|
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: 737.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 25 VEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVKLCAQIARYYADNAKSFLA 104
Cdd:cd07100 1 IEAALDRAHAAFLA-WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 105 PVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREAGAPEGAWTNL 184
Cdd:cd07100 80 DEPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 185 FISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCT 264
Cdd:cd07100 160 LIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 265 AAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEAVKNGAKLHLGGKAVAREGNFFEP 344
Cdd:cd07100 240 AAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 345 TILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYINWLTDTAPEL 424
Cdd:cd07100 320 TVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRL 399
|
410 420 430
....*....|....*....|....*....|
gi 488976554 425 PFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07100 400 PFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
1-452 |
1.15e-171 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 489.63 E-value: 1.15e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 1 MAYQTVNPANNQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQ 80
Cdd:PRK09406 1 MPIATINPATGETVKTFTALTDDEVDAAIARAHARFRD-YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 81 SRGEVKLCAQIARYYADNAKSFLAPVkyPSELG-----EAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAK 155
Cdd:PRK09406 80 AKAEALKCAKGFRYYAEHAEALLADE--PADAAavgasRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 156 HASIVPHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDV 235
Cdd:PRK09406 158 HASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 236 FVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLS 315
Cdd:PRK09406 238 FIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 316 KQVDEAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQ 395
Cdd:PRK09406 318 KQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976554 396 DIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLV 452
Cdd:PRK09406 398 DEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
6-456 |
3.36e-168 |
|
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: 481.55 E-value: 3.36e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEV 85
Cdd:COG1012 26 INPATGEVLARVPAATAEDVDAAVAAARAAF-PAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 86 KLCAQIARYYADNAKSFLAPVkYPSELG--EAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHC 163
Cdd:COG1012 105 DRAADFLRYYAGEARRLYGET-IPSDAPgtRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 164 AETFAHLVREAGAPEGAWTNLFISQDQVAK-IIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDA 242
Cdd:COG1012 184 ALLLAELLEEAGLPAGVLNVVTGDGSEVGAaLVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 243 DLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEAV 322
Cdd:COG1012 264 DLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 323 KNGAKLHLGGKAVARE-GNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAK 401
Cdd:COG1012 344 AEGAELLTGGRRPDGEgGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARAR 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976554 402 RMASAIETGMVYIN-WLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVVRR 456
Cdd:COG1012 424 RVARRLEAGMVWINdGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
6-452 |
7.67e-161 |
|
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: 461.90 E-value: 7.67e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEV 85
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT-WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 86 KLCAQIARYYADNAKSFLAPVKYPSELG-EAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCA 164
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGkRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 165 ETFAHLVREAGAPEGAWTNLFISQDQVAK-IIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDAD 243
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEaLCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 244 LERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEAVK 323
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 324 NGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRM 403
Cdd:cd07103 321 KGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 488976554 404 ASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLV 452
Cdd:cd07103 401 AEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
3-452 |
5.10e-160 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 460.07 E-value: 5.10e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQADALYHsAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR 82
Cdd:pfam00171 9 IEVINPATGEVIATVPAATAEDVDAAIAAARAAFP-AWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 83 GEVKLCAQIARYYADNAKSfLAPVKYPSELGE-AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVP 161
Cdd:pfam00171 88 GEVDRAIDVLRYYAGLARR-LDGETLPSDPGRlAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 162 HCAETFAHLVREAGAPEGAWTNLFISQDQVAK-IIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLD 240
Cdd:pfam00171 167 LTALLLAELFEEAGLPAGVLNVVTGSGAEVGEaLVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 241 DADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDE 320
Cdd:pfam00171 247 DADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVED 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 321 AVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERA 400
Cdd:pfam00171 327 AKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERA 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 488976554 401 KRMASAIETGMVYIN-WLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLV 452
Cdd:pfam00171 407 LRVARRLEAGMVWINdYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
26-454 |
1.65e-150 |
|
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: 435.10 E-value: 1.65e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 26 EAALQQADAlYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVKLCAQIARYYADNAKSFLAP 105
Cdd:cd07078 1 DAAVAAARA-AFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 106 VKYPSELG-EAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREAGAPEGAWTNL 184
Cdd:cd07078 80 VIPSPDPGeLAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 185 FISQDQV-AKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVC 263
Cdd:cd07078 160 TGDGDEVgAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 264 TAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEAVKNGAKLHLGGKAVARE-GNFF 342
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkGYFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 343 EPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYINWLTDTA- 421
Cdd:cd07078 320 PPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAe 399
|
410 420 430
....*....|....*....|....*....|...
gi 488976554 422 PELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07078 400 PSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
5-452 |
1.56e-143 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 418.50 E-value: 1.56e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 5 TVNPANNQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGE 84
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRD-WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSFLAPVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCA 164
Cdd:PRK13968 90 VAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 165 ETFAHLVREAGAPEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADL 244
Cdd:PRK13968 170 QLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 245 ERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEAVKN 324
Cdd:PRK13968 250 ELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 325 GAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMA 404
Cdd:PRK13968 330 GARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMA 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 488976554 405 SAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLV 452
Cdd:PRK13968 410 ARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
6-450 |
4.62e-128 |
|
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: 378.51 E-value: 4.62e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQAdALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEV 85
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERA-RAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 86 KLCAQIARYYADNAKSFLAPVKYPSELG-EAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCA 164
Cdd:cd07102 80 RGMLERARYMISIAEEALADIRVPEKDGfERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 165 ETFAHLVREAGAPEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADL 244
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 245 ERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEAVKN 324
Cdd:cd07102 240 DAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 325 GAKLHLGGK--AVAREG-NFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAK 401
Cdd:cd07102 320 GARALIDGAlfPEDKAGgAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAE 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 488976554 402 RMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQK 450
Cdd:cd07102 400 ALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPK 448
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
6-454 |
6.61e-126 |
|
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: 373.22 E-value: 6.61e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADaLYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEV 85
Cdd:cd07145 4 RNPANGEVIDTVPSLSREEVREAIEVAE-KAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 86 KLCAQIARYYADNAKSFLAPVkYPSELGE------AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASI 159
Cdd:cd07145 83 ERTIRLFKLAAEEAKVLRGET-IPVDAYEynerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 160 VPHCAETFAHLVREAGAPEGAWTNLFISQDQV-AKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVV 238
Cdd:cd07145 162 TPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 239 LDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQV 318
Cdd:cd07145 242 LKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 319 DEAVKNGAKLHLGGKAVarEGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIE 398
Cdd:cd07145 322 NDAVEKGGKILYGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDIN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976554 399 RAKRMASAIETGMVYINWLTDTAPE-LPFGGVKRSGYGRElsdlGIK----EFVNQKLVVV 454
Cdd:cd07145 400 RALKVARELEAGGVVINDSTRFRWDnLPFGGFKKSGIGRE----GVRytmlEMTEEKTIVI 456
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
5-454 |
1.93e-125 |
|
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: 371.88 E-value: 1.93e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 5 TVNPANNQLIKTYPAHSDADVEAALQQAD-ALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRG 83
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARaAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 84 EVKLCAQIARYYA---DNAKSFLAPVKYPSELgeAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIV 160
Cdd:cd07114 81 QVRYLAEWYRYYAglaDKIEGAVIPVDKGDYL--NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 161 PHCAETFAHLVREAGAPEGAwtnlfisqdqVAKIIADDRVQGAAL-----------TGSEKAGSVVAAQAAKHIKKSTLE 229
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGV----------VNVVTGFGPETGEALvehplvakiafTGGTETGRHIARAAAENLAPVTLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 230 LGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKD 309
Cdd:cd07114 229 LGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 310 ALDTLSKQVDEAVKNGAKLHLGGKAVARE----GNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSH 385
Cdd:cd07114 309 QLEKVERYVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSE 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488976554 386 YGLGGAVFSQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07114 389 YGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
6-454 |
4.06e-122 |
|
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: 363.89 E-value: 4.06e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALYHsAWAK-GDIEpRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGE 84
Cdd:cd07088 18 LNPATGEVVATVPAATAEDADRAVDAAEAAQK-AWERlPAIE-RAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSFLAPVkYPSEL-GE-AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPH 162
Cdd:cd07088 96 VEFTADYIDYMAEWARRIEGEI-IPSDRpNEnIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 163 CAETFAHLVREAGAPEGAWTNLFISQDQVAK-IIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDD 241
Cdd:cd07088 175 NALEFAELVDEAGLPAGVLNIVTGRGSVVGDaLVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 242 ADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEA 321
Cdd:cd07088 255 ADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 322 VKNGAKLHLGGKAVARE-GNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERA 400
Cdd:cd07088 335 VEAGATLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTA 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976554 401 KRMASAIETGMVYINwltDTAPELPFG---GVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07088 415 MRATNELEFGETYIN---RENFEAMQGfhaGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
4-452 |
9.05e-122 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 364.01 E-value: 9.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 4 QTVNPANNQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRG 83
Cdd:PLN02278 43 PVYNPATGEVIANVPCMGRAETNDAIASAHDAFPS-WSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 84 EVKLCAQIARYYADNAK---SFLAPVKYPSelGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIV 160
Cdd:PLN02278 122 EVAYGASFLEYFAEEAKrvyGDIIPSPFPD--RRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 161 PHCAETFAHLVREAGAPEGAWTNLFISQDQV-AKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVL 239
Cdd:PLN02278 200 PLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 240 DDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVD 319
Cdd:PLN02278 280 DDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQ 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 320 EAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIER 399
Cdd:PLN02278 360 DAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQR 439
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 488976554 400 AKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLV 452
Cdd:PLN02278 440 AWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
24-454 |
7.13e-119 |
|
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: 354.14 E-value: 7.13e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 24 DVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVKLCAQIARyyadNAKSFL 103
Cdd:cd07104 1 DVDRAYAAAAAAQ-KAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILR----EAAGLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 104 APVK---YPSELG--EAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAET-FAHLVREAGAP 177
Cdd:cd07104 76 RRPEgeiLPSDVPgkESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLlIAEIFEEAGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 178 EGAWTNLFISQDQV-AKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAVKIGVQARL 256
Cdd:cd07104 156 KGVLNVVPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 257 NNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEAVKNGAKLHLGGKAva 336
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 337 rEGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYINW 416
Cdd:cd07104 314 -EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 488976554 417 LT-DTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07104 393 QTvNDEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
7-454 |
2.31e-117 |
|
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: 351.25 E-value: 2.31e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 7 NPANNQLIKTYPAHSDADVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVK 86
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAF-PAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 87 LCAQIARYYADNAKSFLAPVkYPSEL-GE-AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCA 164
Cdd:cd07150 84 FTPELLRAAAGECRRVRGET-LPSDSpGTvSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 165 ETFAHLVREAGAPEGAWTNLFISQDQVA-KIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDAD 243
Cdd:cd07150 163 LKIAEIMEEAGLPKGVFNVVTGGGAEVGdELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 244 LERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEAVK 323
Cdd:cd07150 243 LDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 324 NGAKLHLGGKavaREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRM 403
Cdd:cd07150 323 KGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 488976554 404 ASAIETGMVYINWLT-DTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07150 400 AERLESGMVHINDPTiLDEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
6-453 |
1.55e-116 |
|
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: 349.49 E-value: 1.55e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRG-E 84
Cdd:cd07138 19 INPATEEVIGTVPLGTAADVDRAVAAARRAF-PAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAaQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSFlapvKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCA 164
Cdd:cd07138 98 VGLGIGHLRAAADALKDF----EFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 165 ETFAHLVREAGAPEGAWtNLfisqdqvakIIADDRVQGAAL-----------TGSEKAGSVVAAQAAKHIKKSTLELGGN 233
Cdd:cd07138 174 IILAEILDEAGLPAGVF-NL---------VNGDGPVVGEALsahpdvdmvsfTGSTRAGKRVAEAAADTVKRVALELGGK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 234 DVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDT 313
Cdd:cd07138 244 SANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 314 LSKQVDEAVKNGAKLHLGGK---AVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGG 390
Cdd:cd07138 324 VQGYIQKGIEEGARLVAGGPgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAG 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488976554 391 AVFSQDIERAKRMASAIETGMVYINWlTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVV 453
Cdd:cd07138 404 YVWSADPERARAVARRLRAGQVHING-AAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
3-454 |
1.35e-115 |
|
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: 347.27 E-value: 1.35e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQADALYHSA-WAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS 81
Cdd:cd07091 21 FPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 82 -RGEVKLCAQIARYYA-----------DNAKSFLAPVKypselgeawveHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAG 149
Cdd:cd07091 101 aKGDVALSIKCLRYYAgwadkiqgktiPIDGNFLAYTR-----------REPIGVCGQIIPWNFPLLMLAWKLAPALAAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 150 NPVIAKHASIVPHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIADD-RVQGAALTGSEKAGSVVAAQAAK-HIKKST 227
Cdd:cd07091 170 NTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 228 LELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSS 307
Cdd:cd07091 250 LELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 308 KDALDTLSKQVDEAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYG 387
Cdd:cd07091 330 KAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYG 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976554 388 LGGAVFSQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07091 410 LAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
5-437 |
3.12e-115 |
|
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: 345.70 E-value: 3.12e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 5 TVNPANNQLIKTYPAHSDADVEAALQQA-DALYhsAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR- 82
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAkEAFP--GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 83 GEVKLCAQIARYYADNAKSfLAPVKYPSELGE-AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVP 161
Cdd:cd07093 79 RDIPRAAANFRFFADYILQ-LDGESYPQDGGAlNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 162 HCAETFAHLVREAGAPEGAWtNLFISQDQVA--KIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVL 239
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVV-NVVHGFGPEAgaALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 240 DDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVD 319
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 320 EAVKNGAKLHLGGKAVA----REGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQ 395
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 488976554 396 DIERAKRMASAIETGMVYIN-WLTDTAPeLPFGGVKRSGYGRE 437
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNcWLVRDLR-TPFGGVKASGIGRE 438
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
6-448 |
9.49e-114 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 341.82 E-value: 9.49e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEV 85
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG-WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 86 KLCAQIARYYADNAksflAPVKYPSELGEAWVE--HHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHC 163
Cdd:cd07106 81 GGAVAWLRYTASLD----LPDEVIEDDDTRRVElrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 164 AETFAHLVREAgAPEGawtnlfisqdqVAKIIADDRVQGAAL-----------TGSEKAGSVVAAQAAKHIKKSTLELGG 232
Cdd:cd07106 157 TLKLGELAQEV-LPPG-----------VLNVVSGGDELGPALtshpdirkisfTGSTATGKKVMASAAKTLKRVTLELGG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 233 NDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALD 312
Cdd:cd07106 225 NDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 313 TLSKQVDEAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAV 392
Cdd:cd07106 305 KVKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASV 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976554 393 FSQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVN 448
Cdd:cd07106 385 WSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQ 440
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
6-454 |
9.92e-114 |
|
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: 341.92 E-value: 9.92e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQA-DALYHSAWAKgDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRG- 83
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAArRAFDTGDWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 84 EVKLCAQIARYYADNAKSFLAPVKYPS-----ELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHAS 158
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVpalrgGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 159 IVPHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIADD-RVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFV 237
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 238 VLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQ 317
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 318 VDEAVKNGAKLHLGGKAVAR--EGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQ 395
Cdd:cd07089 321 IARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976554 396 DIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07089 401 DVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
6-454 |
1.66e-112 |
|
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: 338.64 E-value: 1.66e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADAlYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEV 85
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARA-GAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 86 KLCAQIARYYADNAK-----SFLAPVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIV 160
Cdd:cd07094 83 DRAIDTLRLAAEEAErirgeEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 161 PHCAETFAHLVREAGAPEGAWTNLFISQDQVA-KIIADDRVQGAALTGSEKAGSVVAAQAAkhIKKSTLELGGNDVFVVL 239
Cdd:cd07094 163 PLSALELAKILVEAGVPEGVLQVVTGEREVLGdAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 240 DDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVD 319
Cdd:cd07094 241 RDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 320 EAVKNGAKLHLGGKavaREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIER 399
Cdd:cd07094 321 EAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976554 400 AKRMASAIETGMVYINWLTD-TAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07094 398 AFKAAEKLEVGGVMVNDSSAfRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
7-454 |
2.63e-112 |
|
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: 338.03 E-value: 2.63e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 7 NPANNQLIKTYPAHSDADVEAALQQADALYHSAwAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVK 86
Cdd:cd07149 5 SPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM-KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 87 LCAQIARYYADNAKSfLAPVKYP---SELGE---AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIV 160
Cdd:cd07149 84 RAIETLRLSAEEAKR-LAGETIPfdaSPGGEgriGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 161 PHCAETFAHLVREAGAPEGAWTNLFISQDQVAK-IIADDRVQGAALTGSEKAGSVVAAQAAkhIKKSTLELGGNDVFVVL 239
Cdd:cd07149 163 PLSALKLAELLLEAGLPKGALNVVTGSGETVGDaLVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 240 DDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVD 319
Cdd:cd07149 241 ADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 320 EAVKNGAKLHLGGKavaREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIER 399
Cdd:cd07149 321 EAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQK 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976554 400 AKRMASAIETGMVYINWLTD-TAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07149 398 ALKAARELEVGGVMINDSSTfRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
6-454 |
2.47e-111 |
|
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: 335.73 E-value: 2.47e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALyHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEV 85
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAA-QRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 86 KLCAQIARYYADNAKSFLAPVKYPSELG----EAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVP 161
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRKVPTGLLmpnkKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 162 HCAETFAHLVREAGAPEGAWTnLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDD 241
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQ-VVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 242 ADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEA 321
Cdd:cd07099 239 ADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 322 VKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAK 401
Cdd:cd07099 319 VAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAE 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 488976554 402 RMASAIETGMVYIN--WLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07099 399 AIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
3-456 |
3.49e-111 |
|
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: 335.81 E-value: 3.49e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQAdALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR 82
Cdd:cd07151 12 IDVLNPYTGETLAEIPAASKEDVDEAYRAA-AAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKAN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 83 GEVKLCAQIARyyadNAKSFLAPVK-----YPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHA 157
Cdd:cd07151 91 IEWGAAMAITR----EAATFPLRMEgrilpSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 158 SIVPHCAET-FAHLVREAGAPEGAWTNLfisqdqVAKI--IADDRVQGA-----ALTGSEKAGSVVAAQAAKHIKKSTLE 229
Cdd:cd07151 167 SDTPITGGLlLAKIFEEAGLPKGVLNVV------VGAGseIGDAFVEHPvprliSFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 230 LGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKD 309
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 310 ALDTLSKQVDEAVKNGAKLHLGGKAvarEGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLG 389
Cdd:cd07151 321 QVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLS 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976554 390 GAVFSQDIERAKRMASAIETGMVYINWLT-DTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVVRR 456
Cdd:cd07151 398 GAVFTSDLERGVQFARRIDAGMTHINDQPvNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQH 465
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
37-454 |
2.30e-110 |
|
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: 330.35 E-value: 2.30e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 37 HSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVKLCAQIARYYADNAKSFLAPVKYPSELG-EA 115
Cdd:cd06534 7 FKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGgEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 116 WVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREAGAPEGAWTNLFISQDQV-AKI 194
Cdd:cd06534 87 YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVgAAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 195 IADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHEN 274
Cdd:cd06534 167 LSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHES 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 275 IADAFLTKFSeafrqvkigdpldesttlgplsskdaldtlskqvdeavkngaklhlggkavaregnffepTILTGITRDN 354
Cdd:cd06534 247 IYDEFVEKLV------------------------------------------------------------TVLVDVDPDM 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 355 PAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYINWLTDTA-PELPFGGVKRSG 433
Cdd:cd06534 267 PIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgPEAPFGGVKNSG 346
|
410 420
....*....|....*....|.
gi 488976554 434 YGRELSDLGIKEFVNQKLVVV 454
Cdd:cd06534 347 IGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
4-452 |
5.49e-110 |
|
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: 333.22 E-value: 5.49e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 4 QTVNPANNQLIKTYPAHSDADVEAALQQADALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGK-LIKQSR 82
Cdd:cd07144 26 KTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKpYHSNAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 83 GEVKLCAQIARYYADNAKSFLAPVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPH 162
Cdd:cd07144 106 GDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 163 CAETFAHLVREAGAPEGAwTNLFISQDQVA--KIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLD 240
Cdd:cd07144 186 SLLYFANLVKEAGFPPGV-VNIIPGYGAVAgsALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 241 DADLERAVK---IGVqarLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQV-KIGDPLDESTTLGPLSSKDALDTLSK 316
Cdd:cd07144 265 DADLDQAVKwaaAGI---MYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDTVVGPQVSKTQYDRVLS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 317 QVDEAVKNGAKLHLGGKAVARE---GNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVF 393
Cdd:cd07144 342 YIEKGKKEGAKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVF 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976554 394 SQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLV 452
Cdd:cd07144 422 TKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
8-452 |
6.73e-110 |
|
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: 331.99 E-value: 6.73e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 8 PANNQLIKTYPAHSDADVEAALQQA-DALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVK 86
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAArKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 87 LCAQIARYYADNAKSfLAPVKYPSeLGE---AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHC 163
Cdd:cd07118 84 GAADLWRYAASLART-LHGDSYNN-LGDdmlGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 164 AETFAHLVREAGAPEGAWTNLFISQDQVAKIIADD-RVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDA 242
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHpDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 243 DLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEAV 322
Cdd:cd07118 242 DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 323 KNGAKLHLGGKAVA-REGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAK 401
Cdd:cd07118 322 AEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 488976554 402 RMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLV 452
Cdd:cd07118 402 TVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
5-450 |
2.35e-109 |
|
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: 331.58 E-value: 2.35e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 5 TVNPANNQLIKTYPAHSDADVEAALQQA-DALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRG 83
Cdd:cd07119 17 IINPANGEVIATVPEGTAEDAKRAIAAArRAFDSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 84 EVKLCAQIARYYADNAKS---FLAPVKYPSElgeAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIV 160
Cdd:cd07119 97 DIDDVANCFRYYAGLATKetgEVYDVPPHVI---SRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 161 PHCAETFAHLVREAGAPEGAWTNLFISQDQV-AKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVL 239
Cdd:cd07119 174 PLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 240 DDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVD 319
Cdd:cd07119 254 ADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 320 EAVKNGAKLHLGGKAVA----REGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQ 395
Cdd:cd07119 334 LGKEEGARLVCGGKRPTgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTK 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 488976554 396 DIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQK 450
Cdd:cd07119 414 DIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETK 468
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
6-454 |
3.86e-109 |
|
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: 330.69 E-value: 3.86e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQA-DALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR-G 83
Cdd:cd07139 19 VSPATEEVVGRVPEATPADVDAAVAAArRAFDNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRrA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 84 EVKLCAQIARYYADNAKSFLAP-VKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPH 162
Cdd:cd07139 99 QGPGPAALLRYYAALARDFPFEeRRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 163 CAETFAHLVREAGAPEGawtnlfisqdqVAKIIADDRVQGAAL-----------TGSEKAGSVVAAQAAKHIKKSTLELG 231
Cdd:cd07139 179 DAYLLAEAAEEAGLPPG-----------VVNVVPADREVGEYLvrhpgvdkvsfTGSTAAGRRIAAVCGERLARVTLELG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 232 GNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDAL 311
Cdd:cd07139 248 GKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 312 DTLSKQVDEAVKNGAKLHLGGKAVAR--EGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLG 389
Cdd:cd07139 328 ERVEGYIAKGRAEGARLVTGGGRPAGldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLS 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976554 390 GAVFSQDIERAKRMASAIETGMVYINWLTdTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07139 408 GSVWTADVERGLAVARRIRTGTVGVNGFR-LDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
24-452 |
3.98e-109 |
|
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: 329.15 E-value: 3.98e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 24 DVEAALQQADALYHsAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVKLCAQIARYYADNAKSF- 102
Cdd:cd07105 1 DADQAVEAAAAAFP-AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 103 --LAPVKYPSELgeAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREAGAPEGA 180
Cdd:cd07105 80 ggSIPSDKPGTL--AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 181 WTNLFISQDQVAKI----IADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAVKIGVQARL 256
Cdd:cd07105 158 LNVVTHSPEDAPEVvealIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 257 NNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDpldesTTLGPLSSKDALDTLSKQVDEAVKNGAKLHLGGKAVA 336
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 337 RE-GNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYIN 415
Cdd:cd07105 313 SPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
410 420 430
....*....|....*....|....*....|....*...
gi 488976554 416 WLT-DTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLV 452
Cdd:cd07105 393 GMTvHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
6-455 |
5.54e-108 |
|
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: 327.86 E-value: 5.54e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRG-E 84
Cdd:cd07113 20 TNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSF----LAPvKYPSELGE---AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHA 157
Cdd:cd07113 100 VGQSANFLRYFAGWATKIngetLAP-SIPSMQGErytAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 158 SIVPHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFV 237
Cdd:cd07113 179 EFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 238 VLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQ 317
Cdd:cd07113 259 FLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 318 VDEAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDI 397
Cdd:cd07113 339 LDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNL 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 488976554 398 ERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVVR 455
Cdd:cd07113 419 SKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-437 |
8.55e-108 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 327.28 E-value: 8.55e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPAN-NQLIKTYPAHSDADVEAALQQADALYHsAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGE 84
Cdd:cd07097 19 RNPSDtSDVVGKYARASAEDADAAIAAAAAAFP-AWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSfLAPVKYPSELGEAWVEHH--PIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPH 162
Cdd:cd07097 98 VTRAGQIFRYYAGEALR-LSGETLPSTRPGVEVETTrePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 163 CAETFAHLVREAGAPEGAWTNLFISQDQV-AKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDD 241
Cdd:cd07097 177 SAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 242 ADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEA 321
Cdd:cd07097 257 ADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 322 VKNGAKLHLGGKAVAR--EGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIER 399
Cdd:cd07097 337 RSEGAKLVYGGERLKRpdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKH 416
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 488976554 400 AKRMASAIETGMVYINwlTDTA---PELPFGGVKRSGYG-RE 437
Cdd:cd07097 417 ATHFKRRVEAGVVMVN--LPTAgvdYHVPFGGRKGSSYGpRE 456
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
8-454 |
1.11e-105 |
|
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: 321.18 E-value: 1.11e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 8 PANNQLIKTYPAHSDADVEAALQQADALyHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVKL 87
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 88 CAQIARYYADNAKSFLAPVKYPSE---LGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCA 164
Cdd:cd07101 82 VAIVARYYARRAERLLKPRRRRGAipvLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 165 ETFAHLVREAGAPEGAWTNLFISQDQVAKIIADdRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADL 244
Cdd:cd07101 162 LWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVD-NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 245 ERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEAVKN 324
Cdd:cd07101 241 DKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 325 GAKLHLGGKAVAREGN-FFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRM 403
Cdd:cd07101 321 GATVLAGGRARPDLGPyFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976554 404 ASAIETGMVYIN------WLTDTApelPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07101 401 AARLRAGTVNVNegyaaaWASIDA---PMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
7-455 |
1.77e-105 |
|
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: 321.44 E-value: 1.77e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 7 NPANNQLIKTYPAHSDADVEAALQQADALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVK 86
Cdd:cd07082 22 SPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 87 LCAQIARYYADNAK----SFLAPVKYPSELG-EAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVP 161
Cdd:cd07082 102 RTIDYIRDTIEELKrldgDSLPGDWFPGTKGkIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 162 HCAETFAHLVREAGAPEGAWTNLFI-SQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAakHIKKSTLELGGNDVFVVLD 240
Cdd:cd07082 182 LLGIPLAEAFHDAGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQH--PMKRLVLELGGKDPAIVLP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 241 DADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDE 320
Cdd:cd07082 260 DADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 321 AVKNGAKLHLGGKAvaREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERA 400
Cdd:cd07082 340 AVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKA 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 401 KRMASAIETGMVYINWLTDTAPE-LPFGGVKRSGYGRElsdlGIKE----FVNQKLVVVR 455
Cdd:cd07082 418 RKLADALEVGTVNINSKCQRGPDhFPFLGRKDSGIGTQ----GIGDalrsMTRRKGIVIN 473
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
3-437 |
4.64e-105 |
|
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: 320.28 E-value: 4.64e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR 82
Cdd:cd07086 15 FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE-WRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 83 GEVKLCAQIARYYADNAKSFLAPVkYPSE-----LGEAWvehHPIGVLLAVEPWNFPyyqlIRV----LAPNLAAGNPVI 153
Cdd:cd07086 94 GEVQEMIDICDYAVGLSRMLYGLT-IPSErpghrLMEQW---NPLGVVGVITAFNFP----VAVpgwnAAIALVCGNTVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 154 AKHASIVPHCA----ETFAHLVREAGAPEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLE 229
Cdd:cd07086 166 WKPSETTPLTAiavtKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 230 LGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKD 309
Cdd:cd07086 246 LGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 310 ALDTLSKQVDEAVKNGAKLHLGGKAVAR--EGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYG 387
Cdd:cd07086 326 AVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQG 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 488976554 388 LGGAVFSQDIERAKRM--ASAIETGMVYINWLTDTApE--LPFGGVKRSGYGRE 437
Cdd:cd07086 406 LSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGA-EigGAFGGEKETGGGRE 458
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
5-454 |
1.72e-104 |
|
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: 318.23 E-value: 1.72e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 5 TVNPANNQLIKTYPAHSDADVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRG- 83
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAF-EAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 84 EVKLCAQIARYYADNAKSF---LAPVKyPSELGeaWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIV 160
Cdd:cd07115 80 DVPRAADTFRYYAGWADKIegeVIPVR-GPFLN--YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 161 PHCAETFAHLVREAGAPEGAwTNLFISQDQVA--KIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVV 238
Cdd:cd07115 157 PLSALRIAELMAEAGFPAGV-LNVVTGFGEVAgaALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 239 LDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQV 318
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 319 DEAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIE 398
Cdd:cd07115 316 DVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976554 399 RAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07115 396 RAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
3-453 |
1.89e-104 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 318.91 E-value: 1.89e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPAN-NQLIKTYPAHSDADVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS 81
Cdd:cd07131 16 FDSRNPADlEEVVGTFPLSTASDVDAAVEAAREAF-PEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 82 RGEVKLCAQIARYYADNAKSFLAPVkYPSELGE--AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASI 159
Cdd:cd07131 95 RGDVQEAIDMAQYAAGEGRRLFGET-VPSELPNkdAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAED 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 160 VPHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIAD-DRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVV 238
Cdd:cd07131 174 TPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEhPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 239 LDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQV 318
Cdd:cd07131 254 MDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 319 DEAVKNGAKLHLGGKAVAR----EGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFS 394
Cdd:cd07131 334 EIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYT 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 395 QDIERAKRMASAIETGMVYINWLTDTAP-ELPFGGVKRSGYGRELSDLGIKEFVNQKLVV 453
Cdd:cd07131 414 EDVNKAFRARRDLEAGITYVNAPTIGAEvHLPFGGVKKSGNGHREAGTTALDAFTEWKAV 473
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
3-454 |
1.89e-104 |
|
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: 318.15 E-value: 1.89e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQAdALYHSAWAKGDiepRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR 82
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALA-ASYRSTLTRYQ---RSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 83 GEVKLCAQIARYYA-----DNAKSFLAPVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHA 157
Cdd:cd07146 77 YEVGRAADVLRFAAaealrDDGESFSCDLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 158 SIVPHCAETFAHLVREAGAPEGAW---TNLFisQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAkhIKKSTLELGGND 234
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLsvvTGEP--GEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 235 VFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTL 314
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 315 SKQVDEAVKNGAKLHLGGKavaREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFS 394
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976554 395 QDIERAKRMASAIETGMVYINWLTDTAPEL-PFGGVKRSGYG-RELSDLGIKEFVNQKLVVV 454
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNEVPGFRSELsPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
8-456 |
2.45e-103 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 317.59 E-value: 2.45e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 8 PANNQLIKTYPAHSDADVEAALQQADALyHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVKL 87
Cdd:PRK09407 39 PFTGEPLATVPVSTAADVEAAFARARAA-QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 88 CAQIARYYADNAKSFLAPVKYPSE---LGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCA 164
Cdd:PRK09407 118 VALTARYYARRAPKLLAPRRRAGAlpvLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 165 ETFAHLVREAGAPEGAWtnlfisqdQVakIIADDRVQGAAL---------TGSEKAGSVVAAQAAKHIKKSTLELGGNDV 235
Cdd:PRK09407 198 LAAVELLYEAGLPRDLW--------QV--VTGPGPVVGTALvdnadylmfTGSTATGRVLAEQAGRRLIGFSLELGGKNP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 236 FVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLS 315
Cdd:PRK09407 268 MIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVS 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 316 KQVDEAVKNGAKLHLGGKAVAREGN-FFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFS 394
Cdd:PRK09407 348 AHVDDAVAKGATVLAGGKARPDLGPlFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWT 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976554 395 QDIERAKRMASAIETGMVYIN------WLTDTApelPFGGVKRSGYGRELSDLGIKEFVNQKLVVVRR 456
Cdd:PRK09407 428 GDTARGRAIAARIRAGTVNVNegyaaaWGSVDA---PMGGMKDSGLGRRHGAEGLLKYTESQTIATQR 492
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
6-454 |
6.33e-103 |
|
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: 314.26 E-value: 6.33e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR-GE 84
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS-WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSFLAPVKypselGEaWVEHH-------PIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHA 157
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAA-----GE-YLPGHtsmirrePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 158 SIVPHCAETFAHLVREaGAPEGAWTNLFISQDQV-AKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVF 236
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 237 VVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSK 316
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 317 QVDEAvKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQD 396
Cdd:cd07092 314 FVERA-PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 488976554 397 IERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
6-454 |
9.55e-103 |
|
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: 313.79 E-value: 9.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEV 85
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 86 KLCAQIARYYADNAKSFLAPVkYPSELG-EAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCA 164
Cdd:cd07109 82 EAAARYFEYYGGAADKLHGET-IPLGPGyFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 165 ETFAHLVREAGAPEGAWtNLF--ISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDA 242
Cdd:cd07109 161 LRLAELAEEAGLPAGAL-NVVtgLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 243 DLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDEsTTLGPLSSKDALDTLSKQVDEAV 322
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 323 KNGAKLHLGGKAVA---REGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIER 399
Cdd:cd07109 319 ARGARIVAGGRIAEgapAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976554 400 AKRMASAIETGMVYIN-WLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07109 399 ALRVARRLRAGQVFVNnYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
5-455 |
3.71e-102 |
|
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: 312.32 E-value: 3.71e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 5 TVNPANNQLIKTYPAHSDADVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGE 84
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQ-KEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSfLAPVKYPseLGE---AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVP 161
Cdd:cd07090 80 IDSSADCLEYYAGLAPT-LSGEHVP--LPGgsfAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 162 HCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDD 241
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 242 ADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEA 321
Cdd:cd07090 237 ADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 322 VKNGAKLHLGGKAVARE-----GNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQD 396
Cdd:cd07090 317 KQEGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976554 397 IERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVVR 455
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVE 455
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
6-454 |
2.04e-101 |
|
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: 310.33 E-value: 2.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALYHSAWAKGDIEpRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEV 85
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHR-RAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 86 KLCAQIARYYADNAKSFLAPVK----YPSELG-EAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIV 160
Cdd:cd07147 83 ARAIDTFRIAAEEATRIYGEVLpldiSARGEGrQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 161 PHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKhiKKSTLELGGNDVFVVLD 240
Cdd:cd07147 163 PLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIVDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 241 DADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDE 320
Cdd:cd07147 241 DADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 321 AVKNGAKLHLGGKavaREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERA 400
Cdd:cd07147 321 AVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 488976554 401 KRMASAIETGMVYIN----WLTDtapELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07147 398 LRAWDELEVGGVVINdvptFRVD---HMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
6-453 |
4.66e-101 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 310.90 E-value: 4.66e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQA-DALYHSA---WAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS 81
Cdd:PLN02467 28 VNPATEETIGDIPAATAEDVDAAVEAArKAFKRNKgkdWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 82 RGEVKLCAQIARYYADNAKSF----LAPVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKH- 156
Cdd:PLN02467 108 AWDMDDVAGCFEYYADLAEALdakqKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPs 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 157 --ASIVphCAEtFAHLVREAGAPEGAW---TNLfiSQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELG 231
Cdd:PLN02467 188 elASVT--CLE-LADICREVGLPPGVLnvvTGL--GTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 232 GNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDAL 311
Cdd:PLN02467 263 GKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQY 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 312 DTLSKQVDEAVKNGAKLHLGGK--AVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLG 389
Cdd:PLN02467 343 EKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLA 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976554 390 GAVFSQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVV 453
Cdd:PLN02467 423 GAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQVT 486
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
5-453 |
5.29e-101 |
|
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: 309.28 E-value: 5.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 5 TVNPANNQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGE 84
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR-WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSFLA----PVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIV 160
Cdd:cd07110 80 VDDVAGCFEYYADLAEQLDAkaerAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 161 PHCAETFAHLVREAGAPEGAWTNLFISQDQV-AKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVL 239
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAgAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 240 DDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVD 319
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 320 EAVKNGAKLHLGGKAVA--REGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDI 397
Cdd:cd07110 320 RGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976554 398 ERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVV 453
Cdd:cd07110 400 ERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
5-437 |
5.93e-101 |
|
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: 309.77 E-value: 5.93e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 5 TVNPANNQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRG- 83
Cdd:cd07117 20 SYNPANGETLSEITDATDADVDRAVKAAQEAFKT-WRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 84 EVKLCAQIARYYADNAKSFLAPVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVP-- 161
Cdd:cd07117 99 DIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSls 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 162 --HCAETFAHLVreagaPEGAwTNLFISQDQVAK--IIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFV 237
Cdd:cd07117 179 llELAKIIQDVL-----PKGV-VNIVTGKGSKSGeyLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 238 VLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQ 317
Cdd:cd07117 253 IFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 318 VDEAVKNGAKLHLGGKAVARE----GNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVF 393
Cdd:cd07117 333 VDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVF 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 488976554 394 SQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRE 437
Cdd:cd07117 413 TKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRE 456
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
5-454 |
1.71e-99 |
|
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: 305.42 E-value: 1.71e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 5 TVNPANNQLIKTYPAHSDADVEAALQQA-DALYHSAWAKgDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRG 83
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAArRAFDETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 84 EVKLCAQIARYYADNAKSFLAPVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHC 163
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 164 AETFAHLVREA-GAPEGAwTNLFISQ--DQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLD 240
Cdd:cd07120 160 NAAIIRILAEIpSLPAGV-VNLFTESgsEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 241 DADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDE 320
Cdd:cd07120 239 DADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVER 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 321 AVKNGAK-LHLGGKAVAR--EGNFFEPTILTgiTRDNPAYF--EEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQ 395
Cdd:cd07120 319 AIAAGAEvVLRGGPVTEGlaKGAFLRPTLLE--VDDPDADIvqEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976554 396 DIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
3-439 |
1.82e-99 |
|
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: 305.68 E-value: 1.82e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQADALYHS-AWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS 81
Cdd:cd07112 4 FATINPATGRVLAEVAACDAADVDRAVAAARRAFESgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 82 R-GEVKLCAQIARYYADNA-KSF--LAPVKyPSELgeAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHA 157
Cdd:cd07112 84 LaVDVPSAANTFRWYAEAIdKVYgeVAPTG-PDAL--ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 158 SIVPHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIA--DDrVQGAALTGSEKAGSVVAAQAAK-HIKKSTLELGGND 234
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGlhMD-VDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 235 VFVVLDDA-DLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDT 313
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 314 LSKQVDEAVKNGAKLHLGGKAVARE--GNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGA 391
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRVLTEtgGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 488976554 392 VFSQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELS 439
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKS 447
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
2-455 |
3.01e-99 |
|
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: 305.61 E-value: 3.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 2 AYQTVNPANNQLIKTYPAHSDADVEAALQQADALYHSAWA-KGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQ 80
Cdd:cd07143 23 TVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGlKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 81 -SRGEVKLCAQIARYYADNAKSFLAPVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASI 159
Cdd:cd07143 103 aKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 160 VPHCAETFAHLVREAGAPEGAwTNLFISQDQVA--KIIADDRVQGAALTGSEKAGSVVAAQAAK-HIKKSTLELGGNDVF 236
Cdd:cd07143 183 TPLSALYMTKLIPEAGFPPGV-INVVSGYGRTCgnAISSHMDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 237 VVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSK 316
Cdd:cd07143 262 IVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 317 QVDEAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQD 396
Cdd:cd07143 342 YIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNN 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976554 397 IERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVVR 455
Cdd:cd07143 422 INNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
2-455 |
5.92e-98 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 302.21 E-value: 5.92e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 2 AYQTVNPANNQLIKTYPAHSDADVEAALQQADALYHsAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS 81
Cdd:PRK13473 18 KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP-EWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 82 RG-EVKLCAQIARYYADNAKSFLAPVKypselGE------AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIA 154
Cdd:PRK13473 97 LNdEIPAIVDVFRFFAGAARCLEGKAA-----GEyleghtSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 155 KHASIVPHCAETFAHLVREAgAPEGAwTNLFISQDQV--AKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGG 232
Cdd:PRK13473 172 KPSEITPLTALKLAELAADI-LPPGV-LNVVTGRGATvgDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 233 NDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALD 312
Cdd:PRK13473 250 KAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 313 TLSKQVDEAVKNG-AKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGA 391
Cdd:PRK13473 330 RVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASS 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976554 392 VFSQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVVR 455
Cdd:PRK13473 410 VWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
6-456 |
1.77e-97 |
|
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: 300.76 E-value: 1.77e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALyHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGK-LIKQSRGE 84
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAA-QREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKtMVDASLGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSFLAPVKYPSELGE----AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIV 160
Cdd:cd07098 80 ILVTCEKIRWTLKHGEKALRPESRPGGLLMfykrARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 161 PHCAETFAHLVREA---------------GAPEGAwtNLFISQDQVAKIIaddrvqgaaLTGSEKAGSVVAAQAAKHIKK 225
Cdd:cd07098 160 AWSSGFFLSIIREClaacghdpdlvqlvtCLPETA--EALTSHPVIDHIT---------FIGSPPVGKKVMAAAAESLTP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 226 STLELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPL 305
Cdd:cd07098 229 VVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 306 SSKDALDTLSKQVDEAVKNGAKLHLGGKAVAR----EGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLA 381
Cdd:cd07098 309 ISPARFDRLEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIA 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976554 382 NDSHYGLGGAVFSQDIERAKRMASAIETGMVYINWLTDT--APELPFGGVKRSGYGRELSDLGIKEFVNQKLVVVRR 456
Cdd:cd07098 389 NSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTEDR 465
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
3-437 |
2.64e-95 |
|
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: 295.41 E-value: 2.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR 82
Cdd:cd07559 18 FDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT-WGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 83 G-EVKLCAQIARYYAdnaKSFLAPVKYPSELGE---AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHAS 158
Cdd:cd07559 97 AaDIPLAIDHFRYFA---GVIRAQEGSLSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 159 IVP----HCAETFAHLVreagaPEGAwTNLFISQ-DQVAKIIAD-DRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGG 232
Cdd:cd07559 174 QTPlsilVLMELIGDLL-----PKGV-VNVVTGFgSEAGKPLAShPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 233 NDVFVVLDDA-----DLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSS 307
Cdd:cd07559 248 KSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 308 KDALDTLSKQVDEAVKNGAKLHLGGKAVARE----GNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLAND 383
Cdd:cd07559 328 KDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIAND 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 488976554 384 SHYGLGGAVFSQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRE 437
Cdd:cd07559 408 TEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRE 461
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
2-455 |
3.72e-93 |
|
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: 290.02 E-value: 3.72e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 2 AYQTVNPANNQLIKTYPAHSDADVEAALQQADALYH--SAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLI- 78
Cdd:cd07141 23 TFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFs 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 79 KQSRGEVKLCAQIARYYADNAKSFLAPVkYPSElGE--AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKH 156
Cdd:cd07141 103 KSYLVDLPGAIKVLRYYAGWADKIHGKT-IPMD-GDffTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 157 ASIVPHCAETFAHLVREAGAPEGAwTNLFISQDQVA--KIIADDRVQGAALTGSEKAGSVVAAQAAK-HIKKSTLELGGN 233
Cdd:cd07141 181 AEQTPLTALYLASLIKEAGFPPGV-VNVVPGYGPTAgaAISSHPDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 234 DVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDT 313
Cdd:cd07141 260 SPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 314 LSKQVDEAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVF 393
Cdd:cd07141 340 ILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVF 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976554 394 SQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVVR 455
Cdd:cd07141 420 TKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
7-450 |
4.69e-93 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 289.88 E-value: 4.69e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 7 NPANNQLIKTYPAHSDADVEAALQQAD-ALyhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEV 85
Cdd:PRK11241 32 NPANGDKLGSVPKMGADETRAAIDAANrAL--PAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 86 KLCAQIARYYADNAKSFLA---PVKYPSElgEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPH 162
Cdd:PRK11241 110 SYAASFIEWFAEEGKRIYGdtiPGHQADK--RLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 163 CAETFAHLVREAGAPEGAWTNLFISQDQVA-KIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDD 241
Cdd:PRK11241 188 SALALAELAIRAGIPAGVFNVVTGSAGAVGgELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 242 ADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEA 321
Cdd:PRK11241 268 ADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 322 VKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAK 401
Cdd:PRK11241 348 LEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVF 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 488976554 402 RMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQK 450
Cdd:PRK11241 428 RVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
5-454 |
1.54e-92 |
|
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: 287.72 E-value: 1.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 5 TVNPANNQLIKTYPAHSDADVEAALQQADALYHsAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIK-QSRG 83
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP-EWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 84 EVKLCAQIARYYADNAksflapvkypSEL-GE---------AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVI 153
Cdd:cd07108 80 EAAVLADLFRYFGGLA----------GELkGEtlpfgpdvlTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 154 AKHASIVPHCAETFAHLV----------------REAGAPegawtnlFISQDQVAKIiaddrvqgaALTGSEKAGSVVAA 217
Cdd:cd07108 150 LKAAEDAPLAVLLLAEILaqvlpagvlnvitgygEECGAA-------LVDHPDVDKV---------TFTGSTEVGKIIYR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 218 QAAKHIKKSTLELGGNDVFVVLDDADLERAVKiGVQA--RLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDP 295
Cdd:cd07108 214 AAADRLIPVSLELGGKSPMIVFPDADLDDAVD-GAIAgmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 296 LDESTTLGPLSSKDALDTLSKQVDEAVK-NGAKLHLGGK----AVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYV 370
Cdd:cd07108 293 LDEATDIGAIISEKQFAKVCGYIDLGLStSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 371 VKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKE-FVNQ 449
Cdd:cd07108 373 WKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMLEhFTQK 452
|
....*
gi 488976554 450 KLVVV 454
Cdd:cd07108 453 KTVNI 457
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
3-454 |
3.50e-92 |
|
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: 287.47 E-value: 3.50e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQA-DALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS 81
Cdd:cd07140 23 YNTINPTDGSVICKVSLATVEDVDRAVAAAkEAFENGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 82 -RGEVKLCAQIARYYA---DNAKSFLAPVK--YPSElGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAK 155
Cdd:cd07140 103 lKTHVGMSIQTFRYFAgwcDKIQGKTIPINqaRPNR-NLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 156 HASIVPHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIAD-DRVQGAALTGSEKAGSVVAAQAAK-HIKKSTLELGGN 233
Cdd:cd07140 182 PAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDhPDVRKLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 234 DVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDT 313
Cdd:cd07140 262 SPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 314 LSKQVDEAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKND--EEAIQLANDSHYGLGGA 391
Cdd:cd07140 342 LVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEYGLASG 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488976554 392 VFSQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07140 422 VFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
21-435 |
8.02e-92 |
|
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: 285.34 E-value: 8.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 21 SDADVEAALQQAdALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVKLCAQIARYYADNAK 100
Cdd:cd07152 11 DAADVDRAAARA-AAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 101 SFLAPVkYPSELGE-AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAE-TFAHLVREAGAPE 178
Cdd:cd07152 90 QPQGEI-LPSAPGRlSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGvVIARLFEEAGLPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 179 GAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAVKIGVQARLNN 258
Cdd:cd07152 169 GVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 259 AGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEAVKNGAKLHLGGKavaRE 338
Cdd:cd07152 249 QGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGT---YD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 339 GNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYINWLT 418
Cdd:cd07152 326 GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQT 405
|
410
....*....|....*...
gi 488976554 419 -DTAPELPFGGVKRSGYG 435
Cdd:cd07152 406 vNDEPHNPFGGMGASGNG 423
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
52-452 |
9.23e-89 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 276.23 E-value: 9.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 52 LHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVKLCAQIARYYADNAKSFLAPVKYPSELGE-AWVEHHPIGVLLAVEP 130
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGEnILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 131 WNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIA-DDRVQGAALTGSE 209
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAgNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 210 KAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQ 289
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 290 VKIGDPLDEST-TLGPLSSKDALDTLSKQVDEAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQI 368
Cdd:PRK10090 241 VQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 369 YVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVN 448
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQ 400
|
....
gi 488976554 449 QKLV 452
Cdd:PRK10090 401 TQVV 404
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
3-453 |
1.29e-88 |
|
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: 278.22 E-value: 1.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQA-DALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS 81
Cdd:cd07142 21 FPTIDPRNGEVIAHVAEGDAEDVDRAVKAArKAFDEGPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 82 R-GEVKLCAQIARYYA---DNAKSFLAPVKYPSElgeAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHA 157
Cdd:cd07142 101 RyAEVPLAARLFRYYAgwaDKIHGMTLPADGPHH---VYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 158 SIVPHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIADDR-VQGAALTGSEKAGSVVAAQAAK-HIKKSTLELGGNDV 235
Cdd:cd07142 178 EQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 236 FVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLS 315
Cdd:cd07142 258 FIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKIL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 316 KQVDEAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQ 395
Cdd:cd07142 338 SYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSK 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 488976554 396 DIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVV 453
Cdd:cd07142 418 NIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
3-453 |
8.21e-86 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 271.69 E-value: 8.21e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQA-DALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS 81
Cdd:PLN02766 38 FETRDPRTGEVIARIAEGDKEDVDLAVKAArEAFDHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 82 RG-EVKLCAQIARYYADNAKSFLAPVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIV 160
Cdd:PLN02766 118 KAvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 161 PHCAETFAHLVREAGAPEGAwTNLF--ISQDQVAKIIADDRVQGAALTGSEKAG-SVVAAQAAKHIKKSTLELGGNDVFV 237
Cdd:PLN02766 198 PLSALFYAHLAKLAGVPDGV-INVVtgFGPTAGAAIASHMDVDKVSFTGSTEVGrKIMQAAATSNLKQVSLELGGKSPLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 238 VLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQ 317
Cdd:PLN02766 277 IFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSY 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 318 VDEAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDI 397
Cdd:PLN02766 357 IEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDL 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976554 398 ERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVV 453
Cdd:PLN02766 437 DVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVV 492
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
3-437 |
1.23e-83 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 265.59 E-value: 1.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR 82
Cdd:PRK13252 24 FEVINPATGEVLATVQAATPADVEAAVASAKQGQ-KIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 83 gevklCAQIA------RYYADNAKSFLA---PVKypselGEAWV--EHHPIGVLLAVEPWNFPyyqlIRVL----APNLA 147
Cdd:PRK13252 103 -----VVDIVtgadvlEYYAGLAPALEGeqiPLR-----GGSFVytRREPLGVCAGIGAWNYP----IQIAcwksAPALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 148 AGNPVIAKHASIVPHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKST 227
Cdd:PRK13252 169 AGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 228 LELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSS 307
Cdd:PRK13252 249 MELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 308 KDALDTLSKQVDEAVKNGAKLHLGGKAV----AREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLAND 383
Cdd:PRK13252 329 FAHRDKVLGYIEKGKAEGARLLCGGERLteggFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARAND 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 488976554 384 SHYGLGGAVFSQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRE 437
Cdd:PRK13252 409 TEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRE 462
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
3-447 |
9.08e-80 |
|
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: 255.40 E-value: 9.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR 82
Cdd:cd07111 39 FPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES-WSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 83 -GEVKLCAQIARYYADNAksflapvkypSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVP 161
Cdd:cd07111 118 dCDIPLVARHFYHHAGWA----------QLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 162 HCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDD 241
Cdd:cd07111 188 LTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 242 ADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEA 321
Cdd:cd07111 268 ADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 322 VKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAK 401
Cdd:cd07111 348 RAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLAL 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 488976554 402 RMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFV 447
Cdd:cd07111 428 EVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYL 473
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
2-437 |
2.80e-79 |
|
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: 253.67 E-value: 2.80e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 2 AYQTVNPANNQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS 81
Cdd:cd07130 13 VVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE-WRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 82 RGEVKLCAQIARYYADNAKSFLAPVkYPSE-----LGEAWvehHPIGVLLAVEPWNFPyyqlIRVLAPN----LAAGNPV 152
Cdd:cd07130 92 LGEVQEMIDICDFAVGLSRQLYGLT-IPSErpghrMMEQW---NPLGVVGVITAFNFP----VAVWGWNaaiaLVCGNVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 153 IAKHASIVPHCAETFAHLVREA----GAPEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTL 228
Cdd:cd07130 164 VWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 229 ELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSK 308
Cdd:cd07130 244 ELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 309 DALDTLSKQVDEAVKNGAKLHLGGKAVAREGNFFEPTILTGiTRDNPAYFEEFFGPVaqIYVVKND--EEAIQLANDSHY 386
Cdd:cd07130 324 AAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEG-LSDAPIVKEETFAPI--LYVLKFDtlEEAIAWNNEVPQ 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 488976554 387 GLGGAVFSQDIERAKRMASAI--ETGMVYINWLTDTApEL--PFGGVKRSGYGRE 437
Cdd:cd07130 401 GLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSGA-EIggAFGGEKETGGGRE 454
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
5-455 |
6.55e-79 |
|
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: 252.30 E-value: 6.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 5 TVNPANNQLIKTYPAHSDADVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGE 84
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAF-PEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSfLAPVKYPSElGEAW--VEHHPIGVLLAVEPWNFPY-YQLIRVLAPnLAAGNPVIAKHASIVP 161
Cdd:cd07107 80 VMVAAALLDYFAGLVTE-LKGETIPVG-GRNLhyTLREPYGVVARIVAFNHPLmFAAAKIAAP-LAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 162 HCAETFAHLVREAgAPEGAWTNLFISQDQVAKIIADDR-VQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLD 240
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 241 DADLERAVKIGVQA-RLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVD 319
Cdd:cd07107 236 DADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 320 EAVKNGAKLHLGGK----AVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQ 395
Cdd:cd07107 316 SAKREGARLVTGGGrpegPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 396 DIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVVVR 455
Cdd:cd07107 396 DISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVR 455
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
3-435 |
9.48e-79 |
|
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: 253.68 E-value: 9.48e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPAN-NQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS 81
Cdd:cd07124 48 IESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPT-WRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 82 RGEVKLCAQIARYYADNAKSFLAPVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVP 161
Cdd:cd07124 127 DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 162 HCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIADD-RVQGAALTGSEKAGSVVAAQAAK------HIKKSTLELGGND 234
Cdd:cd07124 207 VIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHpDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 235 VFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTL 314
Cdd:cd07124 287 AIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 315 SKQVDEAvKNGAKLHLGGK--AVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAV 392
Cdd:cd07124 367 RRYIEIG-KSEGRLLLGGEvlELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGV 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 488976554 393 FSQD---IERAKRmasAIETGMVYINW-LTDTAPEL-PFGGVKRSGYG 435
Cdd:cd07124 446 FSRSpehLERARR---EFEVGNLYANRkITGALVGRqPFGGFKMSGTG 490
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
6-455 |
1.52e-76 |
|
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: 246.66 E-value: 1.52e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGE- 84
Cdd:cd07085 21 YNPATGEVIARVPLATAEEVDAAVAAAKAAF-PAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 ------VKLCAQIAR----YYADNAKSFLapvkypselgEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIA 154
Cdd:cd07085 100 lrglevVEFACSIPHllkgEYLENVARGI----------DTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 155 KHASIVPHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGND 234
Cdd:cd07085 170 KPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 235 VFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTL 314
Cdd:cd07085 250 HAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 315 SKQVDEAVKNGAKLHLGGKAVA----REGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGG 390
Cdd:cd07085 330 EGLIESGVEEGAKLVLDGRGVKvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGA 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488976554 391 AVFSQDIERAKRMASAIETGMVYINwLTDTAP--ELPFGGVKRSGYGrelsDL------GIKEFVNQKLVVVR 455
Cdd:cd07085 410 AIFTRSGAAARKFQREVDAGMVGIN-VPIPVPlaFFSFGGWKGSFFG----DLhfygkdGVRFYTQTKTVTSR 477
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
3-452 |
1.94e-75 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 244.42 E-value: 1.94e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQADALYHSA-WAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS 81
Cdd:PRK09847 37 FETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 82 -RGEVKLCAQIARYYADNAKSFLAPVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIV 160
Cdd:PRK09847 117 lRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 161 PHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIA-DDRVQGAALTGSEKAGSVVAAQAAK-HIKKSTLELGGNDVFVV 238
Cdd:PRK09847 197 PLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSrHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 239 LDDA-DLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQ 317
Cdd:PRK09847 277 FADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSF 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 318 VDEAVKNGaKLHLGGKAVAREGnFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDI 397
Cdd:PRK09847 357 IREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDL 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 488976554 398 ERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLV 452
Cdd:PRK09847 435 SRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
3-453 |
4.75e-73 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 239.32 E-value: 4.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIkTYPAHSDA-DVEAALQQA-DALYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQ 80
Cdd:PLN02466 75 FPTLDPRTGEVI-AHVAEGDAeDVNRAVAAArKAFDEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 81 SRG-EVKLCAQIARYY---ADNAKSFLAPVKYPSELGeawVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKH 156
Cdd:PLN02466 154 SAKaELPMFARLFRYYagwADKIHGLTVPADGPHHVQ---TLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 157 ASIVPHCAETFAHLVREAGAPEGAwTNLF--ISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAK-HIKKSTLELGGN 233
Cdd:PLN02466 231 AEQTPLSALYAAKLLHEAGLPPGV-LNVVsgFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 234 DVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKF-SEAFRQVkIGDPLDESTTLGPLSSKDALD 312
Cdd:PLN02466 310 SPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAkARALKRV-VGDPFKKGVEQGPQIDSEQFE 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 313 TLSKQVDEAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAV 392
Cdd:PLN02466 389 KILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGV 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976554 393 FSQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRELSDLGIKEFVNQKLVV 453
Cdd:PLN02466 469 FTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
4-454 |
8.82e-70 |
|
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: 228.46 E-value: 8.82e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 4 QTVNPANNQLIKTYPAHSDADVEAALQQADALY--HSAWakgdIEP--RLAVLHKLADLIDSRAEELAKIASQEMGKLIK 79
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFldRNNW----LPAheRIAILERLADLMEERADELALLIAREGGKPLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 80 QSRGE-------VKLCAQIARYyadnaksfLAPVKYPSELGE------AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNL 146
Cdd:cd07148 78 DAKVEvtraidgVELAADELGQ--------LGGREIPMGLTPasagriAFTTREPIGVVVAISAFNHPLNLIVHQVAPAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 147 AAGNPVIAKHASIVPHCAETFAHLVREAGAPEGaWTNLFISQDQVA-KIIADDRVQGAALTGSEKAGSVVAAQAAKHiKK 225
Cdd:cd07148 150 AAGCPVIVKPALATPLSCLAFVDLLHEAGLPEG-WCQAVPCENAVAeKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 226 STLELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPL 305
Cdd:cd07148 228 CALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 306 SSKDALDTLSKQVDEAVKNGAKLHLGGKAVARegNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSH 385
Cdd:cd07148 308 IRPREVDRVEEWVNEAVAAGARLLCGGKRLSD--TTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLP 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976554 386 YGLGGAVFSQDIERAKRMASAIETGMVYIN--------WltdtapeLPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07148 386 VAFQAAVFTKDLDVALKAVRRLDATAVMVNdhtafrvdW-------MPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
24-436 |
1.88e-68 |
|
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: 224.46 E-value: 1.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 24 DVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEVKLCAQIARYYADNAKSFL 103
Cdd:cd07095 1 QVDAAVAAARAAF-PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 104 APVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREAGAPEGAWTN 183
Cdd:cd07095 80 GERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 184 LFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKS-TLELGGNDVFVVLDDADLERAVKIGVQARLNNAGQV 262
Cdd:cd07095 160 VQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKIlALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 263 CTAAKRFILHEN-IADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEAVKNGAKLHLGGKAVAREGNF 341
Cdd:cd07095 240 CTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 342 FEPTILTGITRDNPAYfEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYINWLTDTA 421
Cdd:cd07095 320 LSPGIIDVTDAADVPD-EEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGA 398
|
410
....*....|....*.
gi 488976554 422 P-ELPFGGVKRSGYGR 436
Cdd:cd07095 399 SsTAPFGGVGLSGNHR 414
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
6-435 |
1.34e-66 |
|
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: 221.69 E-value: 1.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPA-NNQLIKTYPAHSDADVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGE 84
Cdd:cd07125 51 IDPAdHERTIGEVSLADAEDVDAALAIAAAAF-AGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSFLAPVKYPSELGE-AWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHC 163
Cdd:cd07125 130 VREAIDFCRYYAAQARELFSDPELPGPTGElNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 164 AETFAHLVREAGAPEGAwTNLFISQDQVA--KIIADDRVQGAALTGSEkagsvvaaQAAKHIKKS---------TL--EL 230
Cdd:cd07125 210 AARAVELLHEAGVPRDV-LQLVPGDGEEIgeALVAHPRIDGVIFTGST--------ETAKLINRAlaerdgpilPLiaET 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 231 GGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDA 310
Cdd:cd07125 281 GGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 311 LDTLSKQVDEAVKNG---AKLHLGgkavAREGNFFEPTILTGitrDNPAYFE-EFFGPVAQIYVVKND--EEAIQLANDS 384
Cdd:cd07125 361 GKLLRAHTELMRGEAwliAPAPLD----DGNGYFVAPGIIEI---VGIFDLTtEVFGPILHVIRFKAEdlDEAIEDINAT 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 488976554 385 HYGLGGAVFSQDIERAKRMASAIETGMVYINWLTDTAPEL--PFGGVKRSGYG 435
Cdd:cd07125 434 GYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGrqPFGGWGLSGTG 486
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
3-433 |
7.63e-65 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 217.11 E-value: 7.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPAN-NQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS 81
Cdd:PRK03137 52 IVSINPANkSEVVGRVSKATKELAEKAMQAALEAFET-WKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 82 RGEVKLCAQIARYYADNAK--SFLAPVK-YPSELGEAWVEhhPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHAS 158
Cdd:PRK03137 131 DADTAEAIDFLEYYARQMLklADGKPVEsRPGEHNRYFYI--PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPAS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 159 IVPHCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIADD-RVQGAALTGSEKAGSVVAAQAAK------HIKKSTLELG 231
Cdd:PRK03137 209 DTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHpKTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 232 GNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPlDESTTLGPLSSKDAL 311
Cdd:PRK03137 289 GKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNAYMGPVINQASF 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 312 DTLSKQVdEAVKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGA 391
Cdd:PRK03137 368 DKIMSYI-EIGKEEGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGA 446
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 488976554 392 VFSQD---IERAKRmasAIETGMVYINWLTDTA--PELPFGGVKRSG 433
Cdd:PRK03137 447 VISNNrehLEKARR---EFHVGNLYFNRGCTGAivGYHPFGGFNMSG 490
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
3-437 |
4.29e-63 |
|
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: 211.54 E-value: 4.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 3 YQTVNPANNQLIKTYPAHSDADVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR 82
Cdd:cd07116 18 FDNITPVTGKVFCEVPRSTAEDIELALDAAHAAK-EAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 83 G-EVKLCAQIARYYADNAKSFLAPVkypSELGEAWVEHH---PIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHAS 158
Cdd:cd07116 97 AaDIPLAIDHFRYFAGCIRAQEGSI---SEIDENTVAYHfhePLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 159 IVPHCAETFAHLVREAgAPEGAWTNLFISQDQVAKIIA-DDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGN--DV 235
Cdd:cd07116 174 QTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLAsSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKspNI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 236 FV--VL--DDADLERAVKIGVQARLNNaGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDAL 311
Cdd:cd07116 253 FFadVMdaDDAFFDKALEGFVMFALNQ-GEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 312 DTLSKQVDEAVKNGAKLHLGGKAVAREGN----FFEPTILTGiTRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYG 387
Cdd:cd07116 332 EKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYG 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 488976554 388 LGGAVFSQDIERAKRMASAIETGMVYINWLTDTAPELPFGGVKRSGYGRE 437
Cdd:cd07116 411 LGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRE 460
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
44-454 |
3.03e-62 |
|
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: 207.76 E-value: 3.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 44 DIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR-GEVKLCAQIARYYADNAKSFLAPVKYPSEL----GEAWVE 118
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAVVLGEIDHALKHLKKWMKPRRVSVPLllqpAKAYVI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 119 HHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREagapegawtnlFISQDQVAKIIADD 198
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPK-----------YFDPEAVAVVEGGV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 199 RVQGAAL---------TGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRF 269
Cdd:cd07087 167 EVATALLaepfdhiffTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 270 ILHENIADAFLTKFSEAFRQVkIGDPLDESTTLGPLSSKDALDTLSKqvdeaVKNGAKLHLGGKaVAREGNFFEPTILTG 349
Cdd:cd07087 247 LVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLAS-----LLDDGKVVIGGQ-VDKEERYIAPTILDD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 350 ITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYINwltDT-----APEL 424
Cdd:cd07087 320 VSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN---DVllhaaIPNL 396
|
410 420 430
....*....|....*....|....*....|
gi 488976554 425 PFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07087 397 PFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
5-437 |
2.68e-60 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 205.07 E-value: 2.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 5 TVNPANNQLIKTYPAHSDADVEAALQqadALYHSA--WAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR 82
Cdd:PLN02315 38 SVNPANNQPIAEVVEASLEDYEEGLR---ACEEAAkiWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 83 GEVKLCAQIARYYADNAKSFLAPVkYPSE-----LGEAWvehHPIGVLLAVEPWNFPyyqlIRVLAPN----LAAGNPVI 153
Cdd:PLN02315 115 GEVQEIIDMCDFAVGLSRQLNGSI-IPSErpnhmMMEVW---NPLGIVGVITAFNFP----CAVLGWNaciaLVCGNCVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 154 AKHASIVPHCAETFAHLVREA----GAPEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLE 229
Cdd:PLN02315 187 WKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 230 LGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKD 309
Cdd:PLN02315 267 LSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 310 ALDTLSKQVDEAVKNGAKLHLGGKAVAREGNFFEPTILTgITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLG 389
Cdd:PLN02315 347 SKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLS 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 488976554 390 GAVFSQDIERAKRM--ASAIETGMVYINWLTDTApEL--PFGGVKRSGYGRE 437
Cdd:PLN02315 426 SSIFTRNPETIFKWigPLGSDCGIVNVNIPTNGA-EIggAFGGEKATGGGRE 476
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
28-454 |
3.45e-58 |
|
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: 197.45 E-value: 3.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 28 ALQQADALyhsAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKlikqSRGEVKLcAQI------ARYYADNAKS 101
Cdd:cd07134 5 AAQQAHAL---ALRASTAAERIAKLKRLKKAILARREEIIAALAADFRK----PAAEVDL-TEIlpvlseINHAIKHLKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 102 FLAPVKYPSELG----EAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREAGAP 177
Cdd:cd07134 77 WMKPKRVRTPLLlfgtKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 178 egawtnlfisqDQVAKIIADDRVQGAAL---------TGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAV 248
Cdd:cd07134 157 -----------DEVAVFEGDAEVAQALLelpfdhiffTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 249 KIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLD-ESTTLGPLSSKDALDTLSKQVDEAVKNGAK 327
Cdd:cd07134 226 KKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARkASPDLARIVNDRHFDRLKGLLDDAVAKGAK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 328 LHLGGKAVArEGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAI 407
Cdd:cd07134 306 VEFGGQFDA-AQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLART 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 488976554 408 ETGMVYINwltDTA-----PELPFGGVKRSGYGRELSDLGIKEFVNQKLVVV 454
Cdd:cd07134 385 SSGGVVVN---DVVlhflnPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
6-435 |
1.78e-56 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 194.72 E-value: 1.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPAN-NQLIKTYPAHSDADVEAALQQADALYHSaWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGE 84
Cdd:cd07083 37 VSPFApSEVVGTTAKADKAEAEAALEAAWAAFKT-WKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSFLAP----VKYPSELGEAWveHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIV 160
Cdd:cd07083 116 VAEAIDFIRYYARAALRLRYPavevVPYPGEDNESF--YVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 161 PHCAETFAHLVREAGAPEGAWTNLFISQDQV-AKIIADDRVQGAALTGSEKAGSVVAAQAAKH------IKKSTLELGGN 233
Cdd:cd07083 194 VVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLapgqtwFKRLYVETGGK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 234 DVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDT 313
Cdd:cd07083 274 NAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 314 LSKQVDEAvKNGAKLHLGGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDE--EAIQLANDSHYGLGGA 391
Cdd:cd07083 354 VLSYIEHG-KNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGG 432
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 488976554 392 VFSQDIERAKRMASAIETGMVYINWLTDTA--PELPFGGVKRSGYG 435
Cdd:cd07083 433 VYSRKREHLEEARREFHVGNLYINRKITGAlvGVQPFGGFKLSGTN 478
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
21-453 |
3.76e-56 |
|
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: 192.05 E-value: 3.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 21 SDADVEAALQQADALYHSAWAKgDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR-GEVKLCAQIARYYADNA 99
Cdd:cd07135 3 PLDEIDSIHSRLRATFRSGKTK-DLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 100 KSFLAPVK-----YPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREA 174
Cdd:cd07135 82 KKWAKDEKvkdgpLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 175 GAPEGAwtnlfisqdQVakiiaddrVQGA-----AL----------TGSEKAGSVVAAQAAKHIKKSTLELGG-NDVFvV 238
Cdd:cd07135 162 LDPDAF---------QV--------VQGGvpettALleqkfdkifyTGSGRVGRIIAEAAAKHLTPVTLELGGkSPVI-V 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 239 LDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPlDESTTLGPLSSKDALDTLSKQV 318
Cdd:cd07135 224 TKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 319 DEAvknGAKLHLGGKAVAREgNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIE 398
Cdd:cd07135 303 DTT---KGKVVIGGEMDEAT-RFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKS 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 399 RAKRMASAIETGMVYINwltDTA-----PELPFGGVKRSGYGRELSDLGIKEFVNQKLVV 453
Cdd:cd07135 379 EIDHILTRTRSGGVVIN---DTLihvgvDNAPFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
2-433 |
1.04e-55 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 192.10 E-value: 1.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 2 AYQTVNPANNQLIKTYPAHSDADVEAALQQA-DALYhsAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQ 80
Cdd:PRK09457 16 AFESRNPVSGEVLWQGNDATAAQVDAAVRAArAAFP--AWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 81 SRGEVK-LCAQIA---RYYADNAksflAPVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKH 156
Cdd:PRK09457 94 AATEVTaMINKIAisiQAYHERT----GEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 157 ASIVPHCAETFAHLVREAGAPEGAwTNLFISQDQVAKIIADDR-VQGAALTGSEKAGSVVAAQAAKHIKKS-TLELGGND 234
Cdd:PRK09457 170 SELTPWVAELTVKLWQQAGLPAGV-LNLVQGGRETGKALAAHPdIDGLLFTGSANTGYLLHRQFAGQPEKIlALEMGGNN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 235 VFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENI-ADAFLTKFSEAFRQVKIGDPLDESTT-LGPLSSKDALD 312
Cdd:PRK09457 249 PLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWDAEPQPfMGAVISEQAAQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 313 TLSKQVDEAVKNGAKLHLGGKAVAREGNFFEPTIL--TGItRDNPAyfEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGG 390
Cdd:PRK09457 329 GLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIIdvTGV-AELPD--EEYFGPLLQVVRYDDFDEAIRLANNTRFGLSA 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 488976554 391 AVFSQDIERAKRMASAIETGMVyiNW---LTDTAPELPFGGVKRSG 433
Cdd:PRK09457 406 GLLSDDREDYDQFLLEIRAGIV--NWnkpLTGASSAAPFGGVGASG 449
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
44-455 |
2.46e-53 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 186.00 E-value: 2.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 44 DIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR-GEVKLCAQIARYYADNAKSFLAPVKYPSEL----GEAWVE 118
Cdd:PTZ00381 27 PLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmTEVLLTVAEIEHLLKHLDEYLKPEKVDTVGvfgpGKSYII 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 119 HHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVreagapegawtNLFISQDQVAKIIADD 198
Cdd:PTZ00381 107 PEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-----------TKYLDPSYVRVIEGGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 199 RVQGAAL---------TGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRF 269
Cdd:PTZ00381 176 EVTTELLkepfdhiffTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 270 ILHENIADAFLTKFSEAFRQVkIGDPLDESTTLGPLSSKDALDTLSKQVDEavkNGAKLHLGGKaVAREGNFFEPTILTG 349
Cdd:PTZ00381 256 LVHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE-VDIENKYVAPTIIVN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 350 ITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYINwltD-----TAPEL 424
Cdd:PTZ00381 331 PDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN---DcvfhlLNPNL 407
|
410 420 430
....*....|....*....|....*....|.
gi 488976554 425 PFGGVKRSGYGRELSDLGIKEFVNQKLVVVR 455
Cdd:PTZ00381 408 PFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
6-435 |
4.38e-52 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 182.65 E-value: 4.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALyHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEV 85
Cdd:PLN00412 36 TNPSTRKTQYKVQACTQEEVNKAMESAKAA-QKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 86 KLCAQIARYYADNAKSFLAPVKYPseLGEAW----------VEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAK 155
Cdd:PLN00412 115 VRSGDLISYTAEEGVRILGEGKFL--VSDSFpgnernkyclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 156 HASIVPHCAETFAHLVREAGAPEGawtnLFISQDQVAKIIAD-----DRVQGAALTG-------SEKAGsVVAAQaakhi 223
Cdd:PLN00412 193 PPTQGAVAALHMVHCFHLAGFPKG----LISCVTGKGSEIGDfltmhPGVNCISFTGgdtgiaiSKKAG-MVPLQ----- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 224 kkstLELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTtLG 303
Cdd:PLN00412 263 ----MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCD-IT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 304 PLSSKDALDTLSKQVDEAVKNGAKLHLGGKavaREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLAND 383
Cdd:PLN00412 338 PVVSESSANFIEGLVMDAKEKGATFCQEWK---REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNA 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 488976554 384 SHYGLGGAVFSQDIERAKRMASAIETGMVYINWLTDTAPE-LPFGGVKRSGYG 435
Cdd:PLN00412 415 SNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIG 467
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
6-415 |
9.36e-47 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 170.31 E-value: 9.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDADVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEV 85
Cdd:PLN02419 134 INPATQEVVSKVPLTTNEEFKAAVSAAKQAF-PLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 86 KLCAQIARYYADNAK----SFLAPVkypSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVP 161
Cdd:PLN02419 213 FRGLEVVEHACGMATlqmgEYLPNV---SNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 162 HCAETFAHLVREAGAPEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDD 241
Cdd:PLN02419 290 GASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 242 ADLERAVKIGVQARLNNAGQVCTAAKRFILHENiADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEA 321
Cdd:PLN02419 370 ANIDATLNALLAAGFGAAGQRCMALSTVVFVGD-AKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSG 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 322 VKNGAKLHLGGKAVA----REGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDI 397
Cdd:PLN02419 449 VDDGAKLLLDGRDIVvpgyEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSG 528
|
410
....*....|....*...
gi 488976554 398 ERAKRMASAIETGMVYIN 415
Cdd:PLN02419 529 AAARKFQMDIEAGQIGIN 546
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
6-415 |
3.68e-44 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 165.76 E-value: 3.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDAD-VEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGE 84
Cdd:PRK11904 567 VSPADRRRVVGEVAFADAEqVEQALAAARAAF-PAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAE 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKS-FLAPVKYPSELGEA-WVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPH 162
Cdd:PRK11904 646 VREAVDFCRYYAAQARRlFGAPEKLPGPTGESnELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPL 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 163 CAETFAHLVREAGAPEGAWTNLFISQDQV-AKIIADDRVQGAALTGS-EKAGSVVAAQAAKHIKKSTL--ELGGNDVFVV 238
Cdd:PRK11904 726 IAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIAGVAFTGStETARIINRTLAARDGPIVPLiaETGGQNAMIV 805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 239 LDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQV 318
Cdd:PRK11904 806 DSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHI 885
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 319 dEAVKNGAKLHLGGK--AVAREGNFFEPTIltgITRDNPAYFE-EFFGPVAQIYVVKNDE-----EAIqlaNDSHYGLGG 390
Cdd:PRK11904 886 -ERMKREARLLAQLPlpAGTENGHFVAPTA---FEIDSISQLErEVFGPILHVIRYKASDldkviDAI---NATGYGLTL 958
|
410 420
....*....|....*....|....*
gi 488976554 391 AVFSQDIERAKRMASAIETGMVYIN 415
Cdd:PRK11904 959 GIHSRIEETADRIADRVRVGNVYVN 983
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
6-415 |
4.72e-44 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 165.42 E-value: 4.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPAN-NQLIKTYPAHSDADVEAALQQADAlYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGE 84
Cdd:PRK11905 572 LNPADhDDVVGTVTEASAEDVERALAAAQA-AFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSFLAPVkypselgeawvEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCA 164
Cdd:PRK11905 651 VREAVDFLRYYAAQARRLLNGP-----------GHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIA 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 165 ETFAHLVREAGAPEGAWTNLFISQDQV-AKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTL---ELGGNDVFVVLD 240
Cdd:PRK11905 720 ARAVRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAMIVDS 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 241 DADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDE 320
Cdd:PRK11905 800 SALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEA 879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 321 AVKNGAKLH-LGGKAVAREGNFFEPTIltgITRDNPAYFE-EFFGPVAQIYVVKNDE-----EAIqlaNDSHYGLGGAVF 393
Cdd:PRK11905 880 MRAAGRLVHqLPLPAETEKGTFVAPTL---IEIDSISDLErEVFGPVLHVVRFKADEldrviDDI---NATGYGLTFGLH 953
|
410 420
....*....|....*....|..
gi 488976554 394 SQDIERAKRMASAIETGMVYIN 415
Cdd:PRK11905 954 SRIDETIAHVTSRIRAGNIYVN 975
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
44-436 |
1.30e-43 |
|
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: 158.82 E-value: 1.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 44 DIEPRLAVLHKLADLIDSRAEELAKIASQEMGKlikqSRGEVKLCaQIA------RYYADNAKSFLAPVKYPSEL----G 113
Cdd:cd07136 18 DVEFRIEQLKKLKQAIKKYENEILEALKKDLGK----SEFEAYMT-EIGfvlseiNYAIKHLKKWMKPKRVKTPLlnfpS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 114 EAWVEHHPIGVLLAVEPWNFPYyQLIrvLAP---NLAAGNPVIAKHASIVPHCAETFAHLVREAgapegawtnlFisQDQ 190
Cdd:cd07136 93 KSYIYYEPYGVVLIIAPWNYPF-QLA--LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET----------F--DEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 191 VAKIIADDRVQGAAL----------TGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAVKIGVQARLNNAG 260
Cdd:cd07136 158 YVAVVEGGVEENQELldqkfdyiffTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 261 QVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLdESTTLGPLSSKDALDTLSKQVDEAvkngaKLHLGGKAvAREGN 340
Cdd:cd07136 238 QTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPL-ESPDYGRIINEKHFDRLAGLLDNG-----KIVFGGNT-DRETL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 341 FFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYINwltDT 420
Cdd:cd07136 311 YIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN---DT 387
|
410 420
....*....|....*....|.
gi 488976554 421 -----APELPFGGVKRSGYGR 436
Cdd:cd07136 388 imhlaNPYLPFGGVGNSGMGS 408
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
6-435 |
2.40e-41 |
|
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: 153.91 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAHSDAD-VEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGE 84
Cdd:TIGR01238 56 TNPADRRDIVGQVFHANLAhVQAAIDSAQQAF-PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKSFLapvkyPSElgeawvEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCA 164
Cdd:TIGR01238 135 VREAVDFCRYYAKQVRDVL-----GEF------SVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 165 ETFAHLVREAGAPEGAWTNLFISQDQV-AKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTL---ELGGNDVFVVLD 240
Cdd:TIGR01238 204 YRAVELMQEAGFPAGTIQLLPGRGADVgAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPliaETGGQNAMIVDS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 241 DADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDE 320
Cdd:TIGR01238 284 TALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEH 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 321 AVKNGAKLH---LGGKAVAREGNFFEPTILTgiTRDNPAYFEEFFGPVAQIYVVKNDE--EAIQLANDSHYGLGGAVFSQ 395
Cdd:TIGR01238 364 MSQTQKKIAqltLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSR 441
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 488976554 396 DIERAKRMASAIETGMVYIN--WLTDTAPELPFGGVKRSGYG 435
Cdd:TIGR01238 442 IETTYRWIEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTG 483
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
44-436 |
4.21e-41 |
|
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: 151.87 E-value: 4.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 44 DIEPRLAVLHKLADLIDSRAEELAKIASQEMGKlikQSRGEVKLC------AQIaRYYADNAKSFLAPVKYPSEL----G 113
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFGH---RSRHETLLAeilpsiAGI-KHARKHLKKWMKPSRRHVGLlflpA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 114 EAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREAgapegawtnlfISQDQVAK 193
Cdd:cd07133 94 KAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-----------FDEDEVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 194 IIADDRVqGAAL----------TGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVC 263
Cdd:cd07133 163 VTGGADV-AAAFsslpfdhllfTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 264 TAAKRFILHENIADAFLTKFSEAFRQVkIGDPLDeSTTLGPLSSKDALDTLSKQVDEAVKNGAKLH--LGGKAVAREGNF 341
Cdd:cd07133 242 VAPDYVLVPEDKLEEFVAAAKAAVAKM-YPTLAD-NPDYTSIINERHYARLQGLLEDARAKGARVIelNPAGEDFAATRK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 342 FEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYINwltDT- 420
Cdd:cd07133 320 LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN---DTl 396
|
410 420
....*....|....*....|
gi 488976554 421 ----APELPFGGVKRSGYGR 436
Cdd:cd07133 397 lhvaQDDLPFGGVGASGMGA 416
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
48-436 |
7.56e-40 |
|
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: 148.33 E-value: 7.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 48 RLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS-RGEVKLCAQIARYYADNAKSFLAPVKYPSEL----GEAWVEHHPI 122
Cdd:cd07137 23 RKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCKLAIKELKKWMAPEKVKTPLttfpAKAEIVSEPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 123 GVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHL-----------VREAGAPEGawTNLFisQDQV 191
Cdd:cd07137 103 GVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLipeyldtkaikVIEGGVPET--TALL--EQKW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 192 AKIIaddrvqgaaLTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAVK-IGVQARLNNAGQVCTAAKRFI 270
Cdd:cd07137 179 DKIF---------FTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRrIAGGKWGCNNGQACIAPDYVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 271 LHENIA----DAFLTKFSEAFRQvkigDPLdESTTLGPLSSKDALDTLSKQVDEAVKNGAKLHlgGKAVAREGNFFEPTI 346
Cdd:cd07137 250 VEESFAptliDALKNTLEKFFGE----NPK-ESKDLSRIVNSHHFQRLSRLLDDPSVADKIVH--GGERDEKNLYIEPTI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 347 LTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYIN--WLTDTAPEL 424
Cdd:cd07137 323 LLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdtVVQYAIDTL 402
|
410
....*....|..
gi 488976554 425 PFGGVKRSGYGR 436
Cdd:cd07137 403 PFGGVGESGFGA 414
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
26-436 |
1.67e-39 |
|
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: 147.75 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 26 EAALQQADALYHSAWAKgDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS-RGEVKLCAQIARYYADNAKSFLA 104
Cdd:cd07132 1 AEAVRRAREAFSSGKTR-PLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAvLSEILLVKNEIKYAISNLPEWMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 105 PVKYPSE----LGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHL---------- 170
Cdd:cd07132 80 PEPVKKNlatlLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELipkyldkecy 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 171 -VREAGAPEgawTNLFISQ--DqvaKIIaddrvqgaaLTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERA 247
Cdd:cd07132 160 pVVLGGVEE---TTELLKQrfD---YIF---------YTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 248 VKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVkIGDPLDESTTLGPLSSKDALDTLSKQVDeavknGAK 327
Cdd:cd07132 225 ARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLS-----GGK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 328 LHLGGKAVAREgNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAI 407
Cdd:cd07132 299 VAIGGQTDEKE-RYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNT 377
|
410 420 430
....*....|....*....|....*....|....
gi 488976554 408 ETGMVYINwltDT-----APELPFGGVKRSGYGR 436
Cdd:cd07132 378 SSGGVCVN---DTimhytLDSLPFGGVGNSGMGA 408
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
6-415 |
2.26e-37 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 145.85 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPAN-NQLIKTYPAHSDADVEAALQQADAlYHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGE 84
Cdd:COG4230 575 RNPADhSDVVGTVVEATAADVEAALAAAQA-AFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAE 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 85 VKLCAQIARYYADNAKsflapvkypsELGEAWVEHHPIGVLLAVEPWNFPyyqlirvLA-------PNLAAGNPVIAKHA 157
Cdd:COG4230 654 VREAVDFCRYYAAQAR----------RLFAAPTVLRGRGVFVCISPWNFP-------LAiftgqvaAALAAGNTVLAKPA 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 158 SIVPHCAetfAHLVR---EAGAPEGAWTNLFISQDQV-AKIIADDRVQGAALTGSekagsvvaAQAAKHIKKsTL----- 228
Cdd:COG4230 717 EQTPLIA---ARAVRllhEAGVPADVLQLLPGDGETVgAALVADPRIAGVAFTGS--------TETARLINR-TLaardg 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 229 -------ELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTT 301
Cdd:COG4230 785 pivpliaETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTD 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 302 LGPLSSKDALDTLSKQVDEAVKNGAKLH-LGGKAVAREGNFFEPTIltgITRDNPAYFE-EFFGPVAQIYVVKNDE---- 375
Cdd:COG4230 865 VGPVIDAEARANLEAHIERMRAEGRLVHqLPLPEECANGTFVAPTL---IEIDSISDLErEVFGPVLHVVRYKADEldkv 941
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 488976554 376 -EAIqlaNDSHYGLGGAVFSQDIERAKRMASAIETGMVYIN 415
Cdd:COG4230 942 iDAI---NATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
6-433 |
1.09e-34 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 135.41 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPAN-NQLIKTYPAHSDADVEAALQQADALYHsAWAKGDIEPRLAVLHKLADLIDS--RAEELAK-IASQemGKLIKQS 81
Cdd:cd07123 51 VMPHDhAHVLATYHYADAALVEKAIEAALEARK-EWARMPFEDRAAIFLKAADLLSGkyRYELNAAtMLGQ--GKNVWQA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 82 rgEVKLCAQIA---RYYADNAKSFLA--PVKYPSElgeAW--VEHHPI-GVLLAVEPWNFPyyqlirVLAPNLAA----- 148
Cdd:cd07123 128 --EIDAACELIdflRFNVKYAEELYAqqPLSSPAG---VWnrLEYRPLeGFVYAVSPFNFT------AIGGNLAGapalm 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 149 GNPVIAKHASIVPHCAETFAHLVREAGAPEGAwTNLFISQDQV--AKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKK- 225
Cdd:cd07123 197 GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGV-INFVPGDGPVvgDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRy 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 226 STL-----ELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDEST 300
Cdd:cd07123 276 RTYprivgETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 301 TLGPLSSKDALDTLSKQVDEAVK-NGAKLHLGGKAVAREGNFFEPTIltgITRDNPAY---FEEFFGPVAQIYVVKND-- 374
Cdd:cd07123 356 FMGAVIDEKAFDRIKGYIDHAKSdPEAEIIAGGKCDDSVGYFVEPTV---IETTDPKHklmTEEIFGPVLTVYVYPDSdf 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976554 375 EEAIQLAND-SHYGLGGAVFSQD---IERAK---RMASaietGMVYINWLTDTA--PELPFGGVKRSG 433
Cdd:cd07123 433 EETLELVDTtSPYALTGAIFAQDrkaIREATdalRNAA----GNFYINDKPTGAvvGQQPFGGARASG 496
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
6-435 |
2.77e-31 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 127.78 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 6 VNPANNQLIKTYPAH-SDADVEAALQQADalyHSA--WAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSR 82
Cdd:PRK11809 664 INPADPRDIVGYVREaTPAEVEQALESAV---NAApiWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAI 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 83 GEVKLCAQIARYYADNAKSFLApvkypselGEAwveHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPH 162
Cdd:PRK11809 741 AEVREAVDFLRYYAGQVRDDFD--------NDT---HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPL 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 163 CAETFAHLVREAGAPEGAWTNLFISQDQV-AKIIADDRVQGAALTGSEKAGSVVAAQAAKHI----KKSTL--ELGGNDV 235
Cdd:PRK11809 810 IAAQAVRILLEAGVPAGVVQLLPGRGETVgAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqgRPIPLiaETGGQNA 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 236 FVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLS 315
Cdd:PRK11809 890 MIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIE 969
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 316 KQVDEAVKNGAKLH---LGGKAVAREGNFFEPTIltgITRDNPAYF-EEFFGPVaqIYVVK----NDEEAIQLANDSHYG 387
Cdd:PRK11809 970 RHIQAMRAKGRPVFqaaRENSEDWQSGTFVPPTL---IELDSFDELkREVFGPV--LHVVRynrnQLDELIEQINASGYG 1044
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 488976554 388 LGGAVFSQDIERAKRMASAIETGMVYINWLTDTA--PELPFGGVKRSGYG 435
Cdd:PRK11809 1045 LTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAvvGVQPFGGEGLSGTG 1094
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
25-456 |
1.07e-28 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 117.91 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 25 VEAALQQADALYHSAWAKgDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQS-RGEVKLCAQIARYYADNAKSFL 103
Cdd:PLN02203 8 LEGSVAELRETYESGRTR-SLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyRDEVGVLTKSANLALSNLKKWM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 104 APVKYPSEL----GEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFA-----HLVREA 174
Cdd:PLN02203 87 APKKAKLPLvafpATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAanipkYLDSKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 175 -----GAPEgawtnlfisqdqVAKIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGN--DVFVVLDDA-DLER 246
Cdd:PLN02203 167 vkvieGGPA------------VGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKcpCIVDSLSSSrDTKV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 247 AVKIGVQARLNN-AGQVCTAAKRFILHENIAdAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVDEAVKNG 325
Cdd:PLN02203 235 AVNRIVGGKWGScAGQACIAIDYVLVEERFA-PILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 326 AKLHlgGKAVAREGNFFEPTILTGITRDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMAS 405
Cdd:PLN02203 314 SIVH--GGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILS 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976554 406 AIETGMVYIN-----WLTDTapeLPFGGVKRSGYGRELSDLGIKEFVNQKLVVVRR 456
Cdd:PLN02203 392 ETSSGSVTFNdaiiqYACDS---LPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRS 444
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
46-455 |
1.29e-27 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 114.76 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 46 EPRLAVLHKLADLIDSRAEELAKIASQEMGKL-IKQSRGEVKLCAQIARYYADNAKSFLAPVKYPSEL----GEAWVEHH 120
Cdd:PLN02174 32 EWRVTQLKKLMIICDNHEPEIVAALRDDLGKPeLESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSLttfpASAEIVSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 121 PIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREAGAP------EGAWTNlfisqdqvAKI 194
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSsavrvvEGAVTE--------TTA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 195 IADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELGGNDVFVVLDDADLERAVKIGVQARLN-NAGQVCTAAKRFILHE 273
Cdd:PLN02174 184 LLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 274 NIADAFLTKFSEAFRQVKIGDPLdESTTLGPLSSKDALDTLSKQVDEAvKNGAKLHLGGKAvAREGNFFEPTILTGITRD 353
Cdd:PLN02174 264 EYAPKVIDAMKKELETFYGKNPM-ESKDMSRIVNSTHFDRLSKLLDEK-EVSDKIVYGGEK-DRENLKIAPTILLDVPLD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 354 NPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIETGMVYINwltDTAPE-----LPFGG 428
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVN---DIAVHlalhtLPFGG 417
|
410 420
....*....|....*....|....*..
gi 488976554 429 VKRSGYGRELSDLGIKEFVNQKLVVVR 455
Cdd:PLN02174 418 VGESGMGAYHGKFSFDAFSHKKAVLYR 444
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
25-455 |
1.56e-24 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 105.40 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 25 VEAALQQADALyHSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKlikQSRGEVKLCAQIA--RYYADNAKSF 102
Cdd:cd07084 1 PERALLAADIS-TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGK---GWMFAENICGDQVqlRARAFVIYSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 103 ---------LAPVKYPSELGEAWvehhPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVRE 173
Cdd:cd07084 77 riphepgnhLGQGLKQQSHGYRW----PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 174 AGA-PEGAWTNLFISQDQVAKIIADDRVQGAALTGSEKAGSVVAAQAakHIKKSTLELGGNDVFVVLDDADLERAV-KIG 251
Cdd:cd07084 153 AGLlPPEDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQAVDYVaWQC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 252 VQARLNNAGQVCTAAKRFILHENIA-DAFLTKFSEAFRQVKIGDpldesTTLGPLSSKdalDTLSKQVDEAVKNGAKLHL 330
Cdd:cd07084 231 VQDMTACSGQKCTAQSMLFVPENWSkTPLVEKLKALLARRKLED-----LLLGPVQTF---TTLAMIAHMENLLGSVLLF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 331 GGKAV------AREGNFFEPTILTGITRDN---PAYFEEFFGPVAQIYVVKNDEEA--IQLANDSHYGLGGAVFSQDIER 399
Cdd:cd07084 303 SGKELknhsipSIYGACVASALFVPIDEILktyELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIF 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 400 AKRMASAIET-GMVY-INWLTDTA--PELPFGGVKRSGYGRELSDLGIKEFVNQKLVVVR 455
Cdd:cd07084 383 LQELIGNLWVaGRTYaILRGRTGVapNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAEQA 442
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
123-438 |
1.57e-24 |
|
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: 106.20 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 123 GVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREAGA-PEGAW-------TNLF---ISQDQV 191
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALqlicgsvGDLLdhlGEQDVV 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 192 A---------KIIADDRVQGAALTGSEKAGSVVAAQAAKHIKKSTLELggnDVFVvlDDADLERAVKigvqarlnnAGQV 262
Cdd:cd07128 226 AftgsaataaKLRAHPNIVARSIRFNAEADSLNAAILGPDATPGTPEF---DLFV--KEVAREMTVK---------AGQK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 263 CTAAKRFILHENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVdEAVKNGAKLHLGGKAV------- 335
Cdd:cd07128 292 CTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRfevvgad 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 336 AREGNFFEPTILTGITRDNPAYFE--EFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIET--GM 411
Cdd:cd07128 371 AEKGAFFPPTLLLCDDPDAATAVHdvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGR 450
|
330 340 350
....*....|....*....|....*....|....*.
gi 488976554 412 VYINWLTDTA---------PELPFGGVKRSGYGREL 438
Cdd:cd07128 451 LLVLNRDSAKestghgsplPQLVHGGPGRAGGGEEL 486
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
25-382 |
1.94e-21 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 96.46 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 25 VEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQEMGKLIKQSRGEV-KLCAQIaRYYADNAK--S 101
Cdd:cd07129 1 VDAAAAAAAAAF-ESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELgRTTGQL-RLFADLVRegS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 102 FLAPVkypseLGEAWVEHHPIG------VLLAVEPW------NFPYyqLIRVL----APNLAAGNPVIAK-HASivpH-- 162
Cdd:cd07129 79 WLDAR-----IDPADPDRQPLPrpdlrrMLVPLGPVavfgasNFPL--AFSVAggdtASALAAGCPVVVKaHPA---Hpg 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 163 ----CAETFAHLVREAGAPEGAWTNLFISQDQV-AKIIADDRVQGAALTGSEKAGSVVAAQAAK--HIKKSTLELGG-ND 234
Cdd:cd07129 149 tselVARAIRAALRATGLPAGVFSLLQGGGREVgVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSvNP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 235 VFvVLDDADLERAVKIG---VQARLNNAGQVCTAAKRFILHENIA-DAFLTKFSEAFRQVKigdpldesttLGPLSSKDA 310
Cdd:cd07129 229 VF-ILPGALAERGEAIAqgfVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAP----------AQTMLTPGI 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976554 311 LDTLSKQVDEAVKNGAKLHLGGKAVAREGNFFEPTIL--TGIT-RDNPAYFEEFFGPVAQIYVVKNDEEAIQLAN 382
Cdd:cd07129 298 AEAYRQGVEALAAAPGVRVLAGGAAAEGGNQAAPTLFkvDAAAfLADPALQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
123-453 |
5.18e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 77.05 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 123 GVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREAGA-PEGAWTnlFI---SQDQVAKIIADD 198
Cdd:PRK11903 150 GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALS--VVcgsSAGLLDHLQPFD 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 199 RVqgaALTGSEKAGSVVAAQAA--KHIKKSTLELGGNDVFVVLDDAD-----LERAVKIGVQARLNNAGQVCTAAKRFIL 271
Cdd:PRK11903 228 VV---SFTGSAETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 272 HENIADAFLTKFSEAFRQVKIGDPLDESTTLGPLSSKDALDTLSKQVdEAVKNGAKLHLGGKAVA------REGNFFEPT 345
Cdd:PRK11903 305 PEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFAlvdadpAVAACVGPT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 346 ILTGITRDNPAYFE--EFFGPVAQIYVVKNDEEAIQLANDSHYGLGGAVFSQDIERAKRMASAIET--GMVYI--NWLTD 419
Cdd:PRK11903 384 LLGASDPDAATAVHdvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADshGRVHVisPDVAA 463
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 488976554 420 TA-------PELPFGGVKRSGYGRELSDLGIKEFVNQKLVV 453
Cdd:PRK11903 464 LHtghgnvmPQSLHGGPGRAGGGEELGGLRALAFYHRRSAV 504
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
43-423 |
3.69e-11 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 64.82 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 43 GDIEPRLAVLHKLADLidsrAEELAKIASQEMGKLIKQSRGEVKLCAQIARYYA-DN----AKSFLAPVKYPSEL--GEA 115
Cdd:cd07126 65 GDVSHRVAHELRKPEV----EDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAgDQvrflARSFNVPGDHQGQQssGYR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 116 WvehhPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAKHASIVPHCAETFAHLVREAGAPEgawTNL-FISQD--QVA 192
Cdd:cd07126 141 W----PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPA---TDVdLIHSDgpTMN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 193 KIIADDRVQGAALTGSEKagsvVAAQAAKHIK-KSTLELGGNDVFVVLDD-ADLERAVKIGVQARLNNAGQVCTAAKRFI 270
Cdd:cd07126 214 KILLEANPRMTLFTGSSK----VAERLALELHgKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILF 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 271 LHENIADA-FLTKFSEAFRQVKIGDpldesTTLGPLsskdaLDTLSKQVDEAVKN-----GAKLHLGGKAVaREGNF--- 341
Cdd:cd07126 290 AHENWVQAgILDKLKALAEQRKLED-----LTIGPV-----LTWTTERILDHVDKllaipGAKVLFGGKPL-TNHSIpsi 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 342 ---FEPT--ILTGITRDNPAYFE----EFFGPVAQIYVVKNDEE--AIQLANDSHYGLGGAVFSQDIERAKRMASAIETG 410
Cdd:cd07126 359 ygaYEPTavFVPLEEIAIEENFElvttEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNG 438
|
410
....*....|....*
gi 488976554 411 MVY--INWLTDTAPE 423
Cdd:cd07126 439 TTYagIRARTTGAPQ 453
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
22-409 |
3.07e-10 |
|
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: 61.87 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 22 DADVEAALQQADALYHSAWAKgdiepRLAVLHKLADLIDSRAEELAKIASQEMGklikqsrgevklcaqIARYYADNAKS 101
Cdd:cd07121 7 DDAVAAAKAAQKQYRKCTLAD-----REKIIEAIREALLSNAEELAEMAVEETG---------------MGRVEDKIAKN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 102 FLAPVKYPSE---LGEAW--------VEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVI------AKHASIVphCA 164
Cdd:cd07121 67 HLAAEKTPGTedlTTTAWsgdngltlVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVfnphpgAKKVSAY--AV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 165 ETFAHLVREAGAPEgawtNLFI-----SQDQVAKIIADDRVQGAALTGsekaGSVVAAQAAKHIKKSTLELGGNDVFVVL 239
Cdd:cd07121 145 ELINKAIAEAGGPD----NLVVtveepTIETTNELMAHPDINLLVVTG----GPAVVKAALSSGKKAIGAGAGNPPVVVD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 240 DDADLERAVKIGVQ--ARLNNAgqVCTAAKRFILHENIADAFLTKFSEAFRQVkigdpldesttlgpLSSKDAldtlSKQ 317
Cdd:cd07121 217 ETADIEKAARDIVQgaSFDNNL--PCIAEKEVIAVDSVADYLIAAMQRNGAYV--------------LNDEQA----EQL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 318 VDEAVKNGAKLHLGGKAVAREGNFFEPTIltGIT-------------RDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDS 384
Cdd:cd07121 277 LEVVLLTNKGATPNKKWVGKDASKILKAA--GIEvpadirliivetdKDHPFVVEEQMMPILPVVRVKNFDEAIELAVEL 354
|
410 420
....*....|....*....|....*..
gi 488976554 385 HYGL--GGAVFSQDIERAKRMASAIET 409
Cdd:cd07121 355 EHGNrhTAIIHSKNVENLTKMARAMQT 381
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
23-409 |
6.11e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 57.99 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 23 ADVEAALQQADALYhSAWAKGDIEPRLAVLHKLADLIDSRAEELAKIASQE--MG----KLIKQsrgevklcaqiaRYYA 96
Cdd:PRK15398 36 ASVDDAVAAAKVAQ-QRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEEtgMGrvedKIAKN------------VAAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 97 DNAK--SFLAPVKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVI------AKHASIvpHCAETFA 168
Cdd:PRK15398 103 EKTPgvEDLTTEALTGDNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVfsphpgAKKVSL--RAIELLN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 169 HLVREAGAPEgawtNLFISQ-----DQVAKIIADDRVQGAALTGsekaGSVVAAQAAKHIKKSTLELGGNDVFVVLDDAD 243
Cdd:PRK15398 181 EAIVAAGGPE----NLVVTVaeptiETAQRLMKHPGIALLVVTG----GPAVVKAAMKSGKKAIGAGAGNPPVVVDETAD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 244 LERAVKIGVQ-ARLNNaGQVCTAAKRFILHENIADAFLTKFsEAFRQVKIgdpldesttlgplsSKDALDTLSKQVdeaV 322
Cdd:PRK15398 253 IEKAARDIVKgASFDN-NLPCIAEKEVIVVDSVADELMRLM-EKNGAVLL--------------TAEQAEKLQKVV---L 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 323 KNGAklHLGGKAVAREGNFF----------EPTILTGIT-RDNPAYFEEFFGPVAQIYVVKNDEEAIQLANDSHYGL--G 389
Cdd:PRK15398 314 KNGG--TVNKKWVGKDAAKIleaaginvpkDTRLLIVETdANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhT 391
|
410 420
....*....|....*....|
gi 488976554 390 GAVFSQDIERAKRMASAIET 409
Cdd:PRK15398 392 AIMHSRNVDNLNKMARAIQT 411
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
63-455 |
4.11e-08 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 55.35 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 63 AEELAKIASQEMGKLIKQSRgEVKLCAQiARYYADNAKSFLAP-VKYPSELGEAWVEHHPIGVLLAVEPWNFPYYQLIRV 141
Cdd:cd07081 38 RIDLAKLAVSETGMGRVEDK-VIKNHFA-AEYIYNVYKDEKTCgVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 142 LAPNLAAGNPVI------AKHASIvpHCAETFAHLVREAGAPEgawtNLFISQDQVAKIIADDRVQ--GAALTGSEKAGS 213
Cdd:cd07081 116 SLISLKTRNSIIfsphprAKKVTQ--RAATLLLQAAVAAGAPE----NLIGWIDNPSIELAQRLMKfpGIGLLLATGGPA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 214 VVAAqAAKHIKKSTLELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKRFILHENIADAFLTKFSEAFRQVKIG 293
Cdd:cd07081 190 VVKA-AYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 294 DPLDEsttLGPLSSKDAlDTLSKQVDEAVKNGAKlhLGGKAVAREGN--FFEPTILTgitrDNPAYFEEFFGPVAQIYVV 371
Cdd:cd07081 269 EELQQ---VQPVILKNG-DVNRDIVGQDAYKIAA--AAGLKVPQETRilIGEVTSLA----EHEPFAHEKLSPVLAMYRA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 372 KN----DEEAIQLANDSHYGLGGAVFSQD---IERAKRMASAIETGMVYINWLTDTA-----------PELPFGGVKRSG 433
Cdd:cd07081 339 ANfadaDAKALALKLEGGCGHTSAMYSDNikaIENMNQFANAMKTSRFVKNGPCSQGglgdlynfrgwPSMTLGCGTWGG 418
|
410 420
....*....|....*....|..
gi 488976554 434 YGRElSDLGIKEFVNQKLVVVR 455
Cdd:cd07081 419 NSVS-ENVGPKHLVNLKTVALR 439
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
50-415 |
2.81e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 52.49 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 50 AVLHKLADLIDSRAEELAKIASQEMG------KLIKQSRGevklCAQIARYYADnaKSFLAPVKYPSELGE---AWvehh 120
Cdd:cd07122 25 KIVEAVAWAAADAAEELAKMAVEETGmgvvedKVIKNHFA----SEYVYNDIKD--MKTVGVIEEDEEKGIveiAE---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 121 PIGVLLAVEPWNFP-----YYQLIrvlapNLAAGNPVI-AKHASIVPHCAETfAHLVREA----GAPEGA--W------- 181
Cdd:cd07122 95 PVGVIAALIPSTNPtstaiFKALI-----ALKTRNAIIfSPHPRAKKCSIEA-AKIMREAavaaGAPEGLiqWieepsie 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 182 -TNLFISQDQVAKIIAddrvqgaalTGSekAGSVVAAQAAKhikKSTLELG-GNDVFVVLDDADLERAV-KIGVQARLNN 258
Cdd:cd07122 169 lTQELMKHPDVDLILA---------TGG--PGMVKAAYSSG---KPAIGVGpGNVPAYIDETADIKRAVkDIILSKTFDN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 259 aGQVCTAAKRFILHENIADAFLTKFSE-------AFRQVKIGDPL--DESTTLGPLSSKDAlDTLSKQVDEAVKNGAKLh 329
Cdd:cd07122 235 -GTICASEQSVIVDDEIYDEVRAELKRrgayflnEEEKEKLEKALfdDGGTLNPDIVGKSA-QKIAELAGIEVPEDTKV- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 330 lggkAVAREgnffeptilTGITRDNPaYFEEFFGPVAQIYVVKNDEEAIQLAND--SHYGLG--GAVFSQDIERAKRMAS 405
Cdd:cd07122 312 ----LVAEE---------TGVGPEEP-LSREKLSPVLAFYRAEDFEEALEKAREllEYGGAGhtAVIHSNDEEVIEEFAL 377
|
410
....*....|
gi 488976554 406 AIETGMVYIN 415
Cdd:cd07122 378 RMPVSRILVN 387
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
121-415 |
5.08e-06 |
|
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: 48.63 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 121 PIGVLLAVEPWNFPYYQLIRVLAPNLAAGNPVIAK-H-ASIVPHC--AETFAHLVREAG-APEGAWTNLFISQDQVAKII 195
Cdd:cd07127 193 PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKpHpAAILPLAitVQVAREVLAEAGfDPNLVTLAADTPEEPIAQTL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 196 ADD-RVQGAALTGSEKAGSVVAAQAAKhiKKSTLELGGNDVFVVLDDADLERAVKIGVQARLNNAGQVCTAAKR-FILHE 273
Cdd:cd07127 273 ATRpEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNiYVPRD 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 274 NIA--------DAFLTKFSEAFRQVkIGDPLDESTTLGPLSSKDALDTLskqvdEAVKNGAKLHLGGKAVAR----EGNF 341
Cdd:cd07127 351 GIQtddgrksfDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARI-----AEARQLGEVLLASEAVAHpefpDARV 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976554 342 FEPTILTGITRDNPAYFEEFFGPVAqiYVVKND--EEAIQLANDS---HYGLGGAVFSQDIERAKRMASAIE-------- 408
Cdd:cd07127 425 RTPLLLKLDASDEAAYAEERFGPIA--FVVATDstDHSIELARESvreHGAMTVGVYSTDPEVVERVQEAALdagvalsi 502
|
....*....
gi 488976554 409 --TGMVYIN 415
Cdd:cd07127 503 nlTGGVFVN 511
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
240-295 |
6.64e-03 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 38.51 E-value: 6.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976554 240 DDADLERAVKIGVQARLNNAGqVCTAAKRFILHENIADAFLTKFSEAFR--QVKI-GDP 295
Cdd:PRK00197 235 ESADLDKALKIVLNAKTQRPS-VCNALETLLVHEAIAEEFLPKLAEALAeaGVELrGDE 292
|
|
| |
