|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
25-454 |
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: 594.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 25 IEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNKIVNYARYFATQGPAFLQP 104
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 105 KNYDklSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQAFEKACQKVGIPEGAFAN 184
Cdd:cd07100 81 EPIE--TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 185 IFATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVC 264
Cdd:cd07100 159 LLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 265 TAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNlNVDEGPGFQF 344
Cdd:cd07100 239 IAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGG-KRPDGPGAFY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 345 SPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQA 424
Cdd:cd07100 318 PPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDP 397
|
410 420 430
....*....|....*....|....*....|
gi 1140776579 425 EVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07100 398 RLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
1-454 |
5.13e-140 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 409.13 E-value: 5.13e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 1 MAYTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGES 80
Cdd:PRK09406 1 MPIATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 81 RTEVNKIVNYARYFATQGPAFLQPKNYDKLSVG-STAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHAS 159
Cdd:PRK09406 81 KAEALKCAKGFRYYAEHAEALLADEPADAAAVGaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 160 IVPQAAQAFEKACQKVGIPEGAFANIFATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAV 239
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 240 LDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQV 319
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 320 EKVVAGGSKILYGNLNVDeGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADV 399
Cdd:PRK09406 321 DDAVAAGATILCGGKRPD-GPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1140776579 400 KHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:PRK09406 400 AEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
6-454 |
1.86e-127 |
|
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: 377.93 E-value: 1.86e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVN 85
Cdd:COG1012 26 INPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFATQGPAfLQPKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAA 165
Cdd:COG1012 106 RAADFLRYYAGEARR-LYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 166 QAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDAD 244
Cdd:COG1012 185 LLLAELLEEAGLPAGVLNVVTGDGSEVgAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 245 IDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVA 324
Cdd:COG1012 265 LDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 325 GGSKILYGNLNVDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQ 404
Cdd:COG1012 345 EGAELLTGGRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARR 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1140776579 405 LATKIETGQVAINQV-LDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:COG1012 425 VARRLEAGMVWINDGtTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTV 475
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
6-454 |
4.97e-126 |
|
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: 373.40 E-value: 4.97e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVN 85
Cdd:pfam00171 12 INPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFATQGpaflqpKNYDKLSVGSTAHVEFSS----IGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIV 161
Cdd:pfam00171 92 RAIDVLRYYAGLA------RRLDGETLPSDPGRLAYTrrepLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 162 PQAAQAFEKACQKVGIPEGAFaNIFATHDQI--DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAV 239
Cdd:pfam00171 166 PLTALLLAELFEEAGLPAGVL-NVVTGSGAEvgEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 240 LDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQV 319
Cdd:pfam00171 245 LEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 320 EKVVAGGSKILYGNlNVDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADV 399
Cdd:pfam00171 325 EDAKEEGAKLLTGG-EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDL 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1140776579 400 KHGNQLATKIETGQVAINQVLDEQAE-VPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:pfam00171 404 ERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
6-454 |
1.48e-117 |
|
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: 351.73 E-value: 1.48e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVN 85
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFATQGPaflqpKNYDKLSVGSTAHVEFSS----IGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIV 161
Cdd:cd07103 82 YAASFLEWFAEEAR-----RIYGRTIPSPAPGKRILVikqpVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 162 PQAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVL 240
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 241 DDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVE 320
Cdd:cd07103 237 DDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 321 KVVAGGSKILYGNlNVDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVK 400
Cdd:cd07103 317 DAVAKGAKVLTGG-KRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1140776579 401 HGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
26-455 |
1.59e-116 |
|
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: 348.43 E-value: 1.59e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 26 EDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNKIVNYARYFATQGPAFLQPK 105
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 106 NYDKLSvGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQAFEKACQKVGIPEGAFANI 185
Cdd:cd07078 81 IPSPDP-GELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 186 FATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVC 264
Cdd:cd07078 160 TGDGDEVgAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 265 TAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEGPGFQF 344
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGYFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 345 SPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLD-EQ 423
Cdd:cd07078 320 PPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAE 399
|
410 420 430
....*....|....*....|....*....|..
gi 1140776579 424 AEVPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:cd07078 400 PSAPFGGVKQSGIGREGGPYGLEEYTEPKTVT 431
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
7-454 |
1.38e-106 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 324.12 E-value: 1.38e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNK 86
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 87 IVNYARYFATQGPAFLQPKnyDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQ 166
Cdd:PRK13968 93 SANLCDWYAEHGPAMLKAE--PTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 167 AFEKACQKVGIPEGAFANIFATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADID 246
Cdd:PRK13968 171 LIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 247 KAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVAGG 326
Cdd:PRK13968 251 LAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 327 SKILYGNLNVdEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLA 406
Cdd:PRK13968 331 ARLLLGGEKI-AGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMA 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1140776579 407 TKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:PRK13968 410 ARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
6-454 |
5.79e-98 |
|
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: 301.88 E-value: 5.79e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYyQKA-KRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEV 84
Cdd:cd07088 18 LNPATGEVVATVPAATAEDADRAVDAAEAA-QKAwERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 85 NKIVNYARYFATQGPAF----LQPKNydklsVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASI 160
Cdd:cd07088 97 EFTADYIDYMAEWARRIegeiIPSDR-----PNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 161 VPQAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAV 239
Cdd:cd07088 172 TPLNALEFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 240 LDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQV 319
Cdd:cd07088 252 MKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 320 EKVVAGGSKILYGNLNVDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADV 399
Cdd:cd07088 332 ERAVEAGATLLTGGKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENL 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1140776579 400 KHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07088 412 NTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
7-454 |
2.02e-97 |
|
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: 300.03 E-value: 2.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNK 86
Cdd:cd07145 5 NPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 87 IVNYARYFATQGP----AFLQPKNYDKLSVGsTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVP 162
Cdd:cd07145 85 TIRLFKLAAEEAKvlrgETIPVDAYEYNERR-IAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 163 QAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLD 241
Cdd:cd07145 164 LTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 242 DADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEK 321
Cdd:cd07145 244 DADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVND 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 322 VVAGGSKILYGNLNVDegpGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKH 401
Cdd:cd07145 324 AVEKGGKILYGGKRDE---GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1140776579 402 GNQLATKIETGQVAIN-QVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07145 401 ALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
6-454 |
3.28e-93 |
|
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: 289.04 E-value: 3.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVN 85
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFATQGpafLQPKNYDKlsvGSTAHVE--FSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQ 163
Cdd:cd07106 82 GAVAWLRYTASLD---LPDEVIED---DDTRRVElrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 164 AAQAFEKACQKVgIPEGAFaNI----------FATHDQIDKIiddprvqgfALTGSEQAGSNLAAKATKNLMKTTLELGG 233
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVL-NVvsggdelgpaLTSHPDIRKI---------SFTGSTATGKKVMASAAKTLKRVTLELGG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 234 TDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKE 313
Cdd:cd07106 225 NDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 314 KLQEQVEKVVAGGSKILYGNlNVDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGA 393
Cdd:cd07106 305 KVKELVEDAKAKGAKVLAGG-EPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGAS 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1140776579 394 IYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07106 384 VWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
6-454 |
6.05e-90 |
|
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: 280.76 E-value: 6.05e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLsstnmgkLIGESRTEVN 85
Cdd:cd07150 4 LNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDL-------LIDEGGSTYG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KivnyARYFATQGPAFL-----QPKNYDKLSVGSTAHVEFSSI-----GIVLAVEPWNFPFTQVMRVFAPNFILGNPVIL 155
Cdd:cd07150 77 K----AWFETTFTPELLraaagECRRVRGETLPSDSPGTVSMSvrrplGVVAGITPFNYPLILATKKVAFALAAGNTVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 156 KHASIVPQAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGT 234
Cdd:cd07150 153 KPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 235 DIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEK 314
Cdd:cd07150 233 NPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 315 LQEQVEKVVAGGSKILYGNLNvdEGPGFQfsPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAI 394
Cdd:cd07150 313 IKRQVEDAVAKGAKLLTGGKY--DGNFYQ--PTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAI 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1140776579 395 YTADVKHGNQLATKIETGQVAINQV-LDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07150 389 LTNDLQRAFKLAERLESGMVHINDPtILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
7-448 |
1.14e-89 |
|
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: 279.90 E-value: 1.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNK 86
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 87 IVNYARYFATQGPAFLQPK---NYDKLsvgsTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQ 163
Cdd:cd07102 82 MLERARYMISIAEEALADIrvpEKDGF----ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 164 AAQAFEKACQKVGIPEGAFANIFATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDA 243
Cdd:cd07102 158 CGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 244 DIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVV 323
Cdd:cd07102 238 DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 324 AGGSKILYG--NLNVDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKH 401
Cdd:cd07102 318 AKGARALIDgaLFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIAR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1140776579 402 GNQLATKIETGQVAINQ--VLDeqAEVPFGGVKSSGYGRELSDWGIYEF 448
Cdd:cd07102 398 AEALGEQLETGTVFMNRcdYLD--PALAWTGVKDSGRGVTLSRLGYDQL 444
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
7-455 |
4.03e-89 |
|
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: 278.44 E-value: 4.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRT-EVN 85
Cdd:cd07092 3 DPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFA-----TQGPAflqPKNYDKlsvGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASI 160
Cdd:cd07092 83 GAVDNFRFFAgaartLEGPA---AGEYLP---GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 161 VPQAAQAFEKACQKVgIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAV 239
Cdd:cd07092 157 TPLTTLLLAELAAEV-LPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 240 LDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQV 319
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 320 E------KVVAGGSKIlygnlnvdEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGA 393
Cdd:cd07092 316 ErapahaRVLTGGRRA--------EGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1140776579 394 IYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVM 449
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
7-454 |
6.46e-89 |
|
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: 278.28 E-value: 6.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKA-ESYYQKA-KRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEV 84
Cdd:cd07114 3 NPATGEPWARVPEASAADVDRAVAAArAAFEGGAwRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 85 NKIVNYARYFAtqGPAflqpknyDKLSvGSTAHVEFSS---------IGIVLAVEPWNFPFTQVMRVFAPNFILGNPVIL 155
Cdd:cd07114 83 RYLAEWYRYYA--GLA-------DKIE-GAVIPVDKGDylnftrrepLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 156 KHASIVPQAAQAFEKACQKVGIPEGAFaNI-----------FATHDQIDKIiddprvqgfALTGSEQAGSNLAAKATKNL 224
Cdd:cd07114 153 KPSEHTPASTLELAKLAEEAGFPPGVV-NVvtgfgpetgeaLVEHPLVAKI---------AFTGGTETGRHIARAAAENL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 225 MKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLA 304
Cdd:cd07114 223 APVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 305 PLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEGP---GFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIK 381
Cdd:cd07114 303 PLATERQLEKVERYVARAREEGARVLTGGERPSGADlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIA 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1140776579 382 MANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07114 383 LANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-454 |
7.63e-87 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 274.26 E-value: 7.63e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNK 86
Cdd:PLN02278 46 NPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 87 IVNYARYFATQGP---AFLQPKNYDKLSVgstaHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQ 163
Cdd:PLN02278 126 GASFLEYFAEEAKrvyGDIIPSPFPDRRL----LVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 164 AAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDD 242
Cdd:PLN02278 202 TALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDD 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 243 ADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKV 322
Cdd:PLN02278 282 ADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 323 VAGGSKILYGNLNVDEGPGFqFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHG 402
Cdd:PLN02278 362 VSKGAKVLLGGKRHSLGGTF-YEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRA 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1140776579 403 NQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:PLN02278 441 WRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
30-455 |
1.46e-86 |
|
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: 269.10 E-value: 1.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 30 DKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNKIVNYARYFATQGPAFLQPKNYDK 109
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 110 LSvGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQAFEKACQKVGIPEGAFANIFATH 189
Cdd:cd06534 81 DP-GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 190 DQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAK 268
Cdd:cd06534 160 DEVgAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 269 RYLVSDKIYDEFLDKVKrefdtyqpgnplneettlaplssqsakeklqeqvekvvaggskilygnlnvdegpgfqfspII 348
Cdd:cd06534 240 RLLVHESIYDEFVEKLV-------------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 349 LTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLD-EQAEVP 427
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAP 338
|
410 420
....*....|....*....|....*...
gi 1140776579 428 FGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLEEYTRTKTVV 366
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
44-448 |
1.70e-86 |
|
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: 270.94 E-value: 1.70e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 44 FAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNKIVNYARYFATQGPAF---LQPKNYDklsvGSTAHVEF 120
Cdd:cd07104 21 PQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPegeILPSDVP----GKESMVRR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 121 SSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVP-----QAAQAFEKAcqkvGIPEGAFaNIFATH-DQI-D 193
Cdd:cd07104 97 VPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIAEIFEEA----GLPKGVL-NVVPGGgSEIgD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 194 KIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVS 273
Cdd:cd07104 172 ALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 274 DKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNlnvdEGPGFQFSPIILTGME 353
Cdd:cd07104 252 ESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG----TYEGLFYQPTVLSDVT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 354 RNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQ--VLDEqAEVPFGGV 431
Cdd:cd07104 328 PDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDqtVNDE-PHVPFGGV 406
|
410
....*....|....*..
gi 1140776579 432 KSSGYGRELSDWGIYEF 448
Cdd:cd07104 407 KASGGGRFGGPASLEEF 423
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
3-454 |
2.32e-85 |
|
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: 269.46 E-value: 2.32e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKA--KRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGES 80
Cdd:cd07091 21 FPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGwwRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 81 -RTEVNKIVNYARYFAtqGPAflqpknyDKLSvGSTahVEFSS----------IGIVLAVEPWNFPFTQVMRVFAPNFIL 149
Cdd:cd07091 101 aKGDVALSIKCLRYYA--GWA-------DKIQ-GKT--IPIDGnflaytrrepIGVCGQIIPWNFPLLMLAWKLAPALAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 150 GNPVILKHASIVPQAAQAFEKACQKVGIPEGAFaNI-----------FATHDQIDKIiddprvqgfALTGSEQAGSNLAA 218
Cdd:cd07091 169 GNTVVLKPAEQTPLSALYLAELIKEAGFPPGVV-NIvpgfgptagaaISSHMDVDKI---------AFTGSTAVGRTIME 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 219 KATK-NLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPL 297
Cdd:cd07091 239 AAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 298 NEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDeGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSED 377
Cdd:cd07091 319 DPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHG-SKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1140776579 378 EMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07091 398 EVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
3-454 |
6.26e-83 |
|
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: 262.68 E-value: 6.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDfakRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRT 82
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALAASYRSTLTRYQ---RSAILNKAAALLEARREEFARLITLESGLCLKDTRY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 83 EVNKIVNYARYFATQ-----GPAFLQPknydkLSVGSTAHVEFS---SIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVI 154
Cdd:cd07146 78 EVGRAADVLRFAAAEalrddGESFSCD-----LTANGKARKIFTlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 155 LKHASIVPQAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKAtkNLMKTTLELGG 233
Cdd:cd07146 153 LKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIgDELITHPDVDLVTFTGGVAVGKAIAATA--GYKRQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 234 TDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKE 313
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 314 KLQEQVEKVVAGGSKILYGNlnvdEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGA 393
Cdd:cd07146 311 QIENRVEEAIAQGARVLLGN----QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSG 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1140776579 394 IYTADVKHGNQLATKIETGQVAINQVLDEQAE-VPFGGVKSSGYG-RELSDWGIYEFANIKTV 454
Cdd:cd07146 387 VCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
7-454 |
2.26e-82 |
|
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: 261.41 E-value: 2.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKA-ESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRT-EV 84
Cdd:cd07089 3 NPATEEVIGTAPDAGAADVDAAIAAArRAFDTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAmQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 85 NKIVNYARYFATQGPAFLQPKNYD---KLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIV 161
Cdd:cd07089 83 DGPIGHLRYFADLADSFPWEFDLPvpaLRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 162 PQAAQAFEKACQKVGIPEGAFaNIFATHDQI--DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAV 239
Cdd:cd07089 163 PLSALLLGEIIAETDLPAGVV-NVVTGSDNAvgEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 240 LDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQV 319
Cdd:cd07089 242 LDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 320 EKVVAGGSKILYGNLNVDEGP-GFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTAD 398
Cdd:cd07089 322 ARGRDEGARLVTGGGRPAGLDkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSAD 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1140776579 399 VKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07089 402 VDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
6-454 |
5.48e-82 |
|
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: 260.22 E-value: 5.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVN 85
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYF---ATQGPAFLQPKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVP 162
Cdd:cd07149 84 RAIETLRLSaeeAKRLAGETIPFDASPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 163 QAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKAtkNLMKTTLELGGTDIFAVLD 241
Cdd:cd07149 164 LSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKA--GLKKVTLELGSNAAVIVDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 242 DADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEK 321
Cdd:cd07149 242 DADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 322 VVAGGSKILYGNLNVdegpGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKH 401
Cdd:cd07149 322 AVEGGARLLTGGKRD----GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQK 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1140776579 402 GNQLATKIETGQVAINQVLDEQAEV-PFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07149 398 ALKAARELEVGGVMINDSSTFRVDHmPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
3-454 |
5.64e-82 |
|
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: 260.70 E-value: 5.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRT 82
Cdd:cd07151 12 IDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 83 EVNKIVNYARYFATQgPAFLQPKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVP 162
Cdd:cd07151 92 EWGAAMAITREAATF-PLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 163 QA-----AQAFEKAcqkvGIPEGAFaNIFATHdqIDKIIDD------PRVQGFalTGSEQAGSNLAAKATKNLMKTTLEL 231
Cdd:cd07151 171 ITgglllAKIFEEA----GLPKGVL-NVVVGA--GSEIGDAfvehpvPRLISF--TGSTPVGRHIGELAGRHLKKVALEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 232 GGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSA 311
Cdd:cd07151 242 GGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 312 KEKLQEQVEKVVAGGSKILYGnlnvdeGP--GFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHG 389
Cdd:cd07151 322 VDGLLDKIEQAVEEGATLLVG------GEaeGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1140776579 390 LGGAIYTADVKHGNQLATKIETGQVAIN-QVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07151 396 LSGAVFTSDLERGVQFARRIDAGMTHINdQPVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
6-455 |
9.49e-82 |
|
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: 259.46 E-value: 9.49e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYyQKA-KRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEV 84
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAA-QRAwAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 85 NKIVNYARYFATQGPAFLQPK--NYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVP 162
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRkvPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 163 QAAQAFEKACQKVGIPEGAFANIF-------ATHDQ-IDKIiddprvqgfALTGSEQAGSNLAAKATKNLMKTTLELGGT 234
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTgdgatgaALIDAgVDKV---------AFTGSVATGRKVMAAAAERLIPVVLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 235 DIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEK 314
Cdd:cd07099 231 DPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 315 LQEQVEKVVAGGSKILYGNLNVDEGPGFqFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAI 394
Cdd:cd07099 311 VRRHVDDAVAKGAKALTGGARSNGGGPF-YEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1140776579 395 YTADVKHGNQLATKIETGQVAINQVLDE--QAEVPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:cd07099 390 FSRDLARAEAIARRLEAGAVSINDVLLTagIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
24-454 |
1.85e-81 |
|
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: 258.28 E-value: 1.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 24 EIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLsstnMGKLIGESRTEVNKIVNYA----RYFA---T 96
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEA----MMEETGATAAWAGFNVDLAagmlREAAsliT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 97 QGPAFLQPKNYDklsvGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQAFEKACQKVG 176
Cdd:cd07105 77 QIIGGSIPSDKP----GTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 177 IPEGAFANIFA----THDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDA 252
Cdd:cd07105 153 LPKGVLNVVTHspedAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 253 AQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNplneeTTLAPLSSQSAKEKLQEQVEKVVAGGSKILYG 332
Cdd:cd07105 233 LFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 333 NLNVDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETG 412
Cdd:cd07105 308 GLADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1140776579 413 QVAIN--QVLDEqAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07105 388 AVHINgmTVHDE-PTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
7-455 |
7.13e-81 |
|
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: 258.01 E-value: 7.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKA--KRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEV 84
Cdd:cd07119 19 NPANGEVIATVPEGTAEDAKRAIAAARRAFDSGewPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 85 NKIVNYARYFATqgpafLQPKNYDKLsVGSTAHVEFSS----IGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASI 160
Cdd:cd07119 99 DDVANCFRYYAG-----LATKETGEV-YDVPPHVISRTvrepVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 161 VPQAAQAFEKACQKVGIPEGAF----------ANIFATHDQIDKIiddprvqgfALTGSEQAGSNLAAKATKNLMKTTLE 230
Cdd:cd07119 173 TPLTTIALFELIEEAGLPAGVVnlvtgsgatvGAELAESPDVDLV---------SFTGGTATGRSIMRAAAGNVKKVALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 231 LGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQS 310
Cdd:cd07119 244 LGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 311 AKEKLQEQVEKVVAGGSKILYGNLNVDEGP---GFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSR 387
Cdd:cd07119 324 HREKVLSYIQLGKEEGARLVCGGKRPTGDElakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTP 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1140776579 388 HGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:cd07119 404 YGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHIN 471
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
41-455 |
2.72e-80 |
|
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: 256.35 E-value: 2.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 41 RVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRT-EVNKIVNYARYFATQGPAF----LQPKnydklSVGST 115
Cdd:cd07139 56 RLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRaQGPGPAALLRYYAALARDFpfeeRRPG-----SGGGH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 116 AHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQAFEKACQKVGIPEGAFaNIFA-------- 187
Cdd:cd07139 131 VLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVV-NVVPadrevgey 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 188 --THDQIDKIiddprvqgfALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCT 265
Cdd:cd07139 210 lvRHPGVDKV---------SFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 266 AAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDE-GPGFQF 344
Cdd:cd07139 281 ALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGlDRGWFV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 345 SPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQ-VLDEQ 423
Cdd:cd07139 361 EPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGfRLDFG 440
|
410 420 430
....*....|....*....|....*....|..
gi 1140776579 424 AevPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:cd07139 441 A--PFGGFKQSGIGREGGPEGLDAYLETKSIY 470
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
6-454 |
1.28e-79 |
|
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: 255.02 E-value: 1.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKR-VDFAKRADLLNRLAGEFEANLEDYARLSSTNMGK-LIGESRTE 83
Cdd:cd07144 28 VNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSkVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKpYHSNALGD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 84 VNKIVNYARYFAtqGPAflqpknyDKLS--VGSTAHVEFS-----SIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILK 156
Cdd:cd07144 108 LDEIIAVIRYYA--GWA-------DKIQgkTIPTSPNKLAytlhePYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 157 HASIVPQAAQAFEKACQKVGIPEGAFaNIF-----------ATHDQIDKIiddprvqgfALTGSEQAGSNLAAKATKNLM 225
Cdd:cd07144 179 PAENTPLSLLYFANLVKEAGFPPGVV-NIIpgygavagsalAEHPDVDKI---------AFTGSTATGRLVMKAAAQNLK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 226 KTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREF-DTYQPGNPLNEETTLA 304
Cdd:cd07144 249 AVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 305 PLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEGP--GFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKM 382
Cdd:cd07144 329 PQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKK 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1140776579 383 ANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07144 409 ANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
6-455 |
1.73e-79 |
|
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: 254.29 E-value: 1.73e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKR-VDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRT-E 83
Cdd:cd07113 20 TNPATEQVIASVASATEADVDAAVASAWRAFVSAWAkTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 84 VNKIVNYARYFA---------TQGPAF--LQPKNYdklsvgsTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNP 152
Cdd:cd07113 100 VGQSANFLRYFAgwatkingeTLAPSIpsMQGERY-------TAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 153 VILKHASIVPQAAQAFEKACQKVGIPEGAFANIFATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELG 232
Cdd:cd07113 173 IVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 233 GTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAK 312
Cdd:cd07113 253 GKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 313 EKLQEQVEKVVAGGSKILYGNLNVDeGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGG 392
Cdd:cd07113 333 DKVCSYLDDARAEGDEIVRGGEALA-GEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTA 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1140776579 393 AIYTADVKHGNQLATKIETGQVAINQ--VLDeqAEVPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:cd07113 412 SVWTNNLSKALRYIPRIEAGTVWVNMhtFLD--PAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
7-454 |
3.01e-79 |
|
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: 253.26 E-value: 3.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRT-EVN 85
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrDIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFA-----TQGPAFLQPKNYdklsvgsTAHVEFSSIGIVLAVEPWNFPFTQV-MRVfAPNFILGNPVILKHAS 159
Cdd:cd07093 83 RAAANFRFFAdyilqLDGESYPQDGGA-------LNYVLRQPVGVAGLITPWNLPLMLLtWKI-APALAFGNTVVLKPSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 160 IVPQAAQAFEKACQKVGIPEGAFANIFAT-HDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFA 238
Cdd:cd07093 155 WTPLTAWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 239 VLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQ 318
Cdd:cd07093 235 VFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 319 VEKVVAGGSKILYGNLNVDEGP---GFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIY 395
Cdd:cd07093 315 VELARAEGATILTGGGRPELPDlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1140776579 396 TADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07093 395 TRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
4-454 |
6.74e-79 |
|
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: 252.35 E-value: 6.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 4 TATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTE 83
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 84 VNKIVNYARYfatqgPAFLQPKNYDK-----LSVGSTAHVEFSS---IGIVLAVEPWNFPFTQVMRVFAPNFILGNPVIL 155
Cdd:cd07094 82 VDRAIDTLRL-----AAEEAERIRGEeipldATQGSDNRLAWTIrepVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 156 KHASIVPQAAQAFEKACQKVGIPEGAFaNIF--ATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNlmKTTLELGG 233
Cdd:cd07094 157 KPASKTPLSALELAKILVEAGVPEGVL-QVVtgEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGK--RIALELGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 234 TDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKE 313
Cdd:cd07094 234 NAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 314 KLQEQVEKVVAGGSKILYGNlnvdEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGA 393
Cdd:cd07094 314 RVERWVEEAVEAGARLLCGG----ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1140776579 394 IYTADVKHGNQLATKIETGQVAINQVLDEQAE-VPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07094 390 IFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDwMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
7-454 |
5.89e-78 |
|
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: 250.24 E-value: 5.89e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYN-GEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVN 85
Cdd:cd07097 20 NPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFAtqGPAF-LQPKNYDklSVGSTAHVEFS--SIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVP 162
Cdd:cd07097 100 RAGQIFRYYA--GEALrLSGETLP--STRPGVEVETTrePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 163 QAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLD 241
Cdd:cd07097 176 ASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 242 DADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEK 321
Cdd:cd07097 256 DADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 322 VVAGGSKILYGNLNVDEG-PGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVK 400
Cdd:cd07097 336 ARSEGAKLVYGGERLKRPdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLK 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1140776579 401 HGNQLATKIETGQVAINQV---LDEQaeVPFGGVKSSGYG-RELSDWGIYEFANIKTV 454
Cdd:cd07097 416 HATHFKRRVEAGVVMVNLPtagVDYH--VPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
7-454 |
1.02e-77 |
|
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: 249.28 E-value: 1.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESR-TEVN 85
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFAtqGPAflqpknyDKLSvGSTAHVEFSS--------IGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKH 157
Cdd:cd07115 83 RAADTFRYYA--GWA-------DKIE-GEVIPVRGPFlnytvrepVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 158 ASIVPQAAQAFEKACQKVGIPEGAFaNIFATHDQI--DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTD 235
Cdd:cd07115 153 AELTPLSALRIAELMAEAGFPAGVL-NVVTGFGEVagAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 236 IFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKL 315
Cdd:cd07115 232 ANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 316 QEQVEKVVAGGSKILYGNLNVDEgPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIY 395
Cdd:cd07115 312 LDYVDVGREEGARLLTGGKRPGA-RGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVW 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1140776579 396 TADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07115 391 TRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
7-455 |
1.64e-77 |
|
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: 248.81 E-value: 1.64e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNK 86
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 87 IVNYARYFATQ--GPAFLQPKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFtqVMRVF--APNFILGNPVILKHASIVP 162
Cdd:cd07110 83 VAGCFEYYADLaeQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPL--LMAAWkvAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 163 QAAQAFEKACQKVGIPEGAFaNI-----------FATHDQIDKIiddprvqgfALTGSEQAGSNLAAKATKNLMKTTLEL 231
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVL-NVvtgtgdeagapLAAHPGIDKI---------SFTGSTATGSQVMQAAAQDIKPVSLEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 232 GGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSA 311
Cdd:cd07110 231 GGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 312 KEKLQEQVEKVVAGGSKILY-GNLNVDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGL 390
Cdd:cd07110 311 YEKVLSFIARGKEEGARLLCgGRRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1140776579 391 GGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:cd07110 391 AAAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
3-454 |
2.18e-77 |
|
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: 248.67 E-value: 2.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAK--RVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGES 80
Cdd:cd07112 4 FATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVwsRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 81 RT-EVNKIVNYARYFATqgpafLQPKNYDKL---SVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILK 156
Cdd:cd07112 84 LAvDVPSAANTFRWYAE-----AIDKVYGEVaptGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 157 HASIVPQAAQAFEKACQKVGIPEGAFaNI-----------FATHDQIDKIiddprvqgfALTGSEQAGSN-LAAKATKNL 224
Cdd:cd07112 159 PAEQSPLTALRLAELALEAGLPAGVL-NVvpgfghtageaLGLHMDVDAL---------AFTGSTEVGRRfLEYSGQSNL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 225 MKTTLELGGTDIFAVLDDA-DIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTL 303
Cdd:cd07112 229 KRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 304 APLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVD-EGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKM 382
Cdd:cd07112 309 GALVSEAHFDKVLGYIESGKAEGARLVAGGKRVLtETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVAL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1140776579 383 ANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07112 389 ANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
6-439 |
1.22e-76 |
|
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: 246.98 E-value: 1.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRT-EV 84
Cdd:cd07117 21 YNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 85 NKIVNYARYFAT---QGPAFLQPKNYDKLSVgstahVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIV 161
Cdd:cd07117 101 PLAADHFRYFAGvirAEEGSANMIDEDTLSI-----VLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 162 PQAAQAFEKACQKVgIPEGAF----------ANIFATHDQIDKIiddprvqgfALTGSEQAGSNLAAKATKNLMKTTLEL 231
Cdd:cd07117 176 SLSLLELAKIIQDV-LPKGVVnivtgkgsksGEYLLNHPGLDKL---------AFTGSTEVGRDVAIAAAKKLIPATLEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 232 GGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSA 311
Cdd:cd07117 246 GGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 312 KEKLQEQVEKVVAGGSKILYGNLNVDEGP---GFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRH 388
Cdd:cd07117 326 LDKILSYVDIAKEEGAKILTGGHRLTENGldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEY 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1140776579 389 GLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRE 439
Cdd:cd07117 406 GLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRE 456
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
7-455 |
1.34e-76 |
|
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: 246.65 E-value: 1.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKA----ESYYQKAKrvdfAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRt 82
Cdd:cd07138 20 NPATEEVIGTVPLGTAADVDRAVAAArrafPAWSATSV----EERAALLERIAEAYEARADELAQAITLEMGAPITLAR- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 83 evnkivnyaryfATQGPAFLQ--------PKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVI 154
Cdd:cd07138 95 ------------AAQVGLGIGhlraaadaLKDFEFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 155 LKHASIVPQAAQAFEKACQKVGIPEGAFaNI-----------FATHDQIDKIiddprvqgfALTGSEQAGSNLAAKATKN 223
Cdd:cd07138 163 LKPSEVAPLSAIILAEILDEAGLPAGVF-NLvngdgpvvgeaLSAHPDVDMV---------SFTGSTRAGKRVAEAAADT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 224 LMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTL 303
Cdd:cd07138 233 VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 304 APLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEGP--GFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIK 381
Cdd:cd07138 313 GPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEGLerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1140776579 382 MANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQV-LDEQAevPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:cd07138 393 IANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAaFNPGA--PFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
2-455 |
6.12e-76 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 245.20 E-value: 6.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 2 AYTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESR 81
Cdd:PRK13473 18 KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 82 T-EVNKIVNYARYFAtqGPA-FLQPKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFtqVMRV--FAPNFILGNPVILKH 157
Cdd:PRK13473 98 NdEIPAIVDVFRFFA--GAArCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPL--MMAAwkLAPALAAGNTVVLKP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 158 ASIVPQAAQAFEKACQKVgIPEGAFaNIFATHDQI--DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTD 235
Cdd:PRK13473 174 SEITPLTALKLAELAADI-LPPGVL-NVVTGRGATvgDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 236 IFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKL 315
Cdd:PRK13473 252 PVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 316 QEQVE--------KVVAGGSKIlygnlnvdEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSR 387
Cdd:PRK13473 332 AGFVErakalghiRVVTGGEAP--------DGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSD 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1140776579 388 HGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:PRK13473 404 YGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVM 471
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
6-439 |
9.87e-76 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 244.95 E-value: 9.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRT-EV 84
Cdd:cd07559 21 YNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLAaDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 85 NKIVNYARYFAtqGPAFLQPKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQA 164
Cdd:cd07559 101 PLAIDHFRYFA--GVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 165 AQAFEKACQKVgIPEGAFaNI-----------FATHDQIDKIiddprvqgfALTGSEQAGSNLAAKATKNLMKTTLELGG 233
Cdd:cd07559 179 ILVLMELIGDL-LPKGVV-NVvtgfgseagkpLASHPRIAKL---------AFTGSTTVGRLIMQYAAENLIPVTLELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 234 --TDIF---AVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSS 308
Cdd:cd07559 248 ksPNIFfddAMDADDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 309 QSAKEKLQEQVEKVVAGGSKILYG----NLNVDEGPGFQFSPIILTGmerNNPM--YDEELFGPVAQIYRFSSEDEMIKM 382
Cdd:cd07559 328 KDQLEKILSYVDIGKEEGAEVLTGgerlTLGGLDKGYFYEPTLIKGG---NNDMriFQEEIFGPVLAVITFKDEEEAIAI 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1140776579 383 ANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRE 439
Cdd:cd07559 405 ANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRE 461
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
7-439 |
1.19e-75 |
|
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: 244.40 E-value: 1.19e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQK-AKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVN 85
Cdd:cd07082 22 SPIDGEVIGSVPALSALEILEAAETAYDAGRGwWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFATQGpaflqpKNYDKLSV---------GSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILK 156
Cdd:cd07082 102 RTIDYIRDTIEEL------KRLDGDSLpgdwfpgtkGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 157 HASIVPQAAQAFEKACQKVGIPEGAFANIFAT-HDQIDKIIDDPRVQGFALTGSEQAGSNLAAKA-TKNLMkttLELGGT 234
Cdd:cd07082 176 PATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHpMKRLV---LELGGK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 235 DIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEK 314
Cdd:cd07082 253 DPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 315 LQEQVEKVVAGGSKILYGnlNVDEGPGFqFSPIIL----TGMErnnpMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGL 390
Cdd:cd07082 333 VEGLIDDAVAKGATVLNG--GGREGGNL-IYPTLLdpvtPDMR----LAWEEPFGPVLPIIRVNDIEEAIELANKSNYGL 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1140776579 391 GGAIYTADVKHGNQLATKIETGQVAINqvldEQAE-----VPFGGVKSSGYGRE 439
Cdd:cd07082 406 QASIFTKDINKARKLADALEVGTVNIN----SKCQrgpdhFPFLGRKDSGIGTQ 455
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
6-452 |
3.47e-75 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 243.28 E-value: 3.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVN 85
Cdd:PRK11241 31 TNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFATQGPaflqpKNYDKLSVGSTAH----VEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIV 161
Cdd:PRK11241 111 YAASFIEWFAEEGK-----RIYGDTIPGHQADkrliVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 162 PQAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVL 240
Cdd:PRK11241 186 PFSALALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 241 DDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVE 320
Cdd:PRK11241 266 DDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 321 KVVAGGSKILYGNLNVDEGPGFqFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVK 400
Cdd:PRK11241 346 DALEKGARVVCGGKAHELGGNF-FQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLS 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1140776579 401 HGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIK 452
Cdd:PRK11241 425 RVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
6-439 |
6.06e-74 |
|
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: 239.07 E-value: 6.06e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVN 85
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFATQGPAF---LQPKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVP 162
Cdd:cd07147 84 RAIDTFRIAAEEATRIygeVLPLDISARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 163 QAAQAFEKACQKVGIPEGAFANIFATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNlmKTTLELGGTDIFAVLDD 242
Cdd:cd07147 164 LSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 243 ADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKV 322
Cdd:cd07147 242 ADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 323 VAGGSKILYGNLNvdEGPGFQfsPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHG 402
Cdd:cd07147 322 VDAGAKLLTGGKR--DGALLE--PTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKA 397
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1140776579 403 NQLATKIETGQVAINQV----LDEQaevPFGGVKSSGYGRE 439
Cdd:cd07147 398 LRAWDELEVGGVVINDVptfrVDHM---PYGGVKDSGIGRE 435
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
6-455 |
1.24e-72 |
|
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: 236.10 E-value: 1.24e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLI-GESRTEV 84
Cdd:cd07108 2 INPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 85 NKIVNYARYFATQGPAF---LQPKNYDKLSVGSTahvefSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIV 161
Cdd:cd07108 82 AVLADLFRYFGGLAGELkgeTLPFGPDVLTYTVR-----EPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 162 PQAAQAFEKACQKVgIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVL 240
Cdd:cd07108 157 PLAVLLLAEILAQV-LPAGVLNVITGYGEECgAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 241 DDADIDKAAKDA-AQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEK----- 314
Cdd:cd07108 236 PDADLDDAVDGAiAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKvcgyi 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 315 ---LQEQVEKVVAGGSKILYGNLnvdeGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLG 391
Cdd:cd07108 316 dlgLSTSGATVLRGGPLPGEGPL----ADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1140776579 392 GAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYE-FANIKTVL 455
Cdd:cd07108 392 AYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMLEhFTQKKTVN 456
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
7-454 |
1.32e-72 |
|
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: 235.70 E-value: 1.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKA-ESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVN 85
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAArRAFDETDWAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFA-----TQGPAF-LQPKNYdklsvgSTAHVEfsSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHAS 159
Cdd:cd07120 83 GAISELRYYAglartEAGRMIePEPGSF------SLVLRE--PMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 160 IVPQAAQAFEKACQKV-GIPEGAfANIFA--THDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDI 236
Cdd:cd07120 155 QTAQINAAIIRILAEIpSLPAGV-VNLFTesGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 237 FAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQ 316
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 317 EQVEKVVAGGSKILYGNLNVDEG--PGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAI 394
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 395 YTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07120 394 WTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
2-454 |
4.97e-72 |
|
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: 235.12 E-value: 4.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 2 AYTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDF--AKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGE 79
Cdd:cd07143 23 TVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVsgSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 80 -SRTEVNKIVNYARYFAtqGPAflqPKNYDKL---SVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVIL 155
Cdd:cd07143 103 aKRVDVQASADTFRYYG--GWA---DKIHGQVietDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 156 KHASIVPQAAQAFEKACQKVGIPEGAF----------ANIFATHDQIDKIiddprvqgfALTGSEQAGSN-LAAKATKNL 224
Cdd:cd07143 178 KPSELTPLSALYMTKLIPEAGFPPGVInvvsgygrtcGNAISSHMDIDKV---------AFTGSTLVGRKvMEAAAKSNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 225 MKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLA 304
Cdd:cd07143 249 KKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 305 PLSSQSAKEKLQEQVEKVVAGGSKIL-----YGNLnvdegpGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEM 379
Cdd:cd07143 329 PQVSQIQYERIMSYIESGKAEGATVEtggkrHGNE------GYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEA 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1140776579 380 IKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07143 403 IKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
3-454 |
7.99e-72 |
|
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: 234.38 E-value: 7.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRT 82
Cdd:cd07086 15 FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 83 EVNKIVNYARYFATQGPaflQPKnydklsvGSTAHVEFSS---------IGIVLAVEPWNFPftqvMRVF----APNFIL 149
Cdd:cd07086 95 EVQEMIDICDYAVGLSR---MLY-------GLTIPSERPGhrlmeqwnpLGVVGVITAFNFP----VAVPgwnaAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 150 GNPVILKHASIVPQAAQA----FEKACQKVGIPEGAFANIFATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNLM 225
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAvtkiLAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 226 KTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAP 305
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 306 LSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEG-PGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMAN 384
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1140776579 385 DSRHGLGGAIYTADVKHGNQL--ATKIETGQVAINqVLDEQAEV--PFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVN-IPTSGAEIggAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
45-454 |
1.37e-71 |
|
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: 233.38 E-value: 1.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 45 AKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNKIVNYARYFATQGPAfLQPKNYDKLSVGSTAHVEFSSIG 124
Cdd:cd07118 43 AERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLART-LHGDSYNNLGDDMLGLVLREPIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 125 IVLAVEPWNFPFTQVMRVfAPnFIL--GNPVILKHASIVPQAAQAFEKACQKVGIPEGAFaNIFATHDQI--DKIIDDPR 200
Cdd:cd07118 122 VVGIITPWNFPFLILSQK-LP-FALaaGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVV-NIVTGYGATvgQAMTEHPD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 201 VQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEF 280
Cdd:cd07118 199 VDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 281 LDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEGPGFQFSPIILTGMERNNPMYD 360
Cdd:cd07118 279 VAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAR 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 361 EELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGREL 440
Cdd:cd07118 359 EEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGREL 438
|
410
....*....|....
gi 1140776579 441 SDWGIYEFANIKTV 454
Cdd:cd07118 439 GRYGVEEYTELKTV 452
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
7-454 |
1.46e-71 |
|
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: 233.28 E-value: 1.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKA-ESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVN 85
Cdd:cd07109 3 DPSTGEVFARIARGGAADVDRAVQAArRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFAT-----QGPAFLQPKNYDKLSV----GSTAHvefssigIVlavePWNFPFTQVMRVFAPNFILGNPVILK 156
Cdd:cd07109 83 AAARYFEYYGGaadklHGETIPLGPGYFVYTVrephGVTGH-------II----PWNYPLQITGRSVAPALAAGNAVVVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 157 HASIVPQAAQAFEKACQKVGIPEGAFaNI-----------FATHDQIDKIiddprvqgfALTGSEQAGSNLAAKATKNLM 225
Cdd:cd07109 152 PAEDAPLTALRLAELAEEAGLPAGAL-NVvtglgaeagaaLVAHPGVDHI---------SFTGSVETGIAVMRAAAENVV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 226 KTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLnEETTLAP 305
Cdd:cd07109 222 PVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 306 LSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEGP--GFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMA 383
Cdd:cd07109 301 LISAKQLDRVEGFVARARARGARIVAGGRIAEGAPagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALA 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1140776579 384 NDSRHGLGGAIYTADVKHGNQLATKIETGQVAINqvlDEQA----EVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07109 381 NGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVN---NYGAgggiELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
3-454 |
1.09e-68 |
|
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: 226.46 E-value: 1.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYNG-EVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESR 81
Cdd:cd07131 16 FDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 82 TEVNKIVNYARYFATQG------------P-----AFLQPknydklsvgstahvefssIGIVLAVEPWNFPFTQVMRVFA 144
Cdd:cd07131 96 GDVQEAIDMAQYAAGEGrrlfgetvpselPnkdamTRRQP------------------IGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 145 PNFILGNPVILKHASIVPQAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKN 223
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 224 LMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTL 303
Cdd:cd07131 238 NKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 304 APLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEG---PGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMI 380
Cdd:cd07131 318 GPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGgyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1140776579 381 KMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAIN-QVLDEQAEVPFGGVKSSGYG-RELSDWGIYEFANIKTV 454
Cdd:cd07131 398 EIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNaPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
5-454 |
1.98e-68 |
|
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: 224.88 E-value: 1.98e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 5 ATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEV 84
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 85 NKIVNYARYFATQGPAfLQPKNYDkLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQA 164
Cdd:cd07090 81 DSSADCLEYYAGLAPT-LSGEHVP-LPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 165 AQAFEKACQKVGIPEGAF---------ANIFATHDQIDKIiddprvqgfALTGSEQAGSNLAAKATKNLMKTTLELGGTD 235
Cdd:cd07090 159 ALLLAEILTEAGLPDGVFnvvqgggetGQLLCEHPDVAKV---------SFTGSVPTGKKVMSAAAKGIKHVTLELGGKS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 236 IFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKL 315
Cdd:cd07090 230 PLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 316 QEQVEKVVAGGSKILYGNLNVDEGP----GFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLG 391
Cdd:cd07090 310 LGYIESAKQEGAKVLCGGERVVPEDglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLA 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1140776579 392 GAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07090 390 AGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
44-437 |
9.12e-68 |
|
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: 222.94 E-value: 9.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 44 FAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVN---KIVNYARYFATQGPAFLQPKNYDKLSvgstaHVEF 120
Cdd:cd07152 34 PRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGaaiGELHEAAGLPTQPQGEILPSAPGRLS-----LARR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 121 SSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQA-----AQAFEKAcqkvGIPEGAFANIFATHDQIDKI 195
Cdd:cd07152 109 VPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSggvviARLFEEA----GLPAGVLHVLPGGADAGEAL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 196 IDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDK 275
Cdd:cd07152 185 VEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHES 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 276 IYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNlnvdEGPGFQFSPIILTGMERN 355
Cdd:cd07152 265 VADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGG----TYDGLFYRPTVLSGVKPG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 356 NPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAIN-QVLDEQAEVPFGGVKSS 434
Cdd:cd07152 341 MPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINdQTVNDEPHNPFGGMGAS 420
|
...
gi 1140776579 435 GYG 437
Cdd:cd07152 421 GNG 423
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
7-455 |
1.58e-67 |
|
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: 222.95 E-value: 1.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGK-----LIGESR 81
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKtmvdaSLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 82 TEVNKIvnyaRYFATQGPAFLQPknyDKLSVGS-----TAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILK 156
Cdd:cd07098 82 VTCEKI----RWTLKHGEKALRP---ESRPGGLlmfykRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 157 HASIVPQAAQAFEKACQK---------------VGIPEGAfaNIFATHDQIDKIIddprvqgfaLTGSEQAGSNLAAKAT 221
Cdd:cd07098 155 VSEQVAWSSGFFLSIIREclaacghdpdlvqlvTCLPETA--EALTSHPVIDHIT---------FIGSPPVGKKVMAAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 222 KNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEET 301
Cdd:cd07098 224 ESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 302 TLAPLSSQSAKEKLQEQVEKVVAGGSKILYG---NLNVDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDE 378
Cdd:cd07098 304 DVGAMISPARFDRLEELVADAVEKGARLLAGgkrYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 379 MIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAIN--------QVLdeqaevPFGGVKSSGYGRELSDWGIYEFAN 450
Cdd:cd07098 384 AVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfgvnyyvQQL------PFGGVKGSGFGRFAGEEGLRGLCN 457
|
....*
gi 1140776579 451 IKTVL 455
Cdd:cd07098 458 PKSVT 462
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
7-454 |
2.30e-66 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 220.76 E-value: 2.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAK-----RADLLNRLAGEFEANLEDYARLSSTNMGKLIGESR 81
Cdd:PLN02467 29 NPATEETIGDIPAATAEDVDAAVEAARKAFKRNKGKDWARttgavRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 82 TEVNKIVNYARYFATQGPAfLQPKNYDKLSVGST---AHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHA 158
Cdd:PLN02467 109 WDMDDVAGCFEYYADLAEA-LDAKQKAPVSLPMEtfkGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 159 SIVPQAAQAFEKACQKVGIPEGAFaNI-----------FATHDQIDKIiddprvqgfALTGSEQAGSNLAAKATKNLMKT 227
Cdd:PLN02467 188 ELASVTCLELADICREVGLPPGVL-NVvtglgteagapLASHPGVDKI---------AFTGSTATGRKIMTAAAQMVKPV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 228 TLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLS 307
Cdd:PLN02467 258 SLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 308 SQSAKEKLQEQVEKVVAGGSKILYGNlnvDEGP----GFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMA 383
Cdd:PLN02467 338 SEGQYEKVLKFISTAKSEGATILCGG---KRPEhlkkGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1140776579 384 NDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:PLN02467 415 NDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
51-454 |
3.74e-66 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 217.68 E-value: 3.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 51 LNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNKIVNYARYFATQGPAF----LQPknyDKlsVGSTAHVEFSSIGIV 126
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYegeiIQS---DR--PGENILLFKRALGVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 127 LAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFA 205
Cdd:PRK10090 76 TGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 206 LTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVK 285
Cdd:PRK10090 156 MTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 286 REFDTYQPGNPLNEET-TLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNlNVDEGPGFQFSPIILTGMERNNPMYDEELF 364
Cdd:PRK10090 236 EAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGG-KAVEGKGYYYPPTLLLDVRQEMSIMHEETF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 365 GPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWG 444
Cdd:PRK10090 315 GPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHG 394
|
410
....*....|
gi 1140776579 445 IYEFANIKTV 454
Cdd:PRK10090 395 LHEYLQTQVV 404
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
8-454 |
6.04e-66 |
|
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: 218.33 E-value: 6.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 8 PYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNKI 87
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 88 VNYARYFATQGPAFLQP-KNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQ 166
Cdd:cd07101 83 AIVARYYARRAERLLKPrRRRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 167 AFEKACQKVGIPEGAFANIFATHDQI-DKIIDdpRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADI 245
Cdd:cd07101 163 WAVELLIEAGLPRDLWQVVTGPGSEVgGAIVD--NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 246 DKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVAG 325
Cdd:cd07101 241 DKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 326 GSKILYGNLNV-DEGPGFqFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQ 404
Cdd:cd07101 321 GATVLAGGRARpDLGPYF-YEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1140776579 405 LATKIETGQVAINQVLDE---QAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07101 400 IAARLRAGTVNVNEGYAAawaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
7-455 |
1.19e-62 |
|
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: 210.43 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTtDKEIEDLLDKAEsyyQKA------KRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGES 80
Cdd:cd07142 25 DPRNGEVIAHVAEG-DAEDVDRAVKAA---RKAfdegpwPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 81 RT-EVNKIVNYARYFA------------TQGPAFLQpknydklsvgsTAHvefSSIGIVLAVEPWNFPFTQVMRVFAPNF 147
Cdd:cd07142 101 RYaEVPLAARLFRYYAgwadkihgmtlpADGPHHVY-----------TLH---EPIGVVGQIIPWNFPLLMFAWKVGPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 148 ILGNPVILKHASIVPQAAQAFEKACQKVGIPEGAFaNI-----------FATHDQIDKIiddprvqgfALTGSEQAGSN- 215
Cdd:cd07142 167 ACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVL-NIvtgfgptagaaIASHMDVDKV---------AFTGSTEVGKIi 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 216 LAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGN 295
Cdd:cd07142 237 MQLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 296 PLNEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEgPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSS 375
Cdd:cd07142 317 PFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGS-KGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 376 EDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAIN--QVLDeqAEVPFGGVKSSGYGRELsdwGIYEFAN--- 450
Cdd:cd07142 396 VDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDVFD--ASIPFGGYKMSGIGREK---GIYALNNylq 470
|
....*
gi 1140776579 451 IKTVL 455
Cdd:cd07142 471 VKAVV 475
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
3-454 |
1.61e-62 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 210.52 E-value: 1.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKA--KRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGES 80
Cdd:PRK09847 37 FETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGdwSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 81 -RTEVNKIVNYARYFAtqgpaflqpKNYDKL-------SVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNP 152
Cdd:PRK09847 117 lRDDIPGAARAIRWYA---------EAIDKVygevattSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 153 VILKHASIVPQAAQAFEKACQKVGIPEGAFaNIFAT--HDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTT-L 229
Cdd:PRK09847 188 VILKPSEKSPLSAIRLAGLAKEAGLPDGVL-NVVTGfgHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMKRVwL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 230 ELGGTD---IFAvlDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPL 306
Cdd:PRK09847 267 EAGGKSaniVFA--DCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 307 SSQSAKEKLQEQVEKVVAGGSKILYGNlnvDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDS 386
Cdd:PRK09847 345 IDCAHADSVHSFIREGESKGQLLLDGR---NAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDS 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1140776579 387 RHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:PRK09847 422 QYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
2-454 |
3.34e-62 |
|
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: 209.51 E-value: 3.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 2 AYTATNPYNGEVIQEFTDTtDKEieDLlDKAESYYQKA-------KRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMG 74
Cdd:cd07141 23 TFPTINPATGEKICEVQEG-DKA--DV-DKAVKAARAAfklgspwRTMDASERGRLLNKLADLIERDRAYLASLETLDNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 75 KLIGESRT-EVNKIVNYARYFAtqGPAflqpknyDKLsVGST--------AHVEFSSIGIVLAVEPWNFPFTQVMRVFAP 145
Cdd:cd07141 99 KPFSKSYLvDLPGAIKVLRYYA--GWA-------DKI-HGKTipmdgdffTYTRHEPVGVCGQIIPWNFPLLMAAWKLAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 146 NFILGNPVILKHASIVPQAAQAFEKACQKVGIPEG-----------AFANIfATHDQIDKIiddprvqgfALTGSEQAGS 214
Cdd:cd07141 169 ALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGvvnvvpgygptAGAAI-SSHPDIDKV---------AFTGSTEVGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 215 NLAAKATK-NLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQP 293
Cdd:cd07141 239 LIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 294 GNPLNEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEgPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRF 373
Cdd:cd07141 319 GNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGD-KGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 374 SSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKT 453
Cdd:cd07141 398 KTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKT 477
|
.
gi 1140776579 454 V 454
Cdd:cd07141 478 V 478
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
3-454 |
6.98e-62 |
|
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: 208.50 E-value: 6.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKA--KRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGES 80
Cdd:cd07140 23 YNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGewGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 81 -RTEVNKIVNYARYFA-----TQGPAFlqPKNYDKLSVGSTaHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVI 154
Cdd:cd07140 103 lKTHVGMSIQTFRYFAgwcdkIQGKTI--PINQARPNRNLT-LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 155 LKHASIVPQAAQAFEKACQKVGIPEGAFaNIFATHDQI--DKIIDDPRVQGFALTGSEQAGSN-LAAKATKNLMKTTLEL 231
Cdd:cd07140 180 LKPAQVTPLTALKFAELTVKAGFPKGVI-NILPGSGSLvgQRLSDHPDVRKLGFTGSTPIGKHiMKSCAVSNLKKVSLEL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 232 GGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSA 311
Cdd:cd07140 259 GGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAH 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 312 KEKLQEQVEKVVAGGSKILYGNLNVDEgPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSED--EMIKMANDSRHG 389
Cdd:cd07140 339 LDKLVEYCERGVKEGATLVYGGKQVDR-PGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDvdGVLQRANDTEYG 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1140776579 390 LGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07140 418 LASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
2-446 |
2.39e-59 |
|
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: 201.67 E-value: 2.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 2 AYTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESR 81
Cdd:cd07130 13 VVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 82 TEVNKIVNYARYfATqgpaflqpknydKLS---VGSTAHVEFSS---------IGIVLAVEPWNFPftqvMRVFAPN--- 146
Cdd:cd07130 93 GEVQEMIDICDF-AV------------GLSrqlYGLTIPSERPGhrmmeqwnpLGVVGVITAFNFP----VAVWGWNaai 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 147 -FILGNPVILKHASIVPQAAQA----FEKACQKVGIPEGAFANIFATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKAT 221
Cdd:cd07130 156 aLVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 222 KNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEET 301
Cdd:cd07130 236 ARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 302 TLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNlNVDEGPGFQFSPIILTgMERNNPMYDEELFGPVAQIYRFSSEDEMIK 381
Cdd:cd07130 316 LVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGG-KVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIA 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1140776579 382 MANDSRHGLGGAIYTADVKHGNQL--ATKIETGQVAINqVLDEQAEV--PFGGVKSSGYGREL-SD-WGIY 446
Cdd:cd07130 394 WNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVN-IGTSGAEIggAFGGEKETGGGRESgSDaWKQY 463
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
2-454 |
8.02e-58 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 198.95 E-value: 8.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 2 AYTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKligeSR 81
Cdd:PRK09407 33 TREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK----AR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 82 T----EVNKIVNYARYFATQGPAFLQPKNYD-KLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILK 156
Cdd:PRK09407 109 RhafeEVLDVALTARYYARRAPKLLAPRRRAgALPVLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 157 HASIVPQAAQAFEKACQKVGIPEGAFanifathdQIdkIIDDPRVQGFAL---------TGSEQAGSNLAAKATKNLMKT 227
Cdd:PRK09407 189 PDSQTPLTALAAVELLYEAGLPRDLW--------QV--VTGPGPVVGTALvdnadylmfTGSTATGRVLAEQAGRRLIGF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 228 TLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLS 307
Cdd:PRK09407 259 SLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 308 SQSAKEKLQEQVEKVVAGGSKILY-GNLNVDEGPGFqFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDS 386
Cdd:PRK09407 339 SEAQLETVSAHVDDAVAKGATVLAgGKARPDLGPLF-YEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDT 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1140776579 387 RHGLGGAIYTADVKHGNQLATKIETGQVAINqvlDEQA------EVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:PRK09407 418 PYGLNASVWTGDTARGRAIAARIRAGTVNVN---EGYAaawgsvDAPMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
3-448 |
1.53e-56 |
|
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: 194.15 E-value: 1.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESR- 81
Cdd:cd07111 39 FPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 82 TEVNKIVNYARYFAtqGPAFLQpknydklsvgSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIV 161
Cdd:cd07111 119 CDIPLVARHFYHHA--GWAQLL----------DTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 162 PQAAQAFEKACQKVGIPEG---------AFANIFATHDQIDKIiddprvqgfALTGSEQAGSNLAAKATKNLMKTTLELG 232
Cdd:cd07111 187 PLTALLFAEICAEAGLPPGvlnivtgngSFGSALANHPGVDKV---------AFTGSTEVGRALRRATAGTGKKLSLELG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 233 GTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAK 312
Cdd:cd07111 258 GKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 313 EKLQEQVEKVVAGGSKILYGNLNVDEgPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGG 392
Cdd:cd07111 338 KRIRELVEEGRAEGADVFQPGADLPS-KGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAA 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1140776579 393 AIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEF 448
Cdd:cd07111 417 SVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
7-437 |
2.87e-56 |
|
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: 193.50 E-value: 2.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNK 86
Cdd:cd07085 22 NPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 87 IVNYARyFATQGPAFLQPKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQ 166
Cdd:cd07085 102 GLEVVE-FACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 167 AFEKACQKVGIPEGAFANIFATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNLmKTTLELGGTDIFA-VLDDADI 245
Cdd:cd07085 181 RLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANG-KRVQALGGAKNHAvVMPDADL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 246 DKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVAG 325
Cdd:cd07085 260 EQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 326 GSKILY-G-NLNVDEGP-GFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHG 402
Cdd:cd07085 340 GAKLVLdGrGVKVPGYEnGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAA 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1140776579 403 NQLATKIETGQVAINqvldeqaeVP---------FGGVKSSGYG 437
Cdd:cd07085 420 RKFQREVDAGMVGIN--------VPipvplaffsFGGWKGSFFG 455
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
7-455 |
4.03e-55 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 191.19 E-value: 4.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTtDKEIEDLLDKAESY---YQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRT- 82
Cdd:PLN02766 42 DPRTGEVIARIAEG-DKEDVDLAVKAAREafdHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAv 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 83 EVNKIVNYARYFAtqGPAFLQPKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVP 162
Cdd:PLN02766 121 DIPAAAGLLRYYA--GAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 163 QAAQAFEKACQKVGIPEG-----------AFANIfATHDQIDKIiddprvqgfALTGSEQAGSN-LAAKATKNLMKTTLE 230
Cdd:PLN02766 199 LSALFYAHLAKLAGVPDGvinvvtgfgptAGAAI-ASHMDVDKV---------SFTGSTEVGRKiMQAAATSNLKQVSLE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 231 LGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQS 310
Cdd:PLN02766 269 LGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQ 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 311 AKEKLQEQVEKVVAGGSKILYGNLNVDEgPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGL 390
Cdd:PLN02766 349 QFEKILSYIEHGKREGATLLTGGKPCGD-KGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGL 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1140776579 391 GGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:PLN02766 428 AAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVV 492
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
6-454 |
5.92e-55 |
|
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: 189.51 E-value: 5.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVN 85
Cdd:cd07107 2 INPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 86 KIVNYARYFATQGPAFlqpkNYDKLSVGsTAHVEFS---SIGIVLAVEPWNFPFT-QVMRVFAPnFILGNPVILKHASIV 161
Cdd:cd07107 82 VAAALLDYFAGLVTEL----KGETIPVG-GRNLHYTlrePYGVVARIVAFNHPLMfAAAKIAAP-LAAGNTVVVKPPEQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 162 PQAAQAFEKACQKVgIPEGAFaNIFATHDQI--DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAV 239
Cdd:cd07107 156 PLSALRLAELAREV-LPPGVF-NILPGDGATagAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 240 LDDADIDKAAKDAAQ-ARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQ 318
Cdd:cd07107 234 FPDADPEAAADAAVAgMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 319 VEKVVAGGSKILYGNlNVDEGP----GFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAI 394
Cdd:cd07107 314 IDSAKREGARLVTGG-GRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 395 YTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTV 454
Cdd:cd07107 393 WTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
3-439 |
5.28e-54 |
|
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: 187.66 E-value: 5.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGES-R 81
Cdd:cd07116 18 FDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETlA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 82 TEVNKIVNYARYFAtqGPAFLQPKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIV 161
Cdd:cd07116 98 ADIPLAIDHFRYFA--GCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 162 PQAAQAFEKACQKVgIPEGAFANIFATHDQIDK-IIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGT--DIF- 237
Cdd:cd07116 176 PASILVLMELIGDL-LPPGVVNVVNGFGLEAGKpLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKspNIFf 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 238 -AVLDDADIDKAAKDAAQARLA-NAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKL 315
Cdd:cd07116 255 aDVMDADDAFFDKALEGFVMFAlNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 316 -------QEQVEKVVAGGSKilyGNLNVDEGPGFQFSPIILTGmernNPM--YDEELFGPVAQIYRFSSEDEMIKMANDS 386
Cdd:cd07116 335 lsyidigKEEGAEVLTGGER---NELGGLLGGGYYVPTTFKGG----NKMriFQEEIFGPVLAVTTFKDEEEALEIANDT 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1140776579 387 RHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRE 439
Cdd:cd07116 408 LYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRE 460
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
20-456 |
6.79e-51 |
|
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: 178.18 E-value: 6.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 20 TTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESR-TEVNKIVNYARYFATQG 98
Cdd:cd07135 2 TPLDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 99 PAFLQPKnydKLSVGS------TAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQAFEKAC 172
Cdd:cd07135 82 KKWAKDE---KVKDGPlafmfgKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 173 QKvGIPEGAFANIFATHDQIDKIIDdprvQGFAL---TGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAA 249
Cdd:cd07135 159 PK-YLDPDAFQVVQGGVPETTALLE----QKFDKifyTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 250 KDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPlNEETTLAPLSSQSA----KEKLQEQVEKVVAG 325
Cdd:cd07135 234 KRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHfnrlKSLLDTTKGKVVIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 326 GSKilygnlnvDEGPGFqFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQL 405
Cdd:cd07135 313 GEM--------DEATRF-IPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHI 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1140776579 406 ATKIETGQVAINQVLDEQA--EVPFGGVKSSGYGRELSDWGIYEFANIKTVLN 456
Cdd:cd07135 384 LTRTRSGGVVINDTLIHVGvdNAPFGGVGDSGYGAYHGKYGFDTFTHERTVVK 436
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
3-455 |
2.24e-50 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 179.23 E-value: 2.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYNGEVIQEftdTTDKEIEDLlDKAESYYQKA------KRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKL 76
Cdd:PLN02466 75 FPTLDPRTGEVIAH---VAEGDAEDV-NRAVAAARKAfdegpwPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 77 IGESR-TEVNKIVNYARYFA--------TQGPAflqpknyDKLSVGSTAHvefSSIGIVLAVEPWNFPFTQVMRVFAPNF 147
Cdd:PLN02466 151 YEQSAkAELPMFARLFRYYAgwadkihgLTVPA-------DGPHHVQTLH---EPIGVAGQIIPWNFPLLMFAWKVGPAL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 148 ILGNPVILKHASIVPQAAQAFEKACQKVGIPEGAFaNI-----------FATHDQIDKIiddprvqgfALTGSEQAGS-- 214
Cdd:PLN02466 221 ACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVL-NVvsgfgptagaaLASHMDVDKL---------AFTGSTDTGKiv 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 215 -NLAAKAtkNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQP 293
Cdd:PLN02466 291 lELAAKS--NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 294 GNPLNEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEgPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRF 373
Cdd:PLN02466 369 GDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGS-KGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKF 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 374 SSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAIN--QVLDeqAEVPFGGVKSSGYGRELsdwGIYEFAN- 450
Cdd:PLN02466 448 KDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVFD--AAIPFGGYKMSGIGREK---GIYSLNNy 522
|
....*..
gi 1140776579 451 --IKTVL 455
Cdd:PLN02466 523 lqVKAVV 529
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
3-437 |
1.84e-49 |
|
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: 176.26 E-value: 1.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYN-GEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESR 81
Cdd:cd07124 48 IESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 82 TEVNKIVNYARYFATQgpaFLQPKNYDKLSV-GSTAHVEFSSIGIVLAVEPWNFPF--TQVMRVFApnFILGNPVILKHA 158
Cdd:cd07124 128 ADVAEAIDFLEYYARE---MLRLRGFPVEMVpGEDNRYVYRPLGVGAVISPWNFPLaiLAGMTTAA--LVTGNTVVLKPA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 159 SIVPQAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATK------NLMKTTLEL 231
Cdd:cd07124 203 EDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEM 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 232 GGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSA 311
Cdd:cd07124 283 GGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 312 KEKLQEQVEKVVAGGSKILYGNLNVDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLG 391
Cdd:cd07124 363 RDRIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLT 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1140776579 392 GAIYTADVKHGNQLATKIETGQVAINQ-----VLDEQaevPFGGVKSSGYG 437
Cdd:cd07124 443 GGVFSRSPEHLERARREFEVGNLYANRkitgaLVGRQ---PFGGFKMSGTG 490
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
3-455 |
3.35e-48 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 171.99 E-value: 3.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYNGEVIQEFTDTTDKEIEDLLDKAesyyQKAKRVDFAK----RADLLNRLAGEFEANLEDYARLSSTNMGKLIG 78
Cdd:PRK13252 24 FEVINPATGEVLATVQAATPADVEAAVASA----KQGQKIWAAMtameRSRILRRAVDILRERNDELAALETLDTGKPIQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 79 EsrTEVNKIVNYA---RYFATQGPAFlqPKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVIL 155
Cdd:PRK13252 100 E--TSVVDIVTGAdvlEYYAGLAPAL--EGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 156 KHASIVPQAAQAFEKACQKVGIPEGAFaNI----------FATHDQIDKIiddprvqgfALTGSEQAGSNLAAKATKNLM 225
Cdd:PRK13252 176 KPSEVTPLTALKLAEIYTEAGLPDGVF-NVvqgdgrvgawLTEHPDIAKV---------SFTGGVPTGKKVMAAAAASLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 226 KTTLELGGTDIFAVLDDADIDKAAKDAAqarLAN---AGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETT 302
Cdd:PRK13252 246 EVTMELGGKSPLIVFDDADLDRAADIAM---LANfysSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 303 LAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEG---PGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEM 379
Cdd:PRK13252 323 FGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGgfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEV 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1140776579 380 IKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEVPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:PRK13252 403 IARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQ 478
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
41-438 |
4.27e-46 |
|
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: 165.14 E-value: 4.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 41 RVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNKIVN--------YARYFATQgpaflqpknyDKLSV 112
Cdd:cd07095 18 ALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGkidisikaYHERTGER----------ATPMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 113 GSTAHVEFSSIGIVLAVEPWNFPftqvmrVFAPN------FILGNPVILKHASIVPQAAQAFEKACQKVGIPEGAFANIF 186
Cdd:cd07095 88 QGRAVLRHRPHGVMAVFGPFNFP------GHLPNghivpaLLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 187 ATHDQIDKIIDDPRVQGFALTGSEQAGSNL----AAKATKNLmktTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQ 262
Cdd:cd07095 162 GGRETGEALAAHEGIDGLLFTGSAATGLLLhrqfAGRPGKIL---ALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 263 VCTAAKRYLVSDKIY-DEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEGPG 341
Cdd:cd07095 239 RCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 342 FqFSPIIL--TGMErnnPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQV 419
Cdd:cd07095 319 F-LSPGIIdvTDAA---DVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRP 394
|
410 420
....*....|....*....|
gi 1140776579 420 LDEQA-EVPFGGVKSSGYGR 438
Cdd:cd07095 395 TTGASsTAPFGGVGLSGNHR 414
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
4-439 |
3.78e-44 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 161.54 E-value: 3.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 4 TATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTE 83
Cdd:PLN02315 37 SSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 84 VNKIVN---YARYFATQGPAFLQPK---NYDKLSVgstahveFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKH 157
Cdd:PLN02315 117 VQEIIDmcdFAVGLSRQLNGSIIPSerpNHMMMEV-------WNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 158 ASIVPQAAQAFEKACQKV----GIPEGAFANIFATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGG 233
Cdd:PLN02315 190 APTTPLITIAMTKLVAEVleknNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 234 TDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKE 313
Cdd:PLN02315 270 NNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 314 KLQEQVEKVVAGGSKILYGNLNVDEGPGFqFSPIILTgMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGA 393
Cdd:PLN02315 350 NFEKGIEIIKSQGGKILTGGSAIESEGNF-VQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSS 427
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1140776579 394 IYTAdvKHGNQLA----TKIETGQVAINqVLDEQAEV--PFGGVKSSGYGRE 439
Cdd:PLN02315 428 IFTR--NPETIFKwigpLGSDCGIVNVN-IPTNGAEIggAFGGEKATGGGRE 476
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
4-437 |
7.54e-44 |
|
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: 159.89 E-value: 7.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 4 TATNPYNGEVIQEFTDTTDKEIEDLLDKA-ESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRT 82
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAhALFLDRNNWLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 83 EV----NKIVNYARYFATQGPAFLqPKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHA 158
Cdd:cd07148 82 EVtraiDGVELAADELGQLGGREI-PMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 159 SIVPQAAQAFEKACQKVGIPEGAFANIFATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNlMKTTLELGGTDIFA 238
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 239 VLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQ 318
Cdd:cd07148 240 VDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 319 VEKVVAGGSKILYGNLNVDEGpgfQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTAD 398
Cdd:cd07148 320 VNEAVAAGARLLCGGKRLSDT---TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKD 396
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1140776579 399 VKHGNQLATKIETGQVAINqvlDEQA----EVPFGGVKSSGYG 437
Cdd:cd07148 397 LDVALKAVRRLDATAVMVN---DHTAfrvdWMPFAGRRQSGYG 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
2-437 |
1.58e-41 |
|
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: 154.66 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 2 AYTATNP-YNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGES 80
Cdd:cd07125 47 GAPVIDPaDHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 81 RTEVNKIVNYARYFATQgpafLQPKNYDKLSVGSTAH---VEFSSIGIVLAVEPWNFP---FT-QVMRVFAPnfilGNPV 153
Cdd:cd07125 127 DAEVREAIDFCRYYAAQ----ARELFSDPELPGPTGElngLELHGRGVFVCISPWNFPlaiFTgQIAAALAA----GNTV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 154 ILKHASIVPQAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLA-AKATKNLMKTTL-- 229
Cdd:cd07125 199 IAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAKLINrALAERDGPILPLia 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 230 ELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQ 309
Cdd:cd07125 279 ETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDK 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 310 SAKEKLQEQVEKvVAGGSKILYgNLNVDEGPGFQFSPIILTGMerNNPMYDEELFGPVAQIYRFSSE--DEMIKMANDSR 387
Cdd:cd07125 359 PAGKLLRAHTEL-MRGEAWLIA-PAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKAEdlDEAIEDINATG 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1140776579 388 HGLGGAIYTADVKHGNQLATKIETGQVAINQ-----VLDEQaevPFGGVKSSGYG 437
Cdd:cd07125 435 YGLTLGIHSRDEREIEYWRERVEAGNLYINRnitgaIVGRQ---PFGGWGLSGTG 486
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
3-435 |
1.69e-41 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 154.32 E-value: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 3 YTATNPYN-GEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAG-------EFEANLedyarlsSTNMG 74
Cdd:PRK03137 52 IVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAiirrrkhEFSAWL-------VKEAG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 75 KLIGESRTEVNKIVNYARYFATQGPaflqpknydKLSVGSTA------HVEFSSI--GIVLAVEPWNFPFTQVMRVFAPN 146
Cdd:PRK03137 125 KPWAEADADTAEAIDFLEYYARQML---------KLADGKPVesrpgeHNRYFYIplGVGVVISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 147 FILGNPVILKHASIVPQAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNL---AAK--- 219
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFITFTGSREVGLRIyerAAKvqp 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 220 ATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPlNE 299
Cdd:PRK03137 276 GQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-ED 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 300 ETTLAPLSSQSAKEKLQEQVE------KVVAGGskilygnlNVDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRF 373
Cdd:PRK03137 355 NAYMGPVINQASFDKIMSYIEigkeegRLVLGG--------EGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKA 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1140776579 374 SSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQ-----VLDEQaevPFGGVKSSG 435
Cdd:PRK03137 427 KDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRgctgaIVGYH---PFGGFNMSG 490
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
2-435 |
6.52e-41 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 152.42 E-value: 6.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 2 AYTATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESR 81
Cdd:PRK09457 16 AFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 82 TEVNKIVN--------YA-RYFATQGPAflqpknydklsVGSTAHVEFSSIGIVLAVEPWNFPftqvmrVFAPN------ 146
Cdd:PRK09457 96 TEVTAMINkiaisiqaYHeRTGEKRSEM-----------ADGAAVLRHRPHGVVAVFGPYNFP------GHLPNghivpa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 147 FILGNPVILKHASIVPQAAQAFEKACQKVGIPEGAF---------ANIFATHDQIDkiiddprvqGFALTGSEQAGSNL- 216
Cdd:PRK09457 159 LLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLnlvqggretGKALAAHPDID---------GLLFTGSANTGYLLh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 217 ---AAKATKNLmktTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIY-DEFLDKVKREFDTYQ 292
Cdd:PRK09457 230 rqfAGQPEKIL---ALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 293 PGNPLNEETT-LAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEGPGFqFSPIIL--TGMeRNNPmyDEELFGPVAQ 369
Cdd:PRK09457 307 VGRWDAEPQPfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGL-LTPGIIdvTGV-AELP--DEEYFGPLLQ 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1140776579 370 IYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQA-EVPFGGVKSSG 435
Cdd:PRK09457 383 VVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASsAAPFGGVGASG 449
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
26-456 |
1.32e-39 |
|
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: 147.67 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 26 EDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGK-LIGESRTEVNKIVNYARYFATQGPAFLQP 104
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKpPAEAYLTEIAVVLGEIDHALKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 105 KNYDK--LSVGSTAHVEFSSIGIVLAVEPWNFPFtqvMRVFAP---NFILGNPVILKHASIVPQAAQAFEKACQKVgIPE 179
Cdd:cd07087 81 RRVSVplLLQPAKAYVIPEPLGVVLIIGPWNYPL---QLALAPligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 180 GAFANIFATHDQIDKIIDdprvQGFAL---TGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQAR 256
Cdd:cd07087 157 EAVAVVEGGVEVATALLA----EPFDHiffTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 257 LANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETtLAPLSSQSAKEKLQE--QVEKVVAGGSkilygnl 334
Cdd:cd07087 233 FLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPD-YGRIINERHFDRLASllDDGKVVIGGQ------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 335 nVDEGPGFqFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQV 414
Cdd:cd07087 305 -VDKEERY-IAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGV 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1140776579 415 AINQVLdEQA---EVPFGGVKSSGYGRELSDWGIYEFANIKTVLN 456
Cdd:cd07087 383 CVNDVL-LHAaipNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
4-437 |
1.06e-38 |
|
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: 146.57 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 4 TATNPYN-GEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRT 82
Cdd:cd07083 35 VSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 83 EVNKIVNYARYFATQGPAFLQPKNYDKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVP 162
Cdd:cd07083 115 DVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 163 QAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTT------LELGGTD 235
Cdd:cd07083 195 VVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLAPGQTwfkrlyVETGGKN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 236 IFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKL 315
Cdd:cd07083 275 AIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 316 QEQVEKVVAGGSKILYGNLnvDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSED--EMIKMANDSRHGLGGA 393
Cdd:cd07083 355 LSYIEHGKNEGQLVLGGKR--LEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGG 432
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1140776579 394 IYTADVKHGNQLATKIETGQVAINQ-----VLDEQaevPFGGVKSSGYG 437
Cdd:cd07083 433 VYSRKREHLEEARREFHVGNLYINRkitgaLVGVQ---PFGGFKLSGTN 478
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
37-456 |
4.85e-36 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 139.01 E-value: 4.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 37 QKAKRVDFAKrADLLNRLAGeFEANLEDYARLSSTNMGKLIGESR-TEVNKIVNYARYFATQGPAFLQPKNYDK--LSVG 113
Cdd:PTZ00381 23 GKTRPLEFRK-QQLRNLLRM-LEENKQEFSEAVHKDLGRHPFETKmTEVLLTVAEIEHLLKHLDEYLKPEKVDTvgVFGP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 114 STAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQAFEKACQK------VGIPEG-AFANIF 186
Cdd:PTZ00381 101 GKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKyldpsyVRVIEGgVEVTTE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 187 ATHDQIDKIIddprvqgfaLTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTA 266
Cdd:PTZ00381 181 LLKEPFDHIF---------FTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 267 AKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEEtTLAPLSSQSAKEKLQEQVEKVvagGSKILYGNlNVDEGPGFqFSP 346
Cdd:PTZ00381 252 PDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSE-DYSRIVNEFHTKRLAELIKDH---GGKVVYGG-EVDIENKY-VAP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 347 IILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAEV 426
Cdd:PTZ00381 326 TIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNP 405
|
410 420 430
....*....|....*....|....*....|..
gi 1140776579 427 --PFGGVKSSGYGRELSDWGIYEFANIKTVLN 456
Cdd:PTZ00381 406 nlPFGGVGNSGMGAYHGKYGFDTFSHPKPVLN 437
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
7-454 |
1.89e-35 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 138.73 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEVNK 86
Cdd:PLN02419 135 NPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 87 IVNYARYFAtqGPAFLQPKNY-DKLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAA 165
Cdd:PLN02419 215 GLEVVEHAC--GMATLQMGEYlPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGAS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 166 QAFEKACQKVGIPEGAFANIFATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADI 245
Cdd:PLN02419 293 VILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 246 DKAAKDAAQARLANAGQVCTA-AKRYLVSD-KIYDEFLDKVKREFDTYQPGNPlneETTLAPLSSQSAKEKLQEQVEKVV 323
Cdd:PLN02419 373 DATLNALLAAGFGAAGQRCMAlSTVVFVGDaKSWEDKLVERAKALKVTCGSEP---DADLGPVISKQAKERICRLIQSGV 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 324 AGGSKILYGNLNVdEGPGFQ----FSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADV 399
Cdd:PLN02419 450 DDGAKLLLDGRDI-VVPGYEkgnfIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSG 528
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1140776579 400 KHGNQLATKIETGQVAINQVLdeqaEVP-----FGGVKSSgYGRELSDW---GIYEFANIKTV 454
Cdd:PLN02419 529 AAARKFQMDIEAGQIGINVPI----PVPlpffsFTGNKAS-FAGDLNFYgkaGVDFFTQIKLV 586
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
37-455 |
1.21e-32 |
|
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: 128.50 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 37 QKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESR-TEVNKIVNYARYFATQGPAFLQPKNY--DKLSVG 113
Cdd:cd07134 12 LALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlTEILPVLSEINHAIKHLKKWMKPKRVrtPLLLFG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 114 STAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILK------HASIVPQA--AQAFEKacQKVGIPEGA---- 181
Cdd:cd07134 92 TKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKpseltpHTSAVIAKiiREAFDE--DEVAVFEGDaeva 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 182 -------FANIFathdqidkiiddprvqgfaLTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQ 254
Cdd:cd07134 170 qallelpFDHIF-------------------FTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 255 ARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDT-YQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGN 333
Cdd:cd07134 231 GKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKfYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 334 lNVDEGPGFqFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQ 413
Cdd:cd07134 311 -QFDAAQRY-IAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1140776579 414 VAINQVLDEQAEV--PFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:cd07134 389 VVVNDVVLHFLNPnlPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
4-437 |
9.06e-32 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 126.79 E-value: 9.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 4 TATNPYNGEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTE 83
Cdd:PLN00412 34 AITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 84 VNKIVNYARYFATQGPAFLQ----------PKN-YDKLSVGSTAhvefsSIGIVLAVEPWNFPFTQVMRVFAPNFILGNP 152
Cdd:PLN00412 114 VVRSGDLISYTAEEGVRILGegkflvsdsfPGNeRNKYCLTSKI-----PLGVVLAIPPFNYPVNLAVSKIAPALIAGNA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 153 VILKHASivpQAA-------QAFEKAcqkvGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEqAGSNLAAKAtkNL 224
Cdd:PLN00412 189 VVLKPPT---QGAvaalhmvHCFHLA----GFPKGLISCVTGKGSEIgDFLTMHPGVNCISFTGGD-TGIAISKKA--GM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 225 MKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPlNEETTLA 304
Cdd:PLN00412 259 VPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDIT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 305 PLSSQSAKEKLQEQVEKVVAGGSKILY-----GNLnvdegpgfqFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEM 379
Cdd:PLN00412 338 PVVSESSANFIEGLVMDAKEKGATFCQewkreGNL---------IWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEG 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1140776579 380 IKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQAE-VPFGGVKSSGYG 437
Cdd:PLN00412 409 IHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIG 467
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
6-437 |
4.74e-27 |
|
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: 113.47 E-value: 4.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYN-GEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEV 84
Cdd:TIGR01238 56 TNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 85 NKIVNYARYFATQGPAFLqpknyDKLSVgstahvefSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQ- 163
Cdd:TIGR01238 136 REAVDFCRYYAKQVRDVL-----GEFSV--------ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLi 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 164 AAQAFEkACQKVGIPEGAFANIFATHDQIDK-IIDDPRVQGFALTGSEQAGSNLA---AKATKNLMKTTLELGGTDIFAV 239
Cdd:TIGR01238 203 AYRAVE-LMQEAGFPAGTIQLLPGRGADVGAaLTSDPRIAGVAFTGSTEVAQLINqtlAQREDAPVPLIAETGGQNAMIV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 240 LDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQV 319
Cdd:TIGR01238 282 DSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 320 EKVVAGGSKilYGNLNVDEGPGFQ---FSPIILTGMERNNPMyDEELFGPVAQIYRFSSE--DEMIKMANDSRHGLGGAI 394
Cdd:TIGR01238 362 EHMSQTQKK--IAQLTLDDSRACQhgtFVAPTLFELDDIAEL-SEEVFGPVLHVVRYKARelDQIVDQINQTGYGLTMGV 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1140776579 395 YTADVKHGNQLATKIETGQVAINQ-----VLDEQaevPFGGVKSSGYG 437
Cdd:TIGR01238 439 HSRIETTYRWIEKHARVGNCYVNRnqvgaVVGVQ---PFGGQGLSGTG 483
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
124-438 |
2.04e-26 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 111.06 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 124 GIVLAVEPWNFPFtqvMRVFAPnfiL------GNPVILKHASIVPQAAQAFEKACQKVGIPE-------GAFANIFATHD 190
Cdd:cd07136 102 GVVLIIAPWNYPF---QLALAP---LigaiaaGNTAVLKPSELTPNTSKVIAKIIEETFDEEyvavvegGVEENQELLDQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 191 QIDKIiddprvqgFaLTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRY 270
Cdd:cd07136 176 KFDYI--------F-FTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 271 LVSDKIYDEFLDKVKREFDTYQPGNPLNEEtTLAPLSSQSAKEKLQE--QVEKVVAGgskilyGNLNVDEgpgFQFSPII 348
Cdd:cd07136 247 LVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGllDNGKIVFG------GNTDRET---LYIEPTI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 349 LTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQA--EV 426
Cdd:cd07136 317 LDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLAnpYL 396
|
330
....*....|..
gi 1140776579 427 PFGGVKSSGYGR 438
Cdd:cd07136 397 PFGGVGNSGMGS 408
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
26-455 |
4.37e-26 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 109.88 E-value: 4.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 26 EDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMG-KLIGESR-TEVNKIVNYARYFATQGPAFLQ 103
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLlAEILPSIAGIKHARKHLKKWMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 104 PK--NYDKLSVGSTAHVEFSSIGIVLAVEPWNFPftqVMRVFAP---NFILGNPVILKHASIVPQAAQAFEKAcqkvgip 178
Cdd:cd07133 81 PSrrHVGLLFLPAKAEVEYQPLGVVGIIVPWNYP---LYLALGPliaALAAGNRVMIKPSEFTPRTSALLAEL------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 179 egaFANIFAThDQIDKIIDDPRV-QGF-AL-------TGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAA 249
Cdd:cd07133 151 ---LAEYFDE-DEVAVVTGGADVaAAFsSLpfdhllfTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 250 KDAAQARLANAGQVCTAAKRYLV-SDKIyDEFLDKVKREFDTYQPGNPLNEETTlaPLSSQSAKEKLQEQVEKVVAGGSK 328
Cdd:cd07133 227 ERIAFGKLLNAGQTCVAPDYVLVpEDKL-EEFVAAAKAAVAKMYPTLADNPDYT--SIINERHYARLQGLLEDARAKGAR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 329 ILY-GNLNVDEGPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLAT 407
Cdd:cd07133 304 VIElNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLR 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1140776579 408 KIETGQVAINQVLDE--QAEVPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:cd07133 384 RTHSGGVTINDTLLHvaQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPVF 433
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
114-455 |
1.52e-23 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 102.82 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 114 STAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQAFEKACQK------VGIPEGAFANIFA 187
Cdd:PLN02174 104 ASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQyldssaVRVVEGAVTETTA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 188 THDQ-IDKIIddprvqgfaLTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLA-NAGQVCT 265
Cdd:PLN02174 184 LLEQkWDKIF---------YTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 266 AAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLnEETTLAPLSSQSAKEKLQEQV-EKVVAggSKILYGNLNVDEgpGFQF 344
Cdd:PLN02174 255 SPDYILTTKEYAPKVIDAMKKELETFYGKNPM-ESKDMSRIVNSTHFDRLSKLLdEKEVS--DKIVYGGEKDRE--NLKI 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 345 SPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQA 424
Cdd:PLN02174 330 APTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLA 409
|
330 340 350
....*....|....*....|....*....|...
gi 1140776579 425 --EVPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:PLN02174 410 lhTLPFGGVGESGMGAYHGKFSFDAFSHKKAVL 442
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
4-409 |
4.54e-23 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 101.58 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 4 TATNPYNGEVIQEfTDTTDKEIEDLLDKAESYYQKAKR-VDFAKRADLLNRLAGEFEANLEDYARLSSTNmGKLIGESRT 82
Cdd:cd07128 18 TLHDAVTGEVVAR-VSSEGLDFAAAVAYAREKGGPALRaLTFHERAAMLKALAKYLMERKEDLYALSAAT-GATRRDSWI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 83 EVNKIVNYARYFATQGPAFLQPKNY------DKLSVGST---AHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPV 153
Cdd:cd07128 96 DIDGGIGTLFAYASLGRRELPNAHFlvegdvEPLSKDGTfvgQHILTPRRGVAVHINAFNFPVWGMLEKFAPALLAGVPV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 154 ILKHASIVPQAAQAFEKACQKVGI-PEGAFANIF-ATHDQIDKIIDDPRVqgfALTGSEQAGSNLAAKA--TKNLMKTTL 229
Cdd:cd07128 176 IVKPATATAYLTEAVVKDIVESGLlPEGALQLICgSVGDLLDHLGEQDVV---AFTGSAATAAKLRAHPniVARSIRFNA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 230 E--------LGGTdifAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEET 301
Cdd:cd07128 253 EadslnaaiLGPD---ATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 302 TLAPLSSQSAKEKLQEQVEKVVAGGsKILYGNLN------VDEGPGFQFSPIILTGmerNNPM-----YDEELFGPVAQI 370
Cdd:cd07128 330 RMGPLVSREQREDVRAAVATLLAEA-EVVFGGPDrfevvgADAEKGAFFPPTLLLC---DDPDaatavHDVEAFGPVATL 405
|
410 420 430
....*....|....*....|....*....|....*....
gi 1140776579 371 YRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKI 409
Cdd:cd07128 406 MPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
124-438 |
1.68e-22 |
|
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: 99.22 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 124 GIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAA--------QAFEKACQKV---GIPEGA--FANIFathd 190
Cdd:cd07132 102 GVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAkllaelipKYLDKECYPVvlgGVEETTelLKQRF---- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 191 qiDKIIddprvqgfaLTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRY 270
Cdd:cd07132 178 --DYIF---------YTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 271 LVSDKIYDEFLDKVK---REFdtYqpGNPLNEETTLAPLSSQSAKEKLQEQVE--KVVAGGSkilygnlnVDEGPGFqFS 345
Cdd:cd07132 247 LCTPEVQEKFVEALKktlKEF--Y--GEDPKESPDYGRIINDRHFQRLKKLLSggKVAIGGQ--------TDEKERY-IA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 346 PIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQVLDEQA- 424
Cdd:cd07132 314 PTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTl 393
|
330
....*....|....*
gi 1140776579 425 -EVPFGGVKSSGYGR 438
Cdd:cd07132 394 dSLPFGGVGNSGMGA 408
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
6-437 |
1.69e-22 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 101.09 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYN-GEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEV 84
Cdd:PRK11905 572 LNPADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEV 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 85 NKIVNYARYFATQGPAFLQPknydklsvgstahVEFSSIGIVLAVEPWNFP---FT-QVmrvfAPNFILGNPVILKHA-- 158
Cdd:PRK11905 652 REAVDFLRYYAAQARRLLNG-------------PGHKPLGPVVCISPWNFPlaiFTgQI----AAALVAGNTVLAKPAeq 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 159 -SIVpqAAQAFEkACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGSEQAG----SNLAAKATKNLMkttL--E 230
Cdd:PRK11905 715 tPLI--AARAVR-LLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVArliqRTLAKRSGPPVP---LiaE 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 231 LGG-----TDIFA----VLDDAdidkaakdaaqarLA----NAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPL 297
Cdd:PRK11905 789 TGGqnamiVDSSAlpeqVVADV-------------IAsafdSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPW 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 298 NEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEGPGFQFSPII-----LTGMERnnpmydeELFGPVAQIYR 372
Cdd:PRK11905 856 RLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLieidsISDLER-------EVFGPVLHVVR 928
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1140776579 373 FSSE--DEMIKMANDSRHGLGGAIYT---ADVKHgnqLATKIETGQVAINQ-----VLDEQaevPFGGVKSSGYG 437
Cdd:PRK11905 929 FKADelDRVIDDINATGYGLTFGLHSridETIAH---VTSRIRAGNIYVNRniigaVVGVQ---PFGGEGLSGTG 997
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
26-419 |
2.70e-22 |
|
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: 98.85 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 26 EDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKlIGESRTEVNKIVNYARYFATQGPAFLQPK 105
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGK-GWMFAENICGDQVQLRARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 106 N-YDKLSVGST--AHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQAFEKACQKVGI-PEGA 181
Cdd:cd07084 81 EpGNHLGQGLKqqSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 182 FANIFATHDQIDKIIDDPRVQGFALTGSEQAGSNLAAKATKnlMKTTLELGGTDIFAVLDDADIDKAAKDAAQARL-ANA 260
Cdd:cd07084 161 VTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQAVDYVAWQCVQDMtACS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 261 GQVCTAAKRYLV-SDKIYDEFLDKVKREFDTYQPGN----PLNEETTLAPLSSqsakekLQEQVEKVVAGGSKILYgNLN 335
Cdd:cd07084 239 GQKCTAQSMLFVpENWSKTPLVEKLKALLARRKLEDlllgPVQTFTTLAMIAH------MENLLGSVLLFSGKELK-NHS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 336 VDEGPGFQFSPIILTGMERNN---PMYDEELFGPVAQI--YRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIE 410
Cdd:cd07084 312 IPSIYGACVASALFVPIDEILktyELVTEEIFGPFAIVveYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLW 391
|
410 420
....*....|....*....|
gi 1140776579 411 -----------TGQVAINQV 419
Cdd:cd07084 392 vagrtyailrgRTGVAPNQN 411
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
2-437 |
3.44e-22 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 99.89 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 2 AYTATNPYNGE-VIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGES 80
Cdd:PRK11904 563 ARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDA 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 81 RTEVNKIVNYARYFATQGPA-FLQPKnydKLS--VGSTAHVEFSSIGIVLAVEPWNFP---FT-QVMRVFAPnfilGNPV 153
Cdd:PRK11904 643 IAEVREAVDFCRYYAAQARRlFGAPE---KLPgpTGESNELRLHGRGVFVCISPWNFPlaiFLgQVAAALAA----GNTV 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 154 ILKHASIVPQAAQAFEKACQKVGIPEGAFANIFATHDQIDK-IIDDPRVQGFALTGSEQAGS----NLAAKATKNLmktT 228
Cdd:PRK11904 716 IAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAaLTADPRIAGVAFTGSTETARiinrTLAARDGPIV---P 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 229 L--ELGG-----TDIFA----VLDDAdidkaakdaAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPL 297
Cdd:PRK11904 793 LiaETGGqnamiVDSTAlpeqVVDDV---------VTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPR 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 298 NEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEGPGFQFSPII--LTGMERnnpmYDEELFGPVAQIYRFSS 375
Cdd:PRK11904 864 LLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAfeIDSISQ----LEREVFGPILHVIRYKA 939
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1140776579 376 E--DEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQ-----VLDEQaevPFGGVKSSGYG 437
Cdd:PRK11904 940 SdlDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRnqigaVVGVQ---PFGGQGLSGTG 1005
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
6-430 |
1.03e-21 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 98.47 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNG-EVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEV 84
Cdd:COG4230 575 RNPADHsDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEV 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 85 NKIVNYARYFATQ------GPAFLQPKnydklsvgstahvefssiGIVLAVEPWNFP---FT-QVmrvfAPNFILGNPVI 154
Cdd:COG4230 655 REAVDFCRYYAAQarrlfaAPTVLRGR------------------GVFVCISPWNFPlaiFTgQV----AAALAAGNTVL 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 155 LKHA---SIVpqAAQAFeKACQKVGIPEGAF-------ANIFAthdqidKIIDDPRVQGFALTGSEQAGS----NLAAKA 220
Cdd:COG4230 713 AKPAeqtPLI--AARAV-RLLHEAGVPADVLqllpgdgETVGA------ALVADPRIAGVAFTGSTETARlinrTLAARD 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 221 TKNLmktTL--ELGG-----TDIFA----VLDDAdidkaakdaaqarLA----NAGQVCTAAKRYLVSDKIYDEFLDKVK 285
Cdd:COG4230 784 GPIV---PLiaETGGqnamiVDSSAlpeqVVDDV-------------LAsafdSAGQRCSALRVLCVQEDIADRVLEMLK 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 286 REFDTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEGPGFQFSPII--LTGMERnnpmYDEEL 363
Cdd:COG4230 848 GAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLieIDSISD----LEREV 923
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1140776579 364 FGPVAQIYRFSSE--DEMIKMANDSRHGLGGAIY-----TADvkhgnQLATKIETGQVAIN--QVldeQAEV---PFGG 430
Cdd:COG4230 924 FGPVLHVVRYKADelDKVIDAINATGYGLTLGVHsrideTID-----RVAARARVGNVYVNrnII---GAVVgvqPFGG 994
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
25-455 |
1.50e-21 |
|
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: 96.33 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 25 IEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGES-RTEVNKIVNYARYFATQGPAFLQ 103
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCKLAIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 104 PKNYdKLSVG---STAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQAFEKACQK------ 174
Cdd:cd07137 81 PEKV-KTPLTtfpAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEyldtka 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 175 VGIPEGAFANIFATHDQ-IDKIIddprvqgfaLTGSEQAGSNLAAKATKNLMKTTLELGGTDIFAVLDDADIDKAAKDAA 253
Cdd:cd07137 160 IKVIEGGVPETTALLEQkWDKIF---------FTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 254 QARL-ANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLnEETTLAPLSSQSAKEKLQEQV-EKVVAggSKILY 331
Cdd:cd07137 231 GGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPK-ESKDLSRIVNSHHFQRLSRLLdDPSVA--DKIVH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 332 GNlNVDEgPGFQFSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGLGGAIYTADVKHGNQLATKIET 411
Cdd:cd07137 308 GG-ERDE-KNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSS 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1140776579 412 GQVAINQVLDEQA--EVPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:cd07137 386 GGVTFNDTVVQYAidTLPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
6-409 |
1.17e-18 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 88.22 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 6 TNPYNGEVIQEfTDTTDKEIEDLLDKAESYYQKAKR-VDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGESRTEV 84
Cdd:PRK11903 24 FDPVTGEELVR-VSATGLDLAAAFAFAREQGGAALRaLTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 85 N----KIVNYARYFATQGPAFLQPKNyDKLSVGSTA-----HVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVIL 155
Cdd:PRK11903 103 DggifTLGYYAKLGAALGDARLLRDG-EAVQLGKDPafqgqHVLVPTRGVALFINAFNFPAWGLWEKAAPALLAGVPVIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 156 KHASIVPQAAQAFEKACQKVGI-PEGAFANIF-ATHDQIDKiiddprVQGF---ALTGSEQAGSNLAAKA--TKNLMKTT 228
Cdd:PRK11903 182 KPATATAWLTQRMVKDVVAAGIlPAGALSVVCgSSAGLLDH------LQPFdvvSFTGSAETAAVLRSHPavVQRSVRVN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 229 LELGGTDIFAVLDDADIDKAAKDAAQARLA-----NAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPLNEETTL 303
Cdd:PRK11903 256 VEADSLNSALLGPDAAPGSEAFDLFVKEVVremtvKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRM 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 304 APLSSQSAKEKLQEQVEKvVAGGSKILYGN-----LNVDEGPGFQFSPIIL--TGMERNNPMYDEELFGPVAQIYRFSSE 376
Cdd:PRK11903 336 GPLVSRAQLAAVRAGLAA-LRAQAEVLFDGggfalVDADPAVAACVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDA 414
|
410 420 430
....*....|....*....|....*....|...
gi 1140776579 377 DEMIKMANDSRHGLGGAIYTADVKHGNQLATKI 409
Cdd:PRK11903 415 AHALALARRGQGSLVASVYSDDAAFLAAAALEL 447
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
7-435 |
1.14e-17 |
|
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: 85.33 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYN-GEVIQEFTDTTDKEIEDLLDKAESYYQKAKRVDFAKRADLLNR----LAGEFeanledYARLSSTNMgklIGESR 81
Cdd:cd07123 52 MPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKaadlLSGKY------RYELNAATM---LGQGK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 82 T----EVNKI----------VNYARYFATQgpaflQPKNYDKlsvGSTAHVEFSSI-GIVLAVEPWNFPFTQVMRVFAPN 146
Cdd:cd07123 123 NvwqaEIDAAcelidflrfnVKYAEELYAQ-----QPLSSPA---GVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 147 fILGNPVILKHASIVPQAAQAFEKACQKVGIPEGAFANIFATHDQI-DKIIDDPRVQGFALTGS--------EQAGSNLA 217
Cdd:cd07123 195 -LMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVgDTVLASPHLAGLHFTGStptfkslwKQIGENLD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 218 AkaTKNLMKTTLELGGTDIFAVLDDADIDKaakdaaqarLANA---------GQVCTAAKRYLVSDKIYDEFLDKVKREF 288
Cdd:cd07123 274 R--YRTYPRIVGETGGKNFHLVHPSADVDS---------LVTAtvrgafeyqGQKCSAASRAYVPESLWPEVKERLLEEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 289 DTYQPGNPLNEETTLAPLSSQSAKEKLQEQVEKVVAG-GSKILYGNlNVDEGPGFQFSPIILTGMERNNPMYDEELFGPV 367
Cdd:cd07123 343 KEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGG-KCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPV 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1140776579 368 AQIYRFSSED--EMIKMAND-SRHGLGGAIYTADVKHGNQLATKIE--TGQVAINQ-----VLDEQaevPFGGVKSSG 435
Cdd:cd07123 422 LTVYVYPDSDfeETLELVDTtSPYALTGAIFAQDRKAIREATDALRnaAGNFYINDkptgaVVGQQ---PFGGARASG 496
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
25-455 |
3.48e-15 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 77.46 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 25 IEDLLDKAESYYQKAKRVDFAKRADLLNRLAGEFEANLEDYARLSSTNMGKLIGES-RTEVNKIVNYARYFATQGPAFLQ 103
Cdd:PLN02203 8 LEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyRDEVGVLTKSANLALSNLKKWMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 104 PKNYD--KLSVGSTAHVEFSSIGIVLAVEPWNFPFTQVMRVFAPNFILGNPVILKHASIVPQAAQAFEKACQK------V 175
Cdd:PLN02203 88 PKKAKlpLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKyldskaV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 176 GIPEG--AFANIFATHdQIDKIIddprvqgfaLTGSEQAGSNLAAKATKNLMKTTLELGGTdIFAVLDDADIDKAAKDAA 253
Cdd:PLN02203 168 KVIEGgpAVGEQLLQH-KWDKIF---------FTGSPRVGRIIMTAAAKHLTPVALELGGK-CPCIVDSLSSSRDTKVAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 254 QARLAN-----AGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPlNEETTLAPLSSQSAKEKLQEQVE-KVVAggS 327
Cdd:PLN02203 237 NRIVGGkwgscAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENP-RESKSMARILNKKHFQRLSNLLKdPRVA--A 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 328 KILYGNlNVDEGPGFqFSPIILTgmernNPMYD-----EELFGPVAQIYRFSSEDEMIKMANDSRHGLggAIY--TADVK 400
Cdd:PLN02203 314 SIVHGG-SIDEKKLF-IEPTILL-----NPPLDsdimtEEIFGPLLPIITVKKIEDSIAFINSKPKPL--AIYafTNNEK 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1140776579 401 HGNQLATKIETGQVAINQVLDEQA--EVPFGGVKSSGYGRELSDWGIYEFANIKTVL 455
Cdd:PLN02203 385 LKRRILSETSSGSVTFNDAIIQYAcdSLPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
7-437 |
1.15e-13 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 73.47 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 7 NPYN-GEVIQEFTDTTDKEIEDLLDKAesyyQKAKRVDFAK----RADLLNRLAGEFEANLEdyarlssTNMGKLIGES- 80
Cdd:PRK11809 665 NPADpRDIVGYVREATPAEVEQALESA----VNAAPIWFATppaeRAAILERAADLMEAQMQ-------TLMGLLVREAg 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 81 RT------EVNKIVNYARYFATQgpaflqpknydklsvgstAHVEFSS-----IGIVLAVEPWNFP---FT-QVMRVFAP 145
Cdd:PRK11809 734 KTfsnaiaEVREAVDFLRYYAGQ------------------VRDDFDNdthrpLGPVVCISPWNFPlaiFTgQVAAALAA 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 146 nfilGNPVILKHASIVPQ-AAQAFeKACQKVGIPEGAFANIFATHDQID-KIIDDPRVQGFALTGSEQAGS----NLAAK 219
Cdd:PRK11809 796 ----GNSVLAKPAEQTPLiAAQAV-RILLEAGVPAGVVQLLPGRGETVGaALVADARVRGVMFTGSTEVARllqrNLAGR 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 220 ATKNLMKTTL--ELGGTDIFAVLDDADIDKAAKDAAQARLANAGQVCTAAKRYLVSDKIYDEFLDKVKREFDTYQPGNPL 297
Cdd:PRK11809 871 LDPQGRPIPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPD 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 298 NEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILygNLNVDEGPGFQFSPIIL-TGMERNNpmYDE---ELFGPVAQIYRF 373
Cdd:PRK11809 951 RLSTDIGPVIDAEAKANIERHIQAMRAKGRPVF--QAARENSEDWQSGTFVPpTLIELDS--FDElkrEVFGPVLHVVRY 1026
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1140776579 374 SSE--DEMIKMANDSRHGLGGAIYTADVKHGNQLATKIETGQVAINQ-----VLDEQaevPFGGVKSSGYG 437
Cdd:PRK11809 1027 NRNqlDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRnmvgaVVGVQ---PFGGEGLSGTG 1094
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
142-398 |
2.68e-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: 56.01 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 142 VFAP-NFIL---------------GNPVILK----HASIVPQAAQAFEKACQKVGIPEGAFANIFAT-HDQIDKIIDDPR 200
Cdd:cd07129 111 VFGAsNFPLafsvaggdtasalaaGCPVVVKahpaHPGTSELVARAIRAALRATGLPAGVFSLLQGGgREVGVALVKHPA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 201 VQGFALTGSEQAGSNLAAKATKnlmKTT-----LELGGTDIFAVLDDAdidkaaKDAAQARLA---------NAGQVCTa 266
Cdd:cd07129 191 IKAVGFTGSRRGGRALFDAAAA---RPEpipfyAELGSVNPVFILPGA------LAERGEAIAqgfvgsltlGAGQFCT- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 267 aKRYLV---SDKIYDEFLDKVKREFDTYQPGNPLNEETTLAplsSQSAKEKLQEQ--VEKVVAGGSKilygnlnvdeGPG 341
Cdd:cd07129 261 -NPGLVlvpAGPAGDAFIAALAEALAAAPAQTMLTPGIAEA---YRQGVEALAAApgVRVLAGGAAA----------EGG 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1140776579 342 FQFSPIIL--TGME-RNNPMYDEELFGPVAQIYRFSSEDEMIKMANdSRHG-LGGAIYTAD 398
Cdd:cd07129 327 NQAAPTLFkvDAAAfLADPALQEEVFGPASLVVRYDDAAELLAVAE-ALEGqLTATIHGEE 386
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|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
82-398 |
9.61e-08 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 54.41 E-value: 9.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 82 TEVNKIVNYARYFATQGpaflqpkNYDKLSVGSTAHVEFSSIGIVLAVEP---WN-FPftqvmRVFApNFILGNPVILK- 156
Cdd:cd07127 162 REMSRIPPTAEWEKPQG-------KHDPLAMEKTFTVVPRGVALVIGCSTfptWNgYP-----GLFA-SLATGNPVIVKp 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 157 H-ASIVPQAAQAfeKACQKVGIPEGAFANI--FATHDQIDKI----IDDPRVQGFALTGSEQAGSNLAAKATKNLMKTtl 229
Cdd:cd07127 229 HpAAILPLAITV--QVAREVLAEAGFDPNLvtLAADTPEEPIaqtlATRPEVRIIDFTGSNAFGDWLEANARQAQVYT-- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 230 ELGGTDIfAVLDDADIDKAAKDAAQARLA-NAGQVCTAAKRYLV-SDKI--------YDEFLDKVKREFDTYQpGNPLNE 299
Cdd:cd07127 305 EKAGVNT-VVVDSTDDLKAMLRNLAFSLSlYSGQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGLL-ADPARA 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 300 ETTLAPLSSQSAKEKLQE--QVEKVVAGGSKIlygnlnvdEGPGFQ----FSPIILTGMERNNPMYDEELFGPVAQIYRF 373
Cdd:cd07127 383 AALLGAIQSPDTLARIAEarQLGEVLLASEAV--------AHPEFPdarvRTPLLLKLDASDEAAYAEERFGPIAFVVAT 454
|
330 340
....*....|....*....|....*...
gi 1140776579 374 SSEDEMIKMANDS--RHG-LGGAIYTAD 398
Cdd:cd07127 455 DSTDHSIELARESvrEHGaMTVGVYSTD 482
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
264-411 |
5.62e-03 |
|
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: 38.76 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 264 CTAAKRYLVSDKIYDEFLDKVKREfDTYQpgnpLNEETTLAPLSSQSAKEKLQEQVEKVVAGGSKILYGNLNVDEGPGfq 343
Cdd:cd07121 240 CIAEKEVIAVDSVADYLIAAMQRN-GAYV----LNDEQAEQLLEVVLLTNKGATPNKKWVGKDASKILKAAGIEVPAD-- 312
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140776579 344 fSPIILTGMERNNPMYDEELFGPVAQIYRFSSEDEMIKMANDSRHGL--GGAIYTADVKHGNQLATKIET 411
Cdd:cd07121 313 -IRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTKMARAMQT 381
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