|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
35-496 |
0e+00 |
|
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: 802.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 35 GETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESGVWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPI 114
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 115 RFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPS 194
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 195 EKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQSNMKRVWLEAGGKSP 274
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 275 HIVFNDCPDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTI 354
Cdd:cd07112 241 NIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 355 LGYIEAGKQQGAVLVCGGEQLMAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGV 434
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655375262 435 WTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
19-498 |
0e+00 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 646.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 19 ICGQAFIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESGVWSRMAPVERKKVMIRFADLLEAH 98
Cdd:PRK09847 18 IENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 99 SDELALLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWK 178
Cdd:PRK09847 98 AEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 179 LGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAG 258
Cdd:PRK09847 178 LGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 259 QSNMKRVWLEAGGKSPHIVFNDCPDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDP 338
Cdd:PRK09847 258 DSNMKRVWLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 339 DTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAetggVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQ 418
Cdd:PRK09847 338 ATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLA----AAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 419 AIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATWIAI 498
Cdd:PRK09847 414 ALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
22-496 |
0e+00 |
|
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: 588.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 22 QAFIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDE 101
Cdd:COG1012 7 PLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPA--WAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 102 LALLETLDMGKPIRFSKsVDVTNAARALRWSGEAVDKIYDEIAPT-ADNEIGMITREPVGVVAAIVPWNFPLLMACWKLG 180
Cdd:COG1012 85 LAALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSdAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 181 PALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQs 260
Cdd:COG1012 164 PALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 261 NMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDT 340
Cdd:COG1012 243 NLKRVTLELGGKNPAIVLDDA-DLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 341 VSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAI 420
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRP-DGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655375262 421 AIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWIN-HYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATWI 496
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINdGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
22-493 |
0e+00 |
|
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: 569.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 22 QAFIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESGVWSRMAPVERKKVMIRFADLLEAHSDE 101
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 102 LALLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGP 181
Cdd:cd07091 85 LAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 182 ALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQSN 261
Cdd:cd07091 165 ALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 262 MKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTV 341
Cdd:cd07091 245 LKKVTLELGGKSPNIVFDDA-DLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 342 SGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmaETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIA 421
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGERH--GSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655375262 422 IGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:cd07091 402 RANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKA 473
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
34-493 |
0e+00 |
|
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: 554.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 34 SGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKP 113
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA--WRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 114 IRFSKsVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKP 193
Cdd:pfam00171 83 LAEAR-GEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 194 SEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKS 273
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTLELGGKN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 274 PHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQT 353
Cdd:pfam00171 241 PLIVLEDA-DLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 354 ILGYIEAGKQQGAVLVCGGEQLMAEtgGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAG 433
Cdd:pfam00171 320 VLKYVEDAKEEGAKLLTGGEAGLDN--GYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655375262 434 VWTADLSKAHRTAKALRSGMVWINHYDGGDM-TAPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
76-496 |
5.42e-178 |
|
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: 506.36 E-value: 5.42e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKsVDVTNAARALRWSGEAVDKIYDEIAPTAD-NEIGMI 154
Cdd:cd07078 14 WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRLHGEVIPSPDpGELAIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 155 TREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALAL 234
Cdd:cd07078 93 RREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALAS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 235 HMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESG 314
Cdd:cd07078 173 HPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDA-DLDAAVKGAVFGAFGNAGQVCTAASRLLVHES 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 315 VKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEqLMAETGGVYVAPTLFREVNN 394
Cdd:cd07078 251 IYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGK-RLEGGKGYFVPPTVLTDVDP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 395 QMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYD-GGDMTAPFGGYKQ 473
Cdd:cd07078 330 DMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSvGAEPSAPFGGVKQ 409
|
410 420
....*....|....*....|...
gi 655375262 474 SGNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd07078 410 SGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
24-496 |
2.47e-177 |
|
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: 506.85 E-value: 2.47e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESGVWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSvDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPAL 183
Cdd:cd07119 81 RLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 184 ASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMvYAGQSNMK 263
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIM-RAAAGNVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 264 RVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSG 343
Cdd:cd07119 239 KVALELGGKNPNIVFADA-DFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 344 AVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmAETG---GVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAI 420
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRP-TGDElakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655375262 421 AIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd07119 397 RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
42-498 |
1.79e-174 |
|
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: 498.50 E-value: 1.79e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 42 SPVDGNKLAAVASCDLADAEAAVASARASFEsgVWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSVD 121
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFE--AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 122 VTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTA 201
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 202 IRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMvYAGQSNMKRVWLEAGGKSPHIVFNDC 281
Cdd:cd07115 161 LRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIM-QGAAGNLKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 282 pDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAG 361
Cdd:cd07115 240 -DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 362 KQQGAVLVCGGEQLMAEtgGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSK 441
Cdd:cd07115 319 REEGARLLTGGKRPGAR--GFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 655375262 442 AHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATWIAI 498
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
71-496 |
1.08e-172 |
|
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: 493.99 E-value: 1.08e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 71 FESGVWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSvDVTNAARALRWSGEAVDKIYDEIAPT-ADN 149
Cdd:cd07114 32 FEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA-QVRYLAEWYRYYAGLADKIEGAVIPVdKGD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 150 EIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVG 229
Cdd:cd07114 111 YLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 230 KALALHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRL 309
Cdd:cd07114 191 EALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIVFDDA-DLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 310 LVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAE--TGGVYVAPT 387
Cdd:cd07114 269 LVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSGAdlGAGYFFEPT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 388 LFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAP 467
Cdd:cd07114 349 ILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSP 428
|
410 420
....*....|....*....|....*....
gi 655375262 468 FGGYKQSGNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd07114 429 FGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
22-493 |
9.57e-172 |
|
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: 492.39 E-value: 9.57e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 22 QAFIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESGVWSRMAPVERKKVMIRFADLLEAHSDE 101
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 102 LALLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGP 181
Cdd:cd07142 85 LAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 182 ALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQSN 261
Cdd:cd07142 165 ALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 262 MKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTV 341
Cdd:cd07142 245 LKPVTLELGGKSPFIVCEDA-DVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 342 SGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmaETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIA 421
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITGGDRI--GSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655375262 422 IGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKA 473
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
41-496 |
4.10e-171 |
|
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: 489.77 E-value: 4.10e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 41 ISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSV 120
Cdd:cd07093 2 FNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG--WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 121 DVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLT 200
Cdd:cd07093 80 DIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 201 AIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVyAGQSNMKRVWLEAGGKSPHIVFND 280
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMR-AAAPNLKPVSLELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 281 CpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEA 360
Cdd:cd07093 239 A-DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 361 GKQQGAVLVCGG--EQLMAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTAD 438
Cdd:cd07093 318 ARAEGATILTGGgrPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 655375262 439 LSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd07093 398 LGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
22-492 |
9.99e-169 |
|
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: 484.93 E-value: 9.99e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 22 QAFIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESG-VWSRMAPVERKKVMIRFADLLEAHSD 100
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGsPWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 101 ELALLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPtADNEIGMITR-EPVGVVAAIVPWNFPLLMACWKL 179
Cdd:cd07141 88 YLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIP-MDGDFFTYTRhEPVGVCGQIIPWNFPLLMAAWKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 180 GPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQ 259
Cdd:cd07141 167 APALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 260 SNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPD 339
Cdd:cd07141 247 SNLKRVTLELGGKSPNIVFADA-DLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 340 TVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmaETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQA 419
Cdd:cd07141 326 TEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRH--GDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEV 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655375262 420 IAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIK 492
Cdd:cd07141 404 IERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVK 476
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
24-492 |
4.47e-164 |
|
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: 472.98 E-value: 4.47e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPAL 183
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 184 ASGNSVILKPSEKSPLTAIRMAAIALEAgIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQsNMK 263
Cdd:cd07559 162 AAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE-NLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 264 RVWLEAGGKSPHIVFND----CPDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPD 339
Cdd:cd07559 240 PVTLELGGKSPNIFFDDamdaDDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 340 TVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGE--QLMAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGME 417
Cdd:cd07559 320 TMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGErlTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655375262 418 QAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIK 492
Cdd:cd07559 400 EAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
24-498 |
5.10e-162 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 468.53 E-value: 5.10e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESGVWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPAL 183
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 184 ASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQSNMK 263
Cdd:PLN02766 184 AAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 264 RVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSG 343
Cdd:PLN02766 264 QVSLELGGKSPLLIFDDA-DVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 344 AVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAEtgGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIG 423
Cdd:PLN02766 343 PQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDK--GYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKA 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655375262 424 NDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATWIAI 498
Cdd:PLN02766 421 NNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
24-493 |
2.59e-158 |
|
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: 457.73 E-value: 2.59e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:cd07138 2 YIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDkiydEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPAL 183
Cdd:cd07138 80 QAITLEMGAPITLARAAQVGLGIGHLRAAADALK----DFEFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 184 ASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQSnMK 263
Cdd:cd07138 156 AAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT-VK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 264 RVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSG 343
Cdd:cd07138 235 RVALELGGKSANIILDDA-DLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 344 AVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAE-TGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAI 422
Cdd:cd07138 314 PLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEGlERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAI 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655375262 423 GNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINhYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:cd07138 394 ANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKS 463
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
24-493 |
3.72e-158 |
|
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: 458.02 E-value: 3.72e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgVWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLADLVEKNRDLLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPAL 183
Cdd:cd07144 90 AIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 184 ASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQsNMK 263
Cdd:cd07144 170 AAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQ-NLK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 264 RVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKS-WQPGHPLDPDTVS 342
Cdd:cd07144 249 AVTLECGGKSPALVFEDA-DLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 343 GAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAETG-GVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIA 421
Cdd:cd07144 328 GPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIK 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655375262 422 IGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:cd07144 408 KANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKA 479
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
24-496 |
3.89e-158 |
|
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: 457.76 E-value: 3.89e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESGVWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPAL 183
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 184 ASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQSNMK 263
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSNLK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 264 RVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSG 343
Cdd:cd07143 250 KVTLELGGKSPNIVFDDA-DLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 344 AVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAEtgGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIG 423
Cdd:cd07143 329 PQVSQIQYERIMSYIESGKAEGATVETGGKRHGNE--GYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655375262 424 NDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
41-498 |
1.62e-157 |
|
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: 455.16 E-value: 1.62e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 41 ISPVDGNKLAAVASCDLADAEAAVASARASFESGvWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSv 120
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESG-WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 121 DVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLT 200
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 201 AIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFND 280
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 281 CpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPL-DPDTvsGAVVDQQQLQTILGYIE 359
Cdd:cd07109 239 A-DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLeDPDL--GPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 360 AGKQQGAVLVCGGEQLM-AETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTAD 438
Cdd:cd07109 316 RARARGARIVAGGRIAEgAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655375262 439 LSKAHRTAKALRSGMVWINHY-DGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKAtwIAI 498
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNNYgAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKT--VAV 454
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
24-498 |
1.62e-155 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 451.57 E-value: 1.62e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:TIGR02299 4 FIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKR--WAELKAAERKRYLHKIADLIEQHADEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSVdVTNAARALRWSGEAV-DKIYDEIAPTaDNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPA 182
Cdd:TIGR02299 82 VLECLDCGQPLRQTRQQ-VIRAAENFRFFADKCeEAMDGRTYPV-DTHLNYTVRVPVGPVGLITPWNAPFMLSTWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 183 LASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVyAGQSNM 262
Cdd:TIGR02299 160 LAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMR-NGADTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 263 KRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVS 342
Cdd:TIGR02299 239 KRFSMELGGKSPVIVFDDA-DLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPETEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 343 GAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAETG-----GVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGME 417
Cdd:TIGR02299 318 GPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPTFRGedlgrGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFKDEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 418 QAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATWIA 497
Cdd:TIGR02299 398 EAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNVALA 477
|
.
gi 655375262 498 I 498
Cdd:TIGR02299 478 L 478
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
24-493 |
3.92e-155 |
|
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: 449.72 E-value: 3.92e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESGVWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKI-YDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPA 182
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 183 LASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGfGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQsNM 262
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE-RL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 263 KRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVS 342
Cdd:cd07139 240 ARVTLELGGKSAAIVLDDA-DLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 343 GAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAI 422
Cdd:cd07139 319 GPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655375262 423 GNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYdGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:cd07139 399 ANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKS 468
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
22-493 |
1.44e-154 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 448.95 E-value: 1.44e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 22 QAFIHGEYCAAVSGETFDCISPVDGNKLAAVASCDladaEAAVASARASFESG--VWSRMAPVERKKVMIRFADLLEAHS 99
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAAT----PADVEAAVASAKQGqkIWAAMTAMERSRILRRAVDILRERN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 100 DELALLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKL 179
Cdd:PRK13252 84 DELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 180 GPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGhTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQ 259
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 260 SnMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPD 339
Cdd:PRK13252 243 S-LKEVTMELGGKSPLIVFDDA-DLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 340 TVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAE--TGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGME 417
Cdd:PRK13252 321 TNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGgfANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDED 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655375262 418 QAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:PRK13252 401 EVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKS 476
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
22-493 |
9.68e-154 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 448.87 E-value: 9.68e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 22 QAFIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESGVWSRMAPVERKKVMIRFADLLEAHSDE 101
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 102 LALLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGP 181
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 182 ALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQSN 261
Cdd:PLN02466 219 ALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 262 MKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTV 341
Cdd:PLN02466 299 LKPVTLELGGKSPFIVCEDA-DVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 342 SGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAEtgGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIA 421
Cdd:PLN02466 378 QGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSK--GYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIR 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655375262 422 IGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:PLN02466 456 RANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKA 527
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
70-496 |
1.77e-153 |
|
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: 444.86 E-value: 1.77e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 70 SFESGVWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSK-----SVDVTN--AARALRWSGEAVDKIyde 142
Cdd:cd07118 31 AFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARgeiegAADLWRyaASLARTLHGDSYNNL--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 143 iaptADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLP 222
Cdd:cd07118 108 ----GDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 223 GFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEV 302
Cdd:cd07118 184 GYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADA-DLDAAADAVVFGVYFNAGEC 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 303 CTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmAETGGV 382
Cdd:cd07118 262 CNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERL-ASAAGL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 383 YVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGG 462
Cdd:cd07118 341 FYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDG 420
|
410 420 430
....*....|....*....|....*....|....
gi 655375262 463 DMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd07118 421 SPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
24-492 |
4.64e-150 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 436.93 E-value: 4.64e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFesGVWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPAL 183
Cdd:TIGR01804 79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 184 ASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGqSNMK 263
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 264 RVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSG 343
Cdd:TIGR01804 238 HVTMELGGKSPLIVFDDA-DLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 344 AVVDQQQLQTILGYIEAGKQQGAVLVCGGE--QLMAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIA 421
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGrpENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655375262 422 IGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIK 492
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
41-493 |
5.28e-146 |
|
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: 426.27 E-value: 5.28e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 41 ISPVDGNKLAAVASCDLADAEAAVASARASFESGVWSrMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSV 120
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 121 DVTNAARALRWSGEAVDKIYDEIAPTADNEIGMIT-----REPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSE 195
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGrrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 196 KSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPH 275
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 276 IVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTIL 355
Cdd:cd07089 240 IVLDDA-DLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 356 GYIEAGKQQGAVLVCGGEQLMAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVW 435
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 655375262 436 TADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
75-496 |
3.15e-143 |
|
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: 419.02 E-value: 3.15e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 75 VWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIrFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMI 154
Cdd:cd07090 34 EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPI-EEARVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 155 TREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTvGKALAL 234
Cdd:cd07090 113 RREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 235 HMDVDTLVFTGSTKIAKQLMVYAGqSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESG 314
Cdd:cd07090 192 HPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIFDDA-DLENAVNGAMMANFLSQGQVCSNGTRVFVQRS 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 315 VKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAE---TGGVYVAPTLFRE 391
Cdd:cd07090 270 IKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLCGGERVVPEdglENGFYVSPCVLTD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 392 VNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGY 471
Cdd:cd07090 350 CTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGY 429
|
410 420
....*....|....*....|....*
gi 655375262 472 KQSGNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd07090 430 KQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
24-496 |
7.04e-141 |
|
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: 413.77 E-value: 7.04e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPAL 183
Cdd:cd07117 82 MVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 184 ASGNSVILKPSEKSPLTAIRMAAIaLEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQsNMK 263
Cdd:cd07117 162 AAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK-KLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 264 RVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSG 343
Cdd:cd07117 240 PATLELGGKSANIIFDDA-NWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 344 AVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAE--TGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIA 421
Cdd:cd07117 319 AQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655375262 422 IGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd07117 399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
41-492 |
1.32e-140 |
|
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: 411.83 E-value: 1.32e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 41 ISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSv 120
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT--WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 121 DVTNAARALRWSGEAVDKIYDEI--APTADNEIgMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSP 198
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTipSPAPGKRI-LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 199 LTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGqSNMKRVWLEAGGKSPHIVF 278
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 279 NDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYI 358
Cdd:cd07103 237 DDA-DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 359 EAGKQQGAVLVCGGEQLmaETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTAD 438
Cdd:cd07103 316 EDAVAKGAKVLTGGKRL--GLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 655375262 439 LSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIK 492
Cdd:cd07103 394 LARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETK 447
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
24-496 |
1.83e-138 |
|
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: 407.41 E-value: 1.83e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGEtfDCISPVDGNK-LAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDEL 102
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSDTSDvVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 103 ALLETLDMGKPIRFSKSvDVTNAARALRWSGEAVDKIYDEIAPTADNEIGM-ITREPVGVVAAIVPWNFPLLMACWKLGP 181
Cdd:cd07097 80 ARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVeTTREPLGVVGLITPWNFPIAIPAWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 182 ALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGqSN 261
Cdd:cd07097 159 ALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-AR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 262 MKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTV 341
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDA-DLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 342 SGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIA 421
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655375262 422 IGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGG-DMTAPFGGYKQSGNG-RDKSLHAFDKYTEIKATWI 496
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGvDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTVYV 473
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
22-496 |
8.88e-136 |
|
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: 401.10 E-value: 8.88e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 22 QAFIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESGVWSRMAPVERKKVMIRFADLLEAHSDE 101
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 102 LALLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPT----ADNEIGMITREPVGVVAAIVPWNFPLLMACW 177
Cdd:cd07140 87 LATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPInqarPNRNLTLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 178 KLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYA 257
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 258 GQSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLD 337
Cdd:cd07140 247 AVSNLKKVSLELGGKSPLIIFADC-DMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 338 PDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmaETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEG-- 415
Cdd:cd07140 326 RSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQV--DRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgd 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 416 MEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATW 495
Cdd:cd07140 404 VDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVT 483
|
.
gi 655375262 496 I 496
Cdd:cd07140 484 I 484
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
76-496 |
6.22e-134 |
|
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: 391.98 E-value: 6.22e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSvDVTNAARALRWSGEAVDKI-YDEIAPTADNEIGMI 154
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLgGPELPSPDPGGEAYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 155 TREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALAL 234
Cdd:cd06534 89 RREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 235 HMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESG 314
Cdd:cd06534 169 HPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDA-DLDAAVEGAVFGAFFNAGQICTAASRLLVHES 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 315 VKEQlialIIDELKswqpghpldpdtvsgavvdqqqlqtilgyieagkqqgavlvcggeqlmaetggvyvapTLFREVNN 394
Cdd:cd06534 247 IYDE----FVEKLV----------------------------------------------------------TVLVDVDP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 395 QMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYD-GGDMTAPFGGYKQ 473
Cdd:cd06534 265 DMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSiGVGPEAPFGGVKN 344
|
410 420
....*....|....*....|...
gi 655375262 474 SGNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd06534 345 SGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
24-492 |
3.68e-132 |
|
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: 391.43 E-value: 3.68e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPAL 183
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 184 ASGNSVILKPSEKSPLTAIRMAAIALEAgIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQsNMK 263
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 264 RVWLEAGGKSPHIVFNDCPDLKAA----AQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPD 339
Cdd:cd07116 240 PVTLELGGKSPNIFFADVMDADDAffdkALEGFVMFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 340 TVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGE--QLMAETGGVYVAPTLFREvNNQMSIAREEIFGPVLSVIEFEGME 417
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGErnELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655375262 418 QAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIK 492
Cdd:cd07116 399 EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
22-492 |
2.25e-131 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 389.27 E-value: 2.25e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 22 QAFIHGEYcAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDE 101
Cdd:PRK13473 4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 102 LALLETLDMGKPIRFSK------SVDVTN----AARAL--RWSGEavdkiYDEiaptadNEIGMITREPVGVVAAIVPWN 169
Cdd:PRK13473 81 FARLESLNCGKPLHLALndeipaIVDVFRffagAARCLegKAAGE-----YLE------GHTSMIRRDPVGVVASIAPWN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 170 FPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAgIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKI 249
Cdd:PRK13473 150 YPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 250 AKQLMVYAGqSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKS 329
Cdd:PRK13473 229 GKHVLSAAA-DSVKRTHLELGGKAPVIVFDDA-DLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVAT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 330 WQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQG-AVLVCGGEqlMAETGGVYVAPTLFREVNNQMSIAREEIFGPVL 408
Cdd:PRK13473 307 LKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGE--APDGKGYYYEPTLLAGARQDDEIVQREVFGPVV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 409 SVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWIN-HYdggdMTA---PFGGYKQSGNGRDKSLHA 484
Cdd:PRK13473 385 SVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNtHF----MLVsemPHGGQKQSGYGKDMSLYG 460
|
....*...
gi 655375262 485 FDKYTEIK 492
Cdd:PRK13473 461 LEDYTVVR 468
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
24-488 |
1.34e-130 |
|
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: 387.52 E-value: 1.34e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSVDVTNAARALRWsgeavdkiYDEIAPTADNEigMITREPVGVVAAIVPWNFPLLMACWKLGPAL 183
Cdd:cd07111 103 VLESLDNGKPIRESRDCDIPLVARHFYH--------HAGWAQLLDTE--LAGWKPVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 184 ASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTvGKALALHMDVDTLVFTGSTKIAKQLM-VYAGQSnm 262
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRrATAGTG-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 263 KRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVS 342
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDA-DLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 343 GAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAEtgGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAI 422
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSK--GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVAL 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655375262 423 GNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKY 488
Cdd:cd07111 407 ANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
76-492 |
3.90e-130 |
|
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: 385.55 E-value: 3.90e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIrFSKSVDVTNAARALRWSG---EAVDKIYDEIAPTADNEI- 151
Cdd:cd07110 35 WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPL-DEAAWDVDDVAGCFEYYAdlaEQLDAKAERAVPLPSEDFk 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 152 GMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKA 231
Cdd:cd07110 114 ARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 232 LALHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLV 311
Cdd:cd07110 194 LAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSPIIVFDDA-DLEKAVEWAMFGCFWNNGQICSATSRLLV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 312 ESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAETGGVYVAPTLFRE 391
Cdd:cd07110 272 HESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGARLLCGGRRPAHLEKGYFIAPTVFAD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 392 VNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGY 471
Cdd:cd07110 352 VPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGY 431
|
410 420
....*....|....*....|.
gi 655375262 472 KQSGNGRDKSLHAFDKYTEIK 492
Cdd:cd07110 432 KRSGIGRELGEWGLDNYLEVK 452
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
24-496 |
1.42e-125 |
|
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: 374.76 E-value: 1.42e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAA-VASCDLADAEAAVASARASFesGVWSRMAPVERKKVMIRFADLLEAHSDEL 102
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVVGtFPLSTASDVDAAVEAAREAF--PEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 103 ALLETLDMGKPIRFSKSvDVTNAARALRWSGEAVDKIYDEIAPTA-DNEIGMITREPVGVVAAIVPWNFPLLMACWKLGP 181
Cdd:cd07131 80 ARLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 182 ALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQSN 261
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 262 mKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTV 341
Cdd:cd07131 239 -KRVALEMGGKNPIIVMDDA-DLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 342 SGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAETG--GVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQA 419
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYekGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655375262 420 IAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYD-GGDMTAPFGGYKQSGNG-RDKSLHAFDKYTEIKATWI 496
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTiGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
41-492 |
9.80e-124 |
|
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: 368.96 E-value: 9.80e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 41 ISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSV 120
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 121 DVTNAARALRWSGEAVDKIYDEIAPT-ADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPL 199
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLEGPAAGEyLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 200 TAIRMAAIALEaGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGqSNMKRVWLEAGGKSPHIVFN 279
Cdd:cd07092 160 TTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAA-DTLKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 280 DCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIE 359
Cdd:cd07092 238 DA-DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 360 AGKqQGAVLVCGGEQlmAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADL 439
Cdd:cd07092 317 RAP-AHARVLTGGRR--AEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 655375262 440 SKAHRTAKALRSGMVWINhyDGGDMTA--PFGGYKQSGNGRDKSLHAFDKYTEIK 492
Cdd:cd07092 394 GRAMRLSARLDFGTVWVN--THIPLAAemPHGGFKQSGYGKDLSIYALEDYTRIK 446
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
22-492 |
4.53e-123 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 369.02 E-value: 4.53e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 22 QAFIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDE 101
Cdd:PLN02278 26 QGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPS--WSKLTASERSKILRRWYDLIIANKED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 102 LALLETLDMGKPIRFSKSvDVTNAARALRWSGEAVDKIYDEIAPT--ADNEIgMITREPVGVVAAIVPWNFPLLMACWKL 179
Cdd:PLN02278 104 LAQLMTLEQGKPLKEAIG-EVAYGASFLEYFAEEAKRVYGDIIPSpfPDRRL-LVLKQPVGVVGAITPWNFPLAMITRKV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 180 GPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQ 259
Cdd:PLN02278 182 GPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 260 SnMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPD 339
Cdd:PLN02278 262 T-VKRVSLELGGNAPFIVFDDA-DLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 340 TVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAetGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQA 419
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSL--GGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEA 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655375262 420 IAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIK 492
Cdd:PLN02278 418 IAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
41-496 |
1.94e-122 |
|
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: 365.93 E-value: 1.94e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 41 ISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSv 120
Cdd:cd07107 2 INPATGQVLARVPAASAADVDRAVAAARAAFPE--WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 121 DVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLT 200
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 201 AIRMAAIALEAgIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQSnMKRVWLEAGGKSPHIVFND 280
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 281 CpDLKAAAQAAASAIAFN-QGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIE 359
Cdd:cd07107 237 A-DPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 360 AGKQQGAVLVCGG--EQLMAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTA 437
Cdd:cd07107 316 SAKREGARLVTGGgrPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655375262 438 DLSKAHRTAKALRSGMVWIN----HYDGgdmtAPFGGYKQSGNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd07107 396 DISQAHRTARRVEAGYVWINgssrHFLG----APFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
24-496 |
9.12e-122 |
|
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: 364.84 E-value: 9.12e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESGvWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSA-WAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSVDVTNAARALR----WSGEAVDKIYDEIAPTADNE--IGMITREPVGVVAAIVPWNFPLLMACW 177
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANFLRyfagWATKINGETLAPSIPSMQGEryTAFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 178 KLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHtVGKALALHMDVDTLVFTGST----KIAKQL 253
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVatgkKIGRQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 254 MvyagqSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPG 333
Cdd:cd07113 241 A-----SDLTRVTLELGGKNAAAFLKDA-DIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 334 HPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAEtgGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEF 413
Cdd:cd07113 315 SPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGE--GYFVQPTLVLARSADSRLMREETFGPVVSFVPY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 414 EGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:cd07113 393 EDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKS 472
|
...
gi 655375262 494 TWI 496
Cdd:cd07113 473 VMI 475
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
24-496 |
4.75e-119 |
|
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: 357.73 E-value: 4.75e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKsVDVTNAARALRWSGEAVDKIYDEIAP-TADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPA 182
Cdd:cd07088 79 KLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPsDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 183 LASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQsNM 262
Cdd:cd07088 158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-NI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 263 KRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVS 342
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDA-DLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 343 GAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAEtGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAI 422
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGE-KGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIEL 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655375262 423 GNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd07088 395 ANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
41-492 |
4.80e-118 |
|
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: 354.74 E-value: 4.80e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 41 ISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSV 120
Cdd:cd07108 2 INPATGQVIGEVPRSRAADVDRAVAAAKAAFPE--WAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 121 DVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLT 200
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 201 AIRMAAIALEAgIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGqsnmKR---VWLEAGGKSPHIV 277
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA----DRlipVSLELGGKSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 278 FNDCPDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGY 357
Cdd:cd07108 235 FPDADLDDAVDGAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 358 IEAGKQ-QGAVLVCGGEQLMAETG--GVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGV 434
Cdd:cd07108 315 IDLGLStSGATVLRGGPLPGEGPLadGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 655375262 435 WTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHA-FDKYTEIK 492
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKK 453
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
22-492 |
2.50e-117 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 354.42 E-value: 2.50e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 22 QAFIHGEYCAAVSGETFDCISPVDGNKLAAVA---SCDLADAEAAVASARASFESGVWSRMAPVERKKVMIRFADLLEAH 98
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPaatAEDVDAAVEAARKAFKRNKGKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 99 SDELALLETLDMGKPIRFSKSvDVTNAARALRW---SGEAVD-KIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLM 174
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAW-DMDDVAGCFEYyadLAEALDaKQKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 175 ACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLM 254
Cdd:PLN02467 168 ATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 255 VYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGH 334
Cdd:PLN02467 248 TAAAQ-MVKPVSLELGGKSPIIVFDDV-DLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 335 PLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFE 414
Cdd:PLN02467 326 PLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFS 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655375262 415 GMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIK 492
Cdd:PLN02467 406 TEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
75-492 |
6.57e-115 |
|
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: 346.64 E-value: 6.57e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 75 VWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKsVDVTNAARALRWSGEAVDKIYDEIAPTADNE---- 150
Cdd:cd07145 36 VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR-VEVERTIRLFKLAAEEAKVLRGETIPVDAYEyner 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 151 -IGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVG 229
Cdd:cd07145 115 rIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 230 KALALHMDVDTLVFTGSTKIAKQLMVYAGqSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRL 309
Cdd:cd07145 195 DEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGGSDPMIVLKDA-DLERAVSIAVRGRFENAGQVCNAVKRI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 310 LVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQlmaeTGGVYVAPTLF 389
Cdd:cd07145 273 LVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGGKR----DEGSFFPPTVL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 390 REVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINhydggDMTA--- 466
Cdd:cd07145 349 ENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVIN-----DSTRfrw 423
|
410 420
....*....|....*....|....*....
gi 655375262 467 ---PFGGYKQSGNGRDKSLHAFDKYTEIK 492
Cdd:cd07145 424 dnlPFGGFKKSGIGREGVRYTMLEMTEEK 452
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
76-496 |
5.36e-113 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 341.43 E-value: 5.36e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKsVDVtnaARALRWSGEAVD-KIYDEIAPTADNEIGMI 154
Cdd:cd07106 35 WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ-FEV---GGAVAWLRYTASlDLPDEVIEDDDTRRVEL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 155 TREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAgIPPGVLNVLPGfGHTVGKALAL 234
Cdd:cd07106 111 RRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 235 HMDVDTLVFTGSTKIAKQLMVYAGqSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESG 314
Cdd:cd07106 189 HPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLPDV-DIDAVAPKLFWGAFINSGQVCAAIKRLYVHES 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 315 VKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmaETGGVYVAPTLFREVNN 394
Cdd:cd07106 267 IYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPL--DGPGYFIPPTIVDDPPE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 395 QMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQS 474
Cdd:cd07106 345 GSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQS 424
|
410 420
....*....|....*....|..
gi 655375262 475 GNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd07106 425 GIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
38-492 |
6.03e-113 |
|
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: 341.50 E-value: 6.03e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 38 FDCISPVDGNKLAAVASCDLADAEAAVASARASFESGvwSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFS 117
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM--KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 118 KsVDVTNAARALRWSGEAVDKIYDEI-----APTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILK 192
Cdd:cd07149 79 R-KEVDRAIETLRLSAEEAKRLAGETipfdaSPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 193 PSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGqsnMKRVWLEAGGK 272
Cdd:cd07149 158 PASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGSN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 273 SPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQ 352
Cdd:cd07149 235 AAVIVDADA-DLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 353 TILGYIEAGKQQGAVLVCGGEQlmaeTGGVYvAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAA 432
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGKR----DGAIL-EPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655375262 433 GVWTADLSKAHRTAKALRSGMVWINhyDGGDMTA---PFGGYKQSGNGRDKSLHAFDKYTEIK 492
Cdd:cd07149 389 GVFTNDLQKALKAARELEVGGVMIN--DSSTFRVdhmPYGGVKESGTGREGPRYAIEEMTEIK 449
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
70-492 |
2.49e-112 |
|
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: 340.09 E-value: 2.49e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 70 SFESGVWSRmAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKsVDVTNAARALRWSGEAVDKIYDEIAPTADN 149
Cdd:cd07120 31 AFDETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR-FEISGAISELRYYAGLARTEAGRMIEPEPG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 150 EIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEA-GIPPGVLNVLPGFGHTV 228
Cdd:cd07120 109 SFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 229 GKALALHMDVDTLVFTGSTKIAKQLMVyAGQSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSR 308
Cdd:cd07120 189 AAHLVASPDVDVISFTGSTATGRAIMA-AAAPTLKRLGLELGGKTPCIVFDDA-DLDAALPKLERALTIFAGQFCMAGSR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 309 LLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGA-VLVCGGEQLMAETGGVYVAPT 387
Cdd:cd07120 267 VLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAeVVLRGGPVTEGLAKGAFLRPT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 388 LFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAP 467
Cdd:cd07120 347 LLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAE 426
|
410 420
....*....|....*....|....*
gi 655375262 468 FGGYKQSGNGRDKSLHAFDKYTEIK 492
Cdd:cd07120 427 EGGYRQSGLGRLHGVAALEDFIEYK 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
76-498 |
1.32e-111 |
|
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: 337.20 E-value: 1.32e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKpIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTA-DNEIGMI 154
Cdd:cd07104 16 WAATPPQERAAILRKAAEILEERRDEIADWLIRESGS-TRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDvPGKESMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 155 TREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLT-AIRMAAIALEAGIPPGVLNVLPGFGHTVGKALA 233
Cdd:cd07104 95 RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGGGSEIGDALV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 234 LHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVES 313
Cdd:cd07104 175 EHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDA-DLDLAVSAAAFGAFLHQGQICMAAGRILVHE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 314 GVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEqlmAEtgGVYVAPTLFREVN 393
Cdd:cd07104 253 SVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT---YE--GLFYQPTVLSDVT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 394 NQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINhydggDMT------AP 467
Cdd:cd07104 328 PDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN-----DQTvndephVP 402
|
410 420 430
....*....|....*....|....*....|.
gi 655375262 468 FGGYKQSGNGRDKSLHAFDKYTEIKatWIAI 498
Cdd:cd07104 403 FGGVKASGGGRFGGPASLEEFTEWQ--WITV 431
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
38-498 |
9.33e-106 |
|
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: 322.74 E-value: 9.33e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 38 FDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFS 117
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPA--WAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 118 kSVDVTNAARALRWSGEAVDKIYDEIAPT-ADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEK 196
Cdd:cd07150 79 -WFETTFTPELLRAAAGECRRVRGETLPSdSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 197 SPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHI 276
Cdd:cd07150 158 TPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 277 VFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILG 356
Cdd:cd07150 237 VLADA-DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 357 YIEAGKQQGAVLVCGGEQlmaetGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWT 436
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKY-----DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILT 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655375262 437 ADLSKAHRTAKALRSGMVWINH---YDGGdmTAPFGGYKQSGNGRDKSLHAFDKYTEIKatWIAI 498
Cdd:cd07150 391 NDLQRAFKLAERLESGMVHINDptiLDEA--HVPFGGVKASGFGREGGEWSMEEFTELK--WITV 451
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
24-493 |
1.50e-101 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 312.96 E-value: 1.50e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAvSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFesGVWSRM-APVeRKKVMIRFADLLEAHSDEL 102
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEWRKVpAPR-RGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 103 ALLETLDMGKPIRFSKSvDVTnaaralrwsgEAVD----------KIYDEIAPTA-DNEIGMITREPVGVVAAIVPWNFP 171
Cdd:cd07086 78 GRLVSLEMGKILPEGLG-EVQ----------EMIDicdyavglsrMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 172 LLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEA----GIPPGVLNVLPGFGhTVGKALALHMDVDTLVFTGST 247
Cdd:cd07086 147 VAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGST 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 248 KIAKQLMVyAGQSNMKRVWLEAGGKSPHIVFnDCPDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDEL 327
Cdd:cd07086 226 EVGRRVGE-TVARRFGRVLLELGGNNAIIVM-DDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 328 KSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAETGGVYVAPTLFREVNNQMSIAREEIFGPV 407
Cdd:cd07086 304 KQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 408 LSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRS--GMVWIN-HYDGGDMTAPFGGYKQSGNGRDKSLHA 484
Cdd:cd07086 384 LYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVNiPTSGAEIGGAFGGEKETGGGRESGSDA 463
|
....*....
gi 655375262 485 FDKYTEIKA 493
Cdd:cd07086 464 WKQYMRRST 472
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
27-498 |
2.73e-98 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 304.23 E-value: 2.73e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 27 GEYCAAVSGETFDCISPVDGNKLAAV--ASCDladaeaavaSARASFESGV-----WSRMAPVERKKVMIRFADLLEAHS 99
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIpaASKE---------DVDEAYRAAAaaqkeWAATLPQERAEILEKAAQILEERR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 100 DELALLETLDMGKP-------IRFSKSVDVTNAARALRWSGeavdKIYDEIAPTADNEIgmiTREPVGVVAAIVPWNFPL 172
Cdd:cd07151 72 DEIVEWLIRESGSTrikanieWGAAMAITREAATFPLRMEG----RILPSDVPGKENRV---YREPLGVVGVISPWNFPL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 173 LMACWKLGPALASGNSVILKPSEKSPLTA-IRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAK 251
Cdd:cd07151 145 HLSMRSVAPALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 252 QLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQ 331
Cdd:cd07151 225 HIGELAGR-HLKKVALELGGNNPFVVLEDA-DIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 332 PGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEqlmAEtgGVYVAPTLFREVNNQMSIAREEIFGPVLSVI 411
Cdd:cd07151 303 YGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGE---AE--GNVLEPTVLSDVTNDMEIAREEIFGPVAPII 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 412 EFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINhydggDMT------APFGGYKQSGNGRDKSLHAF 485
Cdd:cd07151 378 KADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-----DQPvndephVPFGGEKNSGLGRFNGEWAL 452
|
490
....*....|...
gi 655375262 486 DKYTEIKatWIAI 498
Cdd:cd07151 453 EEFTTDK--WISV 463
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
39-492 |
1.75e-97 |
|
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: 301.66 E-value: 1.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 39 DCISPVDGNKLAAVASCDLADAEAAVASARASFEsgVWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSK 118
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAE--NRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 119 sVDVTNAARALRWSGEAVDKIYDEIAP-----TADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKP 193
Cdd:cd07094 80 -VEVDRAIDTLRLAAEEAERIRGEEIPldatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 194 SEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLmvyAGQSNMKRVWLEAGGKS 273
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEAL---RANAGGKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 274 PHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQT 353
Cdd:cd07094 236 PVIVDRDA-DLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 354 ILGYIEAGKQQGAVLVCGGEQlmaetGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAG 433
Cdd:cd07094 315 VERWVEEAVEAGARLLCGGER-----DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655375262 434 VWTADLSKAHRTAKALRSGMVWIN---HYDGGDMtaPFGGYKQSGNGRDKSLHAFDKYTEIK 492
Cdd:cd07094 390 IFTRDLNVAFKAAEKLEVGGVMVNdssAFRTDWM--PFGGVKESGVGREGVPYAMEEMTEEK 449
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
77-492 |
1.21e-96 |
|
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: 299.27 E-value: 1.21e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 77 SRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKsVDVTNAARALRWSGEAVDKIYDE-----IAPTADNEI 151
Cdd:cd07146 35 STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR-YEVGRAADVLRFAAAEALRDDGEsfscdLTANGKARK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 152 GMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKA 231
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 232 LALHMDVDTLVFTGSTKIAKQLmvyAGQSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLV 311
Cdd:cd07146 194 LITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGNDPLIVMDDA-DLERAATLAVAGSYANSGQRCTAVKRILV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 312 ESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQlmaetGGVYVAPTLFRE 391
Cdd:cd07146 270 HESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQR-----QGALYAPTVLDH 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 392 VNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDM-TAPFGG 470
Cdd:cd07146 345 VPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSeLSPFGG 424
|
410 420
....*....|....*....|...
gi 655375262 471 YKQSGNG-RDKSLHAFDKYTEIK 492
Cdd:cd07146 425 VKDSGLGgKEGVREAMKEMTNVK 447
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
34-477 |
2.03e-96 |
|
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: 300.68 E-value: 2.03e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 34 SGETFDCISPVDGNK-LAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGK 112
Cdd:cd07124 44 TEEKIESRNPADPSEvLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 113 PiRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILK 192
Cdd:cd07124 122 N-WAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 193 PSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLM-----VYAGQSNMKRVWL 267
Cdd:cd07124 201 PAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYeraakVQPGQKWLKRVIA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 268 EAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVD 347
Cdd:cd07124 281 EMGGKNAIIVDEDA-DLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVID 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 348 QQQLQTILGYIEAGKQQGAvLVCGGEQLMAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTI 427
Cdd:cd07124 360 KGARDRIRRYIEIGKSEGR-LLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTE 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 655375262 428 YGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTA--PFGGYKQSGNG 477
Cdd:cd07124 439 YGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGrqPFGGFKMSGTG 490
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
22-498 |
8.51e-94 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 292.97 E-value: 8.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 22 QAFIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFEsgVWSRMAPVERKKVMIRFADLLEAHSDE 101
Cdd:PRK11241 12 QALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--AWRALTAKERANILRRWFNLMMEHQDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 102 LALLETLDMGKPIRFSKSvDVTNAARALRWSGEAVDKIYDEIAP--TADNEIgMITREPVGVVAAIVPWNFPLLMACWKL 179
Cdd:PRK11241 90 LARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPghQADKRL-IVIKQPIGVTAAITPWNFPAAMITRKA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 180 GPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQ 259
Cdd:PRK11241 168 GPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 260 sNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPD 339
Cdd:PRK11241 248 -DIKKVSLELGGNAPFIVFDDA-DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 340 TVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQlmAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQA 419
Cdd:PRK11241 326 VTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKA--HELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADV 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655375262 420 IAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATWIAI 498
Cdd:PRK11241 404 IAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
76-496 |
1.74e-93 |
|
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: 290.52 E-value: 1.74e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSvDVTNAARALRW---SGEAVDKiyDEIAPTADNEiG 152
Cdd:cd07100 15 WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYyaeNAEAFLA--DEPIETDAGK-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 153 MITREPVGVVAAIVPWNFPLlmacWK----LGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTV 228
Cdd:cd07100 91 YVRYEPLGVVLGIMPWNFPF----WQvfrfAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 229 GKALAlHMDVDTLVFTGST----KIAKQlmvyAGQsNMKRVWLEAGGKSPHIVFNDcPDLKAAAQAAASAIAFNQGEVCT 304
Cdd:cd07100 167 EAIIA-DPRVRGVTLTGSEragrAVAAE----AGK-NLKKSVLELGGSDPFIVLDD-ADLDKAVKTAVKGRLQNAGQSCI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 305 AGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmaETGGVYV 384
Cdd:cd07100 240 AAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRP--DGPGAFY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 385 APTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDM 464
Cdd:cd07100 318 PPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDP 397
|
410 420 430
....*....|....*....|....*....|..
gi 655375262 465 TAPFGGYKQSGNGRDKSLHAFDKYTEIKATWI 496
Cdd:cd07100 398 RLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
76-498 |
2.59e-93 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 290.25 E-value: 2.59e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKsVDVTNAARALRWSGEAVDKIYDEIAP-TADNEIGMI 154
Cdd:cd07105 16 WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAG-FNVDLAAGMLREAASLITQIIGGSIPsDKPGTLAMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 155 TREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVL---PGFGHTVGKA 231
Cdd:cd07105 95 VKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPEVVEA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 232 LALHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLV 311
Cdd:cd07105 175 LIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDA-DLDAAANAALFGAFLNSGQICMSTERIIV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 312 ESGVKEQLIALIIDELKSWQPGhpldpDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmAETGGVYVAPTLFRE 391
Cdd:cd07105 253 HESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLAD-ESPSGTSMPPTILDN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 392 VNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINH---YDggDMTAPF 468
Cdd:cd07105 327 VTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGmtvHD--EPTLPH 404
|
410 420 430
....*....|....*....|....*....|
gi 655375262 469 GGYKQSGNGRDKSLHAFDKYTEIKatWIAI 498
Cdd:cd07105 405 GGVKSSGYGRFNGKWGIDEFTETK--WITI 432
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
76-477 |
2.06e-91 |
|
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: 285.73 E-value: 2.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKpIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMIT 155
Cdd:cd07152 29 WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGS-IRPKAGFEVGAAIGELHEAAGLPTQPQGEILPSAPGRLSLAR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 156 REPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTA-IRMAAIALEAGIPPGVLNVLPGfGHTVGKALAL 234
Cdd:cd07152 108 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPG-GADAGEALVE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 235 HMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESG 314
Cdd:cd07152 187 DPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDA-DLDLAASNGAWGAFLHQGQICMAAGRHLVHES 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 315 VKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQlmaetGGVYVAPTLFREVNN 394
Cdd:cd07152 265 VADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTY-----DGLFYRPTVLSGVKP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 395 QMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINhydggDMT------APF 468
Cdd:cd07152 340 GMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHIN-----DQTvndephNPF 414
|
....*....
gi 655375262 469 GGYKQSGNG 477
Cdd:cd07152 415 GGMGASGNG 423
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
76-493 |
2.14e-91 |
|
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: 286.06 E-value: 2.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMIT 155
Cdd:cd07102 34 WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEALADIRVPEKDGFERYIR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 156 REPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALH 235
Cdd:cd07102 114 REPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 236 mDVDTLVFTGSTK----IAKqlmvyAGQSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLV 311
Cdd:cd07102 194 -RIDHVSFTGSVAggraIQR-----AAAGRFIKVGLELGGKDPAYVRPDA-DLDAAAESLVDGAFFNSGQSCCSIERIYV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 312 ESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQL-MAETGGVYVAPTLFR 390
Cdd:cd07102 267 HESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALFpEDKAGGAYLAPTVLT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 391 EVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGG 470
Cdd:cd07102 347 NVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTG 426
|
410 420
....*....|....*....|...
gi 655375262 471 YKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:cd07102 427 VKDSGRGVTLSRLGYDQLTRPKS 449
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
77-492 |
1.28e-90 |
|
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: 283.75 E-value: 1.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 77 SRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSvDVTNAARALRWSGEAVDKIYDE-----IAPTADNEI 151
Cdd:cd07147 38 RALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG-EVARAIDTFRIAAEEATRIYGEvlpldISARGEGRQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 152 GMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPgfghtVGKA 231
Cdd:cd07147 117 GLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLP-----CSRD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 232 LALHMDVDT----LVFTGSTKIAKQLMVYAGQsnmKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGS 307
Cdd:cd07147 192 DADLLVTDEriklLSFTGSPAVGWDLKARAGK---KKVVLELGGNAAVIVDSDA-DLDFAAQRIIFGAFYQAGQSCISVQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 308 RLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGeqlmaETGGVYVAPT 387
Cdd:cd07147 268 RVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGG-----KRDGALLEPT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 388 LFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINH---YDGGDM 464
Cdd:cd07147 343 ILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDvptFRVDHM 422
|
410 420
....*....|....*....|....*...
gi 655375262 465 taPFGGYKQSGNGRDKSLHAFDKYTEIK 492
Cdd:cd07147 423 --PYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
76-493 |
4.50e-90 |
|
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: 282.57 E-value: 4.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPiRFSKSVDVTNAARALRWSGEAVDKIYDE----IAPTADNEI 151
Cdd:cd07099 34 WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAGLEVLLALEAIDWAARNAPRVLAPrkvpTGLLMPNKK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 152 GMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTvGKA 231
Cdd:cd07099 113 ATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 232 LALHMdVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLV 311
Cdd:cd07099 192 LIDAG-VDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPMIVLADA-DLERAAAAAVWGAMVNAGQTCISVERVYV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 312 ESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQlmAETGGVYVAPTLFRE 391
Cdd:cd07099 269 HESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGAR--SNGGGPFYEPTVLTD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 392 VNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINH--YDGGDMTAPFG 469
Cdd:cd07099 347 VPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDvlLTAGIPALPFG 426
|
410 420
....*....|....*....|....
gi 655375262 470 GYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:cd07099 427 GVKDSGGGRRHGAEGLREFCRPKA 450
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
22-492 |
1.84e-89 |
|
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: 281.71 E-value: 1.84e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 22 QAFIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDE 101
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 102 LALLETLDMGKPIRFSKSvDVtnaARALrwsgEAVdkiydEIAPTADNE----------IGMIT---REPVGVVAAIVPW 168
Cdd:cd07085 80 LARLITLEHGKTLADARG-DV---LRGL----EVV-----EFACSIPHLlkgeylenvaRGIDTysyRQPLGVVAGITPF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 169 NFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGfGHTVGKALALHMDVDTLVFTGSTK 248
Cdd:cd07085 147 NFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 249 IAKQlmVYA-GQSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDEL 327
Cdd:cd07085 226 VGEY--IYErAAANGKRVQALGGAKNHAVVMPDA-DLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 328 KSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAE--TGGVYVAPTLFREVNNQMSIAREEIFG 405
Cdd:cd07085 303 KKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPgyENGNFVGPTILDNVTPDMKIYKEEIFG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 406 PVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWIN--------HYdggdmtaPFGGYKQSGNG 477
Cdd:cd07085 383 PVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINvpipvplaFF-------SFGGWKGSFFG 455
|
490 500
....*....|....*....|
gi 655375262 478 rdkSLHAFDK-----YTEIK 492
Cdd:cd07085 456 ---DLHFYGKdgvrfYTQTK 472
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
22-491 |
2.71e-89 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 281.00 E-value: 2.71e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 22 QAFIHGEYCAAvSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFEsGVWSRMAPVERKKVMIRFADLLEAHSDE 101
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR-GWWPTMPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 102 LALLETLDMGKPIRFSKSvDVTNAARALRWSGEAVDKIYDE-----IAPTADNEIGMITREPVGVVAAIVPWNFPLLMAC 176
Cdd:cd07082 81 VANLLMWEIGKTLKDALK-EVDRTIDYIRDTIEELKRLDGDslpgdWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 177 WKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMvy 256
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLK-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 257 aGQSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPL 336
Cdd:cd07082 238 -KQHPMKRLVLELGGKDPAIVLPDA-DLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 337 DPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmaetGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGM 416
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGRE----GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 417 EQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHY--DGGDmTAPFGGYKQSGNGRD---KSLHAFDKYTEI 491
Cdd:cd07082 392 EEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcqRGPD-HFPFLGRKDSGIGTQgigDALRSMTRRKGI 470
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
92-496 |
7.49e-78 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 249.27 E-value: 7.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 92 ADLLEAHSDELALLETLDMGKPIRFSkSVDVTNAARALRWSGEAVDKIYDEIAPT-ADNEIGMITREPVGVVAAIVPWNF 170
Cdd:PRK10090 5 AAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSdRPGENILLFKRALGVTTGILPWNF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 171 PLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIA 250
Cdd:PRK10090 84 PFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 251 KQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSW 330
Cdd:PRK10090 164 EKIMAAAAK-NITKVCLELGGKAPAIVMDDA-DLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 331 QPGHPLDPDTVS-GAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQlmAETGGVYVAPTLFREVNNQMSIAREEIFGPVLS 409
Cdd:PRK10090 242 QFGNPAERNDIAmGPLINAAALERVEQKVARAVEEGARVALGGKA--VEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 410 VIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYT 489
Cdd:PRK10090 320 VVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYL 399
|
....*..
gi 655375262 490 EIKATWI 496
Cdd:PRK10090 400 QTQVVYL 406
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
76-493 |
5.09e-76 |
|
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: 246.07 E-value: 5.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIR--FSKSVDVTNAARALRWSGEAVDKiyDEIAPTAdneIGM 153
Cdd:cd07101 34 WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRhaFEEVLDVAIVARYYARRAERLLK--PRRRRGA---IPV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 154 IT-----REPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTV 228
Cdd:cd07101 109 LTrttvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 229 GKALALHmdVDTLVFTGSTKIAKQLMVYAGqSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSR 308
Cdd:cd07101 189 GGAIVDN--ADYVMFTGSTATGRVVAERAG-RRLIGCSLELGGKNPMIVLEDA-DLDKAAAGAVRACFSNAGQLCVSIER 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 309 LLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQlMAETGGVYVAPTL 388
Cdd:cd07101 265 IYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRA-RPDLGPYFYEPTV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 389 FREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINhyDG-----GD 463
Cdd:cd07101 344 LTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVN--EGyaaawAS 421
|
410 420 430
....*....|....*....|....*....|
gi 655375262 464 MTAPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:cd07101 422 IDAPMGGMKDSGLGRRHGAEGLLKYTETQT 451
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
71-475 |
1.49e-75 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 246.77 E-value: 1.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 71 FESgvWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRfSKSVDVTNA-------AR-ALRWS-GEAVDKIYD 141
Cdd:PRK03137 86 FET--WKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWA-EADADTAEAidfleyyARqMLKLAdGKPVESRPG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 142 EiaptaDNEIGMItrePVGVVAAIVPWNFPL-LMACWKLGPaLASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNV 220
Cdd:PRK03137 163 E-----HNRYFYI---PLGVGVVISPWNFPFaIMAGMTLAA-IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 221 LPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLM-----VYAGQSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAI 295
Cdd:PRK03137 234 VPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYeraakVQPGQIWLKRVIAEMGGKDAIVVDEDA-DLDLAAESIVASA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 296 AFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVsGAVVDQQQLQTILGYIEAGKQQGAvLVCGGEQl 375
Cdd:PRK03137 313 FGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYM-GPVINQASFDKIMSYIEIGKEEGR-LVLGGEG- 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 376 mAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVW 455
Cdd:PRK03137 390 -DDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLY 468
|
410 420
....*....|....*....|..
gi 655375262 456 INHYDGGDM--TAPFGGYKQSG 475
Cdd:PRK03137 469 FNRGCTGAIvgYHPFGGFNMSG 490
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
31-490 |
1.01e-73 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 242.09 E-value: 1.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 31 AAVSGETFDCISPVDGNKLAAVASCDladaeaaVASARASFES-----GVWSRMAPVERKKVMIRFADLLEAHSDELALL 105
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVST-------AADVEAAFARaraaqRAWAATPVRERAAVLLRFHDLVLENREELLDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 106 ETLDMGKPIR--FSKSVDVTNAARalrWSGEAVDKIydeIAPtaDNEIGMI--------TREPVGVVAAIVPWNFPLLMA 175
Cdd:PRK09407 100 VQLETGKARRhaFEEVLDVALTAR---YYARRAPKL---LAP--RRRAGALpvltktteLRQPKGVVGVISPWNYPLTLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 176 CWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHmdVDTLVFTGSTKIAKQLMV 255
Cdd:PRK09407 172 VSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 256 YAGqSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHP 335
Cdd:PRK09407 250 QAG-RRLIGFSLELGGKNPMIVLDDA-DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 336 LDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGeQLMAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEG 415
Cdd:PRK09407 328 YDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGG-KARPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVAD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 416 MEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINhyDG-----GDMTAPFGGYKQSGNGRDKSLHAFDKYTE 490
Cdd:PRK09407 407 VDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVN--EGyaaawGSVDAPMGGMKDSGLGRRHGAEGLLKYTE 484
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
76-486 |
4.59e-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: 4.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKS--------VDVTNAAralrwsgeavdkiYDEIAPTA 147
Cdd:cd07095 16 WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDISIKA-------------YHERTGER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 148 DNEIG----MITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPG 223
Cdd:cd07095 83 ATPMAqgraVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 224 fGHTVGKALALHMDVDTLVFTGSTKIAKQL-MVYAGQSNmKRVWLEAGGKSPHIVfNDCPDLKAAAQAAASAIAFNQGEV 302
Cdd:cd07095 163 -GRETGEALAAHEGIDGLLFTGSAATGLLLhRQFAGRPG-KILALEMGGNNPLVV-WDVADIDAAAYLIVQSAFLTAGQR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 303 CTAGSRLLVESGVK-EQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILgyieagKQQGAVLVCGGEQLMA---- 377
Cdd:cd07095 240 CTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYL------LAQQDLLALGGEPLLAmerl 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 378 ETGGVYVAPTLFrEVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWIN 457
Cdd:cd07095 314 VAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWN 392
|
410 420 430
....*....|....*....|....*....|
gi 655375262 458 H-YDGGDMTAPFGGYKQSGNGRDKSLHAFD 486
Cdd:cd07095 393 RpTTGASSTAPFGGVGLSGNHRPSAYYAAD 422
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
76-478 |
7.67e-67 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 222.17 E-value: 7.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIrfsksVD-----VTNAARALRWS---GEAVDKIYDEIAPTA 147
Cdd:cd07098 34 WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTM-----VDaslgeILVTCEKIRWTlkhGEKALRPESRPGGLL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 148 D-NEIGMITREPVGVVAAIVPWNFPLLMAcwkLGPALAS---GNSVILKPSEKSPLTA---IRMAAIALEA-GIPPGVLN 219
Cdd:cd07098 109 MfYKRARVEYEPLGVVGAIVSWNYPFHNL---LGPIIAAlfaGNAIVVKVSEQVAWSSgffLSIIRECLAAcGHDPDLVQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 220 VLPGFGHTvGKALALHMDVDTLVFTGSTKIAKQLMVYAGQSnMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQ 299
Cdd:cd07098 186 LVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLELGGKDPAIVLDDA-DLDQIASIIMRGTFQSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 300 GEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGE--QLMA 377
Cdd:cd07098 263 GQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKryPHPE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 378 ETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWIN 457
Cdd:cd07098 343 YPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIN 422
|
410 420
....*....|....*....|....*
gi 655375262 458 hyDGGDMT----APFGGYKQSGNGR 478
Cdd:cd07098 423 --DFGVNYyvqqLPFGGVKGSGFGR 445
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
83-497 |
3.91e-66 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 220.38 E-value: 3.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 83 ERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSvDVTNAARALRWSGE-AVDKIYDEIAPTADneIG----MITRE 157
Cdd:PRK09406 46 QRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA-EALKCAKGFRYYAEhAEALLADEPADAAA--VGasraYVRYQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 158 PVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALAlhmD 237
Cdd:PRK09406 123 PLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILR---D 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 238 --VDTLVFTGSTKIAKQLMVYAGQSNMKRVwLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGV 315
Cdd:PRK09406 200 prVAAATLTGSEPAGRAVAAIAGDEIKKTV-LELGGSDPFIVMPSA-DLDRAAETAVTARVQNNGQSCIAAKRFIVHADV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 316 KEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmaETGGVYVAPTLFREVNNQ 395
Cdd:PRK09406 278 YDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRP--DGPGWFYPPTVITDITPD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 396 MSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINhydggDMTA-----PFGG 470
Cdd:PRK09406 356 MRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN-----GMTVsypelPFGG 430
|
410 420
....*....|....*....|....*..
gi 655375262 471 YKQSGNGRDKSLHAFDKYTEIKATWIA 497
Cdd:PRK09406 431 VKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
34-493 |
1.20e-65 |
|
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: 220.14 E-value: 1.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 34 SGETFDCISPVD-GNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGK 112
Cdd:cd07083 30 TKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKT--WKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 113 PIR-----FSKSVDVT--NAARALRWSGEAvdkiydEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALAS 185
Cdd:cd07083 108 NWVeaiddVAEAIDFIryYARAALRLRYPA------VEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 186 GNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQ-----S 260
Cdd:cd07083 182 GNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARlapgqT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 261 NMKRVWLEAGGKSPHIVfNDCPDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDT 340
Cdd:cd07083 262 WFKRLYVETGGKNAIIV-DETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 341 VSGAVVDQQQLQTILGYIEAGKQQGAvLVCGGEQLMAEtgGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGME--Q 418
Cdd:cd07083 341 DLGPVIDAEQEAKVLSYIEHGKNEGQ-LVLGGKRLEGE--GYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaE 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655375262 419 AIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTA--PFGGYKQSG-NGRDKSLHAFDKYTEIKA 493
Cdd:cd07083 418 ALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGvqPFGGFKLSGtNAKTGGPHYLRRFLEMKA 495
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
41-495 |
7.74e-62 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 208.95 E-value: 7.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 41 ISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSv 120
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 121 DVTNAARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLT 200
Cdd:PRK13968 89 EVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 201 AIRMAAIALEAGIPPGVLNVLPGFGHTVGKALAlHMDVDTLVFTGSTKIAKQLMVYAGQSnMKRVWLEAGGKSPHIVFND 280
Cdd:PRK13968 169 AQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIN-DSRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDPFIVLND 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 281 CpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEA 360
Cdd:PRK13968 247 A-DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 361 GKQQGAVLVCGGEQLMAEtgGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLS 440
Cdd:PRK13968 326 TLAEGARLLLGGEKIAGA--GNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 655375262 441 KAHRTAKALRSGMVWINHYDGGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKATW 495
Cdd:PRK13968 404 QARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
35-477 |
4.23e-61 |
|
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: 208.59 E-value: 4.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 35 GETFDCISPVDGNK-LAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKP 113
Cdd:cd07125 45 GEGAPVIDPADHERtIGEVSLADAEDVDAALAIAAAAFAG--WSATPVEERAEILEKAADLLEANRGELIALAAAEAGKT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 114 IRFSkSVDVTNAARALRW-SGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILK 192
Cdd:cd07125 123 LADA-DAEVREAIDFCRYyAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 193 PSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMvyagQSNMKRVWL----- 267
Cdd:cd07125 202 PAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLIN----RALAERDGPilpli 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 268 -EAGGKSPHIVfnDCPDLKAAAQAAASAIAF-NQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAV 345
Cdd:cd07125 278 aETGGKNAMIV--DSTALPEQAVKDVVQSAFgSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 346 VDQQQLQTILGYIEAGKQQGAVLvcggEQL-MAETGGVYVAPTLFREVNNqmSIAREEIFGPVLSVIEFEG--MEQAIAI 422
Cdd:cd07125 356 IDKPAGKLLRAHTELMRGEAWLI----APApLDDGNGYFVAPGIIEIVGI--FDLTTEVFGPILHVIRFKAedLDEAIED 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655375262 423 GNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHydggDMTA------PFGGYKQSGNG 477
Cdd:cd07125 430 INATGYGLTLGIHSRDEREIEYWRERVEAGNLYINR----NITGaivgrqPFGGWGLSGTG 486
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
34-478 |
1.14e-60 |
|
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: 206.29 E-value: 1.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 34 SGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFEsgVWSRM-APVeRKKVMIRFADLLEAHSDELALLETLDMGK 112
Cdd:cd07130 10 GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK--EWRDVpAPK-RGEIVRQIGDALRKKKEALGKLVSLEMGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 113 PIRFSKS-----VDVTNAARALRWSgeavdkIYDEIAPTA-DNEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASG 186
Cdd:cd07130 87 ILPEGLGevqemIDICDFAVGLSRQ------LYGLTIPSErPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 187 NSVILKPSEKSPLTAIRMAAIALEA----GIPPGVLNVLPGfGHTVGKALALHMDVDTLVFTGSTKIAKQ--LMVyagQS 260
Cdd:cd07130 161 NVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQvgQAV---AA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 261 NMKRVWLEAGGKSPHIVFnDCPDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDT 340
Cdd:cd07130 237 RFGRSLLELGGNNAIIVM-EDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 341 VSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmaETGGVYVAPTLFrEVNNQMSIAREEIFGPVLSVIEFEGMEQAI 420
Cdd:cd07130 316 LVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVI--DGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLEEAI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655375262 421 AIGNDTIYGLAAGVWTADLSKAHRTAKALRS--GMVWIN-HYDGGDMTAPFGGYKQSGNGR 478
Cdd:cd07130 393 AWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVNiGTSGAEIGGAFGGEKETGGGR 453
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
24-486 |
1.37e-59 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 203.65 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAvSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKS--------VDVTNAARALRwSGEAVDkiydeiaPTADNEIGMITRePVGVVAAIVPWNFPLLMA 175
Cdd:PRK09457 81 EVIARETGKPLWEAATevtaminkIAISIQAYHER-TGEKRS-------EMADGAAVLRHR-PHGVVAVFGPYNFPGHLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 176 CWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGfGHTVGKALALHMDVDTLVFTGSTKIAKQL-M 254
Cdd:PRK09457 152 NGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLhR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 255 VYAGQSNmKRVWLEAGGKSPhIVFNDCPDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVK-EQLIALIIDELKSWQPG 333
Cdd:PRK09457 231 QFAGQPE-KILALEMGGNNP-LVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 334 HPL-DPDTVSGAVVDQQQLQtilGYIEAgkqQGAVLVCGGEQLMA----ETGGVYVAPTLFrEVNNQMSIAREEIFGPVL 408
Cdd:PRK09457 309 RWDaEPQPFMGAVISEQAAQ---GLVAA---QAQLLALGGKSLLEmtqlQAGTGLLTPGII-DVTGVAELPDEEYFGPLL 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655375262 409 SVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMV-WINHYDGGDMTAPFGGYKQSGNGRDKSLHAFD 486
Cdd:PRK09457 382 QVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHRPSAYYAAD 460
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
24-492 |
5.19e-59 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 202.03 E-value: 5.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLT--WGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSvDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMIT-REPVGVVAAIVPWNFPLLMACWKLGPA 182
Cdd:TIGR01722 82 ELITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSiRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 183 LASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGfGHTVGKALALHMDVDTLVFTGSTKIAkQLMVYAGQSNM 262
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIG-RYIHTTGSAHG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 263 KRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEqLIALIIDELKSWQPGHPLDPDTVS 342
Cdd:TIGR01722 239 KRVQALGGAKNHMVVMPDA-DKDAAADALVGAAYGAAGQRCMAISAAVLVGAADE-WVPEIRERAEKIRIGPGDDPGAEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 343 GAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAE--TGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAI 420
Cdd:TIGR01722 317 GPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDgyEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 421 AIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINhydggdMTAP-------FGGYKQSGNGrdkSLHAFDK-----Y 488
Cdd:TIGR01722 397 ALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN------VPIPvplpyfsFTGWKDSFFG---DHHIYGKqgthfY 467
|
....
gi 655375262 489 TEIK 492
Cdd:TIGR01722 468 TRGK 471
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
70-493 |
1.71e-57 |
|
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: 196.59 E-value: 1.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 70 SFESGvwsRMAPVE-RKKVMIRFADLLEAHSDEL--ALLEtlDMGKPIRFSKSVDVTNAARALRwsgEAVDKIYDEIAPT 146
Cdd:cd07087 10 TFLTG---KTRSLEwRKAQLKALKRMLTENEEEIaaALYA--DLGKPPAEAYLTEIAVVLGEID---HALKHLKKWMKPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 147 -ADNEI------GMITREPVGVVAAIVPWNFPLLMAcwkLGP---ALASGNSVILKPSEKSPLTAirmAAIA--LEAGIP 214
Cdd:cd07087 82 rVSVPLllqpakAYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATS---ALLAklIPKYFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 215 PGVLNVLPGFGHTVGKALALHMDVdtLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASA 294
Cdd:cd07087 156 PEAVAVVEGGVEVATALLAEPFDH--IFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDA-NLEVAARRIAWG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 295 IAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLD-PDTvsGAVVDQQQLQTILGYIEAGKqqgavLVCGGE 373
Cdd:cd07087 232 KFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKEsPDY--GRIINERHFDRLASLLDDGK-----VVIGGQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 374 qlmAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGM 453
Cdd:cd07087 305 ---VDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGG 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 655375262 454 VWIN----HYdgGDMTAPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:cd07087 382 VCVNdvllHA--AIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKS 423
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
77-477 |
6.36e-54 |
|
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: 188.01 E-value: 6.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 77 SRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKsVDVTNAARALRWsgeAVDKIYD----EIA----PTAD 148
Cdd:cd07148 39 NWLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK-VEVTRAIDGVEL---AADELGQlggrEIPmgltPASA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 149 NEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGfGHTV 228
Cdd:cd07148 115 GRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPC-ENAV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 229 GKALALHMDVDTLVFTGSTKIAKQLmvyagQSNMK---RVWLEAGGKSPHIVfNDCPDLKAAAQAAASAIAFNQGEVCTA 305
Cdd:cd07148 194 AEKLVTDPRVAFFSFIGSARVGWML-----RSKLApgtRCALEHGGAAPVIV-DRSADLDAMIPPLVKGGFYHAGQVCVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 306 GSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmaetGGVYVA 385
Cdd:cd07148 268 VQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRL----SDTTYA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 386 PTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINhydggDMT 465
Cdd:cd07148 344 PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVN-----DHT 418
|
410
....*....|....*...
gi 655375262 466 A------PFGGYKQSGNG 477
Cdd:cd07148 419 AfrvdwmPFAGRRQSGYG 436
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
75-477 |
3.30e-53 |
|
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: 187.04 E-value: 3.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 75 VWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPirFSKSVD-VTNAARALRWSGEAVDKIYDEIaptadneigm 153
Cdd:TIGR01238 89 TWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKT--IHNAIAeVREAVDFCRYYAKQVRDVLGEF---------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 154 iTREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALA 233
Cdd:TIGR01238 157 -SVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 234 LHMDVDTLVFTGSTKIAKQLMVYAGQSNMKRVWL--EAGGKSPHIVfnDCPDLKAAAQAAASAIAFNQ-GEVCTAGSRLL 310
Cdd:TIGR01238 236 SDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIV--DSTALPEQVVRDVLRSAFDSaGQRCSALRVLC 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 311 VESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQG-AVLVCGGEQLMAETGGVYVAPTLF 389
Cdd:TIGR01238 314 VQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkKIAQLTLDDSRACQHGTFVAPTLF 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 390 rEVNNqMSIAREEIFGPVLSVIEFEGME--QAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDGGDMTA- 466
Cdd:TIGR01238 394 -ELDD-IAELSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGv 471
|
410
....*....|..
gi 655375262 467 -PFGGYKQSGNG 477
Cdd:TIGR01238 472 qPFGGQGLSGTG 483
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
83-485 |
9.14e-53 |
|
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: 184.35 E-value: 9.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 83 ERKKVMIRFADLLEAHSDEL--ALLEtlDMGKPIRfskSVDVTNaaralrwsgeaVDKIYDEIAPTADN----------- 149
Cdd:cd07134 21 ERIAKLKRLKKAILARREEIiaALAA--DFRKPAA---EVDLTE-----------ILPVLSEINHAIKHlkkwmkpkrvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 150 -EIGM------ITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAgIPPGVLNVLP 222
Cdd:cd07134 85 tPLLLfgtkskIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 223 GfGHTVGKALaLHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVfNDCPDLKAAAQAAASAIAFNQGEV 302
Cdd:cd07134 164 G-DAEVAQAL-LELPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIV-DETADLKKAAKKIAWGKFLNAGQT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 303 CTAGSRLLVESGVKEQLIALIIDELKSW--QPGHPLDPDTVSGaVVDQQQLQTILGYIEAGKQQGAVLVCGGEqlmAETG 380
Cdd:cd07134 240 CIAPDYVFVHESVKDAFVEHLKAEIEKFygKDAARKASPDLAR-IVNDRHFDRLKGLLDDAVAKGAKVEFGGQ---FDAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 381 GVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWIN--- 457
Cdd:cd07134 316 QRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNdvv 395
|
410 420
....*....|....*....|....*....
gi 655375262 458 -HYDGGDMtaPFGGYKQSGNGRDKSLHAF 485
Cdd:cd07134 396 lHFLNPNL--PFGGVNNSGIGSYHGVYGF 422
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
154-478 |
2.54e-52 |
|
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: 183.07 E-value: 2.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 154 ITREPVGVVAAIVPWNFPLLMAcwkLGP---ALASGNSVILKPSEKSPLTAIRMAAIaLEAGIPPGVLNVLPGfGHTVGK 230
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAEL-LAEYFDEDEVAVVTG-GADVAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 231 ALAlHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLL 310
Cdd:cd07133 172 AFS-SLPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDA-DLAKAAERIAFGKLLNAGQTCVAPDYVL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 311 VESGVKEQLIALIIDELKSWQPGHPLDPDTVSgaVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAETGGVYVAPTLFR 390
Cdd:cd07133 249 VPEDKLEEFVAAAKAAVAKMYPTLADNPDYTS--IINERHYARLQGLLEDARAKGARVIELNPAGEDFAATRKLPPTLVL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 391 EVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWIN----HYDGGDMta 466
Cdd:cd07133 327 NVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdtllHVAQDDL-- 404
|
330
....*....|..
gi 655375262 467 PFGGYKQSGNGR 478
Cdd:cd07133 405 PFGGVGASGMGA 416
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
76-477 |
6.40e-47 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 175.00 E-value: 6.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIrfSKSVD-VTNAARALR-WSGEAVDKIYDEIA---PTA-DN 149
Cdd:PRK11904 601 WSRTPVEERAAILERAADLLEANRAELIALCVREAGKTL--QDAIAeVREAVDFCRyYAAQARRLFGAPEKlpgPTGeSN 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 150 EIgmiTREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVG 229
Cdd:PRK11904 679 EL---RLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVG 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 230 KALALHMDVDTLVFTGSTKIAKQL-MVYAGQSNmKRVWL--EAGGKSPHIVfnDCPDLKAAAQAAASAIAFNQ-GEVCTA 305
Cdd:PRK11904 756 AALTADPRIAGVAFTGSTETARIInRTLAARDG-PIVPLiaETGGQNAMIV--DSTALPEQVVDDVVTSAFRSaGQRCSA 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 306 GSRLLVESGVKEQLIALII---DELKSwqpGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQgAVLVCGGEQLMAETGGV 382
Cdd:PRK11904 833 LRVLFVQEDIADRVIEMLKgamAELKV---GDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPAGTENGH 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 383 YVAPTLFrEVNNqMSIAREEIFGPVLSVIEF--EGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHyd 460
Cdd:PRK11904 909 FVAPTAF-EIDS-ISQLEREVFGPILHVIRYkaSDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNR-- 984
|
410 420
....*....|....*....|...
gi 655375262 461 ggDM------TAPFGGYKQSGNG 477
Cdd:PRK11904 985 --NQigavvgVQPFGGQGLSGTG 1005
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
24-496 |
1.19e-46 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 169.17 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCdladaeaAVASARASFESG-----VWSRMAPVERKKVMIRFADLLEAH 98
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQAC-------TQEEVNKAMESAkaaqkAWAKTPLWKRAELLHKAAAILKEH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 99 SDELALLETLDMGKPIRFS-----KSVDVTN--AARALRWSGEAVDKIYDEIAPTADNEIGMITREPVGVVAAIVPWNFP 171
Cdd:PLN00412 92 KAPIAECLVKEIAKPAKDAvtevvRSGDLISytAEEGVRILGEGKFLVSDSFPGNERNKYCLTSKIPLGVVLAIPPFNYP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 172 LLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALALHMDVDTLVFT-GSTKIA 250
Cdd:PLN00412 172 VNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 251 kqlmvYAGQSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSW 330
Cdd:PLN00412 252 -----ISKKAGMVPLQMELGGKDACIVLEDA-DLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 331 QPGHPLDPDTVSgAVVDQQQLQTILGYIEAGKQQGAVLVcggEQLMAEtgGVYVAPTLFREVNNQMSIAREEIFGPVLSV 410
Cdd:PLN00412 326 TVGPPEDDCDIT-PVVSESSANFIEGLVMDAKEKGATFC---QEWKRE--GNLIWPLLLDNVRPDMRIAWEEPFGPVLPV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 411 IEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYDG-GDMTAPFGGYKQSGNGRDKSLHAFDKYT 489
Cdd:PLN00412 400 IRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPArGPDHFPFQGLKDSGIGSQGITNSINMMT 479
|
....*..
gi 655375262 490 EIKATWI 496
Cdd:PLN00412 480 KVKSTVI 486
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
75-477 |
3.52e-46 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 173.24 E-value: 3.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 75 VWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPirFSksvdvtNAARALRwsgEAVDKIY---DEIAPTADNEi 151
Cdd:PRK11809 697 IWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKT--FS------NAIAEVR---EAVDFLRyyaGQVRDDFDND- 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 152 gmiTREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKA 231
Cdd:PRK11809 765 ---THRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAA 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 232 LALHMDVDTLVFTGSTKIAKQLmvyagQSNM--------KRVWL--EAGGKSPHIVfnDCPDLKAAAQAAASAIAFNQ-G 300
Cdd:PRK11809 842 LVADARVRGVMFTGSTEVARLL-----QRNLagrldpqgRPIPLiaETGGQNAMIV--DSSALTEQVVADVLASAFDSaG 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 301 EVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQG-AVLVCGGEQLMAET 379
Cdd:PRK11809 915 QRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGrPVFQAARENSEDWQ 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 380 GGVYVAPTLFrEVNnqmSIAR--EEIFGPVLSVIEF--EGMEQAIAIGNDTIYGLAAGVWT-ADLSKAHRTAKAlRSGMV 454
Cdd:PRK11809 995 SGTFVPPTLI-ELD---SFDElkREVFGPVLHVVRYnrNQLDELIEQINASGYGLTLGVHTrIDETIAQVTGSA-HVGNL 1069
|
410 420
....*....|....*....|....*
gi 655375262 455 WINHYDGGDMTA--PFGGYKQSGNG 477
Cdd:PRK11809 1070 YVNRNMVGAVVGvqPFGGEGLSGTG 1094
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
76-477 |
6.45e-46 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 172.36 E-value: 6.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKpirfsksvDVTNAARALRwsgEAVD--KIYdeiAPTADNEIGM 153
Cdd:PRK11905 606 WSATPAAERAAILERAADLMEAHMPELFALAVREAGK--------TLANAIAEVR---EAVDflRYY---AAQARRLLNG 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 154 ITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALA 233
Cdd:PRK11905 672 PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALV 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 234 LHMDVDTLVFTGSTKIAKQLmvyagQSNM-KR----VWL--EAGGKSPHIVfnDCPDLKAAAQAAASAIAFNQ-GEVCTA 305
Cdd:PRK11905 752 ADPRIAGVMFTGSTEVARLI-----QRTLaKRsgppVPLiaETGGQNAMIV--DSSALPEQVVADVIASAFDSaGQRCSA 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 306 GSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLvcggEQLMA--ET-GGV 382
Cdd:PRK11905 825 LRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLpaETeKGT 900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 383 YVAPTLFrEVNNqMSIAREEIFGPVLSVIEF--EGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINHYD 460
Cdd:PRK11905 901 FVAPTLI-EIDS-ISDLEREVFGPVLHVVRFkaDELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNI 978
|
410 420
....*....|....*....|..
gi 655375262 461 GGdmtA-----PFGGYKQSGNG 477
Cdd:PRK11905 979 IG---AvvgvqPFGGEGLSGTG 997
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
152-496 |
1.32e-45 |
|
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: 165.37 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 152 GMITREPVGVVAAIVPWNFPLLMAcwkLGP---ALASGNSVILKPSEKSPLTAIRMAAIaLEAGIPPGVLNVLPGfGHTV 228
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEG-GVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 229 GKALaLHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSR 308
Cdd:cd07136 169 NQEL-LDQKFDYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDA-NLKLAAKRIVWGKFLNAGQTCVAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 309 LLVESGVKEQLIALIIDELKSWQPGHPLD-PDTvsGAVVDQQQLQTILGYIEAGKqqgavLVCGGEqlmAETGGVYVAPT 387
Cdd:cd07136 246 VLVHESVKEKFIKELKEEIKKFYGEDPLEsPDY--GRIINEKHFDRLAGLLDNGK-----IVFGGN---TDRETLYIEPT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 388 LFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWIN----HYDGGD 463
Cdd:cd07136 316 ILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtimHLANPY 395
|
330 340 350
....*....|....*....|....*....|....*...
gi 655375262 464 MtaPFGGYKQSGNGR---DKSLHAFDKYTEI--KATWI 496
Cdd:cd07136 396 L--PFGGVGNSGMGSyhgKYSFDTFSHKKSIlkKSTWF 431
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
24-457 |
6.51e-44 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 163.76 E-value: 6.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 24 FIHGEYCAAVSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFEsgVWSRMAPVERKKVMIRFADLLEAHSDELA 103
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP--LWRNTPITTRQRVMLKFQELIRKNMDKLA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 104 LLETLDMGKPIRFSKSvDVTNAARALRWSGEAVDKIYDEIAPTADNEIGMIT-REPVGVVAAIVPWNFPLLMACWKLGPA 182
Cdd:PLN02419 195 MNITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSiREPLGVCAGICPFNFPAMIPLWMFPVA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 183 LASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVgKALALHMDVDTLVFTGSTKIAKQLMVYAGQSNm 262
Cdd:PLN02419 274 VTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKG- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 263 KRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALiIDELKSWQPGHPLDPDTVS 342
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDA-NIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKL-VERAKALKVTCGSEPDADL 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 343 GAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLMAE--TGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAI 420
Cdd:PLN02419 430 GPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPgyEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAI 509
|
410 420 430
....*....|....*....|....*....|....*..
gi 655375262 421 AIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWIN 457
Cdd:PLN02419 510 SIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
76-477 |
2.03e-43 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 164.73 E-value: 2.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIrfsksvdvTNAARALRwsgEAVD--KIY-DEIAPTADNEIg 152
Cdd:COG4230 609 WSATPVEERAAILERAADLLEAHRAELMALLVREAGKTL--------PDAIAEVR---EAVDfcRYYaAQARRLFAAPT- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 153 miTREPVGVVAAIVPWNFPL------LMAcwklgpALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGH 226
Cdd:COG4230 677 --VLRGRGVFVCISPWNFPLaiftgqVAA------ALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGE 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 227 TVGKALALHMDVDTLVFTGSTK----IAKQLMVYAGQSnmkrVWL--EAGGKSPHIV-----------------FNdcpd 283
Cdd:COG4230 749 TVGAALVADPRIAGVAFTGSTEtarlINRTLAARDGPI----VPLiaETGGQNAMIVdssalpeqvvddvlasaFD---- 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 284 lkaaaqaaasaiafNQGEVCTAGSRLLVESGVKEQLIALII---DELKSwqpGHPLDPDTVSGAVVDQQQLQTILGYIEA 360
Cdd:COG4230 821 --------------SAGQRCSALRVLCVQEDIADRVLEMLKgamAELRV---GDPADLSTDVGPVIDAEARANLEAHIER 883
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 361 GKQQGAvLVCGGEQLMAETGGVYVAPTLFrEVNnqmSIAR--EEIFGPVLSVIEF--EGMEQAI-AIgNDTIYGLAAGVW 435
Cdd:COG4230 884 MRAEGR-LVHQLPLPEECANGTFVAPTLI-EID---SISDleREVFGPVLHVVRYkaDELDKVIdAI-NATGYGLTLGVH 957
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 655375262 436 TADLSKAHRTAKALRSGMVWINHydggDMTA------PFGGYKQSGNG 477
Cdd:COG4230 958 SRIDETIDRVAARARVGNVYVNR----NIIGavvgvqPFGGEGLSGTG 1001
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
154-493 |
2.68e-41 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 154.42 E-value: 2.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 154 ITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIaLEAGIPPGVLNVLPGfGHTVGKALa 233
Cdd:PTZ00381 105 IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL-LTKYLDPSYVRVIEG-GVEVTTEL- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 234 LHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVES 313
Cdd:PTZ00381 182 LKEPFDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSC-NLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 314 GVKEQLIALIIDELKSWQPGHPLDPDTVSgAVVDQQQLQTILGYIEAGKQQgavLVCGGEQLMAETggvYVAPTLFREVN 393
Cdd:PTZ00381 260 SIKDKFIEALKEAIKEFFGEDPKKSEDYS-RIVNEFHTKRLAELIKDHGGK---VVYGGEVDIENK---YVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 394 NQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWIN----HYdgGDMTAPFG 469
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcvfHL--LNPNLPFG 410
|
330 340
....*....|....*....|....
gi 655375262 470 GYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:PTZ00381 411 GVGNSGMGAYHGKYGFDTFSHPKP 434
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
70-489 |
4.33e-41 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 152.76 E-value: 4.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 70 SFESGvwsRMAPVERKKVMIR-FADLLEAHSDELALLETLDMGKPIRFSKSVDVTNAARALRWSGEAVDK-IYDEiaPTA 147
Cdd:cd07135 17 TFRSG---KTKDLEYRLWQLKqLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKwAKDE--KVK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 148 DNEIGM------ITREPVGVVAAIVPWNFPLLMAcwkLGP---ALASGNSVILKPSEKSPLTAIRMAAIaLEAGIPPGVL 218
Cdd:cd07135 92 DGPLAFmfgkprIRKEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 219 NVLPGFGHTVGKALALHMdvDTLVFTGSTKIAKqLMVYAGQSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFN 298
Cdd:cd07135 168 QVVQGGVPETTALLEQKF--DKIFYTGSGRVGR-IIAEAAAKHLTPVTLELGGKSPVIVTKNA-DLELAAKRILWGKFGN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 299 QGEVCTAGSRLLVESGVKEQLialiIDELKSWQ----PGHPLDPDTvSGAVVDQQQLQTILGYIEAGKQQgavLVCGGEq 374
Cdd:cd07135 244 AGQICVAPDYVLVDPSVYDEF----VEELKKVLdefyPGGANASPD-YTRIVNPRHFNRLKSLLDTTKGK---VVIGGE- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 375 lmAETGGVYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMV 454
Cdd:cd07135 315 --MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGV 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 655375262 455 WIN----HydGGDMTAPFGGYKQSGNGRDKSLHAFDKYT 489
Cdd:cd07135 393 VINdtliH--VGVDNAPFGGVGDSGYGAYHGKYGFDTFT 429
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
75-475 |
1.88e-40 |
|
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: 152.74 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 75 VWSRMAPVERKKVMIRFADLLEA-HSDELALLETLDMGKPIrFSKSVDVtnAARA---LRWSGEAVDKIYDE--IAPTAD 148
Cdd:cd07123 84 EWARMPFEDRAAIFLKAADLLSGkYRYELNAATMLGQGKNV-WQAEIDA--ACELidfLRFNVKYAEELYAQqpLSSPAG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 149 NEIGMITREPVGVVAAIVPWNFPLLMACWKLGPALAsGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTV 228
Cdd:cd07123 161 VWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 229 GKALALHMDVDTLVFTGSTKIAKQL--MVYAGQSNMK---RVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVC 303
Cdd:cd07123 240 GDTVLASPHLAGLHFTGSTPTFKSLwkQIGENLDRYRtypRIVGETGGKNFHLVHPSA-DVDSLVTATVRGAFEYQGQKC 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 304 TAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQ-GAVLVCGGEQLMAEtgGV 382
Cdd:cd07123 319 SAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSV--GY 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 383 YVAPTLFREVNNQMSIAREEIFGPVLSVIEFE--GMEQAIAIGNDT-IYGLAAGVWTADlSKAHRTA-KALR--SGMVWI 456
Cdd:cd07123 397 FVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPdsDFEETLELVDTTsPYALTGAIFAQD-RKAIREAtDALRnaAGNFYI 475
|
410 420
....*....|....*....|.
gi 655375262 457 NHYDGGDMTA--PFGGYKQSG 475
Cdd:cd07123 476 NDKPTGAVVGqqPFGGARASG 496
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
152-493 |
1.12e-37 |
|
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: 143.32 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 152 GMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIaLEAGIPPGVLNVLPGfGHTVGKA 231
Cdd:cd07137 95 AEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYLDTKAIKVIEG-GVPETTA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 232 LaLHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPhIVFNDCPDLKAAAQAAASAI-AFNQGEVCTAGSRLL 310
Cdd:cd07137 173 L-LEQKWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCP-VIVDSTVDLKVAVRRIAGGKwGCNNGQACIAPDYVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 311 VESGVKEQLIALIIDELKSWQPGHPLDPDTVSgAVVDQQQLQTILGYIEAGKQQGAVlVCGGEQlmaETGGVYVAPTLFR 390
Cdd:cd07137 250 VEESFAPTLIDALKNTLEKFFGENPKESKDLS-RIVNSHHFQRLSRLLDDPSVADKI-VHGGER---DEKNLYIEPTILL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 391 EVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWIN----HYdgGDMTA 466
Cdd:cd07137 325 DPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdtvvQY--AIDTL 402
|
330 340
....*....|....*....|....*..
gi 655375262 467 PFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:cd07137 403 PFGGVGESGFGAYHGKFSFDAFSHKKA 429
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
70-493 |
5.74e-37 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 141.59 E-value: 5.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 70 SFESGvwsRMAPVE-RKKVMIRFADLLEAHSDELalLETL--DMGKP--------IRFSKSvDVTNAARALR-WSG-EAV 136
Cdd:cd07132 10 AFSSG---KTRPLEfRIQQLEALLRMLEENEDEI--VEALakDLRKPkfeavlseILLVKN-EIKYAISNLPeWMKpEPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 137 DK----IYDEIaptadneigMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIaleag 212
Cdd:cd07132 84 KKnlatLLDDV---------YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 213 IPPGVLN-----VLPGFGHTvgkALALHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAA 287
Cdd:cd07132 150 IPKYLDKecypvVLGGVEET---TELLKQRFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSC-DIDVA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 288 AQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHP-LDPDTvsGAVVDQQQLQTILGYIEAGKqqga 366
Cdd:cd07132 225 ARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPkESPDY--GRIINDRHFQRLKKLLSGGK---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 367 vLVCGGEQLMAETggvYVAPTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTA 446
Cdd:cd07132 299 -VAIGGQTDEKER---YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKIL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 655375262 447 KALRSGMVWIN----HYDGGDMtaPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:cd07132 375 SNTSSGGVCVNdtimHYTLDSL--PFGGVGNSGMGAYHGKYSFDTFSHKRS 423
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
74-414 |
1.45e-36 |
|
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: 140.45 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 74 GVWSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPIRFSKSVD---VTNAARA-LRWSGEAVDKIYDEIAPTADN 149
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICgdqVQLRARAfVIYSYRIPHEPGNHLGQGLKQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 150 EIGMItREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGI-PPGVLNVLPGFGHTv 228
Cdd:cd07084 93 QSHGY-RWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLINGDGKT- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 229 GKALALHMDVDTLVFTGSTKIAKQLMVYAGQSnmkRVWLEAGGKSPHIVFNDCPDLKAAAQAAASAIAFNQGEVCTAGSR 308
Cdd:cd07084 171 MQALLLHPNPKMVLFTGSSRVAEKLALDAKQA---RIYLELAGFNWKVLGPDAQAVDYVAWQCVQDMTACSGQKCTAQSM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 309 LLV-ESGVKEQLialiIDELKSwqpghPLDPDTVSGAVVDQQQLQTILGYIEA-GKQQGAVLVCGGEQLMA----ETGGV 382
Cdd:cd07084 248 LFVpENWSKTPL----VEKLKA-----LLARRKLEDLLLGPVQTFTTLAMIAHmENLLGSVLLFSGKELKNhsipSIYGA 318
|
330 340 350
....*....|....*....|....*....|....*
gi 655375262 383 YVAPTLF---REVNNQMSIAREEIFGPVLSVIEFE 414
Cdd:cd07084 319 CVASALFvpiDEILKTYELVTEEIFGPFAIVVEYK 353
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
23-488 |
3.41e-34 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 134.96 E-value: 3.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 23 AFIHGEYCAavSGETFDCISPVDGNKLAAVASCDLADAEAAVASARASFESgvWSRMAPVERKKVMIRFADLLEAHSDEL 102
Cdd:PLN02315 23 CYVGGEWRA--NGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI--WMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 103 ALLETLDMGKPI-----RFSKSVDVTNAARALRwsgeavDKIYDEIAPTA-DNEIGMITREPVGVVAAIVPWNFPLLMAC 176
Cdd:PLN02315 99 GRLVSLEMGKILaegigEVQEIIDMCDFAVGLS------RQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 177 WKLGPALASGNSVILKPSEKSPLTAIRMAAIALEA----GIPPGVLNVLPGfGHTVGKALALHMDVDTLVFTGSTKIAkq 252
Cdd:PLN02315 173 WNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVG-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 253 LMVY-AGQSNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAIAFNQGEVCTAGSRLLVESGVKEQLIALIIDELKSWQ 331
Cdd:PLN02315 250 LMVQqTVNARFGKCLLELSGNNAIIVMDDA-DIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 332 PGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQLmaETGGVYVAPTLFrEVNNQMSIAREEIFGPVLSVI 411
Cdd:PLN02315 329 IGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAI--ESEGNFVQPTIV-EISPDADVVKEELFGPVLYVM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 412 EFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRS--GMVWIN-HYDGGDMTAPFGGYKQSGNGRDKSLHAFDKY 488
Cdd:PLN02315 406 KFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDSWKQY 485
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
152-493 |
2.04e-31 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 126.38 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 152 GMITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAiALEAGIPPGVLNVLPGfGHTVGKA 231
Cdd:PLN02203 102 AEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAA-NIPKYLDSKAVKVIEG-GPAVGEQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 232 LALHmDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVfnDCPDLKAAAQAAASAIAFNQ-----GEVCTAG 306
Cdd:PLN02203 180 LLQH-KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIV--DSLSSSRDTKVAVNRIVGGKwgscaGQACIAI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 307 SRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSgAVVDQQQLQTILGYIEAGKQQGAVlVCGGEqlmAETGGVYVAP 386
Cdd:PLN02203 256 DYVLVEERFAPILIELLKSTIKKFFGENPRESKSMA-RILNKKHFQRLSNLLKDPRVAASI-VHGGS---IDEKKLFIEP 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 387 TLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWIN----HYdGG 462
Cdd:PLN02203 331 TILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNdaiiQY-AC 409
|
330 340 350
....*....|....*....|....*....|.
gi 655375262 463 DmTAPFGGYKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:PLN02203 410 D-SLPFGGVGESGFGRYHGKYSFDTFSHEKA 439
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
154-493 |
3.03e-27 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 114.37 E-value: 3.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 154 ITREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIaLEAGIPPGVLNVLPGfGHTVGKALa 233
Cdd:PLN02174 108 IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEG-AVTETTAL- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 234 LHMDVDTLVFTGSTKIAKQLMVYAGQsNMKRVWLEAGGKSPHIVFNDCpDLKAAAQAAASAI-AFNQGEVCTAGSRLLVE 312
Cdd:PLN02174 185 LEQKWDKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDT-DLKVTVRRIIAGKwGCNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 313 SGVKEQLIALIIDELKSWQPGHPLDPDTVSgAVVDQQQLQTILGYIEAgKQQGAVLVCGGEQlmaETGGVYVAPTLFREV 392
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPMESKDMS-RIVNSTHFDRLSKLLDE-KEVSDKIVYGGEK---DRENLKIAPTILLDV 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 393 NNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKALRSGMVWINH--YDGGDMTAPFGG 470
Cdd:PLN02174 338 PLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDiaVHLALHTLPFGG 417
|
330 340
....*....|....*....|...
gi 655375262 471 YKQSGNGRDKSLHAFDKYTEIKA 493
Cdd:PLN02174 418 VGESGMGAYHGKFSFDAFSHKKA 440
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
83-449 |
7.89e-19 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 89.38 E-value: 7.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 83 ERKKVMIRFADLLEAHSDELALLETLDMGKpIRFSKSVDVTNAARALRWSGEAVDKIYDEIApTADNEIGMITREPV--- 159
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIATANSGT-TRNDSAVDIDGGIFTLGYYAKLGAALGDARL-LRDGEAVQLGKDPAfqg 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 160 --------GVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGI-PPGVLNVLPGFGHTVGK 230
Cdd:PRK11903 142 qhvlvptrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 231 ALAlhmDVDTLVFTGSTKIAKQLMVYAG--QSNMkRVWLEAGGKSPHIVfndCPDlkaaaqAAASAIAFN---------- 298
Cdd:PRK11903 222 HLQ---PFDVVSFTGSAETAAVLRSHPAvvQRSV-RVNVEADSLNSALL---GPD------AAPGSEAFDlfvkevvrem 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 299 ---QGEVCTAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAGKQQGAVLVCGGEQL 375
Cdd:PRK11903 289 tvkSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFA 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655375262 376 MAET---GGVYVAPTLF--REVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTADLSKAHRTAKAL 449
Cdd:PRK11903 369 LVDAdpaVAACVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALEL 447
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
160-438 |
5.27e-18 |
|
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: 86.55 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 160 GVVAAIVPWNFPllmaCW----KLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGI-PPGVLNVLPGfghTVGKALAL 234
Cdd:cd07128 146 GVAVHINAFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICG---SVGDLLDH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 235 HMDVDTLVFTGSTKIAKQLMVYAG-QSNMKRVWLEAGGKSPHI----VFNDCPDLKAAAQAAASAIAFNQGEVCTAGSRL 309
Cdd:cd07128 219 LGEQDVVAFTGSAATAAKLRAHPNiVARSIRFNAEADSLNAAIlgpdATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 310 LVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQQQLQTILGYIEAgKQQGAVLVCGGEQLMAETG-----GVYV 384
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDRFEVVGadaekGAFF 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 655375262 385 APTLFREVN--NQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIYGLAAGVWTAD 438
Cdd:cd07128 378 PPTLLLCDDpdAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
76-450 |
1.23e-13 |
|
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: 72.96 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELALLETLDMGKPI-RFSKSVDVTN-----AARALRwSGEAVDKIYDeiapTADN 149
Cdd:cd07129 15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEaRLQGELGRTTgqlrlFADLVR-EGSWLDARID----PADP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 150 EIGMITRE-------PVGVVAAIVPWNFPLlmACWKLG----PALASGNSVILKPSEKSPLTAIRMAAIALEA----GIP 214
Cdd:cd07129 90 DRQPLPRPdlrrmlvPLGPVAVFGASNFPL--AFSVAGgdtaSALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 215 PGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLM-VYAGQSNMKRVWLEAGGKSPHIVFndcPD-LKAAAQAAA 292
Cdd:cd07129 168 AGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFdAAAARPEPIPFYAELGSVNPVFIL---PGaLAERGEAIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 293 SA----IAFNQGEVCTA-GSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAvvdQQQLQTILGyieagkQQGAV 367
Cdd:cd07129 245 QGfvgsLTLGAGQFCTNpGLVLVPAGPAGDAFIAALAEALAAAPAQTMLTPGIAEAY---RQGVEALAA------APGVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 368 LVCGGEqlmAETGGVYVAPTLFrEVNNQMSIA----REEIFGPVLSVIEFEGMEQAIAI-----GNdtiygLAAGVW--T 436
Cdd:cd07129 316 VLAGGA---AAEGGNQAAPTLF-KVDAAAFLAdpalQEEVFGPASLVVRYDDAAELLAVaealeGQ-----LTATIHgeE 386
|
410
....*....|....
gi 655375262 437 ADLSKAHRTAKALR 450
Cdd:cd07129 387 DDLALARELLPVLE 400
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
81-348 |
2.05e-13 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, 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. This group includes families ALDH18, ALDH19, and ALDH20 and represents 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: 143396 [Multi-domain] Cd Length: 397 Bit Score: 71.87 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 81 PVERKKVMIRFADLLEAHSDELALLETLDMGKPIRF-----------SKSVDVTNAArALRWSGEAVDKIYDEIAPtaDN 149
Cdd:cd07077 15 DEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSlianwiammgcSESKLYKNID-TERGITASVGHIQDVLLP--DN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 150 EIGMITREPVGVVAAIVPWNFPLLmACWKLGPALASGNSVILKPSEKSPLTAiRMAAIALEAGIPPG----VLNVLPGFG 225
Cdd:cd07077 92 GETYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAPFTN-RALALLFQAADAAHgpkiLVLYVPHPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 226 HTVGKALALHMDVDTLVFTGSTKiakqlMVYAGQ--SNMKRVwLEAGGKSPHIVFNDCPDLKAAAQAAASAIAFNQGeVC 303
Cdd:cd07077 170 DELAEELLSHPKIDLIVATGGRD-----AVDAAVkhSPHIPV-IGFGAGNSPVVVDETADEERASGSVHDSKFFDQN-AC 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 655375262 304 TAGSRLLVESGVKEQLIALIIDELKSWQPGHPLDPDTVSGAVVDQ 348
Cdd:cd07077 243 ASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETKPLSKETTPS 287
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
155-414 |
1.97e-12 |
|
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: 69.06 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 155 TREPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEAGIPPGVLNVLPGFGHTVGKALaL 234
Cdd:cd07126 139 YRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKIL-L 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 235 HMDVDTLVFTGSTKIAKQLMVyagqsNMK-RVWLEAGGKSPHIVFNDCPDLKAAAQAAASAIAFNQGEVCTAGSRLLV-E 312
Cdd:cd07126 218 EANPRMTLFTGSSKVAERLAL-----ELHgKVKLEDAGFDWKILGPDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAhE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 313 SGVKeqliALIIDELKSWQPGHPLDPDTVsGAVVDQQQlQTILGYIEAGKQ-QGAVLVCGGEQLMA----------ETGG 381
Cdd:cd07126 293 NWVQ----AGILDKLKALAEQRKLEDLTI-GPVLTWTT-ERILDHVDKLLAiPGAKVLFGGKPLTNhsipsiygayEPTA 366
|
250 260 270
....*....|....*....|....*....|...
gi 655375262 382 VYVaPTLFREVNNQMSIAREEIFGPVLSVIEFE 414
Cdd:cd07126 367 VFV-PLEEIAIEENFELVTTEVFGPFQVVTEYK 398
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
76-475 |
3.13e-11 |
|
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: 65.58 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 76 WSRMAPVERKKVMIRFADLLEAHSDELA--LLETLDMGKPIRFSKSvdvtnAARALRWSGEAVDKIY---DEIAPTADNE 150
Cdd:cd07127 100 WRDAGARARAGVCLEILQRLNARSFEMAhaVMHTTGQAFMMAFQAG-----GPHAQDRGLEAVAYAWremSRIPPTAEWE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 151 IGMITREPVGVVA--AIVPWNFPLLMAC-----WKLGPA----LASGNSVILKPSEKSPL----TAIRMAAIALEAGIPP 215
Cdd:cd07127 175 KPQGKHDPLAMEKtfTVVPRGVALVIGCstfptWNGYPGlfasLATGNPVIVKPHPAAILplaiTVQVAREVLAEAGFDP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 216 G-VLNVLPGFGHTVGKALALHMDVDTLVFTGSTKIAKQLMVYAGQsnmKRVWLEAGGKSPHIVfNDCPDLKAAAQAAASA 294
Cdd:cd07127 255 NlVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ---AQVYTEKAGVNTVVV-DSTDDLKAMLRNLAFS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 295 IAFNQGEVCTAGSRLLV-------ESGVKE-----QLIALIIDELKSwqpghplDPDtVSGAVVDQQQLQTILGYIEAGK 362
Cdd:cd07127 331 LSLYSGQMCTTPQNIYVprdgiqtDDGRKSfdevaADLAAAIDGLLA-------DPA-RAAALLGAIQSPDTLARIAEAR 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 363 QQGAVLVCGGEQLMAETGGVYV-APTLFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIAIGNDTIY---GLAAGVWTAD 438
Cdd:cd07127 403 QLGEVLLASEAVAHPEFPDARVrTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVRehgAMTVGVYSTD 482
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 655375262 439 LSKAHRTAKALR----------SGMVWINHydggdmTAPFGGYKQSG 475
Cdd:cd07127 483 PEVVERVQEAALdagvalsinlTGGVFVNQ------SAAFSDFHGTG 523
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
141-422 |
7.51e-09 |
|
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: 57.66 E-value: 7.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 141 DEIAP---TADNEIGMIT-REPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAIALEA----G 212
Cdd:cd07081 74 DEKTCgvlTGDENGGTLIiAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 213 IPPGVLNVLPGFGHTVGKALALHMDVDTLVFTGSTKiakqlMVYAGQSNMKRVwLEAGGKSPHIVFNDCPDLKAAAQAAA 292
Cdd:cd07081 154 APENLIGWIDNPSIELAQRLMKFPGIGLLLATGGPA-----VVKAAYSSGKPA-IGVGAGNTPVVIDETADIKRAVQSIV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 293 SAIAFNQGEVCTAGSRLLVesgvkeqlIALIIDELKSWQPGHpldpdtvSGAVVDQQQLQTILGYIEAGKQQGAVLVCGG 372
Cdd:cd07081 228 KSKTFDNGVICASEQSVIV--------VDSVYDEVMRLFEGQ-------GAYKLTAEELQQVQPVILKNGDVNRDIVGQD 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 655375262 373 EQLMAETGGVYVAPT---LFREVNnqmSIAREEIFG-----PVLSVIEFEGMEQAIAI 422
Cdd:cd07081 293 AYKIAAAAGLKVPQEtriLIGEVT---SLAEHEPFAheklsPVLAMYRAANFADADAK 347
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
148-341 |
5.16e-08 |
|
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: 55.19 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 148 DNEIGMITR--EPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPSEKSPLTAIRMAAI----ALEAGIPPGVLNVL 221
Cdd:cd07122 83 EDEEKGIVEiaEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKImreaAVAAGAPEGLIQWI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 222 PGFGHTVGKALALHMDVDTLVFTGSTKiakqlMVYAGQSnmkrvwleAG--------GKSPHIVFNDCpDLKAAAQAAAS 293
Cdd:cd07122 163 EEPSIELTQELMKHPDVDLILATGGPG-----MVKAAYS--------SGkpaigvgpGNVPAYIDETA-DIKRAVKDIIL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655375262 294 AIAFNQGEVCTAGSRLLVESGVKEQLIA--------LIIDELKS------WQPGHPLDPDTV 341
Cdd:cd07122 229 SKTFDNGTICASEQSVIVDDEIYDEVRAelkrrgayFLNEEEKEklekalFDDGGTLNPDIV 290
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
144-421 |
2.69e-05 |
|
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: 46.46 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 144 APTADNEIGMITREPVGVVAAIVPWNFPL-LMACWKLGpALASGNSVILKP---SEKSPLTAIRM--AAIAlEAGIPPGV 217
Cdd:cd07121 83 AWSGDNGLTLVEYAPFGVIGAITPSTNPTeTIINNSIS-MLAAGNAVVFNPhpgAKKVSAYAVELinKAIA-EAGGPDNL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 218 LNVL--PGFGHTvgKALALHMDVDTLVFTGSTKIAKQLMvyagqSNMKRVwLEAGGKSPHIVFNDCPDLKAAAQAAASAI 295
Cdd:cd07121 161 VVTVeePTIETT--NELMAHPDINLLVVTGGPAVVKAAL-----SSGKKA-IGAGAGNPPVVVDETADIEKAARDIVQGA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 296 AFNQGEVCTAGSRLLVESGVKEQLIALIIDElkswqpghpldpdtvsGA-VVDQQQLQtilgyieagKQQGAVLVCGGE- 373
Cdd:cd07121 233 SFDNNLPCIAEKEVIAVDSVADYLIAAMQRN----------------GAyVLNDEQAE---------QLLEVVLLTNKGa 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655375262 374 -----------QLMAETGGVYVAPT---LFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIA 421
Cdd:cd07121 288 tpnkkwvgkdaSKILKAAGIEVPADirlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
144-421 |
3.73e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 39.89 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 144 APTADNEIGMITREPVGVVAAIVPWNFPL-LMACWKLGpALASGNSVILKP---SEKSPLTAIRM--AAIAlEAGIPPGV 217
Cdd:PRK15398 115 ALTGDNGLTLIEYAPFGVIGAVTPSTNPTeTIINNAIS-MLAAGNSVVFSPhpgAKKVSLRAIELlnEAIV-AAGGPENL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 218 LNVL--PGFGHTvgKALALHMDVDTLVFTGSTKIAKQLMvyagQSNmKRVwLEAGGKSPHIVFNDCPDLKAAAQAAASAI 295
Cdd:PRK15398 193 VVTVaePTIETA--QRLMKHPGIALLVVTGGPAVVKAAM----KSG-KKA-IGAGAGNPPVVVDETADIEKAARDIVKGA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 296 AFNQGEVCTAGSRLLVESGVKEQLIALIIDElkswqpghpldpdtvsGAVV----DQQQLQTILgyIEAGKQQGAVLVCG 371
Cdd:PRK15398 265 SFDNNLPCIAEKEVIVVDSVADELMRLMEKN----------------GAVLltaeQAEKLQKVV--LKNGGTVNKKWVGK 326
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 655375262 372 GEQLMAETGGVYVAPT---LFREVNNQMSIAREEIFGPVLSVIEFEGMEQAIA 421
Cdd:PRK15398 327 DAAKILEAAGINVPKDtrlLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIA 379
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
148-245 |
8.70e-03 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 38.63 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655375262 148 DNEIGMIT-REPVGVVAAIVPWNFPLLMACWKLGPALASGNSVILKPS---EKSPLTA---IRMAAIAleAGIPPGVLNV 220
Cdd:PRK13805 97 DDEFGIIEiAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHpraQKSSIAAakiVLDAAVA--AGAPKDIIQW 174
|
90 100
....*....|....*....|....*
gi 655375262 221 LPGFGHTVGKALALHMDVDTLVFTG 245
Cdd:PRK13805 175 IEEPSVELTNALMNHPGIALILATG 199
|
|
| |
