivkEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCALAFEKLLLDAGAPKGLY 180
Cdd:TIGR01238 152 VL-GEFSV----------ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 181 TNVFLTNEQSAKAI-ADSRVKGVALTGSERAGSAVAAEAGAALKKST---MELGGSDAFIVLDDADMETALKWGIWARMN 256
Cdd:TIGR01238 221 QLLPGRGADVGAALtSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVpliAETGGQNAMIVDSTALPEQVVRDVLRSAFD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 257 NTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIEtAVKHGAKLVHGGKRLD- 335
Cdd:TIGR01238 301 SAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIE-HMSQTQKKIAQLTLDDs 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 336 ---RKGWFLEPTILE--NIEKsnpvFHQEFFAPVAMIFRVKSEQ--EAIDLANDSPFGLGGSVITADVERGKRVAAEIET 408
Cdd:TIGR01238 380 racQHGTFVAPTLFEldDIAE----LSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARV 455
|
410 420
....*....|....*....|....*...
gi 737003225 409 GMVFVNSATWTA--PDLPFGGIKNSGYG 434
Cdd:TIGR01238 456 GNCYVNRNQVGAvvGVQPFGGQGLSGTG 483
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
19-414 |
2.01e-30 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 124.93 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 19 LHSDAE-LESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDLSADILDYYAEH 97
Cdd:PRK11904 580 AFADAEqVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQ 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 98 GPR-FLEPKQLHAQSGKA-MIVKEPLGILFCIEPWNFPyyqLARVVGP---NFIAGNVIIVKHAPNVPQCALAFEKLLLD 172
Cdd:PRK11904 660 ARRlFGAPEKLPGPTGESnELRLHGRGVFVCISPWNFP---LAIFLGQvaaALAAGNTVIAKPAEQTPLIAAEAVKLLHE 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 173 AGAPKGLYTnvFLTNEQS---AKAIADSRVKGVALTGS------------ERAGSAVAAEAgaalkkstmELGGSDAFI- 236
Cdd:PRK11904 737 AGIPKDVLQ--LLPGDGAtvgAALTADPRIAGVAFTGStetariinrtlaARDGPIVPLIA---------ETGGQNAMIv 805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 237 --------VLDDAdMETALKwgiwarmnNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEG 308
Cdd:PRK11904 806 dstalpeqVVDDV-VTSAFR--------SAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAE 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 309 ALKLVLGQIEtAVKHGAKLVHGGK--RLDRKGWFLEPTILE--NIEksnpVFHQEFFAPVAMIFRVKSEQ--EAIDLAND 382
Cdd:PRK11904 877 AKANLDAHIE-RMKREARLLAQLPlpAGTENGHFVAPTAFEidSIS----QLEREVFGPILHVIRYKASDldKVIDAINA 951
|
410 420 430
....*....|....*....|....*....|..
gi 737003225 383 SPFGLGGSVITADVERGKRVAAEIETGMVFVN 414
Cdd:PRK11904 952 TGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
25-451 |
8.20e-27 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 112.51 E-value: 8.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 25 LESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEAL-GEVDLSADILDYYAEHGPRFLE 103
Cdd:PLN02203 8 LEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYrDEVGVLTKSANLALSNLKKWMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 104 PKQLH----AQSGKAMIVKEPLGILFCIEPWNFPY-YQLARVVGPnFIAGNVIIVKHAPNVPQCALAFEKLL---LDAGA 175
Cdd:PLN02203 88 PKKAKlplvAFPATAEVVPEPLGVVLIFSSWNFPIgLSLEPLIGA-IAAGNAVVLKPSELAPATSAFLAANIpkyLDSKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 176 PKglytnVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIV--LDDA-DMETAL----- 247
Cdd:PLN02203 167 VK-----VIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVnrivg 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 248 -KWGIWArmnntGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVKhgAK 326
Cdd:PLN02203 242 gKWGSCA-----GQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVA--AS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 327 LVHGGKrLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEI 406
Cdd:PLN02203 315 IVHGGS-IDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSET 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 737003225 407 ETGMVFVNSAT--WTAPDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:PLN02203 394 SSGSVTFNDAIiqYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
21-414 |
2.80e-26 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 112.34 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 21 SDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDLSADILDYYAEHGPR 100
Cdd:COG4230 591 TAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARR 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 101 -FLEPKQLHaqsgkamivkePLGILFCIEPWNFPyyqLARVVGPnfI-----AGNVIIVKHAPNVPQCALAFEKLLLDAG 174
Cdd:COG4230 671 lFAAPTVLR-----------GRGVFVCISPWNFP---LAIFTGQ--VaaalaAGNTVLAKPAEQTPLIAARAVRLLHEAG 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 175 APKGlytnV--FLTNEQS---AKAIADSRVKGVALTGS------------ERAgsavaaeagaalkkSTM-----ELGGS 232
Cdd:COG4230 735 VPAD----VlqLLPGDGEtvgAALVADPRIAGVAFTGStetarlinrtlaARD--------------GPIvpliaETGGQ 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 233 DAFIV---------LDDAdMETALkwgiwarmNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGP 303
Cdd:COG4230 797 NAMIVdssalpeqvVDDV-LASAF--------DSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGP 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 304 LCTEGALKLVLGQIEtAVKHGAKLVHGGKRLD--RKGWFLEPTILE--NIEksnpVFHQEFFAPVAMIFRVKSEQ--EAI 377
Cdd:COG4230 868 VIDAEARANLEAHIE-RMRAEGRLVHQLPLPEecANGTFVAPTLIEidSIS----DLEREVFGPVLHVVRYKADEldKVI 942
|
410 420 430
....*....|....*....|....*....|....*..
gi 737003225 378 DLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVN 414
Cdd:COG4230 943 DAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
21-434 |
4.37e-24 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 105.83 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 21 SDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALGEVDLSADILDYYAEhgpr 100
Cdd:PRK11809 680 TPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAG---- 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 101 flepkQLHAQSGKAMivKEPLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCALAFEKLLLDAGAPKGLY 180
Cdd:PRK11809 756 -----QVRDDFDNDT--HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVV 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 181 TNVFLTNEQ-SAKAIADSRVKGVALTGSERAGSAVAAEAGAALK---KST---MELGGSDAFIVLDDADMETALKWGIWA 253
Cdd:PRK11809 829 QLLPGRGETvGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDpqgRPIpliAETGGQNAMIVDSSALTEQVVADVLAS 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 254 RMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETAVKHGAK---LVHG 330
Cdd:PRK11809 909 AFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPvfqAARE 988
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 331 GKRLDRKGWFLEPTI--LENIEKsnpvFHQEFFAPVAMIFRVKSEQ--EAIDLANDSPFGLGGSVITADVERGKRVAAEI 406
Cdd:PRK11809 989 NSEDWQSGTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRIDETIAQVTGSA 1064
|
410 420 430
....*....|....*....|....*....|
gi 737003225 407 ETGMVFVNSATWTA--PDLPFGGIKNSGYG 434
Cdd:PRK11809 1065 HVGNLYVNRNMVGAvvGVQPFGGEGLSGTG 1094
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
114-451 |
5.81e-24 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 103.97 E-value: 5.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 114 AMIVKEPLGILFCIEPWNFPY-YQLARVVGPnFIAGNVIIVKHAPNVPQCALAFEKLL---LDAGAPKGLYTNVFLTNeq 189
Cdd:PLN02174 106 AEIVSEPLGVVLVISAWNYPFlLSIDPVIGA-ISAGNAVVLKPSELAPASSALLAKLLeqyLDSSAVRVVEGAVTETT-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 190 sakAIADSRVKGVALTGSERAGSAVAAEAGAALKKSTMELGGSDAFIVLDDADMETAL------KWGIwarmnNTGQCCV 263
Cdd:PLN02174 183 ---ALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVrriiagKWGC-----NNGQACI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 264 AAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTE--GALKLVLGQIETAvkhgAKLVHGGKRlDRKGWFL 341
Cdd:PLN02174 255 SPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSThfDRLSKLLDEKEVS----DKIVYGGEK-DRENLKI 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 342 EPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRVAAEIETGMVFVN--SATWT 419
Cdd:PLN02174 330 APTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiAVHLA 409
|
330 340 350
....*....|....*....|....*....|..
gi 737003225 420 APDLPFGGIKNSGYGRELSSLGIDEFVNHKLI 451
Cdd:PLN02174 410 LHTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
13-432 |
1.35e-20 |
|
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: 94.19 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 13 KLKTFPLHSDAELESFLAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPIT-IEMGKLFDEAlgEVDLSADIL 91
Cdd:cd07123 59 VLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATmLGQGKNVWQA--EIDAACELI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 92 D------YYAEHgprfLEPKQ-LHAQSG-KAMIVKEPL-GILFCIEPWNFPyyqlarVVGPNFIA-----GNVIIVKHAP 157
Cdd:cd07123 137 DflrfnvKYAEE----LYAQQpLSSPAGvWNRLEYRPLeGFVYAVSPFNFT------AIGGNLAGapalmGNVVLWKPSD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 158 NVPQCALAFEKLLLDAGAPKGLYTnvFLTNEQSA---KAIADSRVKGVALTGSeragsavaAEAGAALKKSTM------- 227
Cdd:cd07123 207 TAVLSNYLVYKILEEAGLPPGVIN--FVPGDGPVvgdTVLASPHLAGLHFTGS--------TPTFKSLWKQIGenldryr 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 228 -------ELGGSDAFIVLDDADMETALKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATT 300
Cdd:cd07123 277 typrivgETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNF 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 301 LGPLCTEGALKLVLGQIETAVK-HGAKLVHGGKRLDRKGWFLEPTILENIEKSNPVFHQEFFAPVAMIFRVKSEQ--EAI 377
Cdd:cd07123 357 MGAVIDEKAFDRIKGYIDHAKSdPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDfeETL 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737003225 378 DLAND-SPFGLGGSVITADVE------RGKRVAAeietGMVFVNSATWTA--PDLPFGGIKNSG 432
Cdd:cd07123 437 ELVDTtSPYALTGAIFAQDRKaireatDALRNAA----GNFYINDKPTGAvvGQQPFGGARASG 496
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
37-435 |
1.46e-20 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 94.26 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 37 RAWRKTSWAERKAVLTKAAALLRQNREDYARpITIEMGKLFDEALGEVDLSADILDYYAEHGPRFLEPKQLHAQSGKAMI 116
Cdd:cd07128 51 PALRALTFHERAAMLKALAKYLMERKEDLYA-LSAATGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDVEPL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 117 VKE----------PL-GILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCALAFEKLLLDAGA-PKGLYTnvF 184
Cdd:cd07128 130 SKDgtfvgqhiltPRrGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQ--L 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 185 LTNeqSAKAIADsRVKG---VALTGSErAGSAVAAEAGAALKKS---TMELGGSDAFIVLDDA--DMET--ALKWGIWAR 254
Cdd:cd07128 208 ICG--SVGDLLD-HLGEqdvVAFTGSA-ATAAKLRAHPNIVARSirfNAEADSLNAAILGPDAtpGTPEfdLFVKEVARE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 255 MN-NTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGPLCTEGALKLVLGQIETaVKHGAKLVHGGKr 333
Cdd:cd07128 284 MTvKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGP- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 334 lDR---------KGWFLEPTIL-ENIEKSNPVFHQ-EFFAPVAMIFRVKSEQEAIDLANDSPFGLGGSVITADVERGKRV 402
Cdd:cd07128 362 -DRfevvgadaeKGAFFPPTLLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFAREL 440
|
410 420 430
....*....|....*....|....*....|....*....
gi 737003225 403 AAEIET--GMVFVNS----ATWTAPDLPFGGIKNSGYGR 435
Cdd:cd07128 441 VLGAAPyhGRLLVLNrdsaKESTGHGSPLPQLVHGGPGR 479
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
28-421 |
2.63e-19 |
|
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: 89.99 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 28 FLAAAEDQyRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGK----LFDEALGEVDLS--ADILDYYAEHGPRF 101
Cdd:cd07084 5 LLAADIST-KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKgwmfAENICGDQVQLRarAFVIYSYRIPHEPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 102 LEPKQLHAQSGKAMIVkePLGILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCALAFEKLLLDAGA-PKGLY 180
Cdd:cd07084 84 NHLGQGLKQQSHGYRW--PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 181 TNVFLTNEQSAKAIADSRVKGVALTGSERAGSAVAAEAGAAlkKSTMELGGSDAFIVLDDADMETALKWGIWARMN-NTG 259
Cdd:cd07084 162 TLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVAWQCVQDMTaCSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 260 QCCVAAKRFILHESKA-DAFVEAFKKSLEDLTPGDplekaTTLGPLCTEGalklVLGQIETAVKH-GAKLVHGGKRLDRK 337
Cdd:cd07084 240 QKCTAQSMLFVPENWSkTPLVEKLKALLARRKLED-----LLLGPVQTFT----TLAMIAHMENLlGSVLLFSGKELKNH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 338 GWF-----LEPTIL----ENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDL---------------ANDSPFglGGSVIT 393
Cdd:cd07084 311 SIPsiygaCVASALfvpiDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLellermhgsltaaiySNDPIF--LQELIG 388
|
410 420
....*....|....*....|....*...
gi 737003225 394 ADVERGKRVAAEIETGMVFVNSATWTAP 421
Cdd:cd07084 389 NLWVAGRTYAILRGRTGVAPNQNHGGGP 416
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
7-440 |
9.12e-17 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 82.44 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 7 NPYTEEKLKTfplhSDAE---LESFLAAAEDQYR-AWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGKLFDEALG 82
Cdd:PRK11903 25 DPVTGEELVR----VSATgldLAAAFAFAREQGGaALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 83 EVDLSADILDYYAEHGpRFLEPKQLHAQSGKAMIVKEPL-----------GILFCIEPWNFPYYQLARVVGPNFIAGNVI 151
Cdd:PRK11903 101 DIDGGIFTLGYYAKLG-AALGDARLLRDGEAVQLGKDPAfqgqhvlvptrGVALFINAFNFPAWGLWEKAAPALLAGVPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 152 IVKHAPNVPQCALAFEKLLLDAGA-PKGLYTNVFLTNEQSAKAIADSRVkgVALTGSERAGSAVAAEAGAALK--KSTME 228
Cdd:PRK11903 180 IVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFDV--VSFTGSAETAAVLRSHPAVVQRsvRVNVE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 229 LGGSDAFIVLDDADMETA-----LKWGIWARMNNTGQCCVAAKRFILHESKADAFVEAFKKSLEDLTPGDPLEKATTLGP 303
Cdd:PRK11903 258 ADSLNSALLGPDAAPGSEafdlfVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 304 LCTEGALKLVLGQIEtAVKHGAKLVHGGKRL------DRKGWFLEPTIL--ENIEKSNPVFHQEFFAPVAMIFRVKSEQE 375
Cdd:PRK11903 338 LVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFalvdadPAVAACVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAH 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737003225 376 AIDLANDSPFGLGGSVITADVERGKRVAAEIET--GMVFVNSATWTA---------PDLPFGGIKNSGYGRELSSL 440
Cdd:PRK11903 417 ALALARRGQGSLVASVYSDDAAFLAAAALELADshGRVHVISPDVAAlhtghgnvmPQSLHGGPGRAGGGEELGGL 492
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
50-419 |
5.68e-09 |
|
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: 57.89 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 50 VLTKAAALLRQNR-EDY-ARPITIEMGKLFDEALGEVDLSADILDYYAEHGPRFLE-----PKQLHAQSGKAMivKEPLG 122
Cdd:cd07126 67 VSHRVAHELRKPEvEDFfARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLArsfnvPGDHQGQQSSGY--RWPYG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 123 ILFCIEPWNFPYYQLARVVGPNFIAGNVIIVKHAPNVPQCALAFEKLLLDAGAPKglyTNVFLTN---EQSAKAIADSRV 199
Cdd:cd07126 145 PVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPA---TDVDLIHsdgPTMNKILLEANP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 200 KGVALTGSERAGSAVAAEAGAALKkstMELGGSDAFIVLDDADMETALKW----GIWArmnNTGQCCVAAKRFILHESKA 275
Cdd:cd07126 222 RMTLFTGSSKVAERLALELHGKVK---LEDAGFDWKILGPDVSDVDYVAWqcdqDAYA---CSGQKCSAQSILFAHENWV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 276 DA-FVE-----AFKKSLEDLTPGdPLEKATTlgplctegalKLVLGQIETAVK-HGAKLVHGGKRLDRKG-----WFLEP 343
Cdd:cd07126 296 QAgILDklkalAEQRKLEDLTIG-PVLTWTT----------ERILDHVDKLLAiPGAKVLFGGKPLTNHSipsiyGAYEP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 344 TI----LENI--EKSNPVFHQEFFAPVAMIFRVKSEQE--AIDLANDSPFGLGGSVITADVERGKRVAAEIetgmvfVNS 415
Cdd:cd07126 365 TAvfvpLEEIaiEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEVLANT------VNG 438
|
....
gi 737003225 416 ATWT 419
Cdd:cd07126 439 TTYA 442
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
29-414 |
3.02e-08 |
|
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: 55.63 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 29 LAAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDY------------ARpITIEMGKlfdeALGEVDLSADILDYYAE 96
Cdd:cd07129 5 AAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELvarahaetglpeAR-LQGELGR----TTGQLRLFADLVREGSW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 97 HGPRfLEPKQLHAQSG-----KAMIVkePLGILFCIEPWNFPyyqLA-RVVGPNFI----AGNVIIVKHAPNVP----QC 162
Cdd:cd07129 80 LDAR-IDPADPDRQPLprpdlRRMLV--PLGPVAVFGASNFP---LAfSVAGGDTAsalaAGCPVVVKAHPAHPgtseLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 163 ALAFEKLLLDAGAPKGLYTNVFLTN-EQSAKAIADSRVKGVALTGSERagsavaaeAGAALKKST----------MELGG 231
Cdd:cd07129 154 ARAIRAALRATGLPAGVFSLLQGGGrEVGVALVKHPAIKAVGFTGSRR--------GGRALFDAAaarpepipfyAELGS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 232 SDAFIVLDDADME--TALKWGIWARMN-NTGQCCVAAKRFILHESKA-DAFVEAFKKSLEDLTPgdplekattlGPLCTE 307
Cdd:cd07129 226 VNPVFILPGALAErgEAIAQGFVGSLTlGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPA----------QTMLTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 308 GALKLVLGQIETAVKHGAKLVHGGKRLDRKGWFLEPTILE---NIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLANDSP 384
Cdd:cd07129 296 GIAEAYRQGVEALAAAPGVRVLAGGAAAEGGNQAAPTLFKvdaAAFLADPALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
410 420 430
....*....|....*....|....*....|....
gi 737003225 385 FGLGGSVI--TADVERGKRVAAEIE--TGMVFVN 414
Cdd:cd07129 376 GQLTATIHgeEDDLALARELLPVLErkAGRLLFN 409
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
30-427 |
3.78e-04 |
|
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: 42.61 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 30 AAAEDQYRAWRKTSWAERKAVLTKAAALLRQNREDYARPITIEMGklfdeaLGEVDlsadilDYYAEH--------GPRF 101
Cdd:cd07121 11 AAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETG------MGRVE------DKIAKNhlaaektpGTED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 102 LEPKQLHAQSGKAMIVKEPLGILFCIEPWNFPyyqLARVVGpNFI----AGNVIIVKHAPNVPQCAL----AFEKLLLDA 173
Cdd:cd07121 79 LTTTAWSGDNGLTLVEYAPFGVIGAITPSTNP---TETIIN-NSIsmlaAGNAVVFNPHPGAKKVSAyaveLINKAIAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 174 GAPKGLYTNVFLTNEQSAKAIADSR-VKGVALTGSEragsavaaeagaALKKSTMELG--------GSDAFIVLDDADME 244
Cdd:cd07121 155 GGPDNLVVTVEEPTIETTNELMAHPdINLLVVTGGP------------AVVKAALSSGkkaigagaGNPPVVVDETADIE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 245 TAlkwgiwARM--------NNTgqCCVAAKRFILHESKADAFVEAFKKsledltpgdplekattlgplctEGALKLVLGQ 316
Cdd:cd07121 223 KA------ARDivqgasfdNNL--PCIAEKEVIAVDSVADYLIAAMQR----------------------NGAYVLNDEQ 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737003225 317 IEtAVKHGAKLVHGGKRLDRK------GWFLE----------PTILENIEKSNPVFHQEFFAPVAMIFRVKSEQEAIDLA 380
Cdd:cd07121 273 AE-QLLEVVLLTNKGATPNKKwvgkdaSKILKaagievpadiRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELA 351
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 737003225 381 NDSPFGLGGSVI--TADVERGKRVAAEIETGMVFVNSATWTApdLPFGG 427
Cdd:cd07121 352 VELEHGNRHTAIihSKNVENLTKMARAMQTTIFVKNGPSYAG--LGVGG 398
|
|
| |
