|
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: 988.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 1 MARFDLQKLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILR 80
Cdd:PRK13252 1 MSRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 81 ERNDELAALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIAL 160
Cdd:PRK13252 81 ERNDELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 161 WKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGReVGTWLTEHPRIEKVSFTGGTDTGKKVMAS 240
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 241 ASSSsLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPED 320
Cdd:PRK13252 240 AAAS-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 321 ENTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYET 400
Cdd:PRK13252 319 PATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 401 EEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQ 480
Cdd:PRK13252 399 EDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQ 478
|
490
....*....|
gi 504533159 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: 762.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 26 AINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKyVD 105
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 106 IVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTT 185
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 186 LKLAEIYTEAGVPAGVFNVLTGSGrEVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSsLKDVTMELGGKSPLIIFDDA 265
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKG-IKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 266 DLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGK 345
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 346 EQGARLLCGGDRLTEGD-FAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDL 424
Cdd:cd07090 318 QEGAKVLCGGERVVPEDgLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 425 NRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQVELG 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: 715.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 10 YIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 90 ETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAA 169
Cdd:TIGR01804 81 ETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 170 GNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSsLKDV 249
Cdd:TIGR01804 161 GNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGH-LKHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 250 TMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLV 329
Cdd:TIGR01804 240 TMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 330 SFAHMESVLGYIAKGKEQGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRAN 409
Cdd:TIGR01804 320 SAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARAN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504533159 410 DTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIK 477
Cdd:TIGR01804 400 DTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-483 |
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: 636.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 1 MARFDLQkLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILR 80
Cdd:COG1012 1 MTTPEYP-LFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 81 ERNDELAALETLDTGKAFSETKyVDIVTGADVLEYYAGLVPAIEGEQIPLRDT-SFVYTRREPLGVVAGIGAWNYPIQIA 159
Cdd:COG1012 80 ERREELAALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDAPgTRAYVRREPLGVVGAITPWNFPLALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 160 LWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMA 239
Cdd:COG1012 159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 240 SAsSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPE 319
Cdd:COG1012 239 AA-AENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 320 DENTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEgdfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYE 399
Cdd:COG1012 318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDG---EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 400 TEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGES-DAKMPVGGYKQSGVGRENGISSLNNFTRIKS 478
Cdd:COG1012 395 DEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKT 474
|
....*
gi 504533159 479 VQVEL 483
Cdd:COG1012 475 VTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
18-479 |
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: 614.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 18 AGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKA 97
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 98 FSETKYvDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP 177
Cdd:pfam00171 83 LAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 178 SEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASAsSSSLKDVTMELGGKS 257
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAA-AQNLKRVTLELGGKN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 258 PLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESV 337
Cdd:pfam00171 241 PLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 338 LGYIAKGKEQGARLLCGGdrltEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAA 417
Cdd:pfam00171 321 LKYVEDAKEEGAKLLTGG----EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504533159 418 GLVTKDLNRAHRVIHQLEAGICWINAWGESDAKM-PVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:pfam00171 397 GVFTSDLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREGGPYGLEEYTEVKTV 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: 583.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKI--WAAMTAMERSRILRRAVDILRERNDE 85
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 86 LAALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAP 165
Cdd:cd07091 85 LAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 166 ALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSS 245
Cdd:cd07091 165 ALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 246 LKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNF 325
Cdd:cd07091 245 LKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 326 GPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLteGDfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVI 405
Cdd:cd07091 325 GPQVSKAQFDKILSYIESGKKEGATLLTGGERH--GS--KGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504533159 406 RRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
27-479 |
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: 551.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKG--QKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETK-- 102
Cdd:cd07114 2 INPATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRaq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 103 --YVdivtgADVLEYYAGLVPAIEGEQIPLRDTS-FVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSE 179
Cdd:cd07114 82 vrYL-----AEWYRYYAGLADKIEGAVIPVDKGDyLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 180 VTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVmASASSSSLKDVTMELGGKSPL 259
Cdd:cd07114 157 HTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHI-ARAAAENLAPVTLELGGKSPN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 260 IIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLG 339
Cdd:cd07114 236 IVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 340 YIAKGKEQGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGL 419
Cdd:cd07114 316 YVARAREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 420 VTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07114 396 WTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 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: 542.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 10 YIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKG--QKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 88 ALETLDTGKAFSETKYvDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPAL 167
Cdd:cd07119 81 RLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 168 AAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSsLK 247
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN-VK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 248 DVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGP 327
Cdd:cd07119 239 KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 328 LVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRR 407
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504533159 408 ANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQVEL 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: 532.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 47 ERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKyVDIVTGADVLEYYAGLVPAIEGE 126
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 127 QIPLRDTSFV-YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVL 205
Cdd:cd07078 80 VIPSPDPGELaIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 206 TGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASAsSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQV 285
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAA-AENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 286 CTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLtegDFAK 365
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRL---EGGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 366 GAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWG 445
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 504533159 446 ES-DAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07078 396 VGaEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
27-481 |
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: 525.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKYVDI 106
Cdd:cd07093 2 FNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 107 VTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTL 186
Cdd:cd07093 82 PRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 187 KLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMAsASSSSLKDVTMELGGKSPLIIFDDAD 266
Cdd:cd07093 162 LLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMR-AAAPNLKPVSLELGGKNPNIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 267 LDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKE 346
Cdd:cd07093 241 LDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 347 QGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNR 426
Cdd:cd07093 321 EGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 504533159 427 AHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07093 401 AHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
28-483 |
5.14e-180 |
|
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: 511.98 E-value: 5.14e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 28 NPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKYVDIV 107
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 108 TGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLK 187
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 188 LAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMaSASSSSLKDVTMELGGKSPLIIFDDADL 267
Cdd:cd07115 163 IAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIM-QGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 268 DRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKEQ 347
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 348 GARLLCGGDRLTegdfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRA 427
Cdd:cd07115 322 GARLLTGGKRPG----ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 504533159 428 HRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQVEL 483
Cdd:cd07115 398 HRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
22-479 |
1.29e-174 |
|
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: 498.67 E-value: 1.29e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 22 ATFEAINPANGEVLAQVQRATKDDVERAVVSA----EKGQkiWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKA 97
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAArrafESGV--WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 98 FSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP 177
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 178 SEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSSLKDVTMELGGKS 257
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 258 PLIIFD-DADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMES 336
Cdd:cd07112 240 PNIVFAdAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 337 VLGYIAKGKEQGARLLCGGDRLTEGdfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLA 416
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRVLTE--TGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLA 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504533159 417 AGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07112 398 ASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
8-481 |
1.10e-173 |
|
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: 497.26 E-value: 1.10e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKI---WAAMTAMERSRILRRAVDILRERND 84
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 85 ELAALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSA 164
Cdd:cd07141 88 YLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 165 PALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSS 244
Cdd:cd07141 168 PALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 245 SLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTN 324
Cdd:cd07141 248 NLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 325 FGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLteGDfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEV 404
Cdd:cd07141 328 QGPQIDEEQFKKILELIESGKKEGAKLECGGKRH--GD--KGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEV 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504533159 405 IRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07141 404 IERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
8-483 |
3.76e-173 |
|
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: 495.77 E-value: 3.76e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKG-QKIWAAMTAMERSRILRRAVDILRERNDEL 86
Cdd:cd07144 9 GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 87 AALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPA 166
Cdd:cd07144 89 AAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 167 LAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMAsASSSSL 246
Cdd:cd07144 169 LAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMK-AAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 247 KDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVA-RIRIGNPEDENTNF 325
Cdd:cd07144 248 KAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 326 GPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGDfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVI 405
Cdd:cd07144 328 GPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGL-GKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAI 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504533159 406 RRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQVEL 483
Cdd:cd07144 407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
8-479 |
3.84e-171 |
|
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: 490.47 E-value: 3.84e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKG--QKIWAAMTAMERSRILRRAVDILRERNDE 85
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 86 LAALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAP 165
Cdd:cd07142 85 LAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 166 ALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSS 245
Cdd:cd07142 165 ALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 246 LKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNF 325
Cdd:cd07142 245 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 326 GPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLteGDfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVI 405
Cdd:cd07142 325 GPQVDKEQFEKILSYIEHGKEEGATLITGGDRI--GS--KGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504533159 406 RRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
27-479 |
4.90e-171 |
|
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: 489.25 E-value: 4.90e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKyVDI 106
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 107 VTGADVLEYYAGLVPAIEGEQIPLRDTSF-VYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTT 185
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKrILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 186 LKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSsLKDVTMELGGKSPLIIFDDA 265
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADT-VKRVSLELGGNAPFIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 266 DLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGK 345
Cdd:cd07103 240 DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 346 EQGARLLCGGDRLTEGdfakGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLN 425
Cdd:cd07103 320 AKGAKVLTGGKRLGLG----GYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 504533159 426 RAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
9-480 |
3.64e-170 |
|
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: 487.40 E-value: 3.64e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 9 LYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 89 LETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQipLRDTSFVytRREPLGVVAGIGAWNYPI-QIALwKSAPAL 167
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEE--RRGNSLV--VREPIGVCGLITPWNWPLnQIVL-KVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 168 AAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSsLK 247
Cdd:cd07138 156 AAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT-VK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 248 DVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGP 327
Cdd:cd07138 235 RVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 328 LVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGdFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRR 407
Cdd:cd07138 315 LASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEG-LERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAI 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504533159 408 ANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINaWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQ 480
Cdd:cd07138 394 ANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
8-483 |
2.54e-165 |
|
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: 475.68 E-value: 2.54e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 88 ALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPAL 167
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 168 AAGNAMIFKPSEVTSLTTLKLAEIYTEAgVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSsLK 247
Cdd:cd07559 162 AAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAEN-LI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 248 DVTMELGGKSPLIIFDDADLDRA-----ADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDEN 322
Cdd:cd07559 240 PVTLELGGKSPNIFFDDAMDADDdfddkAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 323 TNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEE 402
Cdd:cd07559 320 TMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 403 EVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQVE 482
Cdd:cd07559 400 EAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILVS 479
|
.
gi 504533159 483 L 483
Cdd:cd07559 480 Y 480
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
27-481 |
3.42e-159 |
|
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: 459.39 E-value: 3.42e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQKIWA-AMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETkYVD 105
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA-RAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 106 IVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTT 185
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 186 LKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSSlKDVTMELGGKSPLIIFDDA 265
Cdd:cd07109 161 LRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV-VPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 266 DLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEdENTNFGPLVSFAHMESVLGYIAKGK 345
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 346 EQGARLLCGGdRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLN 425
Cdd:cd07109 319 ARGARIVAGG-RIAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 504533159 426 RAHRVIHQLEAGICWINAWGESDA-KMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07109 398 RALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
9-483 |
2.38e-158 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 458.15 E-value: 2.38e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 9 LYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKG-QKIWA-AMTAMERSRILRRAVDILRERNDEL 86
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERNLDYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 87 AALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPA 166
Cdd:cd07143 89 ASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 167 LAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSSL 246
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 247 KDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFG 326
Cdd:cd07143 249 KKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 327 PLVSFAHMESVLGYIAKGKEQGARLLCGGDRltEGDfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIR 406
Cdd:cd07143 329 PQVSQIQYERIMSYIESGKAEGATVETGGKR--HGN--EGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504533159 407 RANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQVEL 483
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
8-479 |
2.91e-158 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 458.52 E-value: 2.91e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSA----EKGQkiWAAMTAMERSRILRRAVDILRERN 83
Cdd:PLN02766 22 KLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAreafDHGP--WPRMSGFERGRIMMKFADLIEEHI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 84 DELAALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKS 163
Cdd:PLN02766 100 EELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 164 APALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASS 243
Cdd:PLN02766 180 APALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 244 SSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENT 323
Cdd:PLN02766 260 SNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 324 NFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEgdfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEE 403
Cdd:PLN02766 340 RQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGD----KGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504533159 404 VIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
27-479 |
7.36e-158 |
|
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: 456.04 E-value: 7.36e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKY-VD 105
Cdd:cd07110 2 INPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWdVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 106 IVTGAdvLEYYAGLVPAIE---GEQIPLRDTSF-VYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVT 181
Cdd:cd07110 82 DVAGC--FEYYADLAEQLDakaERAVPLPSEDFkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 182 SLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSSlKDVTMELGGKSPLII 261
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDI-KPVSLELGGKSPIIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 262 FDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYI 341
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 342 AKGKEQGARLLCGGDRLTEGDfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVT 421
Cdd:cd07110 319 ARGKEEGARLLCGGRRPAHLE--KGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 504533159 422 KDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
27-481 |
1.09e-157 |
|
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: 455.25 E-value: 1.09e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKYVDI 106
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 107 VTGADVLEYYAGLVPAIEG----EQIPLRdTSFVytRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTS 182
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGpaagEYLPGH-TSMI--RREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 183 LTTLKLAEIYTEaGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSsLKDVTMELGGKSPLIIF 262
Cdd:cd07092 159 LTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADT-LKRVHLELGGKAPVIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 263 DDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIA 342
Cdd:cd07092 237 DDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 343 KGKeQGARLLCGGDRLTegdfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTK 422
Cdd:cd07092 317 RAP-AHARVLTGGRRAE----GPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 504533159 423 DLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
8-479 |
7.67e-157 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 454.96 E-value: 7.67e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKG-----QKIWAAMTAMERSRILRRAVDILRER 82
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 83 NDELAALETLDTGKAFSETKYvDIVTGADVLEYYAGLVPAIEGEQ---IPLRDTSF-VYTRREPLGVVAGIGAWNYPIQI 158
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAW-DMDDVAGCFEYYADLAEALDAKQkapVSLPMETFkGYVLKEPLGVVGLITPWNYPLLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 159 ALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVM 238
Cdd:PLN02467 168 ATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 239 ASAsSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNP 318
Cdd:PLN02467 248 TAA-AQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 319 EDENTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRltEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTY 398
Cdd:PLN02467 327 LEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKR--PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 399 ETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKS 478
Cdd:PLN02467 405 STEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQ 484
|
.
gi 504533159 479 V 479
Cdd:PLN02467 485 V 485
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
27-483 |
1.01e-155 |
|
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: 450.67 E-value: 1.01e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKyVDI 106
Cdd:cd07107 2 INPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAML-GDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 107 VTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTL 186
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 187 KLAEIYTEAgVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSsLKDVTMELGGKSPLIIFDDAD 266
Cdd:cd07107 161 RLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 267 LDRAADTAMMA-NFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGK 345
Cdd:cd07107 239 PEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 346 EQGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLN 425
Cdd:cd07107 319 REGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 504533159 426 RAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQVEL 483
Cdd:cd07107 399 QAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
8-484 |
2.10e-155 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 450.52 E-value: 2.10e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYsDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:PRK13473 4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 88 ALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEG----EQIPlRDTSFVytRREPLGVVAGIGAWNYPIQIALWKS 163
Cdd:PRK13473 83 RLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGkaagEYLE-GHTSMI--RRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 164 APALAAGNAMIFKPSEVTSLTTLKLAEIYTEAgVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASS 243
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 244 SsLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENT 323
Cdd:PRK13473 239 S-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 324 NFGPLVSFAHMESVLGYIAKGKEQG-ARLLCGGDRLtegdFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEE 402
Cdd:PRK13473 318 ELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAP----DGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 403 EVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQVE 482
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
..
gi 504533159 483 LG 484
Cdd:PRK13473 474 HT 475
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
27-481 |
6.61e-154 |
|
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: 445.43 E-value: 6.61e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKyVDI 106
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ-FEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 107 VTGADVLEYYAGLvpAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTL 186
Cdd:cd07106 81 GGAVAWLRYTASL--DLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 187 KLAEIYTEAgVPAGVFNVLTGSGrEVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSsLKDVTMELGGKSPLIIFDDAD 266
Cdd:cd07106 159 KLGELAQEV-LPPGVLNVVSGGD-ELGPALTSHPDIRKISFTGSTATGKKVMASAAKT-LKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 267 LDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKE 346
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 347 QGARLLCGGDRLtEGdfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNR 426
Cdd:cd07106 316 KGAKVLAGGEPL-DG---PGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 504533159 427 AHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
27-481 |
7.51e-153 |
|
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: 443.34 E-value: 7.51e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKYVDI 106
Cdd:cd07108 2 INPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 107 VTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTL 186
Cdd:cd07108 82 AVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 187 KLAEIYTEAgVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASAsSSSLKDVTMELGGKSPLIIFDDAD 266
Cdd:cd07108 162 LLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAA-ADRLIPVSLELGGKSPMIVFPDAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 267 LDRAADTAMMA-NFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGK 345
Cdd:cd07108 240 LDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 346 E-QGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDL 424
Cdd:cd07108 320 StSGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 504533159 425 NRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISS-LNNFTRIKSVQV 481
Cdd:cd07108 400 GRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTVNI 457
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
9-481 |
2.36e-152 |
|
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: 442.40 E-value: 2.36e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 9 LYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEK--GQKIWAAMTAMERSRILRRAVDILRERNDEL 86
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRafDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 87 AALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIplRDTSF---VYTRREPLGVVAGIGAWNYPIQIALWKS 163
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEER--RPGSGgghVLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 164 APALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGsGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASS 243
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 244 SsLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENT 323
Cdd:cd07139 238 R-LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 324 NFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTegDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEE 403
Cdd:cd07139 317 QIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPA--GLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDD 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504533159 404 VIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGeSDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFR-LDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
10-479 |
3.99e-152 |
|
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: 442.07 E-value: 3.99e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 10 YIDGGYsdAGSDATFEAINPAN-GEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
Cdd:cd07097 4 YIDGEW--VAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 89 LETLDTGKAFSETKYvDIVTGADVLEYYAGLVPAIEGEQIP-LRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPAL 167
Cdd:cd07097 82 LLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 168 AAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSSLK 247
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 248 dVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGP 327
Cdd:cd07097 241 -VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 328 LVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGDfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRR 407
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPD--EGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504533159 408 ANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINA-WGESDAKMPVGGYKQSGVG-RENGISSLNNFTRIKSV 479
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLpTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
27-481 |
6.15e-152 |
|
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: 440.62 E-value: 6.15e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSA----EKGQkiWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETK 102
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAArkafDKGP--WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 103 yVDIVTGADVLEYYAGLVPAIEGEQI-PLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVT 181
Cdd:cd07118 80 -GEIEGAADLWRYAASLARTLHGDSYnNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 182 SLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMAsASSSSLKDVTMELGGKSPLII 261
Cdd:cd07118 159 SGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAA-AAARNLKKVSLELGGKNPQIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 262 FDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYI 341
Cdd:cd07118 238 FADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 342 AKGKEQGARLLCGGDRLtegDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVT 421
Cdd:cd07118 318 DAGRAEGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 422 KDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07118 395 KDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
8-483 |
1.46e-151 |
|
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: 440.74 E-value: 1.46e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 88 ALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPAL 167
Cdd:cd07117 82 MVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 168 AAGNAMIFKPSEVTSLTTLKLAEIYTEAgVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVmASASSSSLK 247
Cdd:cd07117 162 AAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDV-AIAAAKKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 248 DVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGP 327
Cdd:cd07117 240 PATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 328 LVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRR 407
Cdd:cd07117 320 QVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDM 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504533159 408 ANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQVEL 483
Cdd:cd07117 400 ANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
5-487 |
3.77e-150 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 439.24 E-value: 3.77e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 5 DLQKLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKG--QKIWAAMTAMERSRILRRAVDILRER 82
Cdd:PLN02466 56 SYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 83 NDELAALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWK 162
Cdd:PLN02466 136 NDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 163 SAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASAS 242
Cdd:PLN02466 216 VGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 243 SSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDEN 322
Cdd:PLN02466 296 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 323 TNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTegdfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEE 402
Cdd:PLN02466 376 VEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG----SKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLD 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 403 EVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQVE 482
Cdd:PLN02466 452 EVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTP 531
|
....*
gi 504533159 483 LGDYA 487
Cdd:PLN02466 532 LKNPA 536
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
8-482 |
9.20e-149 |
|
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: 433.85 E-value: 9.20e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKG--QKIWAAMTAMERSRILRRAVDILRERNDE 85
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 86 LAALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDT----SFVYTRREPLGVVAGIGAWNYPIQIALW 161
Cdd:cd07140 87 LATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQArpnrNLTLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 162 KSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASA 241
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 242 SSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDE 321
Cdd:cd07140 247 AVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 322 NTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEgdfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETE 401
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDR----PGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 402 --EEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07140 403 dvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
...
gi 504533159 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 |
7.38e-148 |
|
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: 430.51 E-value: 7.38e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQKIWA-AMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKYVD 105
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 106 IVTGADVLEYYAGLVPAIEGEQI-------PLRDTSFVytRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPS 178
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWEFDlpvpalrGGPGRRVV--RREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 179 EVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASAsSSSLKDVTMELGGKSP 258
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQA-AATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 259 LIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVL 338
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 339 GYIAKGKEQGARLLCGGDRLTEGDfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAG 418
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAGLD--KGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504533159 419 LVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07089 397 VWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
10-481 |
5.37e-147 |
|
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: 429.07 E-value: 5.37e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 10 YIDGGYSDAGSDATFEAINPANG-EVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 89 LETLDTGKAFSETKyVDIVTGADVLEYYAGLVPAIEGEQIP--LRDtSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPA 166
Cdd:cd07131 82 LVTREMGKPLAEGR-GDVQEAIDMAQYAAGEGRRLFGETVPseLPN-KDAMTRRQPIGVVALITPWNFPVAIPSWKIFPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 167 LAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVmASASSSSL 246
Cdd:cd07131 160 LVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERI-GETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 247 KDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFG 326
Cdd:cd07131 239 KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 327 PLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIR 406
Cdd:cd07131 319 PLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504533159 407 RANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINA--WGeSDAKMPVGGYKQSGVG-RENGISSLNNFTRIKSVQV 481
Cdd:cd07131 399 IANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAptIG-AEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
10-479 |
8.09e-147 |
|
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: 428.22 E-value: 8.09e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 10 YIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 90 ETLDTGKAFSETKyVDIVTGADVLEYYAGLVPAIEGEQIPL-RDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALA 168
Cdd:cd07088 81 IVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSdRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 169 AGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMAsASSSSLKD 248
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIME-AAAENITK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 249 VTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPL 328
Cdd:cd07088 239 VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 329 VSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGdfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRA 408
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGGKRPEGE---KGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504533159 409 NDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
9-481 |
8.32e-141 |
|
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: 413.38 E-value: 8.32e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 9 LYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKG-QKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 88 ALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGE----QIPL----RDTSFvyTRREPLGVVAGIGAWNYPIQIA 159
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGEtlapSIPSmqgeRYTAF--TRREPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 160 LWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGrEVGTWLTEHPRIEKVSFTGGTDTGKKVMA 239
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 240 SASSSsLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPE 319
Cdd:cd07113 239 QAASD-LTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 320 DENTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTegdfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYE 399
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA----GEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 400 TEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07113 394 DEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
..
gi 504533159 480 QV 481
Cdd:cd07113 474 MI 475
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
52-481 |
4.10e-138 |
|
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: 402.38 E-value: 4.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 52 SAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKyVDIVTGADVLEYYAGLVPAIEGEQIPLR 131
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 132 DTSFV-YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGR 210
Cdd:cd06534 81 DPGGEaYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 211 EVGTWLTEHPRIEKVSFTGGTDTGKKVMASAsSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGT 290
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAA-AENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 291 RVFVPKHLQAAFEAKIVervarirignpedentnfgplvsfahmesvlgyiakgkeqgarllcggdrltegdfakgafva 370
Cdd:cd06534 240 RLLVHESIYDEFVEKLV--------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 371 pTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWG-ESDA 449
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSiGVGP 335
|
410 420 430
....*....|....*....|....*....|..
gi 504533159 450 KMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
24-481 |
1.85e-137 |
|
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: 403.63 E-value: 1.85e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 24 FEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKY 103
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 104 vDIVTGADVLEYYAGLVPAIEGEQIP-LRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTS 182
Cdd:cd07150 81 -ETTFTPELLRAAAGECRRVRGETLPsDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 183 LTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVmASASSSSLKDVTMELGGKSPLIIF 262
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREI-AEKAGRHLKKITLELGGKNPLIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 263 DDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIA 342
Cdd:cd07150 239 ADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 343 KGKEQGARLLCGGDRltegdfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTK 422
Cdd:cd07150 319 DAVAKGAKLLTGGKY-------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 423 DLNRAHRVIHQLEAGICWINAWGESD-AKMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07150 392 DLQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
11-479 |
4.32e-133 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 394.44 E-value: 4.32e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 11 IDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALE 90
Cdd:PLN02278 29 IGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 91 TLDTGKAFSETkYVDIVTGADVLEYYAGLVPAIEGEQIPlrdTSFVYTR----REPLGVVAGIGAWNYPIQIALWKSAPA 166
Cdd:PLN02278 109 TLEQGKPLKEA-IGEVAYGASFLEYFAEEAKRVYGDIIP---SPFPDRRllvlKQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 167 LAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMAsASSSSL 246
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMA-GAAATV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 247 KDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFG 326
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 327 PLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGdfakGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIR 406
Cdd:PLN02278 344 PLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLG----GTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIA 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504533159 407 RANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:PLN02278 420 IANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
10-481 |
1.81e-132 |
|
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: 391.93 E-value: 1.81e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 10 YIDGGYSDAGSDaTFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
Cdd:cd07086 2 VIGGEWVGSGGE-TFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 90 ETLDTGKAFSETKyVDIVTGADVLEYYAGLVPAIEGEQIPL-RDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALA 168
Cdd:cd07086 81 VSLEMGKILPEGL-GEVQEMIDICDYAVGLSRMLYGLTIPSeRPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 169 AGNAMIFKPSEVTSLTTLKLAEIYTEA----GVPAGVFNVLTGsGREVGTWLTEHPRIEKVSFTGGTDTGKKVmASASSS 244
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRV-GETVAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 245 SLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTN 324
Cdd:cd07086 238 RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 325 FGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGDfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEV 404
Cdd:cd07086 318 VGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGE--PGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 405 IRRANDTDFGLAAGLVTKDLNRAHRVI--HQLEAGICWINAwGESDAK--MPVGGYKQSGVGRENGISSLNNFTRIKSVQ 480
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAFRWLgpKGSDCGIVNVNI-PTSGAEigGAFGGEKETGGGRESGSDAWKQYMRRSTCT 474
|
.
gi 504533159 481 V 481
Cdd:cd07086 475 I 475
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
24-477 |
5.56e-132 |
|
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: 389.79 E-value: 5.56e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 24 FEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKy 103
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 104 VDIVTGADVLEYYAGLVPAIEGEQIPLRDTSF-----VYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPS 178
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVDAYEYnerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 179 EVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVmASASSSSLKDVTMELGGKSP 258
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLI-ASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 259 LIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVL 338
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 339 GYIAKGKEQGARLLCGGDRLtegdfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAG 418
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKRD------EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504533159 419 LVTKDLNRAHRVIHQLEAGICWINA-----WGesdaKMPVGGYKQSGVGRENGISSLNNFTRIK 477
Cdd:cd07145 393 VFTNDINRALKVARELEAGGVVINDstrfrWD----NLPFGGFKKSGIGREGVRYTMLEMTEEK 452
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
45-481 |
4.85e-130 |
|
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: 384.19 E-value: 4.85e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 45 DVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTG----KAFSETKYVdivtgADVLEYYAGLV 120
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGstrpKAAFEVGAA-----IAILREAAGLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 121 PAIEGEQIP-LRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTT-LKLAEIYTEAGVP 198
Cdd:cd07104 76 RRPEGEILPsDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 199 AGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVmASASSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMAN 278
Cdd:cd07104 156 KGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHI-GELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 279 FYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDrl 358
Cdd:cd07104 235 FLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 359 tegdfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGI 438
Cdd:cd07104 313 -----YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGM 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 504533159 439 CWINAWGESD-AKMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07104 388 VHINDQTVNDePHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
8-483 |
1.99e-128 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 382.32 E-value: 1.99e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSA----EKGQkiWAAMTAMERSRILRRAVDILRERN 83
Cdd:PRK09847 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAArgvfERGD--WSLSSPAKRKAVLNKLADLMEAHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 84 DELAALETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKS 163
Cdd:PRK09847 99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 164 APALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASS 243
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 244 SSLKDVTMELGGKSPLIIFDDADLDRAADTAMMAN-FYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDEN 322
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCPDLQQAASATAAGiFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 323 TNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRltegdfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEE 402
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNA------GLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 403 EVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQVE 482
Cdd:PRK09847 413 QALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWIS 492
|
.
gi 504533159 483 L 483
Cdd:PRK09847 493 L 493
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
24-479 |
2.29e-126 |
|
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: 375.40 E-value: 2.29e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 24 FEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSET-K 102
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDArK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 103 YVD--IVTgadvLEYYAGLVPAIEGEQIPLrDTS------FVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMI 174
Cdd:cd07149 81 EVDraIET----LRLSAEEAKRLAGETIPF-DASpggegrIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 175 FKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASAsssSLKDVTMELG 254
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKA---GLKKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 255 GKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHM 334
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 335 ESVLGYIAKGKEQGARLLCGGDRltegdfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFG 414
Cdd:cd07149 313 ERIEEWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYG 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504533159 415 LAAGLVTKDLNRAHRVIHQLEAGICWINawGESDAK---MPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07149 386 LQAGVFTNDLQKALKAARELEVGGVMIN--DSSTFRvdhMPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
10-481 |
6.65e-125 |
|
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: 372.56 E-value: 6.65e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 10 YIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 90 ETLDTGKAFSETKYVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAA 169
Cdd:cd07116 84 ETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 170 GNAMIFKPSEVTSLTTLKLAEIYTEAgVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASAsSSSLKDV 249
Cdd:cd07116 164 GNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYA-SENIIPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 250 TMELGGKSPLIIFDDADLD-------RAADTAMMAnfYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDEN 322
Cdd:cd07116 242 TLELGGKSPNIFFADVMDAddaffdkALEGFVMFA--LNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 323 TNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGDFAKGAFVAPTVFTDcTDDMVIVREEIFGPVMSILTYETEE 402
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504533159 403 EVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07116 399 EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
9-466 |
1.28e-122 |
|
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: 366.72 E-value: 1.28e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 9 LYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 89 LETLDTGKAFSETKYVDIVTGADVLEYYAGlvpaiegeQIPLRDTSFvyTRREPLGVVAGIGAWNYPIQIALWKSAPALA 168
Cdd:cd07111 104 LESLDNGKPIRESRDCDIPLVARHFYHHAG--------WAQLLDTEL--AGWKPVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 169 AGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGrEVGTWLTEHPRIEKVSFTGGTDTGKkVMASASSSSLKD 248
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGR-ALRRATAGTGKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 249 VTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPL 328
Cdd:cd07111 252 LSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 329 VSFAHMESVLGYIAKGKEQGARLLCGGDRLTegdfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRA 408
Cdd:cd07111 332 VDPAQLKRIRELVEEGRAEGADVFQPGADLP----SKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALA 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 504533159 409 NDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENG 466
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGG 465
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
13-480 |
8.83e-120 |
|
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: 358.93 E-value: 8.83e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 13 GGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETL 92
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 93 DTG----KAFSETKyvdiVTGADVLEYyAGLVPAIEGEQIPlRDT----SFVYtrREPLGVVAGIGAWNYPIQIALWKSA 164
Cdd:cd07151 81 ESGstriKANIEWG----AAMAITREA-ATFPLRMEGRILP-SDVpgkeNRVY--REPLGVVGVISPWNFPLHLSMRSVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 165 PALAAGNAMIFKPSEVTSLTT-LKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVmASASS 243
Cdd:cd07151 153 PALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHI-GELAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 244 SSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENT 323
Cdd:cd07151 232 RHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 324 NFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDrltegdfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEE 403
Cdd:cd07151 312 VVGPLINESQVDGLLDKIEQAVEEGATLLVGGE-------AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 404 VIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESD-AKMPVGGYKQSGVGRENGISSLNNFTRIK--SVQ 480
Cdd:cd07151 385 ALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDePHVPFGGEKNSGLGRFNGEWALEEFTTDKwiSVQ 464
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
27-479 |
1.50e-117 |
|
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: 353.19 E-value: 1.50e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQK--IWAAmTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKyV 104
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 105 DIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLT 184
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 185 TLKLAEIYTEA-GVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSsLKDVTMELGGKSPLIIFD 263
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPT-LKRLGLELGGKTPCIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 264 DADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAK 343
Cdd:cd07120 239 DADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVER 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 344 GKEQGARLLCGGDRLTEGdFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKD 423
Cdd:cd07120 319 AIAAGAEVVLRGGPVTEG-LAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 504533159 424 LNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
25-479 |
1.63e-116 |
|
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: 350.19 E-value: 1.63e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 25 EAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKYv 104
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 105 DIVTGADVLEYYAGLVPAIEGEQIPL-----RDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSE 179
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLdatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 180 VTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASAsssSLKDVTMELGGKSPL 259
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANA---GGKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 260 IIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLG 339
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 340 YIAKGKEQGARLLCGGDRltegdfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGL 419
Cdd:cd07094 318 WVEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGI 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504533159 420 VTKDLNRAHRVIHQLEAGICWINawgESDA----KMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07094 391 FTRDLNVAFKAAEKLEVGGVMVN---DSSAfrtdWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
46-481 |
4.44e-115 |
|
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: 345.60 E-value: 4.44e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 46 VERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKY-VDIVtgADVLEYYAGLVPA-I 123
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEKC--AWICRYYAENAEAfL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 124 EGEQIPLrDTSFVYTRREPLGVVAGIGAWNYPI-QIALWkSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVF 202
Cdd:cd07100 79 ADEPIET-DAGKAYVRYEPLGVVLGIMPWNFPFwQVFRF-AAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 203 NVLTGSGREVGTwLTEHPRIEKVSFTGGTDTGKKVmASASSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSS 282
Cdd:cd07100 157 QNLLIDSDQVEA-IIADPRVRGVTLTGSERAGRAV-AAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 283 GQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLtEGd 362
Cdd:cd07100 235 GQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRP-DG- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 363 faKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWIN 442
Cdd:cd07100 313 --PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 504533159 443 AWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07100 391 GMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
9-479 |
5.72e-115 |
|
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: 348.44 E-value: 5.72e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 9 LYIDGgySDAGSDATFEAINPAN-GEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:cd07124 35 LVIGG--KEVRTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 88 ALETLDTGKAFSETkYVDIVTGADVLEYYAGLVPAIEG---EQIPLRDTSFVYtrrEPLGVVAGIGAWNYPIQIALWKSA 164
Cdd:cd07124 113 AWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGfpvEMVPGEDNRYVY---RPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 165 PALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSS 244
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 245 S-----LKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPE 319
Cdd:cd07124 269 QpgqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 320 DENTNFGPLVSFAHMESVLGYIAKGKEQGaRLLCGGDRLTEGdfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYE 399
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELA--AEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 400 TEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWIN-----AWGESDakmPVGGYKQSGVG-RENGISSLNNF 473
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkitgALVGRQ---PFGGFKMSGTGsKAGGPDYLLQF 502
|
....*.
gi 504533159 474 TRIKSV 479
Cdd:cd07124 503 MQPKTV 508
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
27-479 |
5.56e-113 |
|
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: 341.12 E-value: 5.56e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETkYVDI 106
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADA-GLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 107 VTGADVLEYYAGLVP-AIEGEQIPLRDTSFV---YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTS 182
Cdd:cd07099 80 LLALEAIDWAARNAPrVLAPRKVPTGLLMPNkkaTVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 183 LTTLKLAEIYTEAGVPAGVFNVLTGSGrEVGTWLTEHpRIEKVSFTGGTDTGKKVMASASSSsLKDVTMELGGKSPLIIF 262
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDA-GVDKVAFTGSVATGRKVMAAAAER-LIPVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 263 DDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIA 342
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 343 KGKEQGARLLCGGDRLTEGdfakGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTK 422
Cdd:cd07099 317 DAVAKGAKALTGGARSNGG----GPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 504533159 423 DLNRAHRVIHQLEAGICWIN--AWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07099 393 DLARAEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
7-477 |
4.00e-110 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 334.95 E-value: 4.00e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 7 QKLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDEL 86
Cdd:PRK11241 11 QQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 87 AALETLDTGKAFSETKYvDIVTGADVLEYYAGLVPAIEGEQIPLRDT-SFVYTRREPLGVVAGIGAWNYPIQIALWKSAP 165
Cdd:PRK11241 91 ARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPGHQAdKRLIVIKQPIGVTAAITPWNFPAAMITRKAGP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 166 ALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASAsSSS 245
Cdd:PRK11241 170 ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC-AKD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 246 LKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNF 325
Cdd:PRK11241 249 IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 326 GPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGdfakGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVI 405
Cdd:PRK11241 329 GPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELG----GNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504533159 406 RRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIK 477
Cdd:PRK11241 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
8-479 |
5.82e-110 |
|
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: 334.10 E-value: 5.82e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 88 ALETLDTGKAFSETKyVDIVTGADVLEYYAGLVPAIEGEQIP-LRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPA 166
Cdd:cd07085 82 RLITLEHGKTLADAR-GDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 167 LAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGsGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSSl 246
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 247 KDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVC-TNGTRVFVpKHLQAAFEAKIVERVARIRIGNPEDENTNF 325
Cdd:cd07085 239 KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCmALSVAVAV-GDEADEWIPKLVERAKKLKVGAGDDPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 326 GPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVI 405
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 406 RRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINawgesdakMPV---------GGYKQSGVGREN--GISSLNNFT 474
Cdd:cd07085 398 AIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN--------VPIpvplaffsfGGWKGSFFGDLHfyGKDGVRFYT 469
|
....*
gi 504533159 475 RIKSV 479
Cdd:cd07085 470 QTKTV 474
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
17-479 |
1.69e-109 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 334.54 E-value: 1.69e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 17 DAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGK 96
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 97 ----AFSETkyVDIVTGADvleYYAGLVPAIEGEQ-----IPLRDTSFVYtrREPLGVVAGIGAWNYPIQIALWKSAPAL 167
Cdd:PRK09407 107 arrhAFEEV--LDVALTAR---YYARRAPKLLAPRrragaLPVLTKTTEL--RQPKGVVGVISPWNYPLTLAVSDAIPAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 168 AAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHprIEKVSFTGGTDTGKKVmASASSSSLK 247
Cdd:PRK09407 180 LAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVL-AEQAGRRLI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 248 DVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGP 327
Cdd:PRK09407 257 GFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 328 LVSFAHMESVLGYIAKGKEQGARLLCGGDRLTE-GDFakgaFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIR 406
Cdd:PRK09407 337 LISEAQLETVSAHVDDAVAKGATVLAGGKARPDlGPL----FYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504533159 407 RANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWIN-----AWGESDAkmPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:PRK09407 413 RANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVDA--PMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
25-479 |
1.90e-108 |
|
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: 329.70 E-value: 1.90e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 25 EAINPANGEVLAQVQRATKDDVERAVVSAEKGQKiwaAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKYv 104
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 105 DIVTGADVLEYYAGLVPAIEGEQIPLRDTS-----FVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSE 179
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 180 VTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASAsssSLKDVTMELGGKSPL 259
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATA---GYKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 260 IIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLG 339
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 340 YIAKGKEQGARLLCGGDRltegdfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGL 419
Cdd:cd07146 315 RVEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504533159 420 VTKDLNRAHRVIHQLEAGICwiNAW---GESDAKMPVGGYKQSG-VGRENGISSLNNFTRIKSV 479
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTV--NVNevpGFRSELSPFGGVKDSGlGGKEGVREAMKEMTNVKTY 449
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
27-481 |
4.21e-108 |
|
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: 328.88 E-value: 4.21e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGK----AFSETK 102
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKarrhAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 103 YVDIVTgadvlEYYAGLVPAIEGEQ-----IPLRDTSFVYtrREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP 177
Cdd:cd07101 81 DVAIVA-----RYYARRAERLLKPRrrrgaIPVLTRTTVN--RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 178 SEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHprIEKVSFTGGTDTGKKVmASASSSSLKDVTMELGGKS 257
Cdd:cd07101 154 DSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVV-AERAGRRLIGCSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 258 PLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESV 337
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 338 LGYIAKGKEQGARLLCGGD-RLTEGDFakgaFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLA 416
Cdd:cd07101 311 TAHVDDAVAKGATVLAGGRaRPDLGPY----FYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLN 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 417 AGLVTKDLNRAHRVIHQLEAGICWIN-----AWGESDAkmPVGGYKQSGVGRENGISSLNNFTRIKSVQV 481
Cdd:cd07101 387 ASVWTRDGARGRRIAARLRAGTVNVNegyaaAWASIDA--PMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
24-479 |
4.71e-108 |
|
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: 328.44 E-value: 4.71e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 24 FEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKy 103
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 104 VDIVTGADVLEYYAGLVPAIEGEQIPLrDTS------FVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP 177
Cdd:cd07147 80 GEVARAIDTFRIAAEEATRIYGEVLPL-DISargegrQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 178 SEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSgREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSsslKDVTMELGGKS 257
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 258 PLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESV 337
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 338 LGYIAKGKEQGARLLCGGDRltegdfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAA 417
Cdd:cd07147 315 EGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504533159 418 GLVTKDLNRAHRVIHQLEAGICWIN---AWgESDaKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07147 388 GVFTRDLEKALRAWDELEVGGVVINdvpTF-RVD-HMPYGGVKDSGIGREGVRYAIEEMTEPRLL 450
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
45-479 |
2.33e-107 |
|
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: 326.07 E-value: 2.33e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 45 DVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTG--KAFSEtkyVDIVTGADVLEYYAGLVPA 122
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGatAAWAG---FNVDLAAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 123 IEGEQIP-LRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGV 201
Cdd:cd07105 78 IIGGSIPsDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 202 FNVLTGS---GREVGTWLTEHPRIEKVSFTGGTDTGKKVmASASSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMAN 278
Cdd:cd07105 158 LNVVTHSpedAPEVVEALIAHPAVRKVNFTGSTRVGRII-AETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 279 FYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDentnfGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRL 358
Cdd:cd07105 237 FLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVDDALSKGAKLVVGGLAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 359 TEGDfakGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGI 438
Cdd:cd07105 312 ESPS---GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 504533159 439 CWINawGES---DAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07105 389 VHIN--GMTvhdEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
27-479 |
8.54e-106 |
|
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: 322.66 E-value: 8.54e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKYvDI 106
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG-EI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 107 VTGADVLEYYAGLVPAIEGEQIPLRDTSFV-YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTT 185
Cdd:cd07102 80 RGMLERARYMISIAEEALADIRVPEKDGFErYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 186 LKLAEIYTEAGVPAGVFNVLTGSGrEVGTWLTEHPRIEKVSFTGGTDTGKKVmASASSSSLKDVTMELGGKSPLIIFDDA 265
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSH-ETSAALIADPRIDHVSFTGSVAGGRAI-QRAAAGRFIKVGLELGGKDPAYVRPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 266 DLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGK 345
Cdd:cd07102 238 DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 346 EQGARLLCGGDRLTEGDfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLN 425
Cdd:cd07102 318 AKGARALIDGALFPEDK-AGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 504533159 426 RAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07102 397 RAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
8-479 |
1.44e-102 |
|
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: 315.28 E-value: 1.44e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYSDaGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAA-MTAMERSRILRRAVDILRERNDEL 86
Cdd:cd07082 3 KYLINGEWKE-SSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 87 AALETLDTGKAFSE-TKYVD-----IVTGADVLEYYAGlvPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIAL 160
Cdd:cd07082 82 ANLLMWEIGKTLKDaLKEVDrtidyIRDTIEELKRLDG--DSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 161 WKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMAS 240
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 241 AsssSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPED 320
Cdd:cd07082 240 H---PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 321 ENTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTegdfakGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYET 400
Cdd:cd07082 317 NGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG------GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVND 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 401 EEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGES--DAkMPVGGYKQSGVGREnGIS-SLNNFTRIK 477
Cdd:cd07082 391 IEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRgpDH-FPFLGRKDSGIGTQ-GIGdALRSMTRRK 468
|
..
gi 504533159 478 SV 479
Cdd:cd07082 469 GI 470
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-479 |
2.24e-100 |
|
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: 309.23 E-value: 2.24e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 28 NPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKYVDIV 107
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 108 TGADVLEYYAGlvpaiEGE---QIPLRDTSFV------YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPS 178
Cdd:cd07098 82 VTCEKIRWTLK-----HGEkalRPESRPGGLLmfykraRVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 179 EVTSLTTLKLAEIYTEA----GVPAGVFNVLTGSGrEVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSsLKDVTMELG 254
Cdd:cd07098 157 EQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 255 GKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHM 334
Cdd:cd07098 235 GKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 335 ESVLGYIAKGKEQGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFG 414
Cdd:cd07098 315 DRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504533159 415 LAAGLVTKDLNRAHRVIHQLEAGICWINAWGES--DAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07098 395 LGASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSV 461
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
32-474 |
1.39e-97 |
|
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: 301.13 E-value: 1.39e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 32 GEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTG----KAFSETKyvdiv 107
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGsirpKAGFEVG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 108 TGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTT-L 186
Cdd:cd07152 76 AAIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 187 KLAEIYTEAGVPAGVFNVLTGsGREVGTWLTEHPRIEKVSFTGGTDTGKKVmASASSSSLKDVTMELGGKSPLIIFDDAD 266
Cdd:cd07152 156 VIARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKV-GEAAGRHLKKVSLELGGKNALIVLDDAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 267 LDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKE 346
Cdd:cd07152 234 LDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 347 QGARLLCGGDRltegdfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNR 426
Cdd:cd07152 314 AGARLEAGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGR 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 504533159 427 AHRVIHQLEAGICWINAWGESD-AKMPVGGYKQSGVG-RENGISSLNNFT 474
Cdd:cd07152 387 AMALADRLRTGMLHINDQTVNDePHNPFGGMGASGNGsRFGGPANWEEFT 436
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
9-479 |
3.46e-97 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 302.62 E-value: 3.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 9 LYIDGGYSDagSDATFEAINPAN-GEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:PRK03137 39 LIIGGERIT--TEDKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 88 ALETLDTGKAFSETKyVDIVTGADVLEYYA----GLVPAIEGEQIPLRDTSFVYtrrEPLGVVAGIGAWNYPIQIALWKS 163
Cdd:PRK03137 117 AWLVKEAGKPWAEAD-ADTAEAIDFLEYYArqmlKLADGKPVESRPGEHNRYFY---IPLGVGVVISPWNFPFAIMAGMT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 164 APALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASS 243
Cdd:PRK03137 193 LAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 244 SS-----LKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNP 318
Cdd:PRK03137 273 VQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 319 EDeNTNFGPLVSFAHMESVLGYIAKGKEQGaRLLCGGdrltEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTY 398
Cdd:PRK03137 353 ED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGG----EGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 399 ETEEEVIRRANDTDFGLAAGLVTKD---LNRAHRVIHqleAGICWIN--AWGESDAKMPVGGYKQSGV-GRENGISSLNN 472
Cdd:PRK03137 427 KDFDHALEIANNTEYGLTGAVISNNrehLEKARREFH---VGNLYFNrgCTGAIVGYHPFGGFNMSGTdSKAGGPDYLLL 503
|
....*..
gi 504533159 473 FTRIKSV 479
Cdd:PRK03137 504 FLQAKTV 510
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
72-482 |
8.29e-89 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 277.39 E-value: 8.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 72 LRRAVDILRERNDELAALETLDTGKAFSETKyVDIVTGADVLEYYAGLVPAIEGEQIPL-RDTSFVYTRREPLGVVAGIG 150
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAE-VEVAFTADYIDYMAEWARRYEGEIIQSdRPGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 151 AWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGG 230
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 231 TDTGKKVMASASSSSLKdVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERV 310
Cdd:PRK10090 160 VSAGEKIMAAAAKNITK-VCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 311 ARIRIGNP-EDENTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEgdfaKGAFVAPTVFTDCTDDMVIVREEIF 389
Cdd:PRK10090 239 QAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEG----KGYYYPPTLLLDVRQEMSIMHEETF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 390 GPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAwgESDAKMP--VGGYKQSGVGRENGI 467
Cdd:PRK10090 315 GPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR--ENFEAMQgfHAGWRKSGIGGADGK 392
|
410
....*....|....*
gi 504533159 468 SSLNNFTRIKSVQVE 482
Cdd:PRK10090 393 HGLHEYLQTQVVYLQ 407
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
19-466 |
1.73e-81 |
|
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: 260.60 E-value: 1.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 19 GSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAF 98
Cdd:cd07130 9 GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 99 SE-----TKYVDIVtgadvlEYYAGLVPAIEGEQIPL-RDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNA 172
Cdd:cd07130 89 PEglgevQEMIDIC------DFAVGLSRQLYGLTIPSeRPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 173 MIFKPSEVTSLTTLK----LAEIYTEAGVPAGVFNVLTGsGREVGTWLTEHPRIEKVSFTGGTDTGKKVmASASSSSLKD 248
Cdd:cd07130 163 VVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQV-GQAVAARFGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 249 VTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPL 328
Cdd:cd07130 241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 329 VSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGdfakGAFVAPTVFTdCTDDMVIVREEIFGPVMSILTYETEEEVIRRA 408
Cdd:cd07130 321 HTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGP----GNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWN 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504533159 409 NDTDFGLAAGLVTKDLNRAHRVIHQL--EAGICWINAwGESDAKM--PVGGYKQSGVGRENG 466
Cdd:cd07130 396 NEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNI-GTSGAEIggAFGGEKETGGGRESG 456
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
26-479 |
5.77e-81 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 259.02 E-value: 5.77e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 26 AINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKyVD 105
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR-AE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 106 IVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTT 185
Cdd:PRK13968 90 VAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 186 LKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEhPRIEKVSFTGGTDTGKKVMASASSSsLKDVTMELGGKSPLIIFDDA 265
Cdd:PRK13968 170 QLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDPFIVLNDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 266 DLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGK 345
Cdd:PRK13968 248 DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 346 EQGARLLCGGDRLTegdfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLN 425
Cdd:PRK13968 328 AEGARLLLGGEKIA----GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 504533159 426 RAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:PRK13968 404 QARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
8-479 |
4.13e-80 |
|
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: 257.12 E-value: 4.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 8 KLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 88 ALETLDTGKAFSETKYvDIVTGADVLEYYAGLVPAIEGEQIPLRDTSF-VYTRREPLGVVAGIGAWNYPIQIALWKSAPA 166
Cdd:TIGR01722 82 ELITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETSTQVATRVdVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 167 LAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGsGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSSl 246
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 247 KDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEaKIVERVARIRIGNPEDENTNFG 326
Cdd:TIGR01722 239 KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAADEWVP-EIRERAEKIRIGPGDDPGAEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 327 PLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIR 406
Cdd:TIGR01722 318 PLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 407 RANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINawgesdAKMPV-------GGYKQSGVGREN--GISSLNNFTRIK 477
Cdd:TIGR01722 398 LINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN------VPIPVplpyfsfTGWKDSFFGDHHiyGKQGTHFYTRGK 471
|
..
gi 504533159 478 SV 479
Cdd:TIGR01722 472 TV 473
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
27-479 |
1.53e-78 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 252.35 E-value: 1.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKyVDI 106
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK-AEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 107 VTGADVLEYYAGLVPAI---EGEQIPLRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSL 183
Cdd:PRK09406 85 LKCAKGFRYYAEHAEALladEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 184 TTLKLAEIYTEAGVPAGVF-NVLTGSGrEVGTWLTEhPRIEKVSFTGGTDTGKKVmASASSSSLKDVTMELGGKSPLIIF 262
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFqTLLVGSG-AVEAILRD-PRVAAATLTGSEPAGRAV-AAIAGDEIKKTVLELGGSDPFIVM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 263 DDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIA 342
Cdd:PRK09406 242 PSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 343 KGKEQGARLLCGGDRLtEGDfakGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTK 422
Cdd:PRK09406 322 DAVAAGATILCGGKRP-DGP---GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 504533159 423 DLNRAHRVIHQLEAGICWINAWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:PRK09406 398 DEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
45-463 |
2.38e-77 |
|
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: 248.73 E-value: 2.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 45 DVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKY-VDIVTG-ADV-LEYYAGLVP 121
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTeVAAMAGkIDIsIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 122 --AIEGEQIPLRdtsfvyTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPA 199
Cdd:cd07095 81 erATPMAQGRAV------LRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 200 GVFNVLTGsGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANF 279
Cdd:cd07095 155 GVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 280 YSSGQVCTNGTRVFVPKHLQA-AFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRL 358
Cdd:cd07095 234 LTAGQRCTCARRLIVPDGAVGdAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 359 TEGdfakGAFVAPTVFtDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGI 438
Cdd:cd07095 314 VAG----TAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGI 388
|
410 420 430
....*....|....*....|....*....|
gi 504533159 439 cwINaW-----GESDAkMPVGGYKQSGVGR 463
Cdd:cd07095 389 --VN-WnrpttGASST-APFGGVGLSGNHR 414
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
5-483 |
4.46e-77 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 249.67 E-value: 4.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 5 DLQKLYIDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERND 84
Cdd:PLN00412 14 DVYKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 85 ELAALETLDTGKAFSETKyVDIVTGADVLEYYAGLVPAIEGEQIPLRDTSFVYTRRE--------PLGVVAGIGAWNYPI 156
Cdd:PLN00412 94 PIAECLVKEIAKPAKDAV-TEVVRSGDLISYTAEEGVRILGEGKFLVSDSFPGNERNkycltskiPLGVVLAIPPFNYPV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 157 QIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGtDTGkk 236
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTG-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 237 vMASASSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIG 316
Cdd:PLN00412 250 -IAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 317 NPEDeNTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRltegdfaKGAFVAPTVFTDCTDDMVIVREEIFGPVMSIL 396
Cdd:PLN00412 329 PPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 397 TYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWIN-AWGESDAKMPVGGYKQSGVGRENGISSLNNFTR 475
Cdd:PLN00412 401 RINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINsAPARGPDHFPFQGLKDSGIGSQGITNSINMMTK 480
|
....*...
gi 504533159 476 IKSVQVEL 483
Cdd:PLN00412 481 VKSTVINL 488
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
9-460 |
3.53e-74 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 241.79 E-value: 3.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 9 LYIDGGYSdAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
Cdd:PRK09457 3 LWINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 89 LETLDTGKAFSETKY-VDIVTG--ADVLEYYAglvpAIEGEQI-PLRDTSFVyTRREPLGVVAGIGAWNYPIQIALWKSA 164
Cdd:PRK09457 82 VIARETGKPLWEAATeVTAMINkiAISIQAYH----ERTGEKRsEMADGAAV-LRHRPHGVVAVFGPYNFPGHLPNGHIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 165 PALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGsGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSS 244
Cdd:PRK09457 157 PALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 245 SLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQA-AFEAKIVERVARIRIGNPEDENT 323
Cdd:PRK09457 236 PEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGdAFLARLVAVAKRLTVGRWDAEPQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 324 NF-GPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGdfakGAFVAPTVFtDCTDDMVIVREEIFGPVMSILTYETEE 402
Cdd:PRK09457 316 PFmGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAG----TGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFD 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504533159 403 EVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGIcwINaW-----GESDAkMPVGGYKQSG 460
Cdd:PRK09457 391 EAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGI--VN-WnkpltGASSA-APFGGVGASG 449
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
9-479 |
3.87e-73 |
|
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: 239.79 E-value: 3.87e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 9 LYIDGGYSDAGSDATfeAINPAN-GEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:cd07083 21 LVIGGEWVDTKERMV--SVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 88 ALETLDTGKAFSEtKYVDIVTGADVLEYYAGLVPAIEGEQ-----IPLRDTSFVYtrrEPLGVVAGIGAWNYPIQIALWK 162
Cdd:cd07083 99 ATLTYEVGKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAvevvpYPGEDNESFY---VGLGAGVVISPWNFPVAIFTGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 163 SAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASAS 242
Cdd:cd07083 175 IVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 243 S-----SSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGN 317
Cdd:cd07083 255 RlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 318 PEDENTNFGPLVSFAHMESVLGYIAKGKEQGaRLLCGGDRLTegdfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILT 397
Cdd:cd07083 335 PEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLE----GEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 398 YETEE--EVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWIN--AWGESDAKMPVGGYKQSGVG-RENGISSLNN 472
Cdd:cd07083 410 YKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFKLSGTNaKTGGPHYLRR 489
|
....*..
gi 504533159 473 FTRIKSV 479
Cdd:cd07083 490 FLEMKAV 496
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
11-466 |
5.53e-73 |
|
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: 239.79 E-value: 5.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 11 IDGGysDAGSDATFEAINPANGE-VLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
Cdd:cd07125 37 INGE--ETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 90 ETLDTGKAFSETkyVDIVTGA-DVLEYYAGLV------PAIEGEQIPLRDTSFvytrrEPLGVVAGIGAWNYPIQIALWK 162
Cdd:cd07125 115 AAAEAGKTLADA--DAEVREAiDFCRYYAAQArelfsdPELPGPTGELNGLEL-----HGRGVFVCISPWNFPLAIFTGQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 163 SAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASAS 242
Cdd:cd07125 188 IAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 243 SSSLKDVTM--ELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTnGTRV-FVPKHLQAAFEAKIVERVARIRIGNPE 319
Cdd:cd07125 268 ERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCS-ALRLlYLQEEIAERFIEMLKGAMASLKVGDPW 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 320 DENTNFGPLVSFAHMESVLGYIAKGKEQgARLLCGGDRltegDFAKGAFVAPTVFTDCTDDmvIVREEIFGPVMSILTYE 399
Cdd:cd07125 347 DLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPL----DDGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFK 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504533159 400 TE--EEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWIN-----AWGESDakmPVGGYKQSGVGRENG 466
Cdd:cd07125 420 AEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrnitgAIVGRQ---PFGGWGLSGTGPKAG 490
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
25-462 |
3.89e-70 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 230.38 E-value: 3.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 25 EAINPANGEVLAQVQRATKDDVERAVVSAE---KGQKIWAAmtAMERSRILRRAVDILRERNDELAALETLDTGKAFSET 101
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHalfLDRNNWLP--AHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 102 KyVDIVTGADVLEYYAGLVPAIEGEQIPLRDTS-----FVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFK 176
Cdd:cd07148 80 K-VEVTRAIDGVELAADELGQLGGREIPMGLTPasagrIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 177 PSEVTSLTTLKLAEIYTEAGVPAGVFNVLTgSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSSlkDVTMELGGK 256
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT--RCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 257 SPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMES 336
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 337 VLGYIAKGKEQGARLLCGGDRLTEGDFakgafvAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLA 416
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRLSDTTY------APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQ 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 504533159 417 AGLVTKDLNRAHRVIHQLEAGICWINA-------WgesdakMPVGGYKQSGVG 462
Cdd:cd07148 390 AAVFTKDLDVALKAVRRLDATAVMVNDhtafrvdW------MPFAGRRQSGYG 436
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
68-479 |
1.51e-63 |
|
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: 212.39 E-value: 1.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 68 RSRILRRAVDILRERNDELAALETLDTGKAFSETKYVDI-VTGADVLEYYAGLVPAIEGEQIPLRDTSF---VYTRREPL 143
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIaVVLGEIDHALKHLKKWMKPRRVSVPLLLQpakAYVIPEPL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 144 GVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAgVPAGVFNVLTGsGREVGTWLTEHPrIE 223
Cdd:cd07087 102 GVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-GVEVATALLAEP-FD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 224 KVSFTGGTDTGKKVMASAsSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFE 303
Cdd:cd07087 179 HIFFTGSPAVGKIVMEAA-AKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 304 AKIVERVARIrIGNPEDENTNFGPLVSFAHMESVLGYIAKGKeqgarLLCGGDRLTEGDfakgaFVAPTVFTDCTDDMVI 383
Cdd:cd07087 258 EELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDGK-----VVIGGQVDKEER-----YIAPTILDDVSPDSPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 384 VREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINawgesDA-------KMPVGGY 456
Cdd:cd07087 327 MQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN-----DVllhaaipNLPFGGV 401
|
410 420
....*....|....*....|...
gi 504533159 457 KQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07087 402 GNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
11-485 |
1.57e-63 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 216.92 E-value: 1.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 11 IDGGYSDAGSDATFEAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALE 90
Cdd:PLN02419 118 IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 91 TLDTGKAFSETkYVDIVTGADVLEYYAGLVPAIEGEQIP-LRDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAA 169
Cdd:PLN02419 198 TTEQGKTLKDS-HGDIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTC 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 170 GNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTwLTEHPRIEKVSFTGGTDTGKKVMASASSSSlKDV 249
Cdd:PLN02419 277 GNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIYARAAAKG-KRI 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 250 TMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTN-GTRVFVPKhlQAAFEAKIVERVARIRIGNPEDENTNFGPL 328
Cdd:PLN02419 355 QSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMAlSTVVFVGD--AKSWEDKLVERAKALKVTCGSEPDADLGPV 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 329 VSFAHMESVLGYIAKGKEQGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRA 408
Cdd:PLN02419 433 ISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISII 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 409 NDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINawgesdAKMPV-------GGYKQSGVGREN--GISSLNNFTRIKSV 479
Cdd:PLN02419 513 NKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN------VPIPVplpffsfTGNKASFAGDLNfyGKAGVDFFTQIKLV 586
|
....*.
gi 504533159 480 QVELGD 485
Cdd:PLN02419 587 TQKQKD 592
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
64-479 |
5.53e-57 |
|
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: 195.01 E-value: 5.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 64 TAMERSRILRRAVDILRERNDELA-ALETlDTG-KAFSETKYVDIVTGADVLEYYAGLV-----PAIEGEQIPLRDTSfV 136
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAeAISA-DFGhRSRHETLLAEILPSIAGIKHARKHLkkwmkPSRRHVGLLFLPAK-A 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 137 YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGN-AMIfKPSEVTSLTTLKLAEIYTEAGvPAGVFNVLTGsGREVGTW 215
Cdd:cd07133 96 EVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNrVMI-KPSEFTPRTSALLAELLAEYF-DEDEVAVVTG-GADVAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 216 LTEHPrIEKVSFTGGTDTGKKVMASASSSsLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVP 295
Cdd:cd07133 173 FSSLP-FDHLLFTGSTAVGRHVMRAAAEN-LTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 296 KHLQAAFEAKIVERVARiRIGNPEDeNTNFGPLVSFAHMESVLGYIAKGKEQGARLL-CGGDrltEGDFAKGAFVAPTVF 374
Cdd:cd07133 251 EDKLEEFVAAAKAAVAK-MYPTLAD-NPDYTSIINERHYARLQGLLEDARAKGARVIeLNPA---GEDFAATRKLPPTLV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 375 TDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAW----GESDak 450
Cdd:cd07133 326 LNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTllhvAQDD-- 403
|
410 420
....*....|....*....|....*....
gi 504533159 451 MPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07133 404 LPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
139-479 |
2.14e-56 |
|
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: 193.60 E-value: 2.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 139 RREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFnVLTGsGREVGTWLTE 218
Cdd:cd07134 97 RYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEG-DAEVAQALLE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 219 HPrIEKVSFTGGTDTGKKVMASASSSsLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHL 298
Cdd:cd07134 175 LP-FDHIFFTGSPAVGKIVMAAAAKH-LASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 299 QAAFEAKIVERVARIRIGNPED-ENTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLtegdfAKGAFVAPTVFTDC 377
Cdd:cd07134 253 KDAFVEHLKAEIEKFYGKDAARkASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD-----AAQRYIAPTVLTNV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 378 TDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGE--SDAKMPVGG 455
Cdd:cd07134 328 TPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLhfLNPNLPFGG 407
|
330 340
....*....|....*....|....
gi 504533159 456 YKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07134 408 VNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
27-477 |
1.54e-55 |
|
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: 193.20 E-value: 1.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPAN-GEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETkyVD 105
Cdd:TIGR01238 56 TNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNA--IA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 106 IVTGA-DVLEYYAGLVPAIEGEQiplrdtsfvytRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLT 184
Cdd:TIGR01238 134 EVREAvDFCRYYAKQVRDVLGEF-----------SVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 185 TLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSSLKDVTM--ELGGKSPLIIF 262
Cdd:TIGR01238 203 AYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 263 DDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIA 342
Cdd:TIGR01238 283 STALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 343 KGKeQGARLLCGGDRLTEGDFAKGAFVAPTVFTdcTDDMVIVREEIFGPVMSILTYETEE--EVIRRANDTDFGLAAGLV 420
Cdd:TIGR01238 363 HMS-QTQKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVH 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 421 TKDLNRAHRVIHQLEAGICWIN--AWGESDAKMPVGGYKQSGVG-RENGISSLNNFTRIK 477
Cdd:TIGR01238 440 SRIETTYRWIEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
20-442 |
7.93e-55 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 198.17 E-value: 7.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 20 SDATFEAINPAN-GEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAF 98
Cdd:PRK11905 565 DGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTL 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 99 SETkyVDIVTGA-DVLEYYAglvpaiegEQIplRDTsFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP 177
Cdd:PRK11905 645 ANA--IAEVREAvDFLRYYA--------AQA--RRL-LNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKP 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 178 SEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSSLKDVTM--ELGG 255
Cdd:PRK11905 712 AEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaETGG 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 256 KSPLIIFDDADLDRAADTAMMANFYSSGQVCTnGTRV-FVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHM 334
Cdd:PRK11905 792 QNAMIVDSSALPEQVVADVIASAFDSAGQRCS-ALRVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQ 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 335 ESVLGYIAKGKEQGARLlcggDRLTEG-DFAKGAFVAPTVFTdcTDDMVIVREEIFGPVMSILTYETEE--EVIRRANDT 411
Cdd:PRK11905 871 ANIEAHIEAMRAAGRLV----HQLPLPaETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKADEldRVIDDINAT 944
|
410 420 430
....*....|....*....|....*....|.
gi 504533159 412 DFGLAAGLVTKDLNRAHRVIHQLEAGICWIN 442
Cdd:PRK11905 945 GYGLTFGLHSRIDETIAHVTSRIRAGNIYVN 975
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
137-479 |
3.09e-53 |
|
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: 185.79 E-value: 3.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 137 YTRREPLGVVAGIGAWNYPIQIALwksAP---ALAAGNAMIFKPSEVTSLTTLKLAEIYTEAgVPAGVFNVLTGsGREVG 213
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQLAL---APligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 214 TWLTEHPrIEKVSFTGGTDTGKKVMASASSSsLKDVTMELGGKSPLIIFDDadldraadtammAN------------FYS 281
Cdd:cd07136 170 QELLDQK-FDYIFFTGSVRVGKIVMEAAAKH-LTPVTLELGGKSPCIVDED------------ANlklaakrivwgkFLN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 282 SGQVCTNGTRVFVPKHLQAAFEAKIVErVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKeqgarLLCGGdrltEG 361
Cdd:cd07136 236 AGQTCVAPDYVLVHESVKEKFIKELKE-EIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGK-----IVFGG----NT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 362 DfAKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLE-AGICw 440
Cdd:cd07136 306 D-RETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSfGGGC- 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 504533159 441 INawgesDA-------KMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07136 384 IN-----DTimhlanpYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
17-442 |
5.07e-53 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 192.85 E-value: 5.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 17 DAGSDATFEAINPANG-EVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTG 95
Cdd:COG4230 565 EAASGEARPVRNPADHsDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAG 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 96 K----AFSEtkyvdiVTGA-DVLEYYAGLVPAIEGEQIPLRdtsfvytrrePLGVVAGIGAWNYPI-----QIAlwksAp 165
Cdd:COG4230 645 KtlpdAIAE------VREAvDFCRYYAAQARRLFAAPTVLR----------GRGVFVCISPWNFPLaiftgQVA----A- 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 166 ALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGK---KVMAS-- 240
Cdd:COG4230 704 ALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARlinRTLAArd 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 241 -----------------ASSSSL-----KDVtmelggkspliifddadldraadtaMMANFYSSGQVCtNGTRV-FVPKH 297
Cdd:COG4230 784 gpivpliaetggqnamiVDSSALpeqvvDDV-------------------------LASAFDSAGQRC-SALRVlCVQED 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 298 lqaafeakIVERV--------ARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKEQGaRLLCGGDRLTEGdfAKGAFV 369
Cdd:COG4230 838 --------IADRVlemlkgamAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RLVHQLPLPEEC--ANGTFV 906
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504533159 370 APTVFTdcTDDMVIVREEIFGPVMSILTYETEE--EVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWIN 442
Cdd:COG4230 907 APTLIE--IDSISDLEREVFGPVLHVVRYKADEldKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
10-485 |
3.60e-52 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 184.27 E-value: 3.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 10 YIDGGYSDAGSDATfeAINPANGEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
Cdd:PLN02315 24 YVGGEWRANGPLVS--SVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 90 ETLDTGKAFSET--KYVDIVtgaDVLEYYAGLVPAIEGEQIPL-RDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPA 166
Cdd:PLN02315 102 VSLEMGKILAEGigEVQEII---DMCDFAVGLSRQLNGSIIPSeRPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 167 LAAGNAMIFKPSEVTSLTTLKL----AEIYTEAGVPAGVFNVLTGsGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASAS 242
Cdd:PLN02315 179 LVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 243 SSSLKDVtMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDEN 322
Cdd:PLN02315 258 ARFGKCL-LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 323 TNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGdRLTEGDfakGAFVAPTVfTDCTDDMVIVREEIFGPVMSILTYETEE 402
Cdd:PLN02315 337 TLLGPLHTPESKKNFEKGIEIIKSQGGKILTGG-SAIESE---GNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 403 EVIRRANDTDFGLAAGLVTKDLNRAHRVI--HQLEAGICWIN-AWGESDAKMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:PLN02315 412 EAIEINNSVPQGLSSSIFTRNPETIFKWIgpLGSDCGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
....*.
gi 504533159 480 QVELGD 485
Cdd:PLN02315 492 TINYGN 497
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
79-479 |
6.44e-52 |
|
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: 181.65 E-value: 6.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 79 LRERNDELAALETLDTGKAFSETKYVDIVTG-ADVLEYYAGLVPAIEGEQIPLRDTSF----VYTRREPLGVVAGIGAWN 153
Cdd:cd07135 40 VKDNEEAIVEALKKDLGRPPFETLLTEVSGVkNDILHMLKNLKKWAKDEKVKDGPLAFmfgkPRIRKEPLGVVLIIGPWN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 154 YPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAgVPAGVFNVLTGSGREVGTWLTEhpRIEKVSFTGGTDT 233
Cdd:cd07135 120 YPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQ--KFDKIFYTGSGRV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 234 GKKVmASASSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFeAKIVERVARI 313
Cdd:cd07135 197 GRII-AEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEF-VEELKKVLDE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 314 RIGNPEDENTNFGPLVSFAHMESVLGYIAKGKeqgARLLCGGDRltegDFAKgAFVAPTVFTDCTDDMVIVREEIFGPVM 393
Cdd:cd07135 275 FYPGGANASPDYTRIVNPRHFNRLKSLLDTTK---GKVVIGGEM----DEAT-RFIPPTIVSDVSWDDSLMSEELFGPVL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 394 SILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWIN----AWGESDAkmPVGGYKQSGVGRENGISS 469
Cdd:cd07135 347 PIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdtliHVGVDNA--PFGGVGDSGYGAYHGKYG 424
|
410
....*....|
gi 504533159 470 LNNFTRIKSV 479
Cdd:cd07135 425 FDTFTHERTV 434
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
17-442 |
1.42e-51 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 188.48 E-value: 1.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 17 DAGSDATFEAINPANGE-VLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTG 95
Cdd:PRK11904 557 INGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAG 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 96 KAFSETkyVDIVTGA-DVLEYYAGLVPAIEGEQIPLRDtsfvYT------RREPLGVVAGIGAWNYPIQIALWKSAPALA 168
Cdd:PRK11904 637 KTLQDA--IAEVREAvDFCRYYAAQARRLFGAPEKLPG----PTgesnelRLHGRGVFVCISPWNFPLAIFLGQVAAALA 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 169 AGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGK---KVMAS----- 240
Cdd:PRK11904 711 AGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARiinRTLAArdgpi 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 241 --------------ASSSSL-----KDVtmelggkspliifddadldraadtaMMANFYSSGQVCTnGTRV-FVPKhlqa 300
Cdd:PRK11904 791 vpliaetggqnamiVDSTALpeqvvDDV-------------------------VTSAFRSAGQRCS-ALRVlFVQE---- 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 301 afeaKIVERV--------ARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKeQGARLLCGGDRltEGDFAKGAFVAPT 372
Cdd:PRK11904 841 ----DIADRViemlkgamAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMK-REARLLAQLPL--PAGTENGHFVAPT 913
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504533159 373 VFTdcTDDMVIVREEIFGPVMSILTYETEE--EVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWIN 442
Cdd:PRK11904 914 AFE--IDSISQLEREVFGPILHVIRYKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
68-479 |
2.43e-50 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 179.07 E-value: 2.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 68 RSRILRRAVDILRERNDELAALETLDTGKAFSETKYVDI-VTGADVLEYYAGLVPAIEGEQIplrDTSFV------YTRR 140
Cdd:PTZ00381 31 RKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVlLTVAEIEHLLKHLDEYLKPEKV---DTVGVfgpgksYIIP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 141 EPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEV---TSLTTLKLAEIYteagVPAGVFNVLTGsGREVGTWLT 217
Cdd:PTZ00381 108 EPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELsphTSKLMAKLLTKY----LDPSYVRVIEG-GVEVTTELL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 218 EHPrIEKVSFTGGTDTGKKVMASAsSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKH 297
Cdd:PTZ00381 183 KEP-FDHIFFTGSPRVGKLVMQAA-AENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 298 LQAAFEAKIVERVARIRIGNPEDENtNFGPLVSFAHMESVLGYIakgKEQGARLLCGGdrltEGDFAKgAFVAPTVFTDC 377
Cdd:PTZ00381 261 IKDKFIEALKEAIKEFFGEDPKKSE-DYSRIVNEFHTKRLAELI---KDHGGKVVYGG----EVDIEN-KYVAPTIIVNP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 378 TDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINawgesDA-------K 450
Cdd:PTZ00381 332 DLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN-----DCvfhllnpN 406
|
410 420
....*....|....*....|....*....
gi 504533159 451 MPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:PTZ00381 407 LPFGGVGNSGMGAYHGKYGFDTFSHPKPV 435
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
11-442 |
2.05e-45 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 170.54 E-value: 2.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 11 IDGGYSDAGSDAtfEAINPAN-GEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
Cdd:PRK11809 650 MLEDPVAAGEMS--PVINPADpRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGL 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 90 ETLDTGKAFSETkYVDIVTGADVLEYYAGLVpaiegeqiplRDTSFVYTRRePLGVVAGIGAWNYPIQIALWKSAPALAA 169
Cdd:PRK11809 728 LVREAGKTFSNA-IAEVREAVDFLRYYAGQV----------RDDFDNDTHR-PLGPVVCISPWNFPLAIFTGQVAAALAA 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 170 GNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGkKVMASASSSSLKD- 248
Cdd:PRK11809 796 GNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVA-RLLQRNLAGRLDPq 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 249 -----VTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTnGTRVFVpkhLQaafeAKIVERV--------ARIRI 315
Cdd:PRK11809 875 grpipLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCS-ALRVLC---LQ----DDVADRTlkmlrgamAECRM 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 316 GNPEDENTNFGPLVSFAHMESVLGYIAKGKEQGaRLLCGGDRLTEGDFAKGAFVAPTVFT-DCTDDMvivREEIFGPVMS 394
Cdd:PRK11809 947 GNPDRLSTDIGPVIDAEAKANIERHIQAMRAKG-RPVFQAARENSEDWQSGTFVPPTLIElDSFDEL---KREVFGPVLH 1022
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 504533159 395 ILTYETEE--EVIRRANDTDFGLAAGLVTK-DLNRAHrVIHQLEAGICWIN 442
Cdd:PRK11809 1023 VVRYNRNQldELIEQINASGYGLTLGVHTRiDETIAQ-VTGSAHVGNLYVN 1072
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
10-431 |
6.04e-45 |
|
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: 164.75 E-value: 6.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 10 YIDGGYSdAGSDATFEAINPANGEVLAqvqRATKD--DVERAVVSA-EKGQKIWAAMTAMERSRILRRAVDILRERNDEL 86
Cdd:cd07128 4 YVAGQWH-AGTGDGRTLHDAVTGEVVA---RVSSEglDFAAAVAYArEKGGPALRALTFHERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 87 AALETLdTGKAFSETKyVDIVTGADVLEYYAGLV----PA----IEGEQIPL-RDTSF----VYTRREplGVVAGIGAWN 153
Cdd:cd07128 80 YALSAA-TGATRRDSW-IDIDGGIGTLFAYASLGrrelPNahflVEGDVEPLsKDGTFvgqhILTPRR--GVAVHINAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 154 YPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGV-PAGVFNVLTGSGREVGTWLTEHpriEKVSFTGGTD 232
Cdd:cd07128 156 FPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHLGEQ---DVVAFTGSAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 233 TGKKVMA-----------SASSSSL--------------------KDVTMELGGKSpliifddadldraadtammanfys 281
Cdd:cd07128 233 TAAKLRAhpnivarsirfNAEADSLnaailgpdatpgtpefdlfvKEVAREMTVKA------------------------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 282 sGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKEQGARLLCGGDRLTE- 360
Cdd:cd07128 289 -GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVv 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504533159 361 -GDFAKGAFVAPTVFTdCTDDM--VIVRE-EIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVI 431
Cdd:cd07128 368 gADAEKGAFFPPTLLL-CDDPDaaTAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
27-481 |
1.21e-44 |
|
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: 163.91 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 27 INPAN-GEVLAQVQRATKDDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILR-ERNDELAALETLDTGKAFSETKYV 104
Cdd:cd07123 51 VMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGKNVWQAEID 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 105 DIVTGADVLEYYAGLVPAIEGEQiPLRDTSFVYTRRE--PL-GVVAGIGAWNY-PIQIALwKSAPALAaGNAMIFKPSEV 180
Cdd:cd07123 131 AACELIDFLRFNVKYAEELYAQQ-PLSSPAGVWNRLEyrPLeGFVYAVSPFNFtAIGGNL-AGAPALM-GNVVLWKPSDT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 181 TSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSS-----SLKDVTMELGG 255
Cdd:cd07123 208 AVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldryrTYPRIVGETGG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 256 KSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHME 335
Cdd:cd07123 288 KNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFD 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 336 SVLGYIAKGKEQ-GARLLCGGdrltEGDFAKGAFVAPTVFTdCTD-DMVIVREEIFGPVMSILTYETE--EEVIRRANDT 411
Cdd:cd07123 368 RIKGYIDHAKSDpEAEIIAGG----KCDDSVGYFVEPTVIE-TTDpKHKLMTEEIFGPVLTVYVYPDSdfEETLELVDTT 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504533159 412 -DFGLAAGLVTKD---LNRAHRVIHQlEAGICWINA--WGESDAKMPVGGYKQSGVGRENGisSLNNFTRIKSVQV 481
Cdd:cd07123 443 sPYALTGAIFAQDrkaIREATDALRN-AAGNFYINDkpTGAVVGQQPFGGARASGTNDKAG--SPLNLLRWVSPRT 515
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
136-479 |
1.65e-43 |
|
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: 159.31 E-value: 1.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 136 VYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIyteagVPAGV----FNVLTGsGRE 211
Cdd:cd07132 94 VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLdkecYPVVLG-GVE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 212 VGTWLTEHpRIEKVSFTGGTDTGKKVMAsASSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSGQVCTNGTR 291
Cdd:cd07132 168 ETTELLKQ-RFDYIFYTGSTSVGKIVMQ-AAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 292 VFVPKHLQAAFEAKIVERVARIrIGNPEDENTNFGPLVSFAHMESVLGYIAKGKeqgarLLCGGdrltEGDfAKGAFVAP 371
Cdd:cd07132 246 VLCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLSGGK-----VAIGG----QTD-EKERYIAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 372 TVFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWIN-----AWGE 446
Cdd:cd07132 315 TVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdtimhYTLD 394
|
330 340 350
....*....|....*....|....*....|...
gi 504533159 447 SdakMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07132 395 S---LPFGGVGNSGMGAYHGKYSFDTFSHKRSC 424
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
46-468 |
4.62e-41 |
|
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: 152.78 E-value: 4.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 46 VERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETkyVDIVTGADVLEYYAGLVPAIEG 125
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA--ENICGDQVQLRARAFVIYSYRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 126 EQIPL----RDTSF-VYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAG-VPA 199
Cdd:cd07084 79 PHEPGnhlgQGLKQqSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 200 GVFNVLTGSGReVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSSLKdvtMELGGKSPLIIFDDADLDRAADTAMMANF 279
Cdd:cd07084 159 EDVTLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIY---LELAGFNWKVLGPDAQAVDYVAWQCVQDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 280 Y-SSGQVCTNGTRVFVPKHLQA-AFEAKIVERVARIRignpeDENTNFGPLVSFahmeSVLGYIA-KGKEQGARLLCGG- 355
Cdd:cd07084 235 TaCSGQKCTAQSMLFVPENWSKtPLVEKLKALLARRK-----LEDLLLGPVQTF----TTLAMIAhMENLLGSVLLFSGk 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 356 -DRLTEGDFAKGAFVAPTVFTDCTDDMV---IVREEIFGPVMSILTYETEEE--VIRRANDTDFGLAAGLVTKDLNRAHR 429
Cdd:cd07084 306 eLKNHSIPSIYGACVASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPIFLQE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 504533159 430 VIHQLE-AGICWINAWGESDAkMPV----GGYKQSGVGRENGIS 468
Cdd:cd07084 386 LIGNLWvAGRTYAILRGRTGV-APNqnhgGGPAADPRGAGIGGP 428
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
18-423 |
1.09e-40 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 152.94 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 18 AGSDATFEAINPANGEVLAQVQrATKDDVERAVVSA-EKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGK 96
Cdd:PRK11903 15 AGSGAGTPLFDPVTGEELVRVS-ATGLDLAAAFAFArEQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 97 AFSETKyVDIVTGADVLEYYAGLVPAIeGEQIPLRDTSFVYTRREPL-----------GVVAGIGAWNYPiQIALW-KSA 164
Cdd:PRK11903 94 TRNDSA-VDIDGGIFTLGYYAKLGAAL-GDARLLRDGEAVQLGKDPAfqgqhvlvptrGVALFINAFNFP-AWGLWeKAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 165 PALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGV-PAGVFNVLTGSGREvgtwLTEHPRIEKV-SFTGGTDTGKKVMASAS 242
Cdd:PRK11903 171 PALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAG----LLDHLQPFDVvSFTGSAETAAVLRSHPA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 243 -----------SSSL--------------------KDVTMELGGKspliifddadldraadtammanfysSGQVCTNGTR 291
Cdd:PRK11903 247 vvqrsvrvnveADSLnsallgpdaapgseafdlfvKEVVREMTVK-------------------------SGQKCTAIRR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 292 VFVPKHLQAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKEQgARLLCGGDR--LTEGDFAKGAFV 369
Cdd:PRK11903 302 IFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ-AEVLFDGGGfaLVDADPAVAACV 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 504533159 370 APTVF-TDCTDDMVIVRE-EIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKD 423
Cdd:PRK11903 381 GPTLLgASDPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
141-479 |
1.43e-33 |
|
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: 131.76 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 141 EPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAgVPAGVFNVLTGsGREVGTWLTEHp 220
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQ- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 221 RIEKVSFTGGTDTGKKVMAsASSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYS-SGQVCTNGTRVFVPKHlq 299
Cdd:cd07137 177 KWDKIFFTGSPRVGRIIMA-AAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEES-- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 300 aaFEAKIVE---RVARIRIGNPEDENTNFGPLVSFAHMeSVLGYIAKGKEQGARLLCGGDRltegDfAKGAFVAPTVFTD 376
Cdd:cd07137 254 --FAPTLIDalkNTLEKFFGENPKESKDLSRIVNSHHF-QRLSRLLDDPSVADKIVHGGER----D-EKNLYIEPTILLD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 377 CTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINawgesDA------- 449
Cdd:cd07137 326 PPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFN-----DTvvqyaid 400
|
330 340 350
....*....|....*....|....*....|
gi 504533159 450 KMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:cd07137 401 TLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
141-479 |
1.33e-27 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 115.21 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 141 EPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAeiyteAGVP----AGVFNVLTGsGREVGTWL 216
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA-----ANIPkyldSKAVKVIEG-GPAVGEQL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 217 TEHpRIEKVSFTGGTDTGKKVMASAsSSSLKDVTMELGGKSPLII--FDDADLDRAADTAMMANFYSS--GQVCTNGTRV 292
Cdd:PLN02203 181 LQH-KWDKIFFTGSPRVGRIIMTAA-AKHLTPVALELGGKCPCIVdsLSSSRDTKVAVNRIVGGKWGScaGQACIAIDYV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 293 FVPKHLqAAFEAKIVERVARIRIGNPEDENTNFGPLVSFAHMESVLGYIAKGKEQgARLLCGGdrlteGDFAKGAFVAPT 372
Cdd:PLN02203 259 LVEERF-APILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGG-----SIDEKKLFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 373 VFTDCTDDMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINawgesDA--- 449
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFN-----DAiiq 406
|
330 340 350
....*....|....*....|....*....|....
gi 504533159 450 ----KMPVGGYKQSGVGRENGISSLNNFTRIKSV 479
Cdd:PLN02203 407 yacdSLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
141-479 |
1.39e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 112.45 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 141 EPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYtEAGVPAGVFNVLTGSGREVGTWLTEhp 220
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQ-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 221 RIEKVSFTGGTDTGKKVMAsASSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANF-YSSGQVCTNGTRVFVPKHLQ 299
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMA-AAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 300 AAFEAKIVERVARIRIGNPEdENTNFGPLVSFAHMESvLGYIAKGKEQGARLLCGGDRLTEgdfakGAFVAPTVFTDCTD 379
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPM-ESKDMSRIVNSTHFDR-LSKLLDEKEVSDKIVYGGEKDRE-----NLKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 380 DMVIVREEIFGPVMSILTYETEEEVIRRANDTDFGLAAGLVTKDLNRAHRVIHQLEAGICWINAWGESDA--KMPVGGYK 457
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLPFGGVG 419
|
330 340
....*....|....*....|..
gi 504533159 458 QSGVGRENGISSLNNFTRIKSV 479
Cdd:PLN02174 420 ESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
46-431 |
2.08e-23 |
|
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: 102.62 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 46 VERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTG-----------------KAFsetkyvdivt 108
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGlpearlqgelgrttgqlRLF---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 109 gADVLEYYAGLVPAI-----EGEQIPLRDTSFVYTrrePLGVVAGIGAWNYP--IQIALWKSAPALAAGNAMIFKPSEVT 181
Cdd:cd07129 71 -ADLVREGSWLDARIdpadpDRQPLPRPDLRRMLV---PLGPVAVFGASNFPlaFSVAGGDTASALAAGCPVVVKAHPAH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 182 SLTTLKLAEIYTEA----GVPAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSSSL-KDVTMELGGK 256
Cdd:cd07129 147 PGTSELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 257 SPLIIFddADLDRAADTAMMANFYSS-----GQVCTNGTRVFVPKHLQA-AFEAKIVERVARirignpedenTNFGPLVS 330
Cdd:cd07129 227 NPVFIL--PGALAERGEAIAQGFVGSltlgaGQFCTNPGLVLVPAGPAGdAFIAALAEALAA----------APAQTMLT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 331 FAhmesvlgyIAKGKEQG-ARLL--CGGDRLTEGDFAKGAF-VAPTVF-TDCTD--DMVIVREEIFGPVMSILTYETEEE 403
Cdd:cd07129 295 PG--------IAEAYRQGvEALAaaPGVRVLAGGAAAEGGNqAAPTLFkVDAAAflADPALQEEVFGPASLVVRYDDAAE 366
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 504533159 404 VIRRAN-------------DTDFGLAAGLVTKDLNRAHRVI 431
Cdd:cd07129 367 LLAVAEalegqltatihgeEDDLALARELLPVLERKAGRLL 407
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
49-317 |
2.41e-11 |
|
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: 65.75 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 49 AVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKYVDIVTGAdvlEYYAGLVPAIEGEQI 128
Cdd:cd07081 4 AVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAA---EYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 129 PLRDTSF-VYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTG 207
Cdd:cd07081 81 LTGDENGgTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 208 S----GREVGTWLTEHPRIEKVSFTGGtdtgkKVMASASSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYSSG 283
Cdd:cd07081 161 WidnpSIELAQRLMKFPGIGLLLATGG-----PAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNG 235
|
250 260 270
....*....|....*....|....*....|....
gi 504533159 284 QVCTNGTRVFVPKHLQAAFEAKIVERVARIRIGN 317
Cdd:cd07081 236 VICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAE 269
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
140-431 |
6.26e-11 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 64.44 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 140 REPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEAGVPAGVFNVLTGSGREVGTWLTE- 218
Cdd:cd07126 140 RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEa 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 219 HPRIekVSFTGGTdtgkKVMASASSSSLKDVTMELGGKSPLIIFDDADLDRAADTAMMANFYS-SGQVCTNGTRVFVPKH 297
Cdd:cd07126 220 NPRM--TLFTGSS----KVAERLALELHGKVKLEDAGFDWKILGPDVSDVDYVAWQCDQDAYAcSGQKCSAQSILFAHEN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 298 -LQAAFEAKIVERVARIRIgnpedENTNFGPLVSF------AHMESVLGYiakgkeQGARLLCGGDRLTE-------GDF 363
Cdd:cd07126 294 wVQAGILDKLKALAEQRKL-----EDLTIGPVLTWtterilDHVDKLLAI------PGAKVLFGGKPLTNhsipsiyGAY 362
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 364 AKGAFVAPTVFTDCTDDMVIVREEIFGPVMSILTYETEEE--VIRRANDTDFGLAAGLVTKDLNRAHRVI 431
Cdd:cd07126 363 EPTAVFVPLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEVL 432
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
52-280 |
9.76e-11 |
|
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: 63.40 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 52 SAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAF-------------SETKYVDIVTGAdvlEYYAG 118
Cdd:cd07077 2 SAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIrslianwiammgcSESKLYKNIDTE---RGITA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 119 LVPAIEGEQIPlrDTSFVYTRREPLGVVAGIGAWNYPIqIALWKSAPALAAGNAMIFKPSEVTSLTTlKLAEIYTEAGVP 198
Cdd:cd07077 79 SVGHIQDVLLP--DNGETYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTN-RALALLFQAADA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 199 AGvfnvltGSGREVGTW----------LTEHPRIEKVSFTGGTDTgkkVMASASSSSLKDVTMELGGKSPLIIFDDADLD 268
Cdd:cd07077 155 AH------GPKILVLYVphpsdelaeeLLSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEE 225
|
250
....*....|..
gi 504533159 269 RAADTAMMANFY 280
Cdd:cd07077 226 RASGSVHDSKFF 237
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
45-410 |
1.94e-09 |
|
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: 59.80 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 45 DVERAVVSAEKGQKIWAAMTAMERS----RILRRavdiLRERNDELAALETLDTGKAF------SETKYVDivTGADVLE 114
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAgvclEILQR----LNARSFEMAHAVMHTTGQAFmmafqaGGPHAQD--RGLEAVA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 115 YYA---GLVPAI------EGEQIPLR-DTSFVYTrrePLGVVAGIGAWNYPIqialWKSAPA----LAAGNAMIFKPSEV 180
Cdd:cd07127 159 YAWremSRIPPTaewekpQGKHDPLAmEKTFTVV---PRGVALVIGCSTFPT----WNGYPGlfasLATGNPVIVKPHPA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 181 TSL---TTLKLA-EIYTEAGV-PAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMASASSsslKDVTMELGG 255
Cdd:cd07127 232 AILplaITVQVArEVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ---AQVYTEKAG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 256 KSPLIIfddadLDRAADTAMMANF-YS----SGQVCTNGTRVFVPK--------HLQ-AAFEAKIVERVARIrIGNPEDE 321
Cdd:cd07127 309 VNTVVV-----DSTDDLKAMLRNLaFSlslySGQMCTTPQNIYVPRdgiqtddgRKSfDEVAADLAAAIDGL-LADPARA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 322 NTNFGPLVSfahmESVLGYIAKGKeQGARLLCGGDRLTEGDFAKGAFVAPTVFTDCTDDMVIVREEIFGPV--------- 392
Cdd:cd07127 383 AALLGAIQS----PDTLARIAEAR-QLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIafvvatdst 457
|
410 420 430
....*....|....*....|....*....|....
gi 504533159 393 ----------------MSILTYETEEEVIRRAND 410
Cdd:cd07127 458 dhsielaresvrehgaMTVGVYSTDPEVVERVQE 491
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
46-230 |
6.74e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 51.72 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 46 VERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKYVDIVTGAD-VLEYYAGL--VPA 122
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFASEyVYNDIKDMktVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 123 IEgeqiplRDTSFVYTR-REPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTSLTTLKLAEIYTEA----GV 197
Cdd:cd07122 81 IE------EDEEKGIVEiAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGA 154
|
170 180 190
....*....|....*....|....*....|...
gi 504533159 198 PAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGG 230
Cdd:cd07122 155 PEGLIQWIEEPSIELTQELMKHPDVDLILATGG 187
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
44-240 |
1.66e-06 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 50.29 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 44 DDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKYVDivtgadvLEYYAGLVPAI 123
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKIAK-------NVAAAEKTPGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 124 EGEQIPLR--DTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP----SEVTSLTTLKLAEIYTEAGV 197
Cdd:PRK15398 109 EDLTTEALtgDNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgaKKVSLRAIELLNEAIVAAGG 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504533159 198 PAGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMAS 240
Cdd:PRK15398 189 PENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKS 231
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
44-240 |
4.81e-06 |
|
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: 48.77 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 44 DDVERAVVSAEKGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKAFSETKYVDIVTGADVLEYYAGLVP-A 122
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLAAEKTPGTEDLTTtA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504533159 123 IEGeqiplrDTSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP----SEVTSLTTLKLAEIYTEAGVP 198
Cdd:cd07121 84 WSG------DNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgaKKVSAYAVELINKAIAEAGGP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504533159 199 AGVFNVLTGSGREVGTWLTEHPRIEKVSFTGGTDTGKKVMAS 240
Cdd:cd07121 158 DNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSS 199
|
|
| |
