|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-490 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 1038.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 1 MARFEEQKLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILR 80
Cdd:PRK13252 1 MSRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 81 ERNDELAALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIAL 160
Cdd:PRK13252 81 ERNDELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGReVGQWLTEHPLIEKISFTGGTSTGKKVMAS 240
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 241 ASSSsLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQD 320
Cdd:PRK13252 240 AAAS-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 321 ENTNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDD 400
Cdd:PRK13252 319 PATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 401 EDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQ 480
Cdd:PRK13252 399 EDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQ 478
|
490
....*....|
gi 15600566 481 VELGDYASVF 490
Cdd:PRK13252 479 VEMGPFQSPF 488
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
26-484 |
0e+00 |
|
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: 809.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 26 TINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRsVD 105
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 106 IVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 186 LKLAEIYTEAGVPDGVFNVLTGSGrEVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSsLKEVTMELGGKSPLIIFPDA 265
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKG-IKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 266 DLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGK 345
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 346 AQKARLLCGGERVT-DGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDL 424
Cdd:cd07090 318 QEGAKVLCGGERVVpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 425 ARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQVELG 484
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
10-477 |
0e+00 |
|
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: 749.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 10 YIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAAL 89
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 90 ETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAA 169
Cdd:TIGR01804 81 ETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 170 GNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSsLKEV 249
Cdd:TIGR01804 161 GNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGH-LKHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 250 TMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLV 329
Cdd:TIGR01804 240 TMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 330 SFPHMESVLGYIESGKAQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRAN 409
Cdd:TIGR01804 320 SAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARAN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600566 410 DTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIK 477
Cdd:TIGR01804 400 DTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
5-483 |
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: 689.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 5 EEQKLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERND 84
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 85 ELAALETLDTGKPLAETRsVDIVTGADVLEYYAGLVPAIEGEQIPL-RETSFVYTRREPLGVVAGIGAWNYPVQIALWKS 163
Cdd:COG1012 84 ELAALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSdAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASAsS 243
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA-A 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 244 SSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENT 323
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 324 NFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDgafGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDE 403
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDG---EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 404 AIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESP-AEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQVE 482
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
.
gi 15600566 483 L 483
Cdd:COG1012 479 L 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
15-479 |
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: 652.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 15 YVEASSGaTFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDT 94
Cdd:pfam00171 1 WVDSESE-TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 95 GKPLAETRsVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMI 174
Cdd:pfam00171 80 GKPLAEAR-GEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 175 FKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASAsSSSLKEVTMELG 254
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAA-AQNLKRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 255 GKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHM 334
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 335 ESVLGYIESGKAQKARLLCGGERVtdgaFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYG 414
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGEAG----LDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600566 415 LAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEM-PVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:pfam00171 394 LAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
8-481 |
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: 618.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKV--WAAMTAMQRSRILRRAVDILRERNDE 85
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 86 LAALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAP 165
Cdd:cd07091 85 LAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSS 245
Cdd:cd07091 165 ALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 246 LKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNF 325
Cdd:cd07091 245 LKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 326 GPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAI 405
Cdd:cd07091 325 GPQVSKAQFDKILSYIESGKKEGATLLTGGERHGS----KGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600566 406 RRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
26-479 |
0e+00 |
|
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: 584.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 26 TINPANGEVLAKVQRASREDVERAVQSAVEG--QKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRS 103
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 104 vDIVTGADVLEYYAGLVPAIEGEQIPLRETS-FVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTP 182
Cdd:cd07114 81 -QVRYLAEWYRYYAGLADKIEGAVIPVDKGDyLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 183 LTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVmASASSSSLKEVTMELGGKSPLIIF 262
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHI-ARAAAENLAPVTLELGGKSPNIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 263 PDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIE 342
Cdd:cd07114 239 DDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 343 SGKAQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQ 422
Cdd:cd07114 319 RAREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600566 423 DLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07114 399 DLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
10-483 |
0e+00 |
|
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: 576.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 10 YIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEG--QKVWAAMTAMQRSRILRRAVDILRERNDELA 87
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 88 ALETLDTGKPLAETRSvDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPAL 167
Cdd:cd07119 81 RLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 168 AAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSsLK 247
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN-VK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 248 EVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGP 327
Cdd:cd07119 239 KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 328 LVSFPHMESVLGYIESGKAQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRR 407
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600566 408 ANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQVEL 483
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININL 474
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
47-481 |
0e+00 |
|
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: 568.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 47 ERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRsVDIVTGADVLEYYAGLVPAIEGE 126
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 127 QIPL-RETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVL 205
Cdd:cd07078 80 VIPSpDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 206 TGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASAsSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQV 285
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAA-AENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 286 CTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDgafGK 365
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEG---GK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 366 GAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWG 445
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 15600566 446 ESP-AEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07078 396 VGAePSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
26-481 |
0e+00 |
|
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: 560.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 26 TINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSVD 105
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 106 IVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 186 LKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMAsASSSSLKEVTMELGGKSPLIIFPDA 265
Cdd:cd07093 161 WLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMR-AAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 266 DLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGK 345
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 346 AQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLA 425
Cdd:cd07093 320 AEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600566 426 RAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07093 400 RAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
21-479 |
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: 544.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 21 GATFETINPANGEVLAKVQRASREDVERAVQSAVEG--QKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPL 98
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 99 AETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPS 178
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 179 EVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSSLKEVTMELGGKSP 258
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 259 LIIFPDA-DLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESV 337
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 338 LGYIESGKAQKARLLCGGERVTdgAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAA 417
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRVL--TETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600566 418 GVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
26-483 |
0e+00 |
|
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: 542.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 26 TINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSVD 105
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 106 IVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 186 LKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMaSASSSSLKEVTMELGGKSPLIIFPDA 265
Cdd:cd07115 161 LRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIM-QGAAGNLKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 266 DLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGK 345
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 346 AQKARLLCGGERVTDgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLA 425
Cdd:cd07115 320 EEGARLLTGGKRPGA----RGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600566 426 RAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQVEL 483
Cdd:cd07115 396 RAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
27-479 |
0e+00 |
|
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: 532.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 27 INPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRsVDI 106
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 107 VTGADVLEYYAGLVPAIEGEQIPLRETSF-VYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKrILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 186 LKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSsLKEVTMELGGKSPLIIFPDA 265
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADT-VKRVSLELGGNAPFIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 266 DLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGK 345
Cdd:cd07103 240 DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 346 AQKARLLCGGERVTDGafgkGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLA 425
Cdd:cd07103 320 AKGAKVLTGGKRLGLG----GYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15600566 426 RAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
8-483 |
0e+00 |
|
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: 525.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEG-QKVWAAMTAMQRSRILRRAVDILRERNDEL 86
Cdd:cd07144 9 GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 87 AALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPA 166
Cdd:cd07144 89 AAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMAsASSSSL 246
Cdd:cd07144 169 LAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMK-AAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 247 KEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERV-QRIRLGDPQDENTNF 325
Cdd:cd07144 248 KAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 326 GPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDGAfGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAI 405
Cdd:cd07144 328 GPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGL-GKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAI 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600566 406 RRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQVEL 483
Cdd:cd07144 407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
8-481 |
0e+00 |
|
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: 525.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQK---VWAAMTAMQRSRILRRAVDILRERND 84
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 85 ELAALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSA 164
Cdd:cd07141 88 YLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 165 PALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSS 244
Cdd:cd07141 168 PALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 245 SLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTN 324
Cdd:cd07141 248 NLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 325 FGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEA 404
Cdd:cd07141 328 QGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGD----KGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEV 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600566 405 IRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07141 404 IERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
9-480 |
0e+00 |
|
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: 522.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 9 LYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAA 88
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 89 LETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQipLRETSFVytRREPLGVVAGIGAWNYPV-QIALwKSAPAL 167
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEE--RRGNSLV--VREPIGVCGLITPWNWPLnQIVL-KVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 168 AAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSsLK 247
Cdd:cd07138 156 AAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT-VK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 248 EVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGP 327
Cdd:cd07138 235 RVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 328 LVSFPHMESVLGYIESGKAQKARLLCGGERVTDGaFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRR 407
Cdd:cd07138 315 LASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEG-LERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAI 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600566 408 ANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPaEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQ 480
Cdd:cd07138 394 ANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP-GAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
8-479 |
0e+00 |
|
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: 517.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEG--QKVWAAMTAMQRSRILRRAVDILRERNDE 85
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 86 LAALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAP 165
Cdd:cd07142 85 LAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSS 245
Cdd:cd07142 165 ALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 246 LKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNF 325
Cdd:cd07142 245 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 326 GPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAI 405
Cdd:cd07142 325 GPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGS----KGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600566 406 RRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
8-483 |
4.32e-179 |
|
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: 510.73 E-value: 4.32e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELA 87
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 88 ALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPAL 167
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 168 AAGNAMIFKPSEVTPLTALKLAEIYTEAgVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSsLK 247
Cdd:cd07559 162 AAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAEN-LI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 248 EVTMELGGKSPLIIFPDA-----DLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDEN 322
Cdd:cd07559 240 PVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 323 TNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDED 402
Cdd:cd07559 320 TMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 403 EAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQVE 482
Cdd:cd07559 400 EAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILVS 479
|
.
gi 15600566 483 L 483
Cdd:cd07559 480 Y 480
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
8-484 |
6.05e-177 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 505.21 E-value: 6.05e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVeASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELA 87
Cdd:PRK13473 4 KLLINGELV-AGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 88 ALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEG----EQIPlRETSFVytRREPLGVVAGIGAWNYPVQIALWKS 163
Cdd:PRK13473 83 RLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGkaagEYLE-GHTSMI--RRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAgVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASS 243
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 244 SsLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENT 323
Cdd:PRK13473 239 S-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 324 NFGPLVSFPHMESVLGYIESGKAQK-ARLLCGGERVtdgaFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDED 402
Cdd:PRK13473 318 ELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAP----DGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 403 EAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQVE 482
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
..
gi 15600566 483 LG 484
Cdd:PRK13473 474 HT 475
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
27-481 |
1.76e-175 |
|
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: 500.61 E-value: 1.76e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 27 INPANGEVLAKVQRASREDVERAVQSAVEG-QKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSvD 105
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 106 IVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 186 LKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSSlKEVTMELGGKSPLIIFPDA 265
Cdd:cd07109 161 LRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV-VPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 266 DLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQdENTNFGPLVSFPHMESVLGYIESGK 345
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 346 AQKARLLCGGERVTdGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLA 425
Cdd:cd07109 319 ARGARIVAGGRIAE-GAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600566 426 RAHRAIHRLEAGICWINTWGESPA-EMPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07109 398 RALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
26-483 |
1.97e-172 |
|
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: 493.05 E-value: 1.97e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 26 TINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSvD 105
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 106 IVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 186 LKLAEIYTEAgVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSsLKEVTMELGGKSPLIIFPDA 265
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 266 DLDRAADIAVMA-NFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESG 344
Cdd:cd07107 238 DPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 345 KAQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDL 424
Cdd:cd07107 318 KREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600566 425 ARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQVEL 483
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
27-481 |
8.95e-172 |
|
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: 491.07 E-value: 8.95e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 27 INPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSVDI 106
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 107 VTGADVLEYYAGLVPAIEG----EQIPLReTSFVytRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTP 182
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGpaagEYLPGH-TSMI--RREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 183 LTALKLAEIYTEaGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSsLKEVTMELGGKSPLIIF 262
Cdd:cd07092 159 LTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADT-LKRVHLELGGKAPVIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 263 PDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIE 342
Cdd:cd07092 237 DDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 343 sGKAQKARLLCGGERVTdgafGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQ 422
Cdd:cd07092 317 -RAPAHARVLTGGRRAE----GPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600566 423 DLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
10-479 |
3.41e-171 |
|
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: 490.61 E-value: 3.41e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 10 YIGGRYVEasSGATFETINPAN-GEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAA 88
Cdd:cd07097 4 YIDGEWVA--GGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 89 LETLDTGKPLAETRSvDIVTGADVLEYYAGLVPAIEGEQIP-LRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPAL 167
Cdd:cd07097 82 LLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 168 AAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVmASASSSSLK 247
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRI-AAAAAARGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 248 EVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGP 327
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 328 LVSFPHMESVLGYIESGKAQKARLLCGGERVTDGAfgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRR 407
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPD--EGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600566 408 ANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN--TWGESPaEMPVGGYKQSGVG-RENGLTTLAHYTRIKSV 479
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlpTAGVDY-HVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
8-479 |
9.06e-168 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 482.78 E-value: 9.06e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEG--QKVWAAMTAMQRSRILRRAVDILRERNDE 85
Cdd:PLN02766 22 KLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 86 LAALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAP 165
Cdd:PLN02766 102 LAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSS 245
Cdd:PLN02766 182 ALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 246 LKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNF 325
Cdd:PLN02766 262 LKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 326 GPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAI 405
Cdd:PLN02766 342 GPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGD----KGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAI 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600566 406 RRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:PLN02766 418 KKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
27-481 |
5.24e-167 |
|
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: 479.14 E-value: 5.24e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 27 INPANGEVLAKVQRASREDVERAVQSAVEG--QKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSv 104
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 105 DIVTGADVLEYYAGLVPAIEGEQI-PLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPL 183
Cdd:cd07118 81 EIEGAADLWRYAASLARTLHGDSYnNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 184 TALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMAsASSSSLKEVTMELGGKSPLIIFP 263
Cdd:cd07118 161 TTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAA-AAARNLKKVSLELGGKNPQIVFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 264 DADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIES 343
Cdd:cd07118 240 DADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 344 GKAQKARLLCGGERVtdgAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQD 423
Cdd:cd07118 320 GRAEGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600566 424 LARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07118 397 IDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
9-481 |
4.89e-166 |
|
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: 477.45 E-value: 4.89e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 9 LYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVE--GQKVWAAMTAMQRSRILRRAVDILRERNDEL 86
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRafDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 87 AALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIplRETSF---VYTRREPLGVVAGIGAWNYPVQIALWKS 163
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEER--RPGSGgghVLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGsGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASS 243
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 244 SsLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENT 323
Cdd:cd07139 238 R-LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 324 NFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDgaFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDE 403
Cdd:cd07139 317 QIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAG--LDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDD 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600566 404 AIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAeMPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFG-APFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
9-483 |
4.80e-165 |
|
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: 475.09 E-value: 4.80e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 9 LYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEG-QKVWA-AMTAMQRSRILRRAVDILRERNDEL 86
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERNLDYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 87 AALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPA 166
Cdd:cd07143 89 ASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSSL 246
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 247 KEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFG 326
Cdd:cd07143 249 KKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 327 PLVSFPHMESVLGYIESGKAQKARLLCGGERVTDgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIR 406
Cdd:cd07143 329 PQVSQIQYERIMSYIESGKAEGATVETGGKRHGN----EGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600566 407 RANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQVEL 483
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
8-483 |
1.28e-164 |
|
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: 473.87 E-value: 1.28e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELA 87
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 88 ALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPAL 167
Cdd:cd07117 82 MVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 168 AAGNAMIFKPSEVTPLTALKLAEIYTEAgVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVmASASSSSLK 247
Cdd:cd07117 162 AAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDV-AIAAAKKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 248 EVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGP 327
Cdd:cd07117 240 PATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 328 LVSFPHMESVLGYIESGKAQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRR 407
Cdd:cd07117 320 QVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDM 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600566 408 ANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQVEL 483
Cdd:cd07117 400 ANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
27-481 |
1.60e-164 |
|
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: 472.40 E-value: 1.60e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 27 INPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRsVDI 106
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ-FEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 107 VTGADVLEYYAGLvpAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTAL 186
Cdd:cd07106 81 GGAVAWLRYTASL--DLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 187 KLAEIYTEAgVPDGVFNVLTGSGrEVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSsLKEVTMELGGKSPLIIFPDAD 266
Cdd:cd07106 159 KLGELAQEV-LPPGVLNVVSGGD-ELGPALTSHPDIRKISFTGSTATGKKVMASAAKT-LKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 267 LDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKA 346
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 347 QKARLLCGGERVTdgafGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLAR 426
Cdd:cd07106 316 KGAKVLAGGEPLD----GPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15600566 427 AHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
26-481 |
3.39e-164 |
|
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: 472.23 E-value: 3.39e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 26 TINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSVD 105
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 106 IVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 186 LKLAEIYTEAgVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASAsSSSLKEVTMELGGKSPLIIFPDA 265
Cdd:cd07108 161 LLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAA-ADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 266 DLDRAADIAVMANFFS-SGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESG 344
Cdd:cd07108 239 DLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 345 KA-QKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQD 423
Cdd:cd07108 319 LStSGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600566 424 LARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGL-TTLAHYTRIKSVQV 481
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLeGMLEHFTQKKTVNI 457
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
10-481 |
4.02e-164 |
|
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: 472.60 E-value: 4.02e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 10 YIGGRYVEASSGATFETINPANG-EVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAA 88
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 89 LETLDTGKPLAETRSvDIVTGADVLEYYAGLVPAIEGEQIP--LREtSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPA 166
Cdd:cd07131 82 LVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPseLPN-KDAMTRRQPIGVVALITPWNFPVAIPSWKIFPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVmASASSSSL 246
Cdd:cd07131 160 LVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERI-GETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 247 KEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFG 326
Cdd:cd07131 239 KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 327 PLVSFPHMESVLGYIESGKAQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIR 406
Cdd:cd07131 319 PLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600566 407 RANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN--TWGeSPAEMPVGGYKQSGVG-RENGLTTLAHYTRIKSVQV 481
Cdd:cd07131 399 IANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIG-AEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
26-479 |
9.50e-164 |
|
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: 471.07 E-value: 9.50e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 26 TINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETrSVD 105
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 106 IVTGADVLEYYAGLVPAIE---GEQIPLRETSF-VYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVT 181
Cdd:cd07110 80 VDDVAGCFEYYADLAEQLDakaERAVPLPSEDFkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 182 PLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSSlKEVTMELGGKSPLII 261
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDI-KPVSLELGGKSPIIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 262 FPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYI 341
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 342 ESGKAQKARLLCGGERVTDGafGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVT 421
Cdd:cd07110 319 ARGKEEGARLLCGGRRPAHL--EKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600566 422 QDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
10-479 |
4.77e-163 |
|
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: 469.44 E-value: 4.77e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 10 YIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAAL 89
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 90 ETLDTGKPLAETRsVDIVTGADVLEYYAGLVPAIEGEQIPL-RETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALA 168
Cdd:cd07088 81 IVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSdRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 169 AGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMAsASSSSLKE 248
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIME-AAAENITK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 249 VTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPL 328
Cdd:cd07088 239 VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 329 VSFPHMESVLGYIESGKAQKARLLCGGERVTDgafGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRA 408
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGGKRPEG---EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600566 409 NDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
8-479 |
2.25e-162 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 469.21 E-value: 2.25e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEG-----QKVWAAMTAMQRSRILRRAVDILRER 82
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 83 NDELAALETLDTGKPLAETRSvDIVTGADVLEYYAGLVPAIEGEQ---IPLRETSF-VYTRREPLGVVAGIGAWNYPVQI 158
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAW-DMDDVAGCFEYYADLAEALDAKQkapVSLPMETFkGYVLKEPLGVVGLITPWNYPLLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 159 ALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVM 238
Cdd:PLN02467 168 ATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 239 ASAsSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDP 318
Cdd:PLN02467 248 TAA-AQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 319 QDENTNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDGAfgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVY 398
Cdd:PLN02467 327 LEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLK--KGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 399 DDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKS 478
Cdd:PLN02467 405 STEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQ 484
|
.
gi 15600566 479 V 479
Cdd:PLN02467 485 V 485
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
8-482 |
5.46e-161 |
|
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: 465.05 E-value: 5.46e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKV--WAAMTAMQRSRILRRAVDILRERNDE 85
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 86 LAALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRET----SFVYTRREPLGVVAGIGAWNYPVQIALW 161
Cdd:cd07140 87 LATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQArpnrNLTLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASA 241
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 242 SSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDE 321
Cdd:cd07140 247 AVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 322 NTNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDE 401
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDR----PGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 402 D--EAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07140 403 DvdGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
...
gi 15600566 480 QVE 482
Cdd:cd07140 483 TIE 485
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
27-481 |
1.41e-160 |
|
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: 462.87 E-value: 1.41e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 27 INPANGEVLAKVQRASREDVERAVQSAVEGQKVWA-AMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSVD 105
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 106 IVTGADVLEYYAGLVPAIEGEQ-IPLRETSFVYT----RREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEV 180
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWEFdLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 181 TPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSsLKEVTMELGGKSPLI 260
Cdd:cd07089 162 TPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAT-LKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 261 IFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGY 340
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 341 IESGKAQKARLLCGGERVTDgaFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVV 420
Cdd:cd07089 321 IARGRDEGARLVTGGGRPAG--LDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600566 421 TQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
8-487 |
6.56e-160 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 464.28 E-value: 6.56e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAV----EGQkvWAAMTAMQRSRILRRAVDILRERN 83
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARkafdEGP--WPKMTAYERSRILLRFADLLEKHN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 84 DELAALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKS 163
Cdd:PLN02466 137 DELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASS 243
Cdd:PLN02466 217 GPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 244 SSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENT 323
Cdd:PLN02466 297 SNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 324 NFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDE 403
Cdd:PLN02466 377 EQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGS----KGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDE 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 404 AIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQVEL 483
Cdd:PLN02466 453 VIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTPL 532
|
....
gi 15600566 484 GDYA 487
Cdd:PLN02466 533 KNPA 536
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
51-481 |
5.45e-153 |
|
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: 440.13 E-value: 5.45e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 51 QSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSvDIVTGADVLEYYAGLVPAIEGEQIPL 130
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 131 -RETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSG 209
Cdd:cd06534 80 pDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 210 REVGQWLTEHPLIEKISFTGGTSTGKKVMASAsSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNG 289
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAA-AENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 290 TRVFIHRSQQARFEAKVLervqrirlgdpqdentnfgplvsfphmesvlgyiesgkaqkarllcggervtdgafgkgayv 369
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV-------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 370 apTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWG-ESP 448
Cdd:cd06534 257 --TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSiGVG 334
|
410 420 430
....*....|....*....|....*....|...
gi 15600566 449 AEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd06534 335 PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
9-481 |
8.42e-153 |
|
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: 443.81 E-value: 8.42e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 9 LYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKV-WAAMTAMQRSRILRRAVDILRERNDELA 87
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 88 ALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGE----QIPL----RETSFvyTRREPLGVVAGIGAWNYPVQIA 159
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGEtlapSIPSmqgeRYTAF--TRREPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 160 LWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGrEVGQWLTEHPLIEKISFTGGTSTGKKVMA 239
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 240 SAsSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQ 319
Cdd:cd07113 239 QA-ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 320 DENTNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTdgafGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYD 399
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA----GEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 400 DEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07113 394 DEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
..
gi 15600566 480 QV 481
Cdd:cd07113 474 MI 475
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
11-479 |
1.17e-150 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 439.13 E-value: 1.17e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 11 IGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALE 90
Cdd:PLN02278 29 IGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 91 TLDTGKPLAETRSvDIVTGADVLEYYAGLVPAIEGEQIPlreTSFVYTR----REPLGVVAGIGAWNYPVQIALWKSAPA 166
Cdd:PLN02278 109 TLEQGKPLKEAIG-EVAYGASFLEYFAEEAKRVYGDIIP---SPFPDRRllvlKQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMAsASSSSL 246
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMA-GAAATV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 247 KEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFG 326
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 327 PLVSFPHMESVLGYIESGKAQKARLLCGGERVTDGafgkGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIR 406
Cdd:PLN02278 344 PLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLG----GTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIA 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600566 407 RANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:PLN02278 420 IANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
24-477 |
2.45e-150 |
|
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: 436.78 E-value: 2.45e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 24 FETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRs 103
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 104 VDIVTGADVLEYYAGLVPAIEGEQIPL-----RETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPS 178
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVdayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 179 EVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVmASASSSSLKEVTMELGGKSP 258
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLI-ASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 259 LIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVL 338
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 339 GYIESGKAQKARLLCGGERVtdgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAG 418
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKRD------EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600566 419 VVTQDLARAHRAIHRLEAGICWINtwgESPA----EMPVGGYKQSGVGRENGLTTLAHYTRIK 477
Cdd:cd07145 393 VFTNDINRALKVARELEAGGVVIN---DSTRfrwdNLPFGGFKKSGIGREGVRYTMLEMTEEK 452
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
24-481 |
6.28e-150 |
|
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: 435.61 E-value: 6.28e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 24 FETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETrS 103
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA-W 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 104 VDIVTGADVLEYYAGLVPAIEGEQIP-LRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTP 182
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRGETLPsDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 183 LTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVmASASSSSLKEVTMELGGKSPLIIF 262
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREI-AEKAGRHLKKITLELGGKNPLIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 263 PDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIE 342
Cdd:cd07150 239 ADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 343 SGKAQKARLLCGGERvtdgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQ 422
Cdd:cd07150 319 DAVAKGAKLLTGGKY-------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600566 423 DLARAHRAIHRLEAGICWIN---TWGESPAemPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07150 392 DLQRAFKLAERLESGMVHINdptILDEAHV--PFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
10-481 |
2.19e-149 |
|
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: 435.07 E-value: 2.19e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 10 YIGGRYVeASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAAL 89
Cdd:cd07086 2 VIGGEWV-GSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 90 ETLDTGKPLAETRSvDIVTGADVLEYYAGLVPAIEGEQIPL-RETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALA 168
Cdd:cd07086 81 VSLEMGKILPEGLG-EVQEMIDICDYAVGLSRMLYGLTIPSeRPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 169 AGNAMIFKPSEVTPLTALKLAEIYTEA----GVPDGVFNVLTGsGREVGQWLTEHPLIEKISFTGGTSTGKKVmASASSS 244
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRV-GETVAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 245 SLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTN 324
Cdd:cd07086 238 RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 325 FGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDGAfgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEA 404
Cdd:cd07086 318 VGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGE--PGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 405 IRRANDTEYGLAAGVVTQDLARAHRAI--HRLEAGICWINTwGESPAE--MPVGGYKQSGVGRENGLTTLAHYTRIKSVQ 480
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAFRWLgpKGSDCGIVNVNI-PTSGAEigGAFGGEKETGGGRESGSDAWKQYMRRSTCT 474
|
.
gi 15600566 481 V 481
Cdd:cd07086 475 I 475
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
45-481 |
5.47e-143 |
|
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: 416.93 E-value: 5.47e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 45 DVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTG----KPLAETR-SVDIVTGAdvleyyAGL 119
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGstrpKAAFEVGaAIAILREA------AGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 120 VPAIEGEQIP-LRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLT-ALKLAEIYTEAGV 197
Cdd:cd07104 75 PRRPEGEILPsDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 198 PDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVmASASSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMA 277
Cdd:cd07104 155 PKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHI-GELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 278 NFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKAQKARLLCGGER 357
Cdd:cd07104 234 AFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 358 vtdgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAG 437
Cdd:cd07104 314 -------EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETG 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15600566 438 ICWIN--TWGESPaEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07104 387 MVHINdqTVNDEP-HVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
24-479 |
1.61e-142 |
|
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: 416.61 E-value: 1.61e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 24 FETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRS 103
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 104 -VD--IVTgadvLEYYAGLVPAIEGEQIPLR-----ETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIF 175
Cdd:cd07149 81 eVDraIET----LRLSAEEAKRLAGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 176 KPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASAsssSLKEVTMELGG 255
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKA---GLKKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 256 KSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHME 335
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 336 SVLGYIESGKAQKARLLCGGERvtdgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGL 415
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGL 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600566 416 AAGVVTQDLARAHRAIHRLEAGICWINtwgESPA----EMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07149 387 QAGVFTNDLQKALKAARELEVGGVMIN---DSSTfrvdHMPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
6-483 |
1.38e-141 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 415.83 E-value: 1.38e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 6 EQKLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSA--VEGQKVWAAMTAMQRSRILRRAVDILRERN 83
Cdd:PRK09847 19 ENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAArgVFERGDWSLSSPAKRKAVLNKLADLMEAHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 84 DELAALETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKS 163
Cdd:PRK09847 99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASS 243
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 244 SSLKEVTMELGGKSPLIIFPDA-DLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDEN 322
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 323 TNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERvtdgafGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDED 402
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNA------GLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 403 EAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQVE 482
Cdd:PRK09847 413 QALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWIS 492
|
.
gi 15600566 483 L 483
Cdd:PRK09847 493 L 493
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
10-481 |
2.91e-138 |
|
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: 406.84 E-value: 2.91e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 10 YIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAAL 89
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 90 ETLDTGKPLAETRSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAA 169
Cdd:cd07116 84 ETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 170 GNAMIFKPSEVTPLTALKLAEIYTEAgVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASAsSSSLKEV 249
Cdd:cd07116 164 GNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYA-SENIIPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 250 TMELGGKSPLIIFP------DADLDRAADIAVManF-FSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDEN 322
Cdd:cd07116 242 TLELGGKSPNIFFAdvmdadDAFFDKALEGFVM--FaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 323 TNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDGAFGKGAYVAPTVFTDcRDDMTIVREEIFGPVMSILVYDDED 402
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600566 403 EAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07116 399 EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
9-479 |
1.19e-133 |
|
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: 396.21 E-value: 1.19e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 9 LYIGGRYVEasSGATFETINPAN-GEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELA 87
Cdd:cd07124 35 LVIGGKEVR--TEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 88 ALETLDTGKPLAETrSVDIVTGADVLEYYAGLVPAIEG---EQIPLRETSFVYtrrEPLGVVAGIGAWNYPVQIALWKSA 164
Cdd:cd07124 113 AWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGfpvEMVPGEDNRYVY---RPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 165 PALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSS 244
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 245 S-----LKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQ 319
Cdd:cd07124 269 QpgqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 320 DENTNFGPLVSFPHMESVLGYIESGKaQKARLLCGGERVTDGAfgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYD 399
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEVLELAA--EGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 400 DEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN--TWGESPAEMPVGGYKQSGVG-RENGLTTLAHYTRI 476
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGTGsKAGGPDYLLQFMQP 505
|
...
gi 15600566 477 KSV 479
Cdd:cd07124 506 KTV 508
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
26-479 |
4.65e-133 |
|
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: 392.48 E-value: 4.65e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 26 TINPANGEVLAKVQRASREDVERAVQSAVEGQK--VWAAmTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRs 103
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 104 VDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPL 183
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 184 TALKLAEIYTEA-GVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSsLKEVTMELGGKSPLIIF 262
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPT-LKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 263 PDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIE 342
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 343 SGKAQKARLLCGGERVTDGaFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQ 422
Cdd:cd07120 318 RAIAAGAEVVLRGGPVTEG-LAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600566 423 DLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
27-479 |
8.25e-133 |
|
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: 391.97 E-value: 8.25e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 27 INPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRsVDI 106
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 107 VTGADVLEYYAGLVP-AIEGEQIPLRETSFV---YTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTP 182
Cdd:cd07099 80 LLALEAIDWAARNAPrVLAPRKVPTGLLMPNkkaTVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 183 LTALKLAEIYTEAGVPDGVFNVLTGSGrEVGQWLTEHPlIEKISFTGGTSTGKKVMASASSSsLKEVTMELGGKSPLIIF 262
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDAG-VDKVAFTGSVATGRKVMAAAAER-LIPVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 263 PDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIE 342
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 343 SGKAQKARLLCGGERVTdgafGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQ 422
Cdd:cd07099 317 DAVAKGAKALTGGARSN----GGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600566 423 DLARAHRAIHRLEAGICWIN--TWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07099 393 DLARAEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
9-475 |
1.45e-131 |
|
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: 389.83 E-value: 1.45e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 9 LYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAA 88
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 89 LETLDTGKPLAETRSVDIVTGADVLEYYAGlvpaiegeQIPLRETSFvyTRREPLGVVAGIGAWNYPVQIALWKSAPALA 168
Cdd:cd07111 104 LESLDNGKPIRESRDCDIPLVARHFYHHAG--------WAQLLDTEL--AGWKPVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 169 AGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGrEVGQWLTEHPLIEKISFTGGTSTGKkVMASASSSSLKE 248
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGR-ALRRATAGTGKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 249 VTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPL 328
Cdd:cd07111 252 LSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 329 VSFPHMESVLGYIESGKAQKARLLcggeRVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRA 408
Cdd:cd07111 332 VDPAQLKRIRELVEEGRAEGADVF----QPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600566 409 NDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTR 475
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
25-479 |
2.61e-130 |
|
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: 385.63 E-value: 2.61e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 25 ETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRsV 104
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR-V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 105 DIVTGADVLEYYAGLVPAIEGEQIPL-----RETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSE 179
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLdatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 180 VTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASAsssSLKEVTMELGGKSPL 259
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANA---GGKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 260 IIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLG 339
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 340 YIESGKAQKARLLCGGERvtdgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGV 419
Cdd:cd07094 318 WVEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGI 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600566 420 VTQDLARAHRAIHRLEAGICWINtwgESPA----EMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07094 391 FTRDLNVAFKAAEKLEVGGVMVN---DSSAfrtdWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
13-480 |
1.53e-129 |
|
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: 383.96 E-value: 1.53e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 13 GRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETL 92
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 93 DTGKPLAETRSVDIVTGADVLEYyAGLVPAIEGEQIPLR---ETSFVYtrREPLGVVAGIGAWNYPVQIALWKSAPALAA 169
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREA-ATFPLRMEGRILPSDvpgKENRVY--REPLGVVGVISPWNFPLHLSMRSVAPALAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 170 GNAMIFKPSEVTPLTA-LKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVmASASSSSLKE 248
Cdd:cd07151 158 GNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHI-GELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 249 VTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPL 328
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 329 VSFPHMESVLGYIESGKAQKARLLCGGERVtdgafgkGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRA 408
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGGEAE-------GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELA 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600566 409 NDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN--TWGESPaEMPVGGYKQSGVGRENGLTTLAHYTRIK--SVQ 480
Cdd:cd07151 390 NDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVNDEP-HVPFGGEKNSGLGRFNGEWALEEFTTDKwiSVQ 464
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
46-466 |
2.92e-129 |
|
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: 381.81 E-value: 2.92e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 46 VERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRS-VDIVtgADVLEYYAGLVPA-I 123
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEKC--AWICRYYAENAEAfL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 124 EGEQIPLrETSFVYTRREPLGVVAGIGAWNYPV-QIALWkSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVF 202
Cdd:cd07100 79 ADEPIET-DAGKAYVRYEPLGVVLGIMPWNFPFwQVFRF-AAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 203 NVLTGSGREVGQwLTEHPLIEKISFTGGTSTGKKVmASASSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSS 282
Cdd:cd07100 157 QNLLIDSDQVEA-IIADPRVRGVTLTGSERAGRAV-AAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 283 GQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTdga 362
Cdd:cd07100 235 GQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPD--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 363 fGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN 442
Cdd:cd07100 312 -GPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
|
410 420
....*....|....*....|....
gi 15600566 443 TWGESPAEMPVGGYKQSGVGRENG 466
Cdd:cd07100 391 GMVKSDPRLPFGGVKRSGYGRELG 414
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
8-479 |
7.00e-127 |
|
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: 377.63 E-value: 7.00e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELA 87
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 88 ALETLDTGKPLAETRSvDIVTGADVLEYYAGLVPAIEGEQIPLRETSF-VYTRREPLGVVAGIGAWNYPVQIALWKSAPA 166
Cdd:cd07085 82 RLITLEHGKTLADARG-DVLRGLEVVEFACSIPHLLKGEYLENVARGIdTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGsGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSSl 246
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 247 KEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVC-TNGTRVFIHrSQQARFEAKVLERVQRIRLGDPQDENTNF 325
Cdd:cd07085 239 KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCmALSVAVAVG-DEADEWIPKLVERAKKLKVGAGDDPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 326 GPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAI 405
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600566 406 RRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEM-PVGGYKQSGVGREN--GLTTLAHYTRIKSV 479
Cdd:cd07085 398 AIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFfSFGGWKGSFFGDLHfyGKDGVRFYTQTKTV 474
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
25-479 |
3.92e-124 |
|
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: 369.77 E-value: 3.92e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 25 ETINPANGEVLAKVQRASREDVERAVQSAVEGQKvwaAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRsV 104
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR-Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 105 DIVTGADVLEYYAGLVPAIEGEQIPL-----RETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSE 179
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCdltanGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 180 VTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASAsssSLKEVTMELGGKSPL 259
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATA---GYKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 260 IIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLG 339
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 340 YIESGKAQKARLLCGGERVtdgafgkGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGV 419
Cdd:cd07146 315 RVEEAIAQGARVLLGNQRQ-------GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600566 420 VTQDLARAHRAIHRLEAGICwiNTWgESP---AEM-PVGGYKQSG-VGRENGLTTLAHYTRIKSV 479
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTV--NVN-EVPgfrSELsPFGGVKDSGlGGKEGVREAMKEMTNVKTY 449
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
45-479 |
2.19e-120 |
|
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: 359.58 E-value: 2.19e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 45 DVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPlAETRSVDIVTGADVLEYYAGLVPAIE 124
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 125 GEQIP-LRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFN 203
Cdd:cd07105 80 GGSIPsDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 204 VLTGS---GREVGQWLTEHPLIEKISFTGGTSTGKKVmASASSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFF 280
Cdd:cd07105 160 VVTHSpedAPEVVEALIAHPAVRKVNFTGSTRVGRII-AETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 281 SSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDentnfGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTD 360
Cdd:cd07105 239 NSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVDDALSKGAKLVVGGLADES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 361 GAfgkGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICW 440
Cdd:cd07105 314 PS---GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15600566 441 IN--TWGESPAeMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07105 391 INgmTVHDEPT-LPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
24-479 |
2.35e-120 |
|
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: 360.02 E-value: 2.35e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 24 FETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRS 103
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 104 vDIVTGADVLEYYAGLVPAIEGEQIPLrETS------FVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKP 177
Cdd:cd07147 81 -EVARAIDTFRIAAEEATRIYGEVLPL-DISargegrQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 178 SEVTPLTALKLAEIYTEAGVPDGVFNVLTGSgREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSsslKEVTMELGGKS 257
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 258 PLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESV 337
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 338 LGYIESGKAQKARLLCGGERvtdgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAA 417
Cdd:cd07147 315 EGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600566 418 GVVTQDLARAHRAIHRLEAGICWINtwgESPA----EMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07147 388 GVFTRDLEKALRAWDELEVGGVVIN---DVPTfrvdHMPYGGVKDSGIGREGVRYAIEEMTEPRLL 450
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
16-479 |
2.74e-118 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 357.27 E-value: 2.74e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 16 VEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTG 95
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 96 KplaeTRS------VDIVTGADvleYYAGLVPAIEGEQ-----IPLRETSFVYtrREPLGVVAGIGAWNYPVQIALWKSA 164
Cdd:PRK09407 106 K----ARRhafeevLDVALTAR---YYARRAPKLLAPRrragaLPVLTKTTEL--RQPKGVVGVISPWNYPLTLAVSDAI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 165 PALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHplIEKISFTGGTSTGKKVmASASSS 244
Cdd:PRK09407 177 PALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVL-AEQAGR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 245 SLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTN 324
Cdd:PRK09407 254 RLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSAD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 325 FGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTD-GAFgkgaYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDE 403
Cdd:PRK09407 334 MGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDlGPL----FYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 404 AIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN-----TWGESPAemPVGGYKQSGVGRENGLTTLAHYTRIKS 478
Cdd:PRK09407 410 AVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVDA--PMGGMKDSGLGRRHGAEGLLKYTESQT 487
|
.
gi 15600566 479 V 479
Cdd:PRK09407 488 I 488
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
2-477 |
3.46e-118 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 355.75 E-value: 3.46e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 2 ARFEEQKLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRE 81
Cdd:PRK11241 6 STLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMME 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 82 RNDELAALETLDTGKPLAETRSvDIVTGADVLEYYAGLVPAIEGEQIPLRET-SFVYTRREPLGVVAGIGAWNYPVQIAL 160
Cdd:PRK11241 86 HQDDLARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPGHQAdKRLIVIKQPIGVTAAITPWNFPAAMIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMAS 240
Cdd:PRK11241 165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 241 AsSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQD 320
Cdd:PRK11241 245 C-AKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 321 ENTNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDGafgkGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDD 400
Cdd:PRK11241 324 KGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELG----GNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKD 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600566 401 EDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLAHYTRIK 477
Cdd:PRK11241 400 EADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
27-479 |
5.44e-118 |
|
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: 353.86 E-value: 5.44e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 27 INPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSvDI 106
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG-EI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 107 VTGADVLEYYAGLVPAIEGEQIPLRETSFV-YTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07102 80 RGMLERARYMISIAEEALADIRVPEKDGFErYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 186 LKLAEIYTEAGVPDGVFNVLTGSGrEVGQWLTEHPLIEKISFTGGTSTGKKVmASASSSSLKEVTMELGGKSPLIIFPDA 265
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSH-ETSAALIADPRIDHVSFTGSVAGGRAI-QRAAAGRFIKVGLELGGKDPAYVRPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 266 DLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGK 345
Cdd:cd07102 238 DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 346 AQKARLLCGGERVTDGAfGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLA 425
Cdd:cd07102 318 AKGARALIDGALFPEDK-AGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600566 426 RAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGrenglTTLAHY-----TRIKSV 479
Cdd:cd07102 397 RAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRG-----VTLSRLgydqlTRPKSY 450
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
9-479 |
7.41e-117 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 353.09 E-value: 7.41e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 9 LYIGGRYVEasSGATFETINPAN-GEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELA 87
Cdd:PRK03137 39 LIIGGERIT--TEDKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 88 ALETLDTGKPLAETrSVDIVTGADVLEYYA----GLVPAIEGEQIPLRETSFVYtrrEPLGVVAGIGAWNYPVQIALWKS 163
Cdd:PRK03137 117 AWLVKEAGKPWAEA-DADTAEAIDFLEYYArqmlKLADGKPVESRPGEHNRYFY---IPLGVGVVISPWNFPFAIMAGMT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASS 243
Cdd:PRK03137 193 LAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 244 SS-----LKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDP 318
Cdd:PRK03137 273 VQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 319 qDENTNFGPLVSFPHMESVLGYIESGKaQKARLLCGGERvtDGafGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVY 398
Cdd:PRK03137 353 -EDNAYMGPVINQASFDKIMSYIEIGK-EEGRLVLGGEG--DD--SKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 399 DDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN---TwGESPAEMPVGGYKQSGV-GRENGLTTLAHYT 474
Cdd:PRK03137 427 KDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgcT-GAIVGYHPFGGFNMSGTdSKAGGPDYLLLFL 505
|
....*
gi 15600566 475 RIKSV 479
Cdd:PRK03137 506 QAKTV 510
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
27-481 |
3.07e-116 |
|
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: 349.69 E-value: 3.07e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 27 INPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKplaeTRSV-- 104
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGK----ARRHaf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 105 -DIVTGADVLEYYAGLVPAIEGEQ-----IPLRETSFVYtrREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPS 178
Cdd:cd07101 77 eEVLDVAIVARYYARRAERLLKPRrrrgaIPVLTRTTVN--RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 179 EVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHplIEKISFTGGTSTGKKVmASASSSSLKEVTMELGGKSP 258
Cdd:cd07101 155 SQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVV-AERAGRRLIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 259 LIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVL 338
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 339 GYIESGKAQKARLLCGGERVTD-GAFgkgaYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAA 417
Cdd:cd07101 312 AHVDDAVAKGATVLAGGRARPDlGPY----FYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600566 418 GVVTQDLARAHRAIHRLEAGICWIN-----TWGESPAemPVGGYKQSGVGRENGLTTLAHYTRIKSVQV 481
Cdd:cd07101 388 SVWTRDGARGRRIAARLRAGTVNVNegyaaAWASIDA--PMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
32-462 |
1.79e-111 |
|
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: 336.96 E-value: 1.79e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 32 GEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTG--KPLAEtrsVDIVTG 109
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGsiRPKAG---FEVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 110 ADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTA-LKL 188
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 189 AEIYTEAGVPDGVFNVLTGsGREVGQWLTEHPLIEKISFTGGTSTGKKVmASASSSSLKEVTMELGGKSPLIIFPDADLD 268
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKV-GEAAGRHLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 269 RAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKAQK 348
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 349 ARLLCGGERvtdgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAH 428
Cdd:cd07152 316 ARLEAGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAM 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 15600566 429 RAIHRLEAGICWIN--TWGESPaEMPVGGYKQSGVG 462
Cdd:cd07152 389 ALADRLRTGMLHINdqTVNDEP-HNPFGGMGASGNG 423
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
8-479 |
4.94e-111 |
|
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: 336.85 E-value: 4.94e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEaSSGATFETINPANGEVLAKVQRASREDVERAVQSA-VEGQKVWAAMTAMQRSRILRRAVDILRERNDEL 86
Cdd:cd07082 3 KYLINGEWKE-SSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAyDAGRGWWPTMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 87 AALETLDTGKPLAE-----TRSVDIV--TGADVLEYYAglvPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIA 159
Cdd:cd07082 82 ANLLMWEIGKTLKDalkevDRTIDYIrdTIEELKRLDG---DSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 160 LWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMA 239
Cdd:cd07082 159 VSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 240 SAsssSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQ 319
Cdd:cd07082 239 QH---PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 320 DENTNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTdgafgkGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYD 399
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG------GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 400 DEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGE-SPAEMPVGGYKQSGVGRENGLTTLAHYTRIKS 478
Cdd:cd07082 390 DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrGPDHFPFLGRKDSGIGTQGIGDALRSMTRRKG 469
|
.
gi 15600566 479 V 479
Cdd:cd07082 470 I 470
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-479 |
3.39e-106 |
|
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: 324.25 E-value: 3.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 28 NPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSVDIV 107
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 108 TGADVLEYYAGlvpaiEGEQIpLRETS------FVYTRR----EPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKP 177
Cdd:cd07098 82 VTCEKIRWTLK-----HGEKA-LRPESrpggllMFYKRArveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 178 SEVTPLTALKLAEIYTEA----GVPDGVFNVLTGSGrEVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSsLKEVTMEL 253
Cdd:cd07098 156 SEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 254 GGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPH 333
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 334 MESVLGYIESGKAQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEY 413
Cdd:cd07098 314 FDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEY 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600566 414 GLAAGVVTQDLARAHRAIHRLEAGICWINTWGES--PAEMPVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07098 394 GLGASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSV 461
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
72-482 |
1.35e-98 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 302.81 E-value: 1.35e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 72 LRRAVDILRERNDELAALETLDTGKPLAETRsVDIVTGADVLEYYAGLVPAIEGEQIP---LRETSFVYTRrePLGVVAG 148
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAE-VEVAFTADYIDYMAEWARRYEGEIIQsdrPGENILLFKR--ALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 149 IGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFT 228
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 229 GGTSTGKKVMASASSSSLKeVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLE 308
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITK-VCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 309 RVQRIRLGDPQDENT-NFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTdgafGKGAYVAPTVFTDCRDDMTIVREE 387
Cdd:PRK10090 237 AMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE----GKGYYYPPTLLLDVRQEMSIMHEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 388 IFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTwgESPAEMP--VGGYKQSGVGREN 465
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR--ENFEAMQgfHAGWRKSGIGGAD 390
|
410
....*....|....*..
gi 15600566 466 GLTTLAHYTRIKSVQVE 482
Cdd:PRK10090 391 GKHGLHEYLQTQVVYLQ 407
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
19-466 |
1.25e-93 |
|
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: 292.19 E-value: 1.25e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 19 SSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPL 98
Cdd:cd07130 9 GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 99 AETRSvDIVTGADVLEYYAGLVPAIEGEQIPL-RETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKP 177
Cdd:cd07130 89 PEGLG-EVQEMIDICDFAVGLSRQLYGLTIPSeRPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 178 SEVTPLTALK----LAEIYTEAGVPDGVFNVLTGsGREVGQWLTEHPLIEKISFTGGTSTGKKVmASASSSSLKEVTMEL 253
Cdd:cd07130 168 SPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQV-GQAVAARFGRSLLEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 254 GGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPH 333
Cdd:cd07130 246 GGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 334 MESVLGYIESGKAQKARLLCGGERVTDGAFgkgaYVAPTVFTdCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEY 413
Cdd:cd07130 326 VDNYLAAIEEAKSQGGTVLFGGKVIDGPGN----YVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQ 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600566 414 GLAAGVVTQDLARAHRAIHRL--EAGICWINTwGESPAEM--PVGGYKQSGVGRENG 466
Cdd:cd07130 401 GLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNI-GTSGAEIggAFGGEKETGGGRESG 456
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
26-464 |
1.75e-93 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 291.26 E-value: 1.75e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 26 TINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSvD 105
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA-E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 106 IVTGADVLEYYAGLVPAI---EGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTP 182
Cdd:PRK09406 84 ALKCAKGFRYYAEHAEALladEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 183 LTALKLAEIYTEAGVPDGVF-NVLTGSGrEVGQWLTEhPLIEKISFTGGTSTGKKVmASASSSSLKEVTMELGGKSPLII 261
Cdd:PRK09406 164 QTALYLADLFRRAGFPDGCFqTLLVGSG-AVEAILRD-PRVAAATLTGSEPAGRAV-AAIAGDEIKKTVLELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 262 FPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYI 341
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 342 ESGKAQKARLLCGGERVTdgafGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVT 421
Cdd:PRK09406 321 DDAVAAGATILCGGKRPD----GPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWT 396
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15600566 422 QDLARAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRE 464
Cdd:PRK09406 397 RDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRE 439
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
26-473 |
3.82e-93 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 290.61 E-value: 3.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 26 TINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSvD 105
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-E 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 106 IVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:PRK13968 90 VAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 186 LKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEhPLIEKISFTGGTSTGKKVMASASSSsLKEVTMELGGKSPLIIFPDA 265
Cdd:PRK13968 170 QLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDPFIVLNDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 266 DLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGK 345
Cdd:PRK13968 248 DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 346 AQKARLLCGGERVTdgafGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLA 425
Cdd:PRK13968 328 AEGARLLLGGEKIA----GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15600566 426 RAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGREnglttLAHY 473
Cdd:PRK13968 404 QARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRE-----LSHF 446
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
8-479 |
8.98e-93 |
|
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: 290.24 E-value: 8.98e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELA 87
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 88 ALETLDTGKPLAETRSvDIVTGADVLEYYAGLVPAIEGEQIPLRETSF-VYTRREPLGVVAGIGAWNYPVQIALWKSAPA 166
Cdd:TIGR01722 82 ELITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETSTQVATRVdVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQwLTEHPLIEKISFTGGTSTGKKVMASASSSSl 246
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDR-LLEHPDVKAVSFVGSTPIGRYIHTTGSAHG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 247 KEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTnGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFG 326
Cdd:TIGR01722 239 KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCM-AISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 327 PLVSFPHMESVLGYIESGKAQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIR 406
Cdd:TIGR01722 318 PLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 407 RANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTwgesPAEMPV-----GGYKQSGVGREN--GLTTLAHYTRIKSV 479
Cdd:TIGR01722 398 LINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV----PIPVPLpyfsfTGWKDSFFGDHHiyGKQGTHFYTRGKTV 473
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
45-463 |
1.48e-86 |
|
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: 272.61 E-value: 1.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 45 DVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRS-VDIVTG-ADV-LEYYAGLVP 121
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTeVAAMAGkIDIsIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 122 --AIEGEQIPLRetsfvyTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPD 199
Cdd:cd07095 81 erATPMAQGRAV------LRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 200 GVFNVLTGsGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANF 279
Cdd:cd07095 155 GVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 280 FSSGQVCTNGTRVFIHRSQQA-RFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERV 358
Cdd:cd07095 234 LTAGQRCTCARRLIVPDGAVGdAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 359 TDGafgkGAYVAPTVF--TDCRDdmtIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEA 436
Cdd:cd07095 314 VAG----TAFLSPGIIdvTDAAD---VPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRA 386
|
410 420
....*....|....*....|....*....
gi 15600566 437 GICWIN--TWGeSPAEMPVGGYKQSGVGR 463
Cdd:cd07095 387 GIVNWNrpTTG-ASSTAPFGGVGLSGNHR 414
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
9-460 |
9.33e-83 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 264.51 E-value: 9.33e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 9 LYIGGRYVeASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAA 88
Cdd:PRK09457 3 LWINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 89 LETLDTGKPLAETRS-VDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVytRREPLGVVAGIGAWNYPVQIALWKSAPAL 167
Cdd:PRK09457 82 VIARETGKPLWEAATeVTAMINKIAISIQAYHERTGEKRSEMADGAAVL--RHRPHGVVAVFGPYNFPGHLPNGHIVPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 168 AAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGsGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSSLK 247
Cdd:PRK09457 160 LAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 248 EVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQA-RFEAKVLERVQRIRLGDPQDENTNF- 325
Cdd:PRK09457 239 ILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGdAFLARLVAVAKRLTVGRWDAEPQPFm 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 326 GPLVSFPHMESVLgyiesgKAQKARLLCGGE------RVTDGAfgkgAYVAPTVFtdcrdDMTIVR----EEIFGPVMSI 395
Cdd:PRK09457 319 GAVISEQAAQGLV------AAQAQLLALGGKsllemtQLQAGT----GLLTPGII-----DVTGVAelpdEEYFGPLLQV 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600566 396 LVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGIcwIN----TWGESPAeMPVGGYKQSG 460
Cdd:PRK09457 384 VRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGI--VNwnkpLTGASSA-APFGGVGASG 449
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
8-483 |
2.05e-80 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 258.53 E-value: 2.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 8 KLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELA 87
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 88 ALETLDTGKPLAETRSvDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRRE--------PLGVVAGIGAWNYPVQIA 159
Cdd:PLN00412 97 ECLVKEIAKPAKDAVT-EVVRSGDLISYTAEEGVRILGEGKFLVSDSFPGNERNkycltskiPLGVVLAIPPFNYPVNLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 160 LWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGtSTGkkvMA 239
Cdd:PLN00412 176 VSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTG---IA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 240 SASSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQ 319
Cdd:PLN00412 252 ISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 320 DeNTNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERvtdgafgKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYD 399
Cdd:PLN00412 332 D-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRIN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 400 DEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTW-GESPAEMPVGGYKQSGVGRENGLTTLAHYTRIKS 478
Cdd:PLN00412 404 SVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKS 483
|
....*
gi 15600566 479 VQVEL 483
Cdd:PLN00412 484 TVINL 488
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
25-462 |
8.65e-80 |
|
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: 255.81 E-value: 8.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 25 ETINPANGEVLAKVQRASREDVERAVQSAVE---GQKVWAAmtAMQRSRILRRAVDILRERNDELAALETLDTGKPLAET 101
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHAlflDRNNWLP--AHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 102 RsVDIVTGADVLEYYAGLVPAIEGEQIP--LRETS---FVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFK 176
Cdd:cd07148 80 K-VEVTRAIDGVELAADELGQLGGREIPmgLTPASagrIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 177 PSEVTPLTALKLAEIYTEAGVPDGVFNVLTgSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSSlkEVTMELGGK 256
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT--RCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 257 SPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMES 336
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 337 VLGYIESGKAQKARLLCGGERVTDGAFgkgayvAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLA 416
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRLSDTTY------APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQ 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15600566 417 AGVVTQDLARAHRAIHRLEAGICWINT-------WgespaeMPVGGYKQSGVG 462
Cdd:cd07148 390 AAVFTKDLDVALKAVRRLDATAVMVNDhtafrvdW------MPFAGRRQSGYG 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
4-466 |
7.51e-79 |
|
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: 255.20 E-value: 7.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 4 FEEQKLYIGGRYVEassGATFETINPANGE-VLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRER 82
Cdd:cd07125 31 WEAIPIINGEETET---GEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEAN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 83 NDELAALETLDTGKPLAETrsVDIVTGA-DVLEYYAGLV------PAIEGEQIPLRETSFvytrrEPLGVVAGIGAWNYP 155
Cdd:cd07125 108 RGELIALAAAEAGKTLADA--DAEVREAiDFCRYYAAQArelfsdPELPGPTGELNGLEL-----HGRGVFVCISPWNFP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 156 VQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGK 235
Cdd:cd07125 181 LAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 236 ---KVMASASSSSLKeVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTnGTRV-FIHRSQQARFEAKVLERVQ 311
Cdd:cd07125 261 linRALAERDGPILP-LIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCS-ALRLlYLQEEIAERFIEMLKGAMA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 312 RIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKAQkARLLcggERVTDGAfGKGAYVAPTVFTDCRDDmtIVREEIFGP 391
Cdd:cd07125 339 SLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLI---APAPLDD-GNGYFVAPGIIEIVGIF--DLTTEVFGP 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600566 392 VMSILVYDDE--DEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN--TWGESPAEMPVGGYKQSGVGRENG 466
Cdd:cd07125 412 ILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrnITGAIVGRQPFGGWGLSGTGPKAG 490
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
3-466 |
1.08e-76 |
|
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: 249.03 E-value: 1.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 3 RFEEQKLYIGGRYVEASSGATfeTINPAN-GEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRE 81
Cdd:cd07083 15 FGRAYPLVIGGEWVDTKERMV--SVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 82 RNDELAALETLDTGKPLAETrSVDIVTGADVLEYYAGLVPAIEGEQ-----IPLRETSFVYtrrEPLGVVAGIGAWNYPV 156
Cdd:cd07083 93 RRRELIATLTYEVGKNWVEA-IDDVAEAIDFIRYYARAALRLRYPAvevvpYPGEDNESFY---VGLGAGVVISPWNFPV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 157 QIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKK 236
Cdd:cd07083 169 AIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 237 VMASASS-----SSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQ 311
Cdd:cd07083 249 IYEAAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 312 RIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKaQKARLLCGGERVTdgafGKGAYVAPTVFTDCRDDMTIVREEIFGP 391
Cdd:cd07083 329 RLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGK-NEGQLVLGGKRLE----GEGYFVAPTVVEEVPPKARIAQEEIFGP 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600566 392 VMSILVYDDED--EAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN--TWGESPAEMPVGGYKQSGVGRENG 466
Cdd:cd07083 404 VLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFKLSGTNAKTG 482
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
11-485 |
5.80e-75 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 247.35 E-value: 5.80e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 11 IGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALE 90
Cdd:PLN02419 118 IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 91 TLDTGKPLAETRSvDIVTGADVLEYYAGLVPAIEGEQIP-LRETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAA 169
Cdd:PLN02419 198 TTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTC 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 170 GNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQwLTEHPLIEKISFTGGTSTGKKVMASASSSSlKEV 249
Cdd:PLN02419 277 GNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIYARAAAKG-KRI 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 250 TMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTN-GTRVFIHRSQQarFEAKVLERVQRIRLGDPQDENTNFGPL 328
Cdd:PLN02419 355 QSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMAlSTVVFVGDAKS--WEDKLVERAKALKVTCGSEPDADLGPV 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 329 VSFPHMESVLGYIESGKAQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRA 408
Cdd:PLN02419 433 ISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISII 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 409 NDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTwgESPAEMP---VGGYKQSGVGREN--GLTTLAHYTRIKSVQVEL 483
Cdd:PLN02419 513 NKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPffsFTGNKASFAGDLNfyGKAGVDFFTQIKLVTQKQ 590
|
..
gi 15600566 484 GD 485
Cdd:PLN02419 591 KD 592
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
68-479 |
2.54e-71 |
|
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: 232.80 E-value: 2.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 68 RSRILRRAVDILRERNDELAALETLDTGKPLAETRSVDI-VTGADVLEYYAGLVPAIEGEQIPLRETSF---VYTRREPL 143
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIaVVLGEIDHALKHLKKWMKPRRVSVPLLLQpakAYVIPEPL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 144 GVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFnVLTGsGREVGQWLTEHPLiE 223
Cdd:cd07087 102 GVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVA-VVEG-GVEVATALLAEPF-D 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 224 KISFTGGTSTGKKVMASAsSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFE 303
Cdd:cd07087 179 HIFFTGSPAVGKIVMEAA-AKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 304 AKVLERVQRIrLGDPQDENTNFGPLVSFPHMESVLGYIESGKaqkarLLCGGErvTDGAfgkGAYVAPTVFTDCRDDMTI 383
Cdd:cd07087 258 EELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDGK-----VVIGGQ--VDKE---ERYIAPTILDDVSPDSPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 384 VREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN------TwgeSPaEMPVGGYK 457
Cdd:cd07087 327 MQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvllhaA---IP-NLPFGGVG 402
|
410 420
....*....|....*....|..
gi 15600566 458 QSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07087 403 NSGMGAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
57-466 |
3.49e-71 |
|
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: 232.50 E-value: 3.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 57 QKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSVDIVTgadVLEYYAGLVPAIEGEQIPLRETSFV 136
Cdd:cd07134 11 ALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILP---VLSEINHAIKHLKKWMKPKRVRTPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 137 -------YTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFnVLTGsG 209
Cdd:cd07134 88 llfgtksKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEG-D 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 210 REVGQWLTEHPLiEKISFTGGTSTGKKVMASASSSsLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNG 289
Cdd:cd07134 166 AEVAQALLELPF-DHIFFTGSPAVGKIVMAAAAKH-LASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 290 TRVFIHRSQQARFEAKVLERVQRIRLGDPQD-ENTNFGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTDGAfgkgaY 368
Cdd:cd07134 244 DYVFVHESVKDAFVEHLKAEIEKFYGKDAARkASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR-----Y 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 369 VAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESP 448
Cdd:cd07134 319 IAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHF 398
|
410 420
....*....|....*....|
gi 15600566 449 AE--MPVGGYKQSGVGRENG 466
Cdd:cd07134 399 LNpnLPFGGVNNSGIGSYHG 418
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
64-479 |
5.40e-66 |
|
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: 218.89 E-value: 5.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 64 TAMQRSRILRRAVDILRERNDELA-ALETLDTGKPLAETRSVDIVTGADVLEYYAGLV-----PAIEGEQIPLRETSfVY 137
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAeAISADFGHRSRHETLLAEILPSIAGIKHARKHLkkwmkPSRRHVGLLFLPAK-AE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 138 TRREPLGVVAGIGAWNYPVQIALWKSAPALAAGN-AMIfKPSEVTPLTALKLAEIYTEAGVPDGVfNVLTGsGREVGQWL 216
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNrVMI-KPSEFTPRTSALLAELLAEYFDEDEV-AVVTG-GADVAAAF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 217 TEHP---LIekisFTGGTSTGKKVMASASSSsLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVF 293
Cdd:cd07133 174 SSLPfdhLL----FTGSTAVGRHVMRAAAEN-LTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 294 IHRSQQARFEAKVLERVQRiRLGDPQDeNTNFGPLVSFPHMESVLGYIESGKAQKARLL-CGGERVTDGAFGKgayVAPT 372
Cdd:cd07133 249 VPEDKLEEFVAAAKAAVAK-MYPTLAD-NPDYTSIINERHYARLQGLLEDARAKGARVIeLNPAGEDFAATRK---LPPT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 373 VFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWG--ESPAE 450
Cdd:cd07133 324 LVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLlhVAQDD 403
|
410 420 430
....*....|....*....|....*....|..
gi 15600566 451 MPVGGYKQSGVGR---ENGLTTLAHYtriKSV 479
Cdd:cd07133 404 LPFGGVGASGMGAyhgKEGFLTFSHA---KPV 432
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
79-466 |
9.52e-63 |
|
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: 210.54 E-value: 9.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 79 LRERNDELAALETLDTGKPLAETRSVDIVTG-ADVLEYYAGLVPAIEGEQIPLRETSF----VYTRREPLGVVAGIGAWN 153
Cdd:cd07135 40 VKDNEEAIVEALKKDLGRPPFETLLTEVSGVkNDILHMLKNLKKWAKDEKVKDGPLAFmfgkPRIRKEPLGVVLIIGPWN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 154 YPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAgVPDGVFNVLTGSGREVGQWLTEHplIEKISFTGGTST 233
Cdd:cd07135 120 YPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQK--FDKIFYTGSGRV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 234 GKKVmASASSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFeAKVLERVQRI 313
Cdd:cd07135 197 GRII-AEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEF-VEELKKVLDE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 314 RLGDPQDENTNFGPLVSFPHMESVLGYIESGKaqkarllcgGERVTDGAFGKGA-YVAPTVFTDCRDDMTIVREEIFGPV 392
Cdd:cd07135 275 FYPGGANASPDYTRIVNPRHFNRLKSLLDTTK---------GKVVIGGEMDEATrFIPPTIVSDVSWDDSLMSEELFGPV 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600566 393 MSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGE--SPAEMPVGGYKQSGVGRENG 466
Cdd:cd07135 346 LPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPFGGVGDSGYGAYHG 421
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
137-479 |
4.70e-62 |
|
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: 208.90 E-value: 4.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 137 YTRREPLGVVAGIGAWNYPVQIALwksAP---ALAAGNAMIFKPSEVTPLTALKLAEIYTEAgVPDGVFNVLTGsGREVG 213
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQLAL---APligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 214 QWLTEHPLiEKISFTGGTSTGKKVMASASSSsLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVF 293
Cdd:cd07136 170 QELLDQKF-DYIFFTGSVRVGKIVMEAAAKH-LTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 294 IHRSQQARFEaKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKaqkarLLCGGErvTDGafgKGAYVAPTV 373
Cdd:cd07136 248 VHESVKEKFI-KELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGK-----IVFGGN--TDR---ETLYIEPTI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 374 FTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLE-AGICwIN-------Twg 445
Cdd:cd07136 317 LDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSfGGGC-INdtimhlaN-- 393
|
330 340 350
....*....|....*....|....*....|....*..
gi 15600566 446 espAEMPVGGYKQSGVGR---ENGLTTLAHYtriKSV 479
Cdd:cd07136 394 ---PYLPFGGVGNSGMGSyhgKYSFDTFSHK---KSI 424
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
10-485 |
2.18e-59 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 203.53 E-value: 2.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 10 YIGGRYveASSGATFETINPANGEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAAL 89
Cdd:PLN02315 24 YVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 90 ETLDTGKPLAETRSvDIVTGADVLEYYAGLVPAIEGEQIPL-RETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALA 168
Cdd:PLN02315 102 VSLEMGKILAEGIG-EVQEIIDMCDFAVGLSRQLNGSIIPSeRPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 169 AGNAMIFKPSEVTPLTALKL----AEIYTEAGVPDGVFNVLTGsGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSS 244
Cdd:PLN02315 181 CGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 245 SLKEVtMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTN 324
Cdd:PLN02315 260 FGKCL-LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 325 FGPLVSFPHMESVLGYIESGKAQKARLLCGGERVTdgafGKGAYVAPTVfTDCRDDMTIVREEIFGPVMSILVYDDEDEA 404
Cdd:PLN02315 339 LGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE----SEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 405 IRRANDTEYGLAAGVVTQDLARAHRAI--HRLEAGICWIN--TWGespAEM--PVGGYKQSGVGRENGLTTLAHYTRIKS 478
Cdd:PLN02315 414 IEINNSVPQGLSSSIFTRNPETIFKWIgpLGSDCGIVNVNipTNG---AEIggAFGGEKATGGGREAGSDSWKQYMRRST 490
|
....*..
gi 15600566 479 VQVELGD 485
Cdd:PLN02315 491 CTINYGN 497
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
9-460 |
4.34e-57 |
|
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: 197.81 E-value: 4.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 9 LYIGGRyvEASSGATFETINPAN-GEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILR-ERNDEL 86
Cdd:cd07123 35 LVIGGK--EVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 87 AALETLDTGKPL--AETRSvdIVTGADVLEYYAGLVPAIEGEQiPLRETSFVYTRRE--PL-GVVAGIGAWNYpVQIAL- 160
Cdd:cd07123 113 NAATMLGQGKNVwqAEIDA--ACELIDFLRFNVKYAEELYAQQ-PLSSPAGVWNRLEyrPLeGFVYAVSPFNF-TAIGGn 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 161 WKSAPALAaGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMAS 240
Cdd:cd07123 189 LAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 241 ASSS-----SLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRL 315
Cdd:cd07123 268 IGENldryrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKM 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 316 GDPQDENTNFGPLVSFPHMESVLGYIESGKAQK-ARLLCGGErvTDGAfgKGAYVAPTVF--TDCRDdmTIVREEIFGPV 392
Cdd:cd07123 348 GDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPeAEIIAGGK--CDDS--VGYFVEPTVIetTDPKH--KLMTEEIFGPV 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600566 393 MSILVYDDED--EAIRRANDT-EYGLAAGVVTQD---LARAHRAiHRLEAGICWIN--TWGESPAEMPVGGYKQSG 460
Cdd:cd07123 422 LTVYVYPDSDfeETLELVDTTsPYALTGAIFAQDrkaIREATDA-LRNAAGNFYINdkPTGAVVGQQPFGGARASG 496
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
67-479 |
2.85e-56 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 194.86 E-value: 2.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 67 QRSRILRRAVDILRERNDELAALETLDTGKPLAETRSVDI-VTGADVLEYYAGLVPAIEGEQIPlreTSFV------YTR 139
Cdd:PTZ00381 30 FRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVlLTVAEIEHLLKHLDEYLKPEKVD---TVGVfgpgksYII 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 140 REPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAgVPDGVFNVLTGsGREVGQWLTEH 219
Cdd:PTZ00381 107 PEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLKE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 220 PLiEKISFTGGTSTGKKVMASAsSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQ 299
Cdd:PTZ00381 185 PF-DHIFFTGSPRVGKLVMQAA-AENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 300 ARFEAKVleRVQRIR-LGDPQDENTNFGPLVSFPHMESVLGYIESGKAQkarLLCGGErvtdgaFGKGA-YVAPTVFTDC 377
Cdd:PTZ00381 263 DKFIEAL--KEAIKEfFGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGK---VVYGGE------VDIENkYVAPTIIVNP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 378 RDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINtwgES-----PAEMP 452
Cdd:PTZ00381 332 DLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN---DCvfhllNPNLP 408
|
410 420
....*....|....*....|....*..
gi 15600566 453 VGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:PTZ00381 409 FGGVGNSGMGAYHGKYGFDTFSHPKPV 435
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
17-442 |
1.72e-53 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 194.31 E-value: 1.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 17 EASSGATFETINPAN-GEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTG 95
Cdd:PRK11905 562 GDVDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 96 KPLAEtrSVDIVTGA-DVLEYYAglvpaiegEQIplrETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMI 174
Cdd:PRK11905 642 KTLAN--AIAEVREAvDFLRYYA--------AQA---RRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVL 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 175 FKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSSLKEVTM--E 252
Cdd:PRK11905 709 AKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaE 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 253 LGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTnGTRV-FIhrsqQARFEAKVLER----VQRIRLGDPQDENTNFGP 327
Cdd:PRK11905 789 TGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCS-ALRVlCL----QEDVADRVLTMlkgaMDELRIGDPWRLSTDVGP 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 328 LVSFPHMESVLGYIESGKAQKARLlcggERVT-DGAFGKGAYVAPTVFTdcRDDMTIVREEIFGPVMSILVY--DDEDEA 404
Cdd:PRK11905 864 VIDAEAQANIEAHIEAMRAAGRLV----HQLPlPAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFkaDELDRV 937
|
410 420 430
....*....|....*....|....*....|....*...
gi 15600566 405 IRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN 442
Cdd:PRK11905 938 IDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN 975
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1-442 |
4.96e-53 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 192.72 E-value: 4.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 1 MARFEEQKLYIGGryVEASSGATFETINPANGE-VLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDIL 79
Cdd:PRK11904 543 IAAFLEKQWQAGP--IINGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLL 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 80 RERNDELAALETLDTGKPLAEtrSVDIVTGA-DVLEYYAGLVPAIEGEQIPLR----ETSFVytRREPLGVVAGIGAWNY 154
Cdd:PRK11904 621 EANRAELIALCVREAGKTLQD--AIAEVREAvDFCRYYAAQARRLFGAPEKLPgptgESNEL--RLHGRGVFVCISPWNF 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 155 PVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTg 234
Cdd:PRK11904 697 PLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTET- 775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 235 kkvmASASSSSLKE-----VTM--ELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTnGTRV-FIHRSqqarfeakV 306
Cdd:PRK11904 776 ----ARIINRTLAArdgpiVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCS-ALRVlFVQED--------I 842
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 307 LERV--------QRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKaQKARLLCGGERvtDGAFGKGAYVAPTVFTdcR 378
Cdd:PRK11904 843 ADRViemlkgamAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMK-REARLLAQLPL--PAGTENGHFVAPTAFE--I 917
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600566 379 DDMTIVREEIFGPVMSILVY--DDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN 442
Cdd:PRK11904 918 DSISQLEREVFGPILHVIRYkaSDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
11-466 |
5.60e-52 |
|
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: 183.57 E-value: 5.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 11 IGGRYVeaSSGATFETINPAN-GEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAAL 89
Cdd:TIGR01238 42 IGHSYK--ADGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 90 ETLDTGKPLAEtrSVDIVTGA-DVLEYYAGLVPAIEGEQiplretsfvytRREPLGVVAGIGAWNYPVQIALWKSAPALA 168
Cdd:TIGR01238 120 CVREAGKTIHN--AIAEVREAvDFCRYYAKQVRDVLGEF-----------SVESRGVFVCISPWNFPLAIFTGQISAALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 169 AGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSSLKE 248
Cdd:TIGR01238 187 AGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 249 VTM--ELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRVFIHRSQQARFEAKVLERVQRIRLGDPQDENTNFG 326
Cdd:TIGR01238 267 VPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 327 PLVSFPHMESVLGYIESGKaQKARLLCGGERVTDGAFGKGAYVAPTVFTdcRDDMTIVREEIFGPVMSILVY--DDEDEA 404
Cdd:TIGR01238 347 PVIDAEAKQNLLAHIEHMS-QTQKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYkaRELDQI 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600566 405 IRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN--TWGESPAEMPVGGYKQSGVGRENG 466
Cdd:TIGR01238 424 VDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
136-466 |
2.11e-51 |
|
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: 180.50 E-value: 2.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 136 VYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEI---YTEagvPDgVFNVLTGsGREV 212
Cdd:cd07132 94 VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELipkYLD---KE-CYPVVLG-GVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 213 GQWLTEHPLiEKISFTGGTSTGKKVMAsASSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCTNGTRV 292
Cdd:cd07132 169 TTELLKQRF-DYIFYTGSTSVGKIVMQ-AAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 293 FIHRSQQARFEAKVLERVQRIRLGDPQdENTNFGPLVSFPHMESVLGYIESGKaqkarLLCGGErvTDgafGKGAYVAPT 372
Cdd:cd07132 247 LCTPEVQEKFVEALKKTLKEFYGEDPK-ESPDYGRIINDRHFQRLKKLLSGGK-----VAIGGQ--TD---EKERYIAPT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 373 VFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN--TWGESPAE 450
Cdd:cd07132 316 VLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdtIMHYTLDS 395
|
330
....*....|....*.
gi 15600566 451 MPVGGYKQSGVGRENG 466
Cdd:cd07132 396 LPFGGVGNSGMGAYHG 411
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
17-442 |
8.41e-51 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 186.30 E-value: 8.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 17 EASSGATFETINPANG-EVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTG 95
Cdd:COG4230 565 EAASGEARPVRNPADHsDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAG 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 96 KPL----AETR-SVDIvtgadvLEYYAGLVPAIEGEQIPLRetsfvytrrePLGVVAGIGAWNYPVQIALWKSAPALAAG 170
Cdd:COG4230 645 KTLpdaiAEVReAVDF------CRYYAAQARRLFAAPTVLR----------GRGVFVCISPWNFPLAIFTGQVAAALAAG 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 171 NAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGK---KVMASASSSSLK 247
Cdd:COG4230 709 NTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARlinRTLAARDGPIVP 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 248 EVTmELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVCtNGTRV-FIhrsqQARFEAKVLERV----QRIRLGDPQDEN 322
Cdd:COG4230 789 LIA-ETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRC-SALRVlCV----QEDIADRVLEMLkgamAELRVGDPADLS 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 323 TNFGPLVSFPHMESVLGYIESGKAqKARLLCGGERVTDGAfgKGAYVAPTVFTdcRDDMTIVREEIFGPVMSILVY--DD 400
Cdd:COG4230 863 TDVGPVIDAEARANLEAHIERMRA-EGRLVHQLPLPEECA--NGTFVAPTLIE--IDSISDLEREVFGPVLHVVRYkaDE 937
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15600566 401 EDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWIN 442
Cdd:COG4230 938 LDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
10-480 |
1.09e-46 |
|
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: 169.37 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 10 YIGGRYVeASSGATFETINPANGEVLAkvqRASRE--DVERAVQSAVE-GQKVWAAMTAMQRSRILRRAVDILRERNDEL 86
Cdd:cd07128 4 YVAGQWH-AGTGDGRTLHDAVTGEVVA---RVSSEglDFAAAVAYAREkGGPALRALTFHERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 87 AALETLDTGkplaeTRS---VDIVTGADVLEYYAGLV----PA----IEGEQIPL-RETSF----VYTRREplGVVAGIG 150
Cdd:cd07128 80 YALSAATGA-----TRRdswIDIDGGIGTLFAYASLGrrelPNahflVEGDVEPLsKDGTFvgqhILTPRR--GVAVHIN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 151 AWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGV-PDGVFNVLTGSGREVGQWLTEHPLIekiSFTG 229
Cdd:cd07128 153 AFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHLGEQDVV---AFTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 230 GTSTGKKVMASAS--SSSLKeVTMELGGKSPLIIFPDA-------DL---DRAADIAVMAnffssGQVCTNGTRVFIHRS 297
Cdd:cd07128 230 SAATAAKLRAHPNivARSIR-FNAEADSLNAAILGPDAtpgtpefDLfvkEVAREMTVKA-----GQKCTAIRRAFVPEA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 298 QQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKAQKARLLCGGER--VTDGAFGKGAYVAPTVFT 375
Cdd:cd07128 304 RVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRfeVVGADAEKGAFFPPTLLL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 376 dCRDDM--TIVRE-EIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQD----------LARAHRAIHRLEAGICWIN 442
Cdd:cd07128 384 -CDDPDaaTAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDpafarelvlgAAPYHGRLLVLNRDSAKES 462
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15600566 443 TWGESPaeMPV---GGYKQSGVGRE-NGLTTLAHYTRIKSVQ 480
Cdd:cd07128 463 TGHGSP--LPQlvhGGPGRAGGGEElGGLRGVKHYMQRTAVQ 502
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
46-480 |
1.78e-45 |
|
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: 164.72 E-value: 1.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 46 VERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPlaETRSVDIVTGADVLEYYAGLVPAIEG 125
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG--WMFAENICGDQVQLRARAFVIYSYRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 126 EQIPLRETSF-----VYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAG-VPD 199
Cdd:cd07084 79 PHEPGNHLGQglkqqSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 200 GVFNVLTGSGReVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSslkEVTMELGGKSPLIIFPDAD-LDRAADIAVMAN 278
Cdd:cd07084 159 EDVTLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA---RIYLELAGFNWKVLGPDAQaVDYVAWQCVQDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 279 FFSSGQVCTNGTRVFIHRSQQARfeaKVLERVQRIrLGDPQDENTNFGPLVSFphmeSVLGYIESGKAQKARLLCGG--- 355
Cdd:cd07084 235 TACSGQKCTAQSMLFVPENWSKT---PLVEKLKAL-LARRKLEDLLLGPVQTF----TTLAMIAHMENLLGSVLLFSgke 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 356 ERVTDGAFGKGAYVAPTVFTDCRDDMT---IVREEIFGPVMSILVYDDEDEA--IRRANDTEYGLAAGVVTQDLARAHRA 430
Cdd:cd07084 307 LKNHSIPSIYGACVASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQEL 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15600566 431 IHRLE-AGICWINTWGES---PAEMPVGGYKQSGVGRENGLTTLAH-YTRIKSVQ 480
Cdd:cd07084 387 IGNLWvAGRTYAILRGRTgvaPNQNHGGGPAADPRGAGIGGPEAIKlVWRCHAEQ 441
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
17-421 |
1.71e-40 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 155.90 E-value: 1.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 17 EASSGATFETINPAN-GEVLAKVQRASREDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTG 95
Cdd:PRK11809 654 PVAAGEMSPVINPADpRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAG 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 96 KPL----AETRSvdivtGADVLEYYAGLVpaiegeqiplrETSFVYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGN 171
Cdd:PRK11809 734 KTFsnaiAEVRE-----AVDFLRYYAGQV-----------RDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGN 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 172 AMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGK---KVMASASSSSLKE 248
Cdd:PRK11809 798 SVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARllqRNLAGRLDPQGRP 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 249 VTM--ELGGKSPLIIfpdadlDRAA-------DIAVMAnFFSSGQVCTnGTRVFIhrsqqarFEAKVLERV--------Q 311
Cdd:PRK11809 878 IPLiaETGGQNAMIV------DSSAlteqvvaDVLASA-FDSAGQRCS-ALRVLC-------LQDDVADRTlkmlrgamA 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 312 RIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKAqKARLLCGGERVTDGAFGKGAYVAPTVFT-DCRDDMTivrEEIFG 390
Cdd:PRK11809 943 ECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRA-KGRPVFQAARENSEDWQSGTFVPPTLIElDSFDELK---REVFG 1018
|
410 420 430
....*....|....*....|....*....|...
gi 15600566 391 PVMSILVY--DDEDEAIRRANDTEYGLAAGVVT 421
Cdd:PRK11809 1019 PVLHVVRYnrNQLDELIEQINASGYGLTLGVHT 1051
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
10-480 |
3.57e-38 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 146.00 E-value: 3.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 10 YIGGRYVEASsGATFETINPANGEVLAKVQrASREDVERAVQSAVE-GQKVWAAMTAMQRSRILRRAVDILRERNDELAA 88
Cdd:PRK11903 8 YVAGRWQAGS-GAGTPLFDPVTGEELVRVS-ATGLDLAAAFAFAREqGGAALRALTYAQRAALLAAIVKVLQANRDAYYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 89 LETLDTGKPLAETrSVDIVTGADVLEYYAGLVPAIeGEQIPLRETSFVYTRREPL-----------GVVAGIGAWNYPVQ 157
Cdd:PRK11903 86 IATANSGTTRNDS-AVDIDGGIFTLGYYAKLGAAL-GDARLLRDGEAVQLGKDPAfqgqhvlvptrGVALFINAFNFPAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 158 iALW-KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGV-PDGVFNVLTGSGREVGQWLTEhplIEKISFTGGTSTGK 235
Cdd:PRK11903 164 -GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQP---FDVVSFTGSAETAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 236 KVMASAS--SSSLKeVTMELGGKSPLIIFPDADLDRAA----------DIAVmanffSSGQVCTNGTRVFIHRSQQARFE 303
Cdd:PRK11903 240 VLRSHPAvvQRSVR-VNVEADSLNSALLGPDAAPGSEAfdlfvkevvrEMTV-----KSGQKCTAIRRIFVPEALYDAVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 304 AKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKAQkARLLCGGERV--TDGAFGKGAYVAPTVF-TDCRDD 380
Cdd:PRK11903 314 EALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ-AEVLFDGGGFalVDADPAVAACVGPTLLgASDPDA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 381 MTIVRE-EIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQD----------LARAHRAIHRLEAGICWINTwGESPA 449
Cdd:PRK11903 393 ATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDaaflaaaaleLADSHGRVHVISPDVAALHT-GHGNV 471
|
490 500 510
....*....|....*....|....*....|....*
gi 15600566 450 eMPV---GGYKQSGVGRE-NGLTTLAHYTRIKSVQ 480
Cdd:PRK11903 472 -MPQslhGGPGRAGGGEElGGLRALAFYHRRSAVQ 505
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
141-479 |
2.49e-35 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 136.39 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 141 EPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAgVPDGVFNVLTGsGREVGQWLTEHP 220
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 221 LiEKISFTGGTSTGKKVMAsASSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFS-SGQVCTNGTRVFIhrsqQ 299
Cdd:cd07137 178 W-DKIFFTGSPRVGRIIMA-AAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLV----E 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 300 ARFEAKVLERVQRIRL---GDPQDENTNFGPLVSFPHMESVLGYIESGKAQkARLLCGGERVTDgafgkGAYVAPTVFTD 376
Cdd:cd07137 252 ESFAPTLIDALKNTLEkffGENPKESKDLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGGERDEK-----NLYIEPTILLD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 377 CRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPA--EMPVG 454
Cdd:cd07137 326 PPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAidTLPFG 405
|
330 340
....*....|....*....|....*
gi 15600566 455 GYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:cd07137 406 GVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
46-436 |
6.95e-35 |
|
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: 135.75 E-value: 6.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 46 VERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGkpLAETRsvdiVTG------------ADVL 113
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEAR----LQGelgrttgqlrlfADLV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 114 EYYAGLVPAIEgEQIPLRETSF---VYTRREPLGVVAGIGAWNYPV--QIALWKSAPALAAGNAMIFKPSEVTPLTALKL 188
Cdd:cd07129 75 REGSWLDARID-PADPDRQPLPrpdLRRMLVPLGPVAVFGASNFPLafSVAGGDTASALAAGCPVVVKAHPAHPGTSELV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 189 AEIYTEA----GVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSSL-KEVTMELGGKSPLIIFP 263
Cdd:cd07129 154 ARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSVNPVFILP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 264 DADLDRAADIAvmANFFSS-----GQVCTNGTRVFIHRSQQA-RFEAKVLERVQRIrlgDPQdentnfgPLVSFPHMESV 337
Cdd:cd07129 234 GALAERGEAIA--QGFVGSltlgaGQFCTNPGLVLVPAGPAGdAFIAALAEALAAA---PAQ-------TMLTPGIAEAY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 338 LGYIESGKAQKARLLCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIvREEIFGPVMSILVYDDEDEAIRRANDTEYGLAA 417
Cdd:cd07129 302 RQGVEALAAAPGVRVLAGGAAAEGGNQAAPTLFKVDAAAFLADPAL-QEEVFGPASLVVRYDDAAELLAVAEALEGQLTA 380
|
410 420
....*....|....*....|.
gi 15600566 418 GVV--TQDLARAHRAIHRLEA 436
Cdd:cd07129 381 TIHgeEDDLALARELLPVLER 401
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
141-479 |
5.87e-28 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 116.36 E-value: 5.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 141 EPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVfNVLTGsGREVGQWLTEHP 220
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV-KVIEG-GPAVGEQLLQHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 221 LiEKISFTGGTSTGKKVMASAsSSSLKEVTMELGGKSPLIIfpdADLDRAADIAVMANF-----FSS--GQVCTNGTRVF 293
Cdd:PLN02203 185 W-DKIFFTGSPRVGRIIMTAA-AKHLTPVALELGGKCPCIV---DSLSSSRDTKVAVNRivggkWGScaGQACIAIDYVL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 294 IHRsQQARFEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKAQkARLLCGGervtdGAFGKGAYVAPTV 373
Cdd:PLN02203 260 VEE-RFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGG-----SIDEKKLFIEPTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 374 FTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPA--EM 451
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdSL 412
|
330 340
....*....|....*....|....*...
gi 15600566 452 PVGGYKQSGVGRENGLTTLAHYTRIKSV 479
Cdd:PLN02203 413 PFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
141-479 |
1.63e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 112.06 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 141 EPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYtEAGVPDGVFNVLTGSGREVGQWLTEHp 220
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQK- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 221 lIEKISFTGGTSTGKKVMAsASSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANF-FSSGQVCTNGTRVFIHRSQQ 299
Cdd:PLN02174 189 -WDKIFYTGSSKIGRVIMA-AAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 300 ARFEAKVLERVQRIRLGDPQdENTNFGPLVSFPHMESVLGYIESgKAQKARLLCGGERVTDgafgkGAYVAPTVFTDCRD 379
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPM-ESKDMSRIVNSTHFDRLSKLLDE-KEVSDKIVYGGEKDRE-----NLKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 380 DMTIVREEIFGPVMSILVYDDEDEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPA--EMPVGGYK 457
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLPFGGVG 419
|
330 340
....*....|....*....|..
gi 15600566 458 QSGVGRENGLTTLAHYTRIKSV 479
Cdd:PLN02174 420 ESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
49-297 |
9.00e-16 |
|
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: 79.23 E-value: 9.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 49 AVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSVDIVTGAdvlEYYAGLVPAIEGEQI 128
Cdd:cd07081 4 AVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAA---EYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 129 PLRETSF-VYTRREPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKP----SEVTPLTALKLAEIYTEAGVPDGVFN 203
Cdd:cd07081 81 LTGDENGgTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 204 VLTGSGREVGQWLTEHPLIEKISFTGGTStgkkvMASASSSSLKEVTMELGGKSPLIIFPDADLDRAADIAVMANFFSSG 283
Cdd:cd07081 161 WIDNPSIELAQRLMKFPGIGLLLATGGPA-----VVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNG 235
|
250
....*....|....
gi 15600566 284 QVCTNGTRVFIHRS 297
Cdd:cd07081 236 VICASEQSVIVVDS 249
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
51-297 |
3.08e-14 |
|
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: 74.18 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 51 QSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKP-------------LAETRSVDIVTGAdvlEYYA 117
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYirslianwiammgCSESKLYKNIDTE---RGIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 118 GLVPAIEGEQIPlrETSFVYTRREPLGVVAGIGAWNYPVqIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEA-- 195
Cdd:cd07077 78 ASVGHIQDVLLP--DNGETYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAda 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 196 --GVPDGVFNVLTGSGREVgQWLTEHPLIEKISFTGGTSTgkkVMASASSSSLKEVTMELGGKSPLIIFPDADLDRAADI 273
Cdd:cd07077 155 ahGPKILVLYVPHPSDELA-EELLSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGS 230
|
250 260
....*....|....*....|....
gi 15600566 274 AVMANFFsSGQVCTNGTRVFIHRS 297
Cdd:cd07077 231 VHDSKFF-DQNACASEQNLYVVDD 253
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
142-438 |
3.36e-13 |
|
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: 71.74 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 142 PLGVVAGIGAWNYPVqialWKSAPA----LAAGNAMIFKPSevtPLTALKLA-------EIYTEAGV-PDGVFNVLTGSG 209
Cdd:cd07127 193 PRGVALVIGCSTFPT----WNGYPGlfasLATGNPVIVKPH---PAAILPLAitvqvarEVLAEAGFdPNLVTLAADTPE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 210 REVGQWLTEHPLIEKISFTGGTSTGKKVMASASSsslKEVTMELGGKSPLIIFPDADLdraadIAVMANF-FS----SGQ 284
Cdd:cd07127 266 EPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ---AQVYTEKAGVNTVVVDSTDDL-----KAMLRNLaFSlslySGQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 285 VCTNGTRVFIHR----SQQAR-----FEAKVLERVQRIrLGDPQDENTNFGPLVSfphmESVLGYIESGkAQKARLLCGG 355
Cdd:cd07127 338 MCTTPQNIYVPRdgiqTDDGRksfdeVAADLAAAIDGL-LADPARAAALLGAIQS----PDTLARIAEA-RQLGEVLLAS 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 356 ERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDEDEAIRRANDT--EYG-LAAGVVTQDLARAHRAIH 432
Cdd:cd07127 412 EAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESvrEHGaMTVGVYSTDPEVVERVQE 491
|
....*..
gi 15600566 433 -RLEAGI 438
Cdd:cd07127 492 aALDAGV 498
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
46-445 |
1.48e-12 |
|
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: 69.44 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 46 VERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAETRSVDIVTGAD-VLEYYAGL--VPA 122
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFASEyVYNDIKDMktVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 123 I-EGEQIPLRETSfvytrrEPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEA----GV 197
Cdd:cd07122 81 IeEDEEKGIVEIA------EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 198 PDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTStgkkvMASASSSSLKEVtmeLG---GKSPLIIFPDADLDRAADIA 274
Cdd:cd07122 155 PEGLIQWIEEPSIELTQELMKHPDVDLILATGGPG-----MVKAAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 275 VMANFFSSGQVCTngtrvfihrSQQAR-FEAKVLERVQRirlgdpqdentnfgplvsfpHMESVLGYI----ESGKAQKA 349
Cdd:cd07122 227 ILSKTFDNGTICA---------SEQSViVDDEIYDEVRA--------------------ELKRRGAYFlneeEKEKLEKA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 350 rLLCGGERVTDGAFGKGAYV----------APTVFTDCRDDMTIVRE----EIFGPVMSILVYDDEDEAIRRAND-TEYG 414
Cdd:cd07122 278 -LFDDGGTLNPDIVGKSAQKiaelagievpEDTKVLVAEETGVGPEEplsrEKLSPVLAFYRAEDFEEALEKARElLEYG 356
|
410 420 430
....*....|....*....|....*....|....
gi 15600566 415 LA---AGVVTQDLARAHRAIHRLEAGICWINTWG 445
Cdd:cd07122 357 GAghtAVIHSNDEEVIEEFALRMPVSRILVNTPS 390
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
140-423 |
9.75e-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: 67.14 E-value: 9.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 140 REPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWLTE- 218
Cdd:cd07126 140 RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEa 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 219 HPliEKISFTGGTSTGKKVmasasSSSLK-EVTMELGGKSPLIIFPD-ADLDRAADIAVMANFFSSGQVCTNGTRVFIHR 296
Cdd:cd07126 220 NP--RMTLFTGSSKVAERL-----ALELHgKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 297 S-QQARFEAKVLERVQRIRLgdpqdENTNFGPLVSFPHmESVLGYIESGKA-QKARLLCGGERVTD-------GAFGKGA 367
Cdd:cd07126 293 NwVQAGILDKLKALAEQRKL-----EDLTIGPVLTWTT-ERILDHVDKLLAiPGAKVLFGGKPLTNhsipsiyGAYEPTA 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600566 368 YVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDED-----EAIRRandTEYGLAAGVVTQD 423
Cdd:cd07126 367 VFVPLEEIAIEENFELVTTEVFGPFQVVTEYKDEQlplvlEALER---MHAHLTAAVVSND 424
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
44-279 |
1.32e-08 |
|
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: 56.86 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 44 EDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTG------KPLAETRSVDIVTGADVLEyya 117
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGmgrvedKIAKNHLAAEKTPGTEDLT--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 118 glVPAIEGEQ-IPLRETSfvytrrePLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKP----SEVTPLTALKLAEIY 192
Cdd:cd07121 81 --TTAWSGDNgLTLVEYA-------PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgaKKVSAYAVELINKAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 193 TEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASAsssslKEVTMELGGKSPLIIFPDADLDRAA- 271
Cdd:cd07121 152 AEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSG-----KKAIGAGAGNPPVVVDETADIEKAAr 226
|
....*...
gi 15600566 272 DIAVMANF 279
Cdd:cd07121 227 DIVQGASF 234
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
44-279 |
4.37e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 55.29 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 44 EDVERAVQSAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTG------KPLAETRSVDIVTGADVLEYYA 117
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedKIAKNVAAAEKTPGVEDLTTEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 118 -----GLVpaiegeqipLRETSfvytrrePLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKP----SEVTPLTALKL 188
Cdd:PRK15398 116 ltgdnGLT---------LIEYA-------PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgaKKVSLRAIELL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 189 AEIYTEAGVPDGVFNVLTGSGREVGQWLTEHPLIEKISFTGGT-------STGKKVMASASssslkevtmelgGKSPLII 261
Cdd:PRK15398 180 NEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPavvkaamKSGKKAIGAGA------------GNPPVVV 247
|
250
....*....|....*....
gi 15600566 262 FPDADLDRAA-DIAVMANF 279
Cdd:PRK15398 248 DETADIEKAArDIVKGASF 266
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
141-286 |
8.71e-06 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 48.26 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600566 141 EPLGVVAGIGAWNYPVQIALWKSAPALAAGNAMIFKPS----EVTPLTALKLAEIYTEAGVPDGVFNVLTGSGREVGQWL 216
Cdd:PRK13805 107 EPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHpraqKSSIAAAKIVLDAAVAAGAPKDIIQWIEEPSVELTNAL 186
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600566 217 TEHPLIEKISFTGGTStgkkvMASASSSSLKEVtmeLG---GKSPLIIFPDADLDRA-ADIaVMANFFSSGQVC 286
Cdd:PRK13805 187 MNHPGIALILATGGPG-----MVKAAYSSGKPA---LGvgaGNVPAYIDKTADIKRAvNDI-LLSKTFDNGMIC 251
|
|
| |
