|
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: 993.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 1 MSRMAEQQLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILR 80
Cdd:PRK13252 1 MSRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 81 ERNDELAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIAL 160
Cdd:PRK13252 81 ERNDELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGaETGQYLTEHPGIAKVSFTGGVASGKKVMAn 240
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMA- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 241 SAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFD 320
Cdd:PRK13252 239 AAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 321 PQTNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYES 400
Cdd:PRK13252 319 PATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 401 EDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQ 480
Cdd:PRK13252 399 EDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQ 478
|
490
....*....|
gi 446011217 481 VEMAKFQSIF 490
Cdd:PRK13252 479 VEMGPFQSPF 488
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
26-483 |
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: 820.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 26 TINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYsETSTVD 105
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPI-EEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 186 LKLAEIYSEAGLPDGVFNVLPGGGaETGQYLTEHPGIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVFDDA 265
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMS-AAAKGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 266 DLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGK 345
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 346 EEGARVLCGGDVLK-GDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADL 424
Cdd:cd07090 318 QEGAKVLCGGERVVpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446011217 425 NRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQVEM 483
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEM 456
|
|
| 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: 798.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 10 YIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKL 89
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 90 ETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAA 169
Cdd:TIGR01804 81 ETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 170 GNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANsAASSLKEV 249
Cdd:TIGR01804 161 GNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAA-AAGHLKHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 250 TMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLV 329
Cdd:TIGR01804 240 TMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 330 SFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRAN 409
Cdd:TIGR01804 320 SAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARAN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446011217 410 DTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVK 477
Cdd:TIGR01804 400 DTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
6-481 |
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: 631.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 6 EQQLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDE 85
Cdd:COG1012 5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 86 LAKLETLDTGKAYSEtSTVDIVTGADVLEYYAGLIPALEGSQIPL-RETSFVYTRREPLGVVAGIGAWNYPIQIALWKSA 164
Cdd:COG1012 85 LAALLTLETGKPLAE-ARGEVDRAADFLRYYAGEARRLYGETIPSdAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 165 PALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANsAAS 244
Cdd:COG1012 164 PALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA-AAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 245 SLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTN 324
Cdd:COG1012 243 NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 325 FSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGfdnGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEV 404
Cdd:COG1012 323 MGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEG---GYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446011217 405 IRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESP-AEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:COG1012 400 IALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
|
| 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: 620.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 18 ATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKA 97
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 98 YSETSTvDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP 177
Cdd:pfam00171 83 LAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 178 SEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANsAASSLKEVTMELGGKS 257
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEA-AAQNLKRVTLELGGKN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 258 PLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNV 337
Cdd:pfam00171 241 PLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 338 LRYIAKGKEEGARVLCGGDvlkgDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAA 417
Cdd:pfam00171 321 LKYVEDAKEEGAKLLTGGE----AGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446011217 418 GIVTADLNRAHRVIHQLEAGICWINTWGESPAEM-PVGGYKHSGIGRENGVMTLQSYTQVKSI 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: 579.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKI--WAAMTAMERSRILRRAVDILRERNDE 85
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 86 LAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAP 165
Cdd:cd07091 85 LAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 166 ALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASS 245
Cdd:cd07091 165 ALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 246 LKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNF 325
Cdd:cd07091 245 LKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 326 SPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVI 405
Cdd:cd07091 325 GPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGY----FIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446011217 406 RRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
26-479 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 549.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 26 TINPANGNVLATVQAAGREDVDRAVKSAQQG--QKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETST 103
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 104 vDIVTGADVLEYYAGLIPALEGSQIPLRETS-FVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTP 182
Cdd:cd07114 81 -QVRYLAEWYRYYAGLADKIEGAVIPVDKGDyLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 183 LTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANsAASSLKEVTMELGGKSPLIVF 262
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARA-AAENLAPVTLELGGKSPNIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 263 DDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIA 342
Cdd:cd07114 239 DDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 343 KGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTA 422
Cdd:cd07114 319 RAREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446011217 423 DLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07114 399 DLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
10-479 |
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: 530.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 10 YIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQG--QKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 88 KLETLDTGKAYSETSTvDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPAL 167
Cdd:cd07119 81 RLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 168 AAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMaNSAASSLK 247
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIM-RAAAGNVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 248 EVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSP 327
Cdd:cd07119 239 KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 328 LVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRR 407
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446011217 408 ANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| 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: 530.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 47 DRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEtSTVDIVTGADVLEYYAGLIPALEGS 126
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEE-ALGEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 127 QIPL-RETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVL 205
Cdd:cd07078 80 VIPSpDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 206 PGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANsAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQV 285
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRA-AAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 286 CTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGdgfDN 365
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEG---GK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 366 GAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWG 445
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 446011217 446 ESP-AEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07078 396 VGAePSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
26-481 |
0e+00 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 522.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 26 TINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVD 105
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 186 LKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANsAASSLKEVTMELGGKSPLIVFDDA 265
Cdd:cd07093 161 WLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRA-AAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 266 DLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGK 345
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 346 EEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLN 425
Cdd:cd07093 320 AEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446011217 426 RAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07093 400 RAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
26-481 |
2.03e-178 |
|
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: 508.13 E-value: 2.03e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 26 TINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVD 105
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 186 LKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANsAASSLKEVTMELGGKSPLIVFDDA 265
Cdd:cd07115 161 LRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQG-AAGNLKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 266 DLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGK 345
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 346 EEGARVLCGGdvlKGDGfDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLN 425
Cdd:cd07115 320 EEGARLLTGG---KRPG-ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446011217 426 RAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07115 396 RAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
21-479 |
1.17e-173 |
|
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: 496.35 E-value: 1.17e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 21 GRTFETINPANGNVLATVQAAGREDVDRAVKSAQQ----GQkiWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGK 96
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRafesGV--WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 97 AYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFK 176
Cdd:cd07112 79 PISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 177 PSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSLKEVTMELGGK 256
Cdd:cd07112 159 PAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 257 SPLIVFD-DADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRD 335
Cdd:cd07112 239 SPNIVFAdAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 336 NVLRYIAKGKEEGARVLCGGDVLKGDGfdNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGL 415
Cdd:cd07112 319 KVLGYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446011217 416 AAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07112 397 AASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
8-481 |
3.82e-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: 495.71 E-value: 3.82e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKI---WAAMTAMERSRILRRAVDILRERND 84
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 85 ELAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSA 164
Cdd:cd07141 88 YLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 165 PALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAAS 244
Cdd:cd07141 168 PALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 245 SLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTN 324
Cdd:cd07141 248 NLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 325 FSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEV 404
Cdd:cd07141 328 QGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEV 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446011217 405 IRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07141 404 IERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
27-479 |
4.52e-169 |
|
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: 484.24 E-value: 4.52e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 27 INPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEtSTVDI 106
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAE-ARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 107 VTGADVLEYYAGLIPALEGSQIPLRETSF-VYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKrILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 186 LKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANsAASSLKEVTMELGGKSPLIVFDDA 265
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQ-AADTVKRVSLELGGNAPFIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 266 DLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGK 345
Cdd:cd07103 240 DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 346 EEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLN 425
Cdd:cd07103 320 AKGAKVLTGGKRLGLGGY----FYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 446011217 426 RAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
9-483 |
2.79e-168 |
|
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: 483.45 E-value: 2.79e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 9 LYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQG-QKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:cd07144 10 LFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 88 KLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPAL 167
Cdd:cd07144 90 AIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 168 AAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMAnSAASSLK 247
Cdd:cd07144 170 AAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMK-AAAQNLK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 248 EVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARV-ERIRAGDVFDPQTNFS 326
Cdd:cd07144 249 AVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 327 PLVSFPHRDNVLRYIAKGKEEGARVLCGGDVlKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIR 406
Cdd:cd07144 329 PQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK-APEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIK 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446011217 407 RANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQVEM 483
Cdd:cd07144 408 KANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
9-480 |
1.31e-167 |
|
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: 481.23 E-value: 1.31e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 9 LYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAK 88
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 89 LETLDTGKAYSETSTVDIVTGADVLEYYAGLipalegsqipLRETSFVYTR------REPLGVVAGIGAWNYPI-QIALw 161
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADA----------LKDFEFEERRgnslvvREPIGVCGLITPWNWPLnQIVL- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANs 241
Cdd:cd07138 150 KVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 242 AASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDP 321
Cdd:cd07138 229 AADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 322 QTNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGdVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESE 401
Cdd:cd07138 309 ATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG-PGRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446011217 402 DEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPaEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQ 480
Cdd:cd07138 388 DEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP-GAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
8-479 |
1.82e-166 |
|
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: 478.53 E-value: 1.82e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQG--QKIWAAMTAMERSRILRRAVDILRERNDE 85
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 86 LAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAP 165
Cdd:cd07142 85 LAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 166 ALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASS 245
Cdd:cd07142 165 ALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 246 LKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNF 325
Cdd:cd07142 245 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 326 SPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVI 405
Cdd:cd07142 325 GPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGY----YIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446011217 406 RRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
8-481 |
3.37e-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: 3.37e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 88 KLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPAL 167
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 168 AAGNAMIFKPSEVTPLTALKLAEIYSEAgLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMaNSAASSLK 247
Cdd:cd07559 162 AAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIM-QYAAENLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 248 EVTMELGGKSPLIVFDDADLDLAADI-----AMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQ 322
Cdd:cd07559 240 PVTLELGGKSPNIFFDDAMDADDDFDdkaeeGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 323 TNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESED 402
Cdd:cd07559 320 TMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446011217 403 EVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07559 400 EAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILV 478
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
9-481 |
1.02e-160 |
|
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: 463.59 E-value: 1.02e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 9 LYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQ--GQKIWAAMTAMERSRILRRAVDILRERNDEL 86
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRafDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 87 AKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIplRETSF---VYTRREPLGVVAGIGAWNYPIQIALWKS 163
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEER--RPGSGgghVLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 164 APALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGgAETGQYLTEHPGIAKVSFTGGVASGKKVMAnSAA 243
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD-REVGEYLVRHPGVDKVSFTGSTAAGRRIAA-VCG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 244 SSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQT 323
Cdd:cd07139 237 ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 324 NFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLkgDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDE 403
Cdd:cd07139 317 QIGPLASARQRERVEGYIAKGRAEGARLVTGGGRP--AGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDD 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446011217 404 VIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAeMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFG-APFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
27-481 |
1.47e-158 |
|
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: 457.56 E-value: 1.47e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 27 INPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVDI 106
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 107 VTGADVLEYYAGLIPALEGSqiplRETSFV-----YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVT 181
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGP----AAGEYLpghtsMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 182 PLTALKLAEIYSEaGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIV 261
Cdd:cd07092 158 PLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVAR-AAADTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 262 FDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYI 341
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 342 AKGKEeGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVT 421
Cdd:cd07092 316 ERAPA-HARVLTGGRRAEGPGY----FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWT 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 422 ADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07092 391 RDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
26-481 |
3.41e-158 |
|
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: 456.84 E-value: 3.41e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 26 TINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTvD 105
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 186 LKLAEIYSEAgLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVFDDA 265
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMR-AAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 266 -DLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKG 344
Cdd:cd07107 238 dPEAAADAAVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 345 KEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADL 424
Cdd:cd07107 318 KREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446011217 425 NRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
8-481 |
4.27e-157 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 454.75 E-value: 4.27e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYtSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:PRK13473 4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 88 KLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQ----IPlRETSFVytRREPLGVVAGIGAWNYPIQIALWKS 163
Cdd:PRK13473 83 RLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAageyLE-GHTSMI--RRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 164 APALAAGNAMIFKPSEVTPLTALKLAEIYSEAgLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMAnSAA 243
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS-AAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 244 SSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQT 323
Cdd:PRK13473 238 DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 324 NFSPLVSFPHRDNVLRYIAKGKEEG-ARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESED 402
Cdd:PRK13473 318 ELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGY----YYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446011217 403 EVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMV 472
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
26-479 |
2.30e-156 |
|
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: 452.19 E-value: 2.30e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 26 TINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETStVD 105
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA-WD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGLIPALE---GSQIPLRETSF-VYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVT 181
Cdd:cd07110 80 VDDVAGCFEYYADLAEQLDakaERAVPLPSEDFkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 182 PLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMaNSAASSLKEVTMELGGKSPLIV 261
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVM-QAAAQDIKPVSLELGGKSPIIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 262 FDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYI 341
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 342 AKGKEEGARVLCGGDVLkgDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVT 421
Cdd:cd07110 319 ARGKEEGARLLCGGRRP--AHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446011217 422 ADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
27-481 |
2.62e-156 |
|
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: 451.69 E-value: 2.62e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 27 INPANGNVLATVQAAGREDVDRAVKSAQQGQKIWA-AMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTvD 105
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 186 LKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVFDDA 265
Cdd:cd07109 161 LRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMR-AAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 266 DLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAG-DVFDPqtNFSPLVSFPHRDNVLRYIAKG 344
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGpGLEDP--DLGPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 345 KEEGARVLCGGDVLKGDGfDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADL 424
Cdd:cd07109 318 RARGARIVAGGRIAEGAP-AGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446011217 425 NRAHRVIHQLEAGICWINTWGESPA-EMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
8-479 |
1.48e-155 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 451.88 E-value: 1.48e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQG-----QKIWAAMTAMERSRILRRAVDILRER 82
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 83 NDELAKLETLDTGKAYSEtSTVDIVTGADVLEYYAGLIPALEGSQ---IPLRETSF-VYTRREPLGVVAGIGAWNYPIQI 158
Cdd:PLN02467 89 KSELAKLETLDCGKPLDE-AAWDMDDVAGCFEYYADLAEALDAKQkapVSLPMETFkGYVLKEPLGVVGLITPWNYPLLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 159 ALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVM 238
Cdd:PLN02467 168 ATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 239 AnSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDV 318
Cdd:PLN02467 248 T-AAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 319 FDPQTNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDvlKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTY 398
Cdd:PLN02467 327 LEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGK--RPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 399 ESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKS 478
Cdd:PLN02467 405 STEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQ 484
|
.
gi 446011217 479 I 479
Cdd:PLN02467 485 V 485
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
8-479 |
1.69e-155 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 451.58 E-value: 1.69e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQG--QKIWAAMTAMERSRILRRAVDILRERNDE 85
Cdd:PLN02766 22 KLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 86 LAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAP 165
Cdd:PLN02766 102 LAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 166 ALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASS 245
Cdd:PLN02766 182 ALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 246 LKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNF 325
Cdd:PLN02766 262 LKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 326 SPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLkgdgFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVI 405
Cdd:PLN02766 342 GPQVDKQQFEKILSYIEHGKREGATLLTGGKPC----GDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAI 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446011217 406 RRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:PLN02766 418 KKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
27-481 |
1.22e-153 |
|
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: 445.15 E-value: 1.22e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 27 INPANGNVLATVQAAGREDVDRAVKSAQQGQKIWA-AMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVD 105
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGLIPALEGSQ-IPLRETSFVYT----RREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEV 180
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWEFdLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 181 TPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLI 260
Cdd:cd07089 162 TPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMA-QAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 261 VFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRY 340
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 341 IAKGKEEGARVLCGGDvlKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIV 420
Cdd:cd07089 321 IARGRDEGARLVTGGG--RPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446011217 421 TADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
8-483 |
5.43e-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: 439.20 E-value: 5.43e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 88 KLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPAL 167
Cdd:cd07117 82 MVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 168 AAGNAMIFKPSEVTPLTALKLAEIYSEAgLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVmANSAASSLK 247
Cdd:cd07117 162 AAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDV-AIAAAKKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 248 EVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSP 327
Cdd:cd07117 240 PATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 328 LVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRR 407
Cdd:cd07117 320 QVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDM 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446011217 408 ANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQVEM 483
Cdd:cd07117 400 ANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
10-479 |
5.36e-148 |
|
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: 431.29 E-value: 5.36e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 10 YIHGGYTSATSGRtfETINPAN-GNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAK 88
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 89 LETLDTGKAYSEtSTVDIVTGADVLEYYAGLIPALEGSQIP-LRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPAL 167
Cdd:cd07097 82 LLTREEGKTLPE-ARGEVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 168 AAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVmANSAASSLK 247
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRI-AAAAAARGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 248 EVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSP 327
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 328 LVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDgfDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRR 407
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGERLKRP--DEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446011217 408 ANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWIN--TWGESPaEMPVGGYKHSGIG-RENGVMTLQSYTQVKSI 479
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlpTAGVDY-HVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
27-481 |
2.95e-147 |
|
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: 428.49 E-value: 2.95e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 27 INPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEtSTVDI 106
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAE-AQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 107 VTGADVLEYYAGLipALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTAL 186
Cdd:cd07106 81 GGAVAWLRYTASL--DLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 187 KLAEIYSEAgLPDGVFNVLPGGGaETGQYLTEHPGIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVFDDAD 266
Cdd:cd07106 159 KLGELAQEV-LPPGVLNVVSGGD-ELGPALTSHPDIRKISFTGSTATGKKVMA-SAAKTLKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 267 LDLaadIAM---MANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAK 343
Cdd:cd07106 236 IDA---VAPklfWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 344 GKEEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTAD 423
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGY----FIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSD 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446011217 424 LNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07106 389 LERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
27-481 |
2.96e-147 |
|
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: 428.68 E-value: 2.96e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 27 INPANGNVLATVQAAGREDVDRAVKSAQQG--QKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEtSTV 104
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQ-ARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 105 DIVTGADVLEYYAGLIPALEG-SQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPL 183
Cdd:cd07118 81 EIEGAADLWRYAASLARTLHGdSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 184 TALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANsAASSLKEVTMELGGKSPLIVFD 263
Cdd:cd07118 161 TTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAA-AARNLKKVSLELGGKNPQIVFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 264 DADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAK 343
Cdd:cd07118 240 DADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 344 GKEEGARVLCGGDVLkgdGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTAD 423
Cdd:cd07118 320 GRAEGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446011217 424 LNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07118 397 IDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
9-483 |
9.50e-147 |
|
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: 428.49 E-value: 9.50e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 9 LYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQG-QKIWA-AMTAMERSRILRRAVDILRERNDEL 86
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERNLDYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 87 AKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPA 166
Cdd:cd07143 89 ASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 167 LAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSL 246
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 247 KEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFS 326
Cdd:cd07143 249 KKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 327 PLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIR 406
Cdd:cd07143 329 PQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY----FIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446011217 407 RANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQVEM 483
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
10-479 |
3.29e-146 |
|
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: 426.68 E-value: 3.29e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 10 YIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKL 89
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 90 ETLDTGKAYSEtSTVDIVTGADVLEYYAGLIPALEGSQIP---LRETSFVYtrREPLGVVAGIGAWNYPIQIALWKSAPA 166
Cdd:cd07088 81 IVEEQGKTLSL-ARVEVEFTADYIDYMAEWARRIEGEIIPsdrPNENIFIF--KVPIGVVAGILPWNFPFFLIARKLAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 167 LAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANsAASSL 246
Cdd:cd07088 158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEA-AAENI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 247 KEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFS 326
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 327 PLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGfdnGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIR 406
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEK---GYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446011217 407 RANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
8-479 |
1.10e-145 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 428.07 E-value: 1.10e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQG--QKIWAAMTAMERSRILRRAVDILRERNDE 85
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 86 LAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAP 165
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 166 ALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASS 245
Cdd:PLN02466 219 ALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 246 LKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNF 325
Cdd:PLN02466 299 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 326 SPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVI 405
Cdd:PLN02466 379 GPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVI 454
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446011217 406 RRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:PLN02466 455 RRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
26-481 |
1.49e-145 |
|
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: 424.47 E-value: 1.49e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 26 TINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVD 105
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 186 LKLAEIYSEAgLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVFDDA 265
Cdd:cd07108 161 LLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYR-AAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 266 DLDLAADIAMMANFFS-SGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKG 344
Cdd:cd07108 239 DLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 345 KEE-GARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTAD 423
Cdd:cd07108 319 LSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 424 LNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGV--MtLQSYTQVKSIQV 481
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLegM-LEHFTQKKTVNI 457
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
10-481 |
2.81e-142 |
|
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: 417.13 E-value: 2.81e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 10 YIHGGYTSATSGRTFETINPANG-NVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAK 88
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 89 LETLDTGKAYSETSTvDIVTGADVLEYYAGLIPALEG----SQIPlreTSFVYTRREPLGVVAGIGAWNYPIQIALWKSA 164
Cdd:cd07131 82 LVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGetvpSELP---NKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 165 PALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVmANSAAS 244
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERI-GETCAR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 245 SLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTN 324
Cdd:cd07131 237 PNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 325 FSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEV 404
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 405 IRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWIN--TWGeSPAEMPVGGYKHSGIG-RENGVMTLQSYTQVKSIQV 481
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIG-AEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
8-482 |
6.97e-142 |
|
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: 416.51 E-value: 6.97e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQG--QKIWAAMTAMERSRILRRAVDILRERNDE 85
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 86 LAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRET----SFVYTRREPLGVVAGIGAWNYPIQIALW 161
Cdd:cd07140 87 LATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQArpnrNLTLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANS 241
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 242 AASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDP 321
Cdd:cd07140 247 AVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 322 QTNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESE 401
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 402 D--EVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07140 403 DvdGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
...
gi 446011217 480 QVE 482
Cdd:cd07140 483 TIE 485
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
51-481 |
6.01e-140 |
|
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: 407.00 E-value: 6.01e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 51 KSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEtSTVDIVTGADVLEYYAGLIPALEGSQIPL 130
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEE-ALGEVARAIDTFRYAAGLADKLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 131 -RETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGG 209
Cdd:cd06534 80 pDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 210 AETGQYLTEHPGIAKVSFTGGVASGKKVMANsAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNG 289
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKA-AAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 290 TRVFVPAKCKAAFEQKILarveriragdvfdpqtnfsplvsfphrdnvlryiakgkeegarvlcggdvlkgdgfdngawv 369
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV-------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 370 apTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWG-ESP 448
Cdd:cd06534 257 --TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSiGVG 334
|
410 420 430
....*....|....*....|....*....|...
gi 446011217 449 AEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd06534 335 PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
24-481 |
9.13e-136 |
|
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: 399.40 E-value: 9.13e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 24 FETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTG----KAYS 99
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGstygKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 100 ETS-TVDIVTGAdvleyyAGLIPALEGSQIP-LRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP 177
Cdd:cd07150 81 ETTfTPELLRAA------AGECRRVRGETLPsDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 178 SEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVmANSAASSLKEVTMELGGKS 257
Cdd:cd07150 155 SEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREI-AEKAGRHLKKITLELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 258 PLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNV 337
Cdd:cd07150 234 PLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 338 LRYIAKGKEEGARVLCGGDVlkgdgfdNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAA 417
Cdd:cd07150 314 KRQVEDAVAKGAKLLTGGKY-------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446011217 418 GIVTADLNRAHRVIHQLEAGICWIN---TWGESPAemPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07150 387 AILTNDLQRAFKLAERLESGMVHINdptILDEAHV--PFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
45-481 |
6.74e-134 |
|
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: 393.82 E-value: 6.74e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 45 DVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTG----KAYSETS-TVDIVTGAdvleyyAGL 119
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGstrpKAAFEVGaAIAILREA------AGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 120 IPALEGSQIP-LRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLT-ALKLAEIYSEAGL 197
Cdd:cd07104 75 PRRPEGEILPsDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 198 PDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVmANSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMA 277
Cdd:cd07104 155 PKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHI-GELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 278 NFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDV 357
Cdd:cd07104 234 AFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 358 lkgdgfdNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAG 437
Cdd:cd07104 314 -------EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETG 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446011217 438 ICWIN--TWGESPaEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07104 387 MVHINdqTVNDEP-HVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
9-481 |
3.49e-133 |
|
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: 393.73 E-value: 3.49e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 9 LYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQG-QKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 88 KLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGS----QIPL----RETSFvyTRREPLGVVAGIGAWNYPIQIA 159
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGEtlapSIPSmqgeRYTAF--TRREPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 160 LWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGaETGQYLTEHPGIAKVSFTGGVASGKKVmA 239
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKI-G 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 240 NSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVF 319
Cdd:cd07113 238 RQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 320 DPQTNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYE 399
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGY----FVQPTLVLARSADSRLMREETFGPVVSFVPYE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 400 SEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07113 394 DEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
..
gi 446011217 480 QV 481
Cdd:cd07113 474 MI 475
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
24-479 |
6.83e-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: 6.83e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 24 FETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEtST 103
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ-SR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 104 VDIVTGADVLEYYAGLIPALEGSQIPL-----RETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPS 178
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVdayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 179 EVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVmANSAASSLKEVTMELGGKSP 258
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLI-ASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 259 LIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVL 338
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 339 RYIAKGKEEGARVLCGGDVlkgdgfDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAG 418
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446011217 419 IVTADLNRAHRVIHQLEAGICWINtwgESPA----EMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07145 393 VFTNDINRALKVARELEAGGVVIN---DSTRfrwdNLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
10-481 |
1.38e-127 |
|
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: 379.49 E-value: 1.38e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 10 YIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKL 89
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 90 ETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAA 169
Cdd:cd07116 84 ETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 170 GNAMIFKPSEVTPLTALKLAEIYSEAgLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMaNSAASSLKEV 249
Cdd:cd07116 164 GNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIM-QYASENIIPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 250 TMELGGKSPLIVFDDADLD-------LAADIAMMAnfFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQ 322
Cdd:cd07116 242 TLELGGKSPNIFFADVMDAddaffdkALEGFVMFA--LNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 323 TNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDcRDEMTIVREEIFGPVMSLLTYESED 402
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446011217 403 EVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07116 399 EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
8-477 |
4.17e-127 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 379.03 E-value: 4.17e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:PLN02278 26 QGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 88 KLETLDTGKAYSEtSTVDIVTGADVLEYYAGLIPALEGSQIPlreTSFVYTR----REPLGVVAGIGAWNYPIQIALWKS 163
Cdd:PLN02278 106 QLMTLEQGKPLKE-AIGEVAYGASFLEYFAEEAKRVYGDIIP---SPFPDRRllvlKQPVGVVGAITPWNFPLAMITRKV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 164 APALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMAnSAA 243
Cdd:PLN02278 182 GPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMA-GAA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 244 SSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQT 323
Cdd:PLN02278 261 ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 324 NFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKgdgfDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDE 403
Cdd:PLN02278 341 TQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHS----LGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEE 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446011217 404 VIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVK 477
Cdd:PLN02278 417 AIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
6-483 |
9.95e-127 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 378.08 E-value: 9.95e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 6 EQQLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQ--GQKIWAAMTAMERSRILRRAVDILRERN 83
Cdd:PRK09847 19 ENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGvfERGDWSLSSPAKRKAVLNKLADLMEAHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 84 DELAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKS 163
Cdd:PRK09847 99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 164 APALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAA 243
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 244 SSLKEVTMELGGKSPLIVFDDADLDLAADIAMMAN-FFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQ 322
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCPDLQQAASATAAGiFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 323 TNFSPLVSFPHRDNVLRYIAKGKEEGARVLcggdvlkgDGFDNG--AWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYES 400
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLL--------DGRNAGlaAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 401 EDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQ 480
Cdd:PRK09847 411 EEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIW 490
|
...
gi 446011217 481 VEM 483
Cdd:PRK09847 491 ISL 493
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
24-479 |
2.93e-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: 375.01 E-value: 2.93e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 24 FETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETST 103
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 104 -VD--IVTgadvLEYYAGLIPALEGSQIPLR-----ETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIF 175
Cdd:cd07149 81 eVDraIET----LRLSAEEAKRLAGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 176 KPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVmanSAASSLKEVTMELGG 255
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAI---ARKAGLKKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 256 KSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRD 335
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 336 NVLRYIAKGKEEGARVLCGGDVlkgdgfdNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGL 415
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGL 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446011217 416 AAGIVTADLNRAHRVIHQLEAGICWINtwgESPA----EMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07149 387 QAGVFTNDLQKALKAARELEVGGVMIN---DSSTfrvdHMPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
10-481 |
4.60e-124 |
|
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: 370.36 E-value: 4.60e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 10 YIHGGYTSATSGrTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKL 89
Cdd:cd07086 2 VIGGEWVGSGGE-TFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 90 ETLDTGKAYSETSTvDIVTGADVLEYYAGLIPALEGSQIPL-RETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALA 168
Cdd:cd07086 81 VSLEMGKILPEGLG-EVQEMIDICDYAVGLSRMLYGLTIPSeRPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 169 AGNAMIFKPSEVTPLTALKLAEIYSEA----GLPDGVFNVLPGGGaETGQYLTEHPGIAKVSFTGGVASGKKVmANSAAS 244
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRV-GETVAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 245 SLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTN 324
Cdd:cd07086 238 RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 325 FSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLkgDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEV 404
Cdd:cd07086 318 VGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRI--DGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 405 IRRANDTDYGLAAGIVTADLNRAHRVI--HQLEAGICWINTwGESPAE--MPVGGYKHSGIGRENGVMTLQSYTQVKSIQ 480
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAFRWLgpKGSDCGIVNVNI-PTSGAEigGAFGGEKETGGGRESGSDAWKQYMRRSTCT 474
|
.
gi 446011217 481 V 481
Cdd:cd07086 475 I 475
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
13-480 |
1.24e-122 |
|
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: 366.24 E-value: 1.24e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 13 GGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETL 92
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 93 DTGKAYSEtSTVDI-VTGADVLEYyAGLIPALEG----SQIPLREtSFVYtrREPLGVVAGIGAWNYPIQIALWKSAPAL 167
Cdd:cd07151 81 ESGSTRIK-ANIEWgAAMAITREA-ATFPLRMEGrilpSDVPGKE-NRVY--REPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 168 AAGNAMIFKPSEVTPLTA-LKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPgIAKV-SFTGGVASGKKVmANSAASS 245
Cdd:cd07151 156 ALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHP-VPRLiSFTGSTPVGRHI-GELAGRH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 246 LKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNF 325
Cdd:cd07151 234 LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 326 SPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVlkgdgfdNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVI 405
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEAL 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446011217 406 RRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWIN--TWGESPaEMPVGGYKHSGIGRENGVMTLQSYTQVK--SIQ 480
Cdd:cd07151 387 ELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVNDEP-HVPFGGEKNSGLGRFNGEWALEEFTTDKwiSVQ 464
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
9-473 |
1.71e-121 |
|
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: 364.02 E-value: 1.71e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 9 LYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAK 88
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 89 LETLDTGKAYSETSTVDIVTGADVLEYYAGlipalegsQIPLRETSFvyTRREPLGVVAGIGAWNYPIQIALWKSAPALA 168
Cdd:cd07111 104 LESLDNGKPIRESRDCDIPLVARHFYHHAG--------WAQLLDTEL--AGWKPVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 169 AGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAeTGQYLTEHPGIAKVSFTGGVASGKkVMANSAASSLKE 248
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGR-ALRRATAGTGKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 249 VTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPL 328
Cdd:cd07111 252 LSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 329 VSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRA 408
Cdd:cd07111 332 VDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGP----FYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446011217 409 NDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSY 473
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
27-479 |
1.38e-118 |
|
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: 355.38 E-value: 1.38e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 27 INPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEtSTVDI 106
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRAD-AGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 107 VTGADVLEYYAGLIP-ALEGSQIPLRETSFV---YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTP 182
Cdd:cd07099 80 LLALEAIDWAARNAPrVLAPRKVPTGLLMPNkkaTVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 183 LTALKLAEIYSEAGLPDGVFNVLPGGGaETGQYLTEHpGIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVF 262
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDA-GVDKVAFTGSVATGRKVMA-AAAERLIPVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 263 DDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIA 342
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 343 KGKEEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTA 422
Cdd:cd07099 317 DAVAKGAKALTGGARSNGGGP----FYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446011217 423 DLNRAHRVIHQLEAGICWIN--TWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07099 393 DLARAEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
26-479 |
4.33e-116 |
|
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: 349.33 E-value: 4.33e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 26 TINPANGNVLATVQAAGREDVDRAVKSAQQGQK--IWAAmTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEtST 103
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGE-AR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 104 VDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPL 183
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 184 TALKLAEIYSEA-GLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANsAASSLKEVTMELGGKSPLIVF 262
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAA-AAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 263 DDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIA 342
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 343 KGKEEGARVLC-GGDVlkGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVT 421
Cdd:cd07120 318 RAIAAGAEVVLrGGPV--TEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446011217 422 ADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07120 396 RDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
46-481 |
1.12e-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: 347.14 E-value: 1.12e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 46 VDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSE-TSTVDIVtgADVLEYYAGLIPA-L 123
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEaRAEVEKC--AWICRYYAENAEAfL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 124 EGSQIPLrETSFVYTRREPLGVVAGIGAWNYPI-QIALWkSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVF 202
Cdd:cd07100 79 ADEPIET-DAGKAYVRYEPLGVVLGIMPWNFPFwQVFRF-AAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 203 NVLPGGGAETGQyLTEHPGIAKVSFTGGVASGKKVmANSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSS 282
Cdd:cd07100 157 QNLLIDSDQVEA-IIADPRVRGVTLTGSERAGRAV-AAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 283 GQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDG 362
Cdd:cd07100 235 GQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 363 fdngAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWIN 442
Cdd:cd07100 315 ----AFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 446011217 443 TWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07100 391 GMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
25-479 |
5.96e-114 |
|
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: 343.65 E-value: 5.96e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 25 ETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETsTV 104
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-RV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 105 DIVTGADVLEYYAGLIPALEGSQIPL-----RETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSE 179
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLdatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 180 VTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAassLKEVTMELGGKSPL 259
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 260 IVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLR 339
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 340 YIAKGKEEGARVLCGGDVlkgdgfdNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGI 419
Cdd:cd07094 318 WVEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGI 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446011217 420 VTADLNRAHRVIHQLEAGICWINtwgESPA----EMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07094 391 FTRDLNVAFKAAEKLEVGGVMVN---DSSAfrtdWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
45-479 |
2.15e-111 |
|
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: 336.47 E-value: 2.15e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 45 DVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGkAYSETSTVDIVTGADVLEYYAGLIPALE 124
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG-ATAAWAGFNVDLAAGMLREAASLITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 125 GSQIP-LRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFN 203
Cdd:cd07105 80 GGSIPsDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 204 VL---PGGGAETGQYLTEHPGIAKVSFTGGVASGKKVmANSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFF 280
Cdd:cd07105 160 VVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRII-AETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 281 SSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPqtnfsPLVSFPHRDNVLRYIAKGKEEGARVLCGGdvlKG 360
Cdd:cd07105 239 NSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVLG-----SLVSAAAADRVKELVDDALSKGAKLVVGG---LA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 361 DGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICW 440
Cdd:cd07105 311 DESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446011217 441 IN--TWGESPAeMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07105 391 INgmTVHDEPT-LPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
20-479 |
2.97e-110 |
|
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: 336.12 E-value: 2.97e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 20 SGRTFETINPAN-GNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAY 98
Cdd:cd07124 44 TEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNW 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 99 SEtSTVDIVTGADVLEYYAGLIPALEG---SQIPLRETSFVYtrrEPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIF 175
Cdd:cd07124 124 AE-ADADVAEAIDFLEYYAREMLRLRGfpvEMVPGEDNRYVY---RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 176 KPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASS-----LKEVT 250
Cdd:cd07124 200 KPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQpgqkwLKRVI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 251 MELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVS 330
Cdd:cd07124 280 AEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVID 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 331 FPHRDNVLRYIAKGKEEGaRVLCGGDVLkgDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRAND 410
Cdd:cd07124 360 KGARDRIRRYIEIGKSEG-RLLLGGEVL--ELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIAND 436
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446011217 411 TDYGLAAGIVTADLNRAHRVIHQLEAGICWIN--TWGESPAEMPVGGYKHSGIG-RENGVMTLQSYTQVKSI 479
Cdd:cd07124 437 TEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGTGsKAGGPDYLLQFMQPKTV 508
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
8-479 |
3.56e-107 |
|
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: 327.17 E-value: 3.56e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 88 KLETLDTGKAYSEtSTVDIVTGADVLEYYAGLIPALEGsqiplrETSFV-------YTRREPLGVVAGIGAWNYPIQIAL 160
Cdd:cd07085 82 RLITLEHGKTLAD-ARGDVLRGLEVVEFACSIPHLLKG------EYLENvargidtYSYRQPLGVVAGITPFNFPAMIPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGaETGQYLTEHPGIAKVSFTGGVASGKKVMAN 240
Cdd:cd07085 155 WMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGK-EAVNALLDHPDIKAVSFVGSTPVGEYIYER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 241 SAASSlKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVC-TNGTRVFVPAKCKAaFEQKILARVERIRAGDVF 319
Cdd:cd07085 234 AAANG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCmALSVAVAVGDEADE-WIPKLVERAKKLKVGAGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 320 DPQTNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYE 399
Cdd:cd07085 312 DPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 400 SEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEM-PVGGYKHSGIGREN--GVMTLQSYTQV 476
Cdd:cd07085 392 TLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFfSFGGWKGSFFGDLHfyGKDGVRFYTQT 471
|
...
gi 446011217 477 KSI 479
Cdd:cd07085 472 KTV 474
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
2-477 |
1.92e-105 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 323.01 E-value: 1.92e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 2 SRMAEQQLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRE 81
Cdd:PRK11241 6 STLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMME 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 82 RNDELAKLETLDTGKAYSETSTvDIVTGADVLEYYAGLIPALEGSQIPLRET-SFVYTRREPLGVVAGIGAWNYPIQIAL 160
Cdd:PRK11241 86 HQDDLARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPGHQAdKRLIVIKQPIGVTAAITPWNFPAAMIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMAn 240
Cdd:PRK11241 165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLME- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 241 SAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFD 320
Cdd:PRK11241 244 QCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 321 PQTNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGD--VLKGDGFDngawvaPTVFTDCRDEMTIVREEIFGPVMSLLTY 398
Cdd:PRK11241 324 KGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKahELGGNFFQ------PTILVDVPANAKVAKEETFGPLAPLFRF 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446011217 399 ESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVK 477
Cdd:PRK11241 398 KDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
18-479 |
5.95e-105 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 322.98 E-value: 5.95e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 18 ATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGK- 96
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 97 ---AYSETSTVDIVTGadvleYYAGLIPALEGSQ-----IPLRETSFVYtrREPLGVVAGIGAWNYPIQIALWKSAPALA 168
Cdd:PRK09407 108 rrhAFEEVLDVALTAR-----YYARRAPKLLAPRrragaLPVLTKTTEL--RQPKGVVGVISPWNYPLTLAVSDAIPALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 169 AGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHpgIAKVSFTGGVASGKKVmANSAASSLKE 248
Cdd:PRK09407 181 AGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVL-AEQAGRRLIG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 249 VTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPL 328
Cdd:PRK09407 258 FSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 329 VSFPHRDNVLRYIAKGKEEGARVLCGG----DVlkGDGFdngawVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEV 404
Cdd:PRK09407 338 ISEAQLETVSAHVDDAVAKGATVLAGGkarpDL--GPLF-----YEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 405 IRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWIN-----TWGESPAemPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:PRK09407 411 VERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVDA--PMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
27-481 |
5.58e-104 |
|
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: 318.10 E-value: 5.58e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 27 INPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGK----AYSETS 102
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKarrhAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 103 TVDIVTgadvlEYYAGLIPAL-----EGSQIPLRETSFVYtrREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP 177
Cdd:cd07101 81 DVAIVA-----RYYARRAERLlkprrRRGAIPVLTRTTVN--RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 178 SEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIakVSFTGGVASGKKVmANSAASSLKEVTMELGGKS 257
Cdd:cd07101 154 DSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVV-AERAGRRLIGCSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 258 PLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNV 337
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 338 LRYIAKGKEEGARVLCGG----DVlkGDGFdngawVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDY 413
Cdd:cd07101 311 TAHVDDAVAKGATVLAGGrarpDL--GPYF-----YEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDY 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446011217 414 GLAAGIVTADLNRAHRVIHQLEAGICWIN-----TWGESPAemPVGGYKHSGIGRENGVMTLQSYTQVKSIQV 481
Cdd:cd07101 384 GLNASVWTRDGARGRRIAARLRAGTVNVNegyaaAWASIDA--PMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
25-479 |
1.36e-102 |
|
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: 314.30 E-value: 1.36e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 25 ETINPANGNVLATVQAAGREDVDRAVKSAQQGQKiwaAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETStV 104
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR-Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 105 DIVTGADVLEYYAGLIPALEGSQIPL-----RETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSE 179
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCdltanGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 180 VTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVmanSAASSLKEVTMELGGKSPL 259
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 260 IVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLR 339
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 340 YIAKGKEEGARVLCGGDvlkgdgfDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGI 419
Cdd:cd07146 315 RVEEAIAQGARVLLGNQ-------RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446011217 420 VTADLNRAHRVIHQLEAGICwiNTWgESP---AEM-PVGGYKHSGIGRENGVM-TLQSYTQVKSI 479
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTV--NVN-EVPgfrSELsPFGGVKDSGLGGKEGVReAMKEMTNVKTY 449
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
27-479 |
3.44e-102 |
|
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: 313.41 E-value: 3.44e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 27 INPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTvDI 106
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG-EI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 107 VTGADVLEYYAGLIPALEGSQIPLRETSFV-YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:cd07102 80 RGMLERARYMISIAEEALADIRVPEKDGFErYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 186 LKLAEIYSEAGLPDGVFNVLPGGGaETGQYLTEHPGIAKVSFTGGVASGKKVmANSAASSLKEVTMELGGKSPLIVFDDA 265
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSH-ETSAALIADPRIDHVSFTGSVAGGRAI-QRAAAGRFIKVGLELGGKDPAYVRPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 266 DLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGK 345
Cdd:cd07102 238 DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 346 EEGARVLCGGDVLKgDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLN 425
Cdd:cd07102 318 AKGARALIDGALFP-EDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 446011217 426 RAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07102 397 RAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
32-475 |
9.09e-100 |
|
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: 306.91 E-value: 9.09e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 32 GNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTG----KAYSETSTvdiv 107
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGsirpKAGFEVGA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 108 tGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTA-L 186
Cdd:cd07152 77 -AIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 187 KLAEIYSEAGLPDGVFNVLPGGgAETGQYLTEHPGIAKVSFTGGVASGKKVMANsAASSLKEVTMELGGKSPLIVFDDAD 266
Cdd:cd07152 156 VIARLFEEAGLPAGVLHVLPGG-ADAGEALVEDPNVAMISFTGSTAVGRKVGEA-AGRHLKKVSLELGGKNALIVLDDAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 267 LDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGKE 346
Cdd:cd07152 234 LDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 347 EGARVLCGGDVlkgdgfdNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNR 426
Cdd:cd07152 314 AGARLEAGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGR 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446011217 427 AHRVIHQLEAGICWIN--TWGESPaEMPVGGYKHSGIG-RENGVMTLQSYTQ 475
Cdd:cd07152 387 AMALADRLRTGMLHINdqTVNDEP-HNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
24-478 |
6.19e-98 |
|
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: 302.63 E-value: 6.19e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 24 FETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEtST 103
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD-AR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 104 VDIVTGADVLEYYAGLIPALEGSQIPLrETS------FVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP 177
Cdd:cd07147 80 GEVARAIDTFRIAAEEATRIYGEVLPL-DISargegrQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 178 SEVTPLTALKLAEIYSEAGLPDGVFNVLPgGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAAsslKEVTMELGGKS 257
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFSVLP-CSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 258 PLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNV 337
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 338 LRYIAKGKEEGARVLCGGDVlkgdgfdNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAA 417
Cdd:cd07147 315 EGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446011217 418 GIVTADLNRAHRVIHQLEAGICWINtwgESPA----EMPVGGYKHSGIGRENGVMTLQSYTQVKS 478
Cdd:cd07147 388 GVFTRDLEKALRAWDELEVGGVVIN---DVPTfrvdHMPYGGVKDSGIGREGVRYAIEEMTEPRL 449
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-479 |
3.16e-93 |
|
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: 290.74 E-value: 3.16e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 28 NPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVDIV 107
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 108 TGADVLEYyagLIPALEGSQIP-LRETSFV------YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEV 180
Cdd:cd07098 82 VTCEKIRW---TLKHGEKALRPeSRPGGLLmfykraRVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 181 TPLTALKLAEIYSEA----GLPDGVFNVLPGGGaETGQYLTEHPGIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGK 256
Cdd:cd07098 159 VAWSSGFFLSIIREClaacGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMA-AAAESLTPVVLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 257 SPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDN 336
Cdd:cd07098 237 DPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 337 VLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLA 416
Cdd:cd07098 317 LEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446011217 417 AGIVTADLNRAHRVIHQLEAGICWINTWGES--PAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSV 461
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
20-479 |
6.03e-91 |
|
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: 285.23 E-value: 6.03e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 20 SGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAA-MTAMERSRILRRAVDILRERNDELAKLETLDTGKAY 98
Cdd:cd07082 14 SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 99 SEtSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFV-----YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAM 173
Cdd:cd07082 94 KD-ALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTkgkiaQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 174 IFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMansAASSLKEVTMEL 253
Cdd:cd07082 173 VFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLK---KQHPMKRLVLEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 254 GGKSPLIVFddadldLAADIAMMAN-----FFS-SGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSP 327
Cdd:cd07082 250 GGKDPAIVL------PDADLELAAKeivkgALSySGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 328 LVSFPHRDNVLRYIAKGKEEGARVLCGGdvlkgdGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRR 407
Cdd:cd07082 324 LIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446011217 408 ANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGE-SPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrGPDHFPFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
72-480 |
6.73e-88 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 275.08 E-value: 6.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 72 LRRAVDILRERNDELAKLETLDTGKAYSETStVDIVTGADVLEYYAGLIPALEGSQIP---LRETSFVYTRrePLGVVAG 148
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAE-VEVAFTADYIDYMAEWARRYEGEIIQsdrPGENILLFKR--ALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 149 IGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFT 228
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 229 GGVASGKKVMAnSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILA 308
Cdd:PRK10090 158 GSVSAGEKIMA-AAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 309 RVERIRAGDVFD-PQTNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREE 387
Cdd:PRK10090 237 AMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGY----YYPPTLLLDVRQEMSIMHEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 388 IFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTwgESPAEMP--VGGYKHSGIGREN 465
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR--ENFEAMQgfHAGWRKSGIGGAD 390
|
410
....*....|....*..
gi 446011217 466 GVMTLQSY--TQVKSIQ 480
Cdd:PRK10090 391 GKHGLHEYlqTQVVYLQ 407
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
8-479 |
6.16e-87 |
|
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: 274.84 E-value: 6.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 88 KLETLDTGKAYSETSTvDIVTGADVLEYYAGLIPALEGSQIPLRETSF-VYTRREPLGVVAGIGAWNYPIQIALWKSAPA 166
Cdd:TIGR01722 82 ELITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETSTQVATRVdVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 167 LAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLpGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSl 246
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVV-HGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 247 KEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEqKILARVERIRAGDVFDPQTNFS 326
Cdd:TIGR01722 239 KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAADEWVP-EIRERAEKIRIGPGDDPGAEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 327 PLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIR 406
Cdd:TIGR01722 318 PLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 407 RANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTwgesPAEMPV-----GGYKHSGIGREN--GVMTLQSYTQVKSI 479
Cdd:TIGR01722 398 LINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV----PIPVPLpyfsfTGWKDSFFGDHHiyGKQGTHFYTRGKTV 473
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
19-460 |
6.69e-87 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 276.05 E-value: 6.69e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 19 TSGRTFETINPAN-GNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKA 97
Cdd:PRK03137 47 TTEDKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 98 YSETStVDIVTGADVLEYYA----GLIPALEGSQIPLRETSFVYtrrEPLGVVAGIGAWNYPIQIALWKSAPALAAGNAM 173
Cdd:PRK03137 127 WAEAD-ADTAEAIDFLEYYArqmlKLADGKPVESRPGEHNRYFY---IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 174 IFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASS-----LKE 248
Cdd:PRK03137 203 LLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQpgqiwLKR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 249 VTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPqTNFSPL 328
Cdd:PRK03137 283 VIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN-AYMGPV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 329 VSFPHRDNVLRYIAKGKEEGaRVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRA 408
Cdd:PRK03137 362 INQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGY----FIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIA 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446011217 409 NDTDYGLAAGIVTAD---LNRAHRVIHqleAGICWIN---TwGESPAEMPVGGYKHSG 460
Cdd:PRK03137 437 NNTEYGLTGAVISNNrehLEKARREFH---VGNLYFNrgcT-GAIVGYHPFGGFNMSG 490
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
26-464 |
2.10e-84 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 267.76 E-value: 2.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 26 TINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSeTSTVD 105
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLA-SAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGLIPAL---EGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTP 182
Cdd:PRK09406 84 ALKCAKGFRYYAEHAEALladEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 183 LTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEhPGIAKVSFTGGVASGKKVmANSAASSLKEVTMELGGKSPLIVF 262
Cdd:PRK09406 164 QTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRD-PRVAAATLTGSEPAGRAV-AAIAGDEIKKTVLELGGSDPFIVM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 263 DDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIA 342
Cdd:PRK09406 242 PSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 343 KGKEEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTA 422
Cdd:PRK09406 322 DAVAAGATILCGGKRPDGPGW----FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446011217 423 DLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRE 464
Cdd:PRK09406 398 DEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRE 439
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
26-479 |
2.67e-78 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 252.09 E-value: 2.67e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 26 TINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEtSTVD 105
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQ-ARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:PRK13968 90 VAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 186 LKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEhPGIAKVSFTGGVASGKKVMANSAASsLKEVTMELGGKSPLIVFDDA 265
Cdd:PRK13968 170 QLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDPFIVLNDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 266 DLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGK 345
Cdd:PRK13968 248 DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 346 EEGARVLCGGDVLKGDgfdnGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLN 425
Cdd:PRK13968 328 AEGARLLLGGEKIAGA----GNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 446011217 426 RAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:PRK13968 404 QARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
20-466 |
1.38e-77 |
|
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: 250.59 E-value: 1.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 20 SGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYS 99
Cdd:cd07130 10 GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 100 EtstvdivtGA-------DVLEYYAGLIPALEGSQIPL-RETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGN 171
Cdd:cd07130 90 E--------GLgevqemiDICDFAVGLSRQLYGLTIPSeRPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 172 AMIFKPSEVTPLTALKLAEIYSEA----GLPDGVFNVLPgGGAETGQYLTEHPGIAKVSFTGGVASGKKVmANSAASSLK 247
Cdd:cd07130 162 VVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVC-GGADVGEALVKDPRVPLVSFTGSTAVGRQV-GQAVAARFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 248 EVTMELGGKSPLIVFddadLDLAADIAMMANFFS----SGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQT 323
Cdd:cd07130 240 RSLLELGGNNAIIVM----EDADLDLAVRAVLFAavgtAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 324 NFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFdngaWVAPTVFTDCRDeMTIVREEIFGPVMSLLTYESEDE 403
Cdd:cd07130 316 LVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGN----YVEPTIVEGLSD-APIVKEETFAPILYVLKFDTLEE 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446011217 404 VIRRANDTDYGLAAGIVTADLNRAHRVIHQL--EAGICWINTwGESPAEM--PVGGYKHSGIGRENG 466
Cdd:cd07130 391 AIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNI-GTSGAEIggAFGGEKETGGGRESG 456
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
45-463 |
1.24e-75 |
|
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: 244.10 E-value: 1.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 45 DVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETST-VDIVTG-----ADVLEYYAG 118
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTeVAAMAGkidisIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 119 lIPALEGSQIPLRetsfvyTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLP 198
Cdd:cd07095 81 -ERATPMAQGRAV------LRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 199 DGVFNVLPGGGaETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMAN 278
Cdd:cd07095 154 PGVLNLVQGGR-ETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 279 FFSSGQVCTNGTRVFVPAKCKA-AFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGKEEGARVLcggdv 357
Cdd:cd07095 233 FLTAGQRCTCARRLIVPDGAVGdAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 358 LKGDGFD-NGAWVAPTVFtDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEA 436
Cdd:cd07095 308 LAMERLVaGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRA 386
|
410 420
....*....|....*....|....*....
gi 446011217 437 GICWIN--TWGeSPAEMPVGGYKHSGIGR 463
Cdd:cd07095 387 GIVNWNrpTTG-ASSTAPFGGVGLSGNHR 414
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
25-462 |
2.48e-71 |
|
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: 233.46 E-value: 2.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 25 ETINPANGNVLATVQAAGREDVDRAVKSAQQ---GQKIWAAmtAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEt 101
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHAlflDRNNWLP--AHERIAILERLADLMEERADELALLIAREGGKPLVD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 102 STVDIVTGADVLEYYAGLIPALEGSQIP--LRETS---FVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFK 176
Cdd:cd07148 79 AKVEVTRAIDGVELAADELGQLGGREIPmgLTPASagrIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 177 PSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGgAETGQYLTEHPGIAKVSFTGGVASGkkVMANSAASSLKEVTMELGGK 256
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCE-NAVAEKLVTDPRVAFFSFIGSARVG--WMLRSKLAPGTRCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 257 SPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDN 336
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 337 VLRYIAKGKEEGARVLCGGDVLKGDGFdngawvAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLA 416
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRLSDTTY------APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQ 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 446011217 417 AGIVTADLNRAHRVIHQLEAGICWINT-------WgespaeMPVGGYKHSGIG 462
Cdd:cd07148 390 AAVFTKDLDVALKAVRRLDATAVMVNDhtafrvdW------MPFAGRRQSGYG 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
27-466 |
1.60e-69 |
|
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: 230.55 E-value: 1.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 27 INPANGN-VLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETsTVD 105
Cdd:cd07125 51 IDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADA-DAE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGL------IPALEGSQIPLRETSFvytrrEPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSE 179
Cdd:cd07125 130 VREAIDFCRYYAAQarelfsDPELPGPTGELNGLEL-----HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 180 VTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVmaNSAASSLKEVTM----ELGG 255
Cdd:cd07125 205 QTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLI--NRALAERDGPILpliaETGG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 256 KSPLIVFDDADLDLAADIAMMANFFSSGQVCTnGTRV-FVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHR 334
Cdd:cd07125 283 KNAMIVDSTALPEQAVKDVVQSAFGSAGQRCS-ALRLlYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 335 DNVLRYIAKGKEEgARVLCGGDVLKGDGFdngaWVAPTVFTDcrDEMTIVREEIFGPVMSLLTYESE--DEVIRRANDTD 412
Cdd:cd07125 362 KLLRAHTELMRGE-AWLIAPAPLDDGNGY----FVAPGIIEI--VGIFDLTTEVFGPILHVIRFKAEdlDEAIEDINATG 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446011217 413 YGLAAGIVTADLNRAHRVIHQLEAGICWIN--TWGESPAEMPVGGYKHSGIGRENG 466
Cdd:cd07125 435 YGLTLGIHSRDEREIEYWRERVEAGNLYINrnITGAIVGRQPFGGWGLSGTGPKAG 490
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
27-466 |
4.53e-68 |
|
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: 226.31 E-value: 4.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 27 INPAN-GNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTvD 105
Cdd:cd07083 37 VSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAID-D 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGLIPALEGSQ-----IPLRETSFVYtrrEPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEV 180
Cdd:cd07083 116 VAEAIDFIRYYARAALRLRYPAvevvpYPGEDNESFY---VGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAED 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 181 TPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKV---MANSAA--SSLKEVTMELGG 255
Cdd:cd07083 193 AVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIyeaAARLAPgqTWFKRLYVETGG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 256 KSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRD 335
Cdd:cd07083 273 KNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 336 NVLRYIAKGKEEGaRVLCGGDVLKGDGFdngaWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESED--EVIRRANDTDY 413
Cdd:cd07083 353 KVLSYIEHGKNEG-QLVLGGKRLEGEGY----FVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPY 427
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446011217 414 GLAAGIVTADLNRAHRVIHQLEAGICWIN--TWGESPAEMPVGGYKHSGIGRENG 466
Cdd:cd07083 428 GLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFKLSGTNAKTG 482
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
9-460 |
1.64e-67 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 224.45 E-value: 1.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 9 LYIHGGYTsATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAK 88
Cdd:PRK09457 3 LWINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 89 LETLDTGKAYSETST-VDIVTG--ADVLEYYAGLIPalEGSQIPLRETSFVytRREPLGVVAGIGAWNYPIQIALWKSAP 165
Cdd:PRK09457 82 VIARETGKPLWEAATeVTAMINkiAISIQAYHERTG--EKRSEMADGAAVL--RHRPHGVVAVFGPYNFPGHLPNGHIVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 166 ALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPgGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASS 245
Cdd:PRK09457 158 ALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQ-GGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 246 LKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPakcKAAFEQKILARV----ERIRAGDVF-D 320
Cdd:PRK09457 237 EKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVP---QGAQGDAFLARLvavaKRLTVGRWDaE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 321 PQTNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDgfdnGAWVAPTVFtdcrdEMTIVR----EEIFGPVMSLL 396
Cdd:PRK09457 314 PQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAG----TGLLTPGII-----DVTGVAelpdEEYFGPLLQVV 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446011217 397 TYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGIcwIN----TWGESPAeMPVGGYKHSG 460
Cdd:PRK09457 385 RYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGI--VNwnkpLTGASSA-APFGGVGASG 449
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
10-485 |
3.98e-66 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 221.17 E-value: 3.98e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 10 YIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKL 89
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 90 ETLDTGKAySETSTVDIVTGADVLEYYA--GLIPALEGSQI-----PLRE-TSFVYTRREPLGVVAGIGAWNYPIQIALW 161
Cdd:PLN00412 99 LVKEIAKP-AKDAVTEVVRSGDLISYTAeeGVRILGEGKFLvsdsfPGNErNKYCLTSKIPLGVVLAIPPFNYPVNLAVS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASgkkvMANS 241
Cdd:PLN00412 178 KIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDTG----IAIS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 242 AASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDp 321
Cdd:PLN00412 254 KKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 322 QTNFSPLVSFPHRDNVLRYIAKGKEEGARvLCggDVLKGDGfdNGAWvaPTVFTDCRDEMTIVREEIFGPVMSLLTYESE 401
Cdd:PLN00412 333 DCDITPVVSESSANFIEGLVMDAKEKGAT-FC--QEWKREG--NLIW--PLLLDNVRPDMRIAWEEPFGPVLPVIRINSV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 402 DEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTW-GESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQ 480
Cdd:PLN00412 406 EEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKSTV 485
|
....*
gi 446011217 481 VEMAK 485
Cdd:PLN00412 486 INLPK 490
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
11-479 |
1.42e-62 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 214.23 E-value: 1.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 11 IHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLE 90
Cdd:PLN02419 118 IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 91 TLDTGKAYSEtSTVDIVTGADVLEYYAGLIPALEGSQIP-LRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAA 169
Cdd:PLN02419 198 TTEQGKTLKD-SHGDIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTC 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 170 GNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGaETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSlKEV 249
Cdd:PLN02419 277 GNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTN-DTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKG-KRI 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 250 TMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKaAFEQKILARVERIRAGDVFDPQTNFSPLV 329
Cdd:PLN02419 355 QSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAK-SWEDKLVERAKALKVTCGSEPDADLGPVI 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 330 SFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRAN 409
Cdd:PLN02419 434 SKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIIN 513
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446011217 410 DTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTwgESPAEMP---VGGYKHSGIGREN--GVMTLQSYTQVKSI 479
Cdd:PLN02419 514 KNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPffsFTGNKASFAGDLNfyGKAGVDFFTQIKLV 586
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
48-467 |
8.26e-61 |
|
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: 205.15 E-value: 8.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 48 RAVKSAQQGQKI-WAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEtstVDIVTGADVLEYYAGLIPALEGS 126
Cdd:cd07134 1 RRVFAAQQAHALaLRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAE---VDLTEILPVLSEINHAIKHLKKW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 127 QIPLRETSFV-------YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPD 199
Cdd:cd07134 78 MKPKRVRTPLllfgtksKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 200 GVFNVlpGGGAETGQYLTEHPgIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANF 279
Cdd:cd07134 158 EVAVF--EGDAEVAQALLELP-FDHIFFTGSPAVGKIVMA-AAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 280 FSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQT-NFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVL 358
Cdd:cd07134 234 LNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 359 KGDGFdngawVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGI 438
Cdd:cd07134 314 AAQRY-----IAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGG 388
|
410 420 430
....*....|....*....|....*....|.
gi 446011217 439 CWINTWGESPAE--MPVGGYKHSGIGRENGV 467
Cdd:cd07134 389 VVVNDVVLHFLNpnLPFGGVNNSGIGSYHGV 419
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
68-479 |
2.04e-59 |
|
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: 201.60 E-value: 2.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 68 RSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVDIVTGADVLEYYaglIPALEGSQIPLR-ETSFV------YTRR 140
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHA---LKHLKKWMKPRRvSVPLLlqpakaYVIP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 141 EPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAgLPDGVFNVLPGGGAETgQYLTEHP 220
Cdd:cd07087 99 EPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVA-TALLAEP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 221 gIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKA 300
Cdd:cd07087 177 -FDHIFFTGSPAVGKIVME-AAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 301 AFEQKIlarVERIRA--GDvfDPQ--TNFSPLVSFPHRDNVLRYIAKGKeegarVLCGGDVLKGDGFdngawVAPTVFTD 376
Cdd:cd07087 255 ELIEEL---KKAIKEfyGE--DPKesPDYGRIINERHFDRLASLLDDGK-----VVIGGQVDKEERY-----IAPTILDD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 377 CRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWIN------TwgeSPaE 450
Cdd:cd07087 320 VSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvllhaA---IP-N 395
|
410 420
....*....|....*....|....*....
gi 446011217 451 MPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07087 396 LPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
64-463 |
4.09e-58 |
|
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: 198.09 E-value: 4.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 64 TAMERSRILRRAVDILRERNDELAKLETLDTG-KAYSETSTVDIVTGADVLEYYAG-----LIPALEGSQIPLRETSfVY 137
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLLAEILPSIAGIKHARKhlkkwMKPSRRHVGLLFLPAK-AE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 138 TRREPLGVVAGIGAWNYPIQIALWKSAPALAAGN-AMIfKPSEVTPLTALKLAEIYSEAGLPDGVFNVLpgGGAETGQYL 216
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNrVMI-KPSEFTPRTSALLAELLAEYFDEDEVAVVT--GGADVAAAF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 217 TEHPgIAKVSFTGGVASGKKVMANsAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPA 296
Cdd:cd07133 174 SSLP-FDHLLFTGSTAVGRHVMRA-AAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 297 KCKAAFEQKILARVERiRAGDVFDPQtNFSPLVSFPHRDNVLRYIAKGKEEGARVL-CGGDvlkGDGFDNGAWVAPTVFT 375
Cdd:cd07133 252 DKLEEFVAAAKAAVAK-MYPTLADNP-DYTSIINERHYARLQGLLEDARAKGARVIeLNPA---GEDFAATRKLPPTLVL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 376 DCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGE--SPAEMPV 453
Cdd:cd07133 327 NVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLhvAQDDLPF 406
|
410
....*....|
gi 446011217 454 GGYKHSGIGR 463
Cdd:cd07133 407 GGVGASGMGA 416
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
137-479 |
5.28e-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: 182.03 E-value: 5.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 137 YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAgLPDGVFNVLPGGGAETGQYL 216
Cdd:cd07135 103 RIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 217 TEHPGiaKVSFTGGVASGKKVmANSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPA 296
Cdd:cd07135 182 EQKFD--KIFYTGSGRVGRII-AEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 297 KCKAAFEQKiLARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGKeegarvlcgGDVLKGDGFDNGA-WVAPTVFT 375
Cdd:cd07135 259 SVYDEFVEE-LKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTK---------GKVVIGGEMDEATrFIPPTIVS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 376 DCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGE--SPAEMPV 453
Cdd:cd07135 329 DVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPF 408
|
330 340
....*....|....*....|....*.
gi 446011217 454 GGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07135 409 GGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
20-442 |
1.95e-50 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 185.02 E-value: 1.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 20 SGRTFETINPANG-NVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAY 98
Cdd:PRK11904 560 EGEARPVVSPADRrRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 99 SETstVDIVTGA-DVLEYYAGLIPALEGSQIPLR----ETSFVytRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAM 173
Cdd:PRK11904 640 QDA--IAEVREAvDFCRYYAAQARRLFGAPEKLPgptgESNEL--RLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTV 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 174 IFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSLKEVTM-- 251
Cdd:PRK11904 716 IAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVPLia 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 252 ELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTnGTRV-FVPAK---------CKAAFEQKIlarveriraGDVFDP 321
Cdd:PRK11904 796 ETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCS-ALRVlFVQEDiadrviemlKGAMAELKV---------GDPRLL 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 322 QTNFSPLVSFPHRDNVLRYIAKGKEEgARVLCGGDVlkGDGFDNGAWVAPTVFTdcRDEMTIVREEIFGPVMSLLTYESE 401
Cdd:PRK11904 866 STDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPL--PAGTENGHFVAPTAFE--IDSISQLEREVFGPILHVIRYKAS 940
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446011217 402 --DEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWIN 442
Cdd:PRK11904 941 dlDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
27-477 |
5.57e-50 |
|
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: 178.18 E-value: 5.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 27 INPAN-GNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEtSTVD 105
Cdd:TIGR01238 56 TNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHN-AIAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGLIpalegsqiplrETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:TIGR01238 135 VREAVDFCRYYAKQV-----------RDVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 186 LKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSLKEVTM--ELGGKSPLIVFD 263
Cdd:TIGR01238 204 YRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 264 DADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAK 343
Cdd:TIGR01238 284 TALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEH 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 344 GKEEGARVlcgGDVLKGDGFD--NGAWVAPTVFTdcRDEMTIVREEIFGPVMSLLTYESE--DEVIRRANDTDYGLAAGI 419
Cdd:TIGR01238 364 MSQTQKKI---AQLTLDDSRAcqHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKARelDQIVDQINQTGYGLTMGV 438
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446011217 420 VTADLNRAHRVIHQLEAGICWIN--TWGESPAEMPVGGYKHSGIG-RENGVMTLQSYTQVK 477
Cdd:TIGR01238 439 HSRIETTYRWIEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
18-442 |
4.28e-49 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 181.29 E-value: 4.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 18 ATSGRTFETINPANGN-VLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGK 96
Cdd:COG4230 566 AASGEARPVRNPADHSdVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGK 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 97 ----AYSEtstvdiVTGA-DVLEYYAGLIPALEGSQIPLRetsfvytrrePLGVVAGIGAWNYPIQIALWKSAPALAAGN 171
Cdd:COG4230 646 tlpdAIAE------VREAvDFCRYYAAQARRLFAAPTVLR----------GRGVFVCISPWNFPLAIFTGQVAAALAAGN 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 172 AMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSLKEVTM 251
Cdd:COG4230 710 TVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVPL 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 252 --ELGGKSPLIVfddadldlaadiAMMANFFSSGQVCtNGTRV-FVPAKCkaafEQKILARV----ERIRAGDVFDPQTN 324
Cdd:COG4230 790 iaETGGQNAMIVdssalpeqvvddVLASAFDSAGQRC-SALRVlCVQEDI----ADRVLEMLkgamAELRVGDPADLSTD 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 325 FSPLVSFPHRDNVLRYIAKGKEEGaRVLCGGDVlkGDGFDNGAWVAPTVFT-DCRDEMTivrEEIFGPVMSLLTYESE-- 401
Cdd:COG4230 865 VGPVIDAEARANLEAHIERMRAEG-RLVHQLPL--PEECANGTFVAPTLIEiDSISDLE---REVFGPVLHVVRYKADel 938
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446011217 402 DEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWIN 442
Cdd:COG4230 939 DKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
20-473 |
1.18e-48 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 174.64 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 20 SGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYS 99
Cdd:PLN02315 32 NGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 100 EtSTVDIVTGADVLEYYAGLIPALEGSQIPL-RETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPS 178
Cdd:PLN02315 112 E-GIGEVQEIIDMCDFAVGLSRQLNGSIIPSeRPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 179 EVTPLTALKL----AEIYSEAGLPDGVFNVLpGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSLKEVtMELG 254
Cdd:PLN02315 191 PTTPLITIAMtklvAEVLEKNNLPGAIFTSF-CGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCL-LELS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 255 GKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHR 334
Cdd:PLN02315 269 GNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 335 DNVLRYIAKGKEEGARVLCGGDVLKGDgfdnGAWVAPTVfTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYG 414
Cdd:PLN02315 349 KNFEKGIEIIKSQGGKILTGGSAIESE----GNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQG 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446011217 415 LAAGIVTadlnRAHRVI------HQLEAGICWIN--TWGespAEM--PVGGYKHSGIGRENGVMTLQSY 473
Cdd:PLN02315 424 LSSSIFT----RNPETIfkwigpLGSDCGIVNVNipTNG---AEIggAFGGEKATGGGREAGSDSWKQY 485
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
17-442 |
4.21e-48 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 178.52 E-value: 4.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 17 SATSGRTFETINPAN-GNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTG 95
Cdd:PRK11905 562 GDVDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 96 KAYSETstVDIVTGA-DVLEYYAglipalegSQIplrETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMI 174
Cdd:PRK11905 642 KTLANA--IAEVREAvDFLRYYA--------AQA---RRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVL 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 175 FKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSLKEVTM--E 252
Cdd:PRK11905 709 AKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaE 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 253 LGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTnGTRVF---------VPAKCKAAFEQkilarverIRAGDVFDPQT 323
Cdd:PRK11905 789 TGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCS-ALRVLclqedvadrVLTMLKGAMDE--------LRIGDPWRLST 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 324 NFSPLVSFPHRDNVLRYIAKGKEEGARVLcggDVLKGDGFDNGAWVAPTVFTdcRDEMTIVREEIFGPVMSLLTYESE-- 401
Cdd:PRK11905 860 DVGPVIDAEAQANIEAHIEAMRAAGRLVH---QLPLPAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKADel 934
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446011217 402 DEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWIN 442
Cdd:PRK11905 935 DRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN 975
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
137-479 |
9.32e-48 |
|
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: 170.76 E-value: 9.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 137 YTRREPLGVVAGIGAWNYPIQIALwksAP---ALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLpgGGAETG 213
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQLAL---APligAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAVVE--GGVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 214 QYLTEHPgIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVfddadlDLAADIAMMA------NFFSSGQVCT 287
Cdd:cd07136 170 QELLDQK-FDYIFFTGSVRVGKIVME-AAAKHLTPVTLELGGKSPCIV------DEDANLKLAAkrivwgKFLNAGQTCV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 288 NGTRVFVPAKCKAAFEqKILARVERIRAGDvfDPQTN--FSPLVSFPHRDNVLRYIAKGKeegarVLCGGDVLKGDgfdn 365
Cdd:cd07136 242 APDYVLVHESVKEKFI-KELKEEIKKFYGE--DPLESpdYGRIINEKHFDRLAGLLDNGK-----IVFGGNTDRET---- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 366 gAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLE-AGICwIN-- 442
Cdd:cd07136 310 -LYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSfGGGC-INdt 387
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446011217 443 -----TwgespAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07136 388 imhlaN-----PYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
137-479 |
6.80e-47 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 169.44 E-value: 6.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 137 YTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAgLPDGVFNVLPGGGAETgQYL 216
Cdd:PTZ00381 104 YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVT-TEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 217 TEHPgIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPA 296
Cdd:PTZ00381 182 LKEP-FDHIFFTGSPRVGKLVMQ-AAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 297 KCKAAFEQKIlaRVERIRA-GDVFDPQTNFSPLVSFPHRDNVLRYIakgKEEGARVLCGGDVLKgdgfdNGAWVAPTVFT 375
Cdd:PTZ00381 260 SIKDKFIEAL--KEAIKEFfGEDPKKSEDYSRIVNEFHTKRLAELI---KDHGGKVVYGGEVDI-----ENKYVAPTIIV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 376 DCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINtwgES-----PAE 450
Cdd:PTZ00381 330 NPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN---DCvfhllNPN 406
|
330 340
....*....|....*....|....*....
gi 446011217 451 MPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:PTZ00381 407 LPFGGVGNSGMGAYHGKYGFDTFSHPKPV 435
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
136-479 |
5.49e-44 |
|
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: 160.46 E-value: 5.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 136 VYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEI---YseagLPDGVFNVLPGGGAET 212
Cdd:cd07132 94 VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELipkY----LDKECYPVVLGGVEET 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 213 GQYLTEHpgIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRV 292
Cdd:cd07132 170 TELLKQR--FDYIFYTGSTSVGKIVMQ-AAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 293 FvpakCKAAFEQKIlarVERIRA------GDvfDPQT--NFSPLVSFPHRDNVLRYIakgkeEGARVLCGGDVLKGDGFd 364
Cdd:cd07132 247 L----CTPEVQEKF---VEALKKtlkefyGE--DPKEspDYGRIINDRHFQRLKKLL-----SGGKVAIGGQTDEKERY- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 365 ngawVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWIN-- 442
Cdd:cd07132 312 ----IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdt 387
|
330 340 350
....*....|....*....|....*....|....*..
gi 446011217 443 TWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07132 388 IMHYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSC 424
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
20-479 |
3.94e-41 |
|
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: 154.28 E-value: 3.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 20 SGRTFETINPAN-GNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILR-ERNDELAKLETLDTGKA 97
Cdd:cd07123 44 TGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGKN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 98 YSETSTVDIVTGADVLEYYAGLIPALEGSQiPLRETSFVYTRRE--PL-GVVAGIGAWNY-PIQIALwKSAPALAaGNAM 173
Cdd:cd07123 124 VWQAEIDAACELIDFLRFNVKYAEELYAQQ-PLSSPAGVWNRLEyrPLeGFVYAVSPFNFtAIGGNL-AGAPALM-GNVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 174 IFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVAS----GKKVMANSAA-SSLKE 248
Cdd:cd07123 201 LWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTfkslWKQIGENLDRyRTYPR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 249 VTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPL 328
Cdd:cd07123 281 IVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 329 VSFPHRDNVLRYIAKGKEE-GARVLCGGdvlKGDGfDNGAWVAPTVF--TDCRDEmtIVREEIFGPVMSLLTYESED--E 403
Cdd:cd07123 361 IDEKAFDRIKGYIDHAKSDpEAEIIAGG---KCDD-SVGYFVEPTVIetTDPKHK--LMTEEIFGPVLTVYVYPDSDfeE 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 404 VIRRANDT-DYGLAAGIVTAD---LNRAHRVIHQlEAGICWIN--TWGESPAEMPVGGYKHSGIG-RENGVMTLQSYTQV 476
Cdd:cd07123 435 TLELVDTTsPYALTGAIFAQDrkaIREATDALRN-AAGNFYINdkPTGAVVGQQPFGGARASGTNdKAGSPLNLLRWVSP 513
|
...
gi 446011217 477 KSI 479
Cdd:cd07123 514 RTI 516
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
46-484 |
2.85e-39 |
|
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: 147.77 E-value: 2.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 46 VDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKaySETSTVDIVTGADVLEYYAGLIPALEG 125
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGK--GWMFAENICGDQVQLRARAFVIYSYRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 126 SQIPLRETSF-----VYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAG-LPD 199
Cdd:cd07084 79 PHEPGNHLGQglkqqSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 200 GVFNVLPGGGaETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASslkEVTMELGGKSPLIVFDDADLDLaadiAMMANF 279
Cdd:cd07084 159 EDVTLINGDG-KTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA---RIYLELAGFNWKVLGPDAQAVD----YVAWQC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 280 -----FSSGQVCTNGTRVFVPAKC-KAAFEQKILARVERIRAGDVfdpqtnfspLVSFPHRDNVLRYIAKGKEEGARVLC 353
Cdd:cd07084 231 vqdmtACSGQKCTAQSMLFVPENWsKTPLVEKLKALLARRKLEDL---------LLGPVQTFTTLAMIAHMENLLGSVLL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 354 -GGDVLKGDGFDN--GAWVAPTVFTDCRDEMT---IVREEIFGPVMSLLTYESEDE--VIRRANDTDYGLAAGIVTADLN 425
Cdd:cd07084 302 fSGKELKNHSIPSiyGACVASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPI 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446011217 426 RAHRVIHQLE-AGICWINTWGESPAE-MPVGGYKHSGIGRENGVMTLQSYTQVKSIQVEMA 484
Cdd:cd07084 382 FLQELIGNLWvAGRTYAILRGRTGVApNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAEQA 442
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
8-431 |
3.39e-39 |
|
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: 148.96 E-value: 3.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 8 QLYIHGGYTsATSGRTFETINPANGNVLATVQAAGReDVDRAVKSAQQ-GQKIWAAMTAMERSRILRRAVDILRERNDEL 86
Cdd:cd07128 2 QSYVAGQWH-AGTGDGRTLHDAVTGEVVARVSSEGL-DFAAAVAYAREkGGPALRALTFHERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 87 AKLETLdTGkAYSETSTVDIVTGADVLEYYAGL----IPA----LEGSQIPL-RETSF----VYTRREplGVVAGIGAWN 153
Cdd:cd07128 80 YALSAA-TG-ATRRDSWIDIDGGIGTLFAYASLgrreLPNahflVEGDVEPLsKDGTFvgqhILTPRR--GVAVHINAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 154 YPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAG-LPDGVFNVLPGGGAETGQYLTEHPgiaKVSFTGGVA 232
Cdd:cd07128 156 FPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQD---VVAFTGSAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 233 SGKK------VMANSA-----ASSL--------------------KEVTMELGGKSplivfddadldlaadiammanffs 281
Cdd:cd07128 233 TAAKlrahpnIVARSIrfnaeADSLnaailgpdatpgtpefdlfvKEVAREMTVKA------------------------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 282 sGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGD 361
Cdd:cd07128 289 -GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVV 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446011217 362 GFDN--GAWVAPTVFTdCRDEM--TIVRE-EIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVI 431
Cdd:cd07128 368 GADAekGAFFPPTLLL-CDDPDaaTAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
27-442 |
9.24e-39 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 150.89 E-value: 9.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 27 INPAN-GNVLATVQAAGREDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSeTSTVD 105
Cdd:PRK11809 664 INPADpRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFS-NAIAE 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 106 IVTGADVLEYYAGlipalegsQIplrETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTA 185
Cdd:PRK11809 743 VREAVDFLRYYAG--------QV---RDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIA 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 186 LKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGG--VAsgkKVMANSAASSLKE------VTMELGGKS 257
Cdd:PRK11809 812 AQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSteVA---RLLQRNLAGRLDPqgrpipLIAETGGQN 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 258 PLIVFDDADLDLAADIAMMANFFSSGQVCTnGTRVF---------VPAKCKAAFEQKILARVERIragdvfdpQTNFSPL 328
Cdd:PRK11809 889 AMIVDSSALTEQVVADVLASAFDSAGQRCS-ALRVLclqddvadrTLKMLRGAMAECRMGNPDRL--------STDIGPV 959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 329 VSFPHRDNVLRYIAKGKEEGARVLcGGDVLKGDGFDNGAWVAPTVFT-DCRDEMTivrEEIFGPVMSLLTYESE--DEVI 405
Cdd:PRK11809 960 IDAEAKANIERHIQAMRAKGRPVF-QAARENSEDWQSGTFVPPTLIElDSFDELK---REVFGPVLHVVRYNRNqlDELI 1035
|
410 420 430
....*....|....*....|....*....|....*...
gi 446011217 406 RRANDTDYGLAAGIVT-ADLNRAHrVIHQLEAGICWIN 442
Cdd:PRK11809 1036 EQINASGYGLTLGVHTrIDETIAQ-VTGSAHVGNLYVN 1072
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
28-423 |
2.26e-29 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 120.96 E-value: 2.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 28 NPANGNVLATVQAAGReDVDRAVKSA-QQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSEtSTVDI 106
Cdd:PRK11903 25 DPVTGEELVRVSATGL-DLAAAFAFArEQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRND-SAVDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 107 VTGADVLEYYAGLIPALEGSQIpLRETSFVYTRREPL-----------GVVAGIGAWNYPiQIALW-KSAPALAAGNAMI 174
Cdd:PRK11903 103 DGGIFTLGYYAKLGAALGDARL-LRDGEAVQLGKDPAfqgqhvlvptrGVALFINAFNFP-AWGLWeKAAPALLAGVPVI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 175 FKPSEVTPLTALKLAEIYSEAG-LPDGVFNVLPG------------------GGAETGQYLTEHPGIAKVSFTGGVAS-- 233
Cdd:PRK11903 181 VKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGssaglldhlqpfdvvsftGSAETAAVLRSHPAVVQRSVRVNVEAds 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 234 ------GKKVMANSAASSL--KEVTMELGGKSplivfddadldlaadiammanffssGQVCTNGTRVFVPAKCKAAFEQK 305
Cdd:PRK11903 261 lnsallGPDAAPGSEAFDLfvKEVVREMTVKS-------------------------GQKCTAIRRIFVPEALYDAVAEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 306 ILARVERIRAGDVFDPQTNFSPLVSFPHRDNVLRYIAKGKEEgARVLCGGDVLKGDGFDN--GAWVAPTVF-TDCRDEMT 382
Cdd:PRK11903 316 LAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ-AEVLFDGGGFALVDADPavAACVGPTLLgASDPDAAT 394
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446011217 383 IVRE-EIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTAD 423
Cdd:PRK11903 395 AVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
141-479 |
2.49e-29 |
|
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: 119.44 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 141 EPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAgLPDGVFNVLPGGGAETGQyLTEHP 220
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVPETTA-LLEQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 221 GiAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFS-SGQVCTNGTRVFVPAKCK 299
Cdd:cd07137 178 W-DKIFFTGSPRVGRIIMA-AAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEESFA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 300 AAFEQKILARVERIRAGDVFDPQtNFSPLVSFPHRDNvLRYIAKGKEEGARVLCGGDVlkgDgfDNGAWVAPTVFTDCRD 379
Cdd:cd07137 256 PTLIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQR-LSRLLDDPSVADKIVHGGER---D--EKNLYIEPTILLDPPL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 380 EMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPA--EMPVGGYK 457
Cdd:cd07137 329 DSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAidTLPFGGVG 408
|
330 340
....*....|....*....|..
gi 446011217 458 HSGIGRENGVMTLQSYTQVKSI 479
Cdd:cd07137 409 ESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
46-431 |
2.86e-28 |
|
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: 116.87 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 46 VDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDEL---AKLET-LDTGKAYSETS--TVDIVTGADVLE---YY 116
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELvarAHAETgLPEARLQGELGrtTGQLRLFADLVRegsWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 117 AGLI--PALEGSQIP---LREtsfvytRREPLGVVAGIGAWNYP--IQIALWKSAPALAAGNAMIFKPSEVTPLTALKLA 189
Cdd:cd07129 81 DARIdpADPDRQPLPrpdLRR------MLVPLGPVAVFGASNFPlaFSVAGGDTASALAAGCPVVVKAHPAHPGTSELVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 190 EIYSEA----GLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASGKKVMAnsAASSLKE---VTMELGGKSPLIVF 262
Cdd:cd07129 155 RAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFD--AAAARPEpipFYAELGSVNPVFIL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 263 DDADLDLAADIAmmANFFSS-----GQVCTNGTRVFVPAkcKAAFEQKILARVERIRAgdvFDPQTNFSPlvsfphrdNV 337
Cdd:cd07129 233 PGALAERGEAIA--QGFVGSltlgaGQFCTNPGLVLVPA--GPAGDAFIAALAEALAA---APAQTMLTP--------GI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 338 LRYIAKGKEE-----GARVLCGGDVLkgdgfDNGAWVAPTVF-TDCRDEMT--IVREEIFGPVMSLLTYESEDEVIRRAN 409
Cdd:cd07129 298 AEAYRQGVEAlaaapGVRVLAGGAAA-----EGGNQAAPTLFkVDAAAFLAdpALQEEVFGPASLVVRYDDAAELLAVAE 372
|
410 420 430
....*....|....*....|....*....|....*
gi 446011217 410 -------------DTDYGLAAGIVTADLNRAHRVI 431
Cdd:cd07129 373 alegqltatihgeEDDLALARELLPVLERKAGRLL 407
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
141-479 |
2.26e-25 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 108.66 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 141 EPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLpgGGAETGQYLTEHP 220
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIE--GGPAVGEQLLQHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 221 GiAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVFDDADLDLAADIA--MMANFFSS--GQVCTNGTRVFVPA 296
Cdd:PLN02203 185 W-DKIFFTGSPRVGRIIMT-AAAKHLTPVALELGGKCPCIVDSLSSSRDTKVAVnrIVGGKWGScaGQACIAIDYVLVEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 297 KCKAAFEQKILARVERIRAGDVFDPQTnFSPLVSFPHRDNVLRYIaKGKEEGARVLCGGdvlkgdGFD-NGAWVAPTVFT 375
Cdd:PLN02203 263 RFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLL-KDPRVAASIVHGG------SIDeKKLFIEPTILL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 376 DCRDEMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPA--EMPV 453
Cdd:PLN02203 335 NPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdSLPF 414
|
330 340
....*....|....*....|....*.
gi 446011217 454 GGYKHSGIGRENGVMTLQSYTQVKSI 479
Cdd:PLN02203 415 GGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
141-479 |
5.33e-24 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 104.74 E-value: 5.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 141 EPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYsEAGLPDGVFNVLPGGGAETGQYLTEHp 220
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQK- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 221 gIAKVSFTGGVASGKKVMAnSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANF-FSSGQVCTNGTRVFVPAKCK 299
Cdd:PLN02174 189 -WDKIFYTGSSKIGRVIMA-AAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 300 AAFEQKILARVERIRAGDVFDPQtNFSPLVSFPHRDNVLRYIAKgKEEGARVLCGGDVLKgdgfdNGAWVAPTVFTDCRD 379
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLDE-KEVSDKIVYGGEKDR-----ENLKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 380 EMTIVREEIFGPVMSLLTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPA--EMPVGGYK 457
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLPFGGVG 419
|
330 340
....*....|....*....|..
gi 446011217 458 HSGIGRENGVMTLQSYTQVKSI 479
Cdd:PLN02174 420 ESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
46-294 |
1.31e-13 |
|
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: 72.68 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 46 VDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVDIVTGAdvlEYYAGLIPALEG 125
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAA---EYIYNVYKDEKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 126 SQIPLRETSF-VYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP----SEVTPLTALKLAEIYSEAGLPDG 200
Cdd:cd07081 78 CGVLTGDENGgTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 201 VFNVLPGGGAETGQYLTEHPGIAKVSFTGGVAsgkkvMANSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFF 280
Cdd:cd07081 158 LIGWIDNPSIELAQRLMKFPGIGLLLATGGPA-----VVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTF 232
|
250
....*....|....
gi 446011217 281 SSGQVCTNGTRVFV 294
Cdd:cd07081 233 DNGVICASEQSVIV 246
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
49-311 |
3.74e-10 |
|
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: 61.47 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 49 AVKSAQQGQkiwAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGS-- 126
Cdd:cd07077 2 SAKNAQRTL---AVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGIta 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 127 ------QIPLRETSFVYTRREPLGVVAGIGAWNYPIqIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEA---GL 197
Cdd:cd07077 79 svghiqDVLLPDNGETYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 198 PDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVASgkkVMANSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMA 277
Cdd:cd07077 158 PKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270
....*....|....*....|....*....|....
gi 446011217 278 NFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVE 311
Cdd:cd07077 235 KFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVV 268
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
18-408 |
4.66e-10 |
|
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: 61.73 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 18 ATSGRTFETINP-ANGNVLATVQAAGRE--------DVDRAVKSAQQGQKIWAAMTAMERS----RILRRavdiLRERND 84
Cdd:cd07127 49 ALLGQRFDLDQPgASGWVGGEVSPYGVElgvtypqcDPDALLAAARAAMPGWRDAGARARAgvclEILQR----LNARSF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 85 ELAKLETLDTGKAY------SETSTVDivTGADVLEYYA---GLIPAL------EGSQIPLR-ETSFVYTrrePLGVVAG 148
Cdd:cd07127 125 EMAHAVMHTTGQAFmmafqaGGPHAQD--RGLEAVAYAWremSRIPPTaewekpQGKHDPLAmEKTFTVV---PRGVALV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 149 IGAWNYPIqialWKSAPA----LAAGNAMIFKPSevtPLTALKLA-------EIYSEAGL-PDGVFNVLPGGGAETGQYL 216
Cdd:cd07127 200 IGCSTFPT----WNGYPGlfasLATGNPVIVKPH---PAAILPLAitvqvarEVLAEAGFdPNLVTLAADTPEEPIAQTL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 217 TEHPGIAKVSFTGGVASGKKVMANSAAsslKEVTMELGGKSPLIVfddadLDLAADIAMMANF-FS----SGQVCTNGTR 291
Cdd:cd07127 273 ATRPEVRIIDFTGSNAFGDWLEANARQ---AQVYTEKAGVNTVVV-----DSTDDLKAMLRNLaFSlslySGQMCTTPQN 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 292 VFVPA---------KCKAAFEQKILARVERIRAgdvfDPQTNfSPLVSFPHRDNVLRYIAKGKeEGARVLCGGDVLKGDG 362
Cdd:cd07127 345 IYVPRdgiqtddgrKSFDEVAADLAAAIDGLLA----DPARA-AALLGAIQSPDTLARIAEAR-QLGEVLLASEAVAHPE 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446011217 363 FDNGAWVAPTVFTDCRDEMTIVREEIFGPVMSLLTYESEDEVIRRA 408
Cdd:cd07127 419 FPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELA 464
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
44-239 |
2.18e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 56.45 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 44 EDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETStvdIVTGADVLEYYAG---LI 120
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDK---IAKNVAAAEKTPGvedLT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 121 P-ALEGSQ-IPLRETSfvytrrePLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP----SEVTPLTALKLAEIYSE 194
Cdd:PRK15398 113 TeALTGDNgLTLIEYA-------PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgaKKVSLRAIELLNEAIVA 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446011217 195 AGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVA-------SGKKVMA 239
Cdd:PRK15398 186 AGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAvvkaamkSGKKAIG 237
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
46-245 |
9.28e-08 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 54.42 E-value: 9.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 46 VDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVDIVTGAD-VLEYY-----AGL 119
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFASEyVYNDIkdmktVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 120 I---PALEGSQIPlretsfvytrrEPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEA- 195
Cdd:cd07122 81 IeedEEKGIVEIA-----------EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAa 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446011217 196 ---GLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVAsgkkvMANSAASS 245
Cdd:cd07122 150 vaaGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGGPG-----MVKAAYSS 197
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
44-239 |
1.73e-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: 50.31 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 44 EDVDRAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELAKLETLDTG------KAYSETSTVDIVTGADVLEyya 117
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGmgrvedKIAKNHLAAEKTPGTEDLT--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 118 glIPALEGsqiplrETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKP----SEVTPLTALKLAEIYS 193
Cdd:cd07121 81 --TTAWSG------DNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgaKKVSAYAVELINKAIA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446011217 194 EAGLPDGVFNVLPGGGAETGQYLTEHPGIAKVSFTGGVA-------SGKKVMA 239
Cdd:cd07121 153 EAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAvvkaalsSGKKAIG 205
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
140-431 |
2.40e-06 |
|
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: 49.80 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 140 REPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYLTE- 218
Cdd:cd07126 140 RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEa 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 219 HPGIakVSFTGgvasGKKVMANSAASSLKEVTMELGGKSPLIVfdDADLDLAADIAMMAN---FFSSGQVCTNGTRVFVP 295
Cdd:cd07126 220 NPRM--TLFTG----SSKVAERLALELHGKVKLEDAGFDWKIL--GPDVSDVDYVAWQCDqdaYACSGQKCSAQSILFAH 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 296 AK-CKAAFEQKILARVERIRAGDV-FDPQTNFSPLVSFPHRDNVLRYiakgkeEGARVLCGGDVLKGDGFDN--GAWVAP 371
Cdd:cd07126 292 ENwVQAGILDKLKALAEQRKLEDLtIGPVLTWTTERILDHVDKLLAI------PGAKVLFGGKPLTNHSIPSiyGAYEPT 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446011217 372 TVFT---DCRDEMT--IVREEIFGPVMSLLTYESEDE--VIRRANDTDYGLAAGIVTADLNRAHRVI 431
Cdd:cd07126 366 AVFVpleEIAIEENfeLVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEVL 432
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
141-247 |
2.44e-04 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 43.64 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446011217 141 EPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPS----EVTPLTALKLAEIYSEAGLPDGVFNVLPGGGAETGQYL 216
Cdd:PRK13805 107 EPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHpraqKSSIAAAKIVLDAAVAAGAPKDIIQWIEEPSVELTNAL 186
|
90 100 110
....*....|....*....|....*....|.
gi 446011217 217 TEHPGIAKVSFTGGVAsgkkvMANSAASSLK 247
Cdd:PRK13805 187 MNHPGIALILATGGPG-----MVKAAYSSGK 212
|
|
| |
