|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
50-506 |
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: 647.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAVD 129
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 130 AYRSVANFRFFAGLIREkadSPNEIFEMD-NATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTP 208
Cdd:cd07093 81 IPRAAANFRFFADYILQ---LDGESYPQDgGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 209 MTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFD 288
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 289 DCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVAL 368
Cdd:cd07093 238 DADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 369 AQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGD 448
Cdd:cd07093 318 ARAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 663513266 449 LDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNICL 506
Cdd:cd07093 398 LGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
25-508 |
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: 578.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 25 DLLNYIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALE 104
Cdd:COG1012 5 EYPLFIGGEWV-----AAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 105 TKYEDIAALESRDTGKPIALARAvDAYRSVANFRFFAGLIReKADSPNEIFEMDNATNVVVSKPVGVAALITPWNLPLYL 184
Cdd:COG1012 80 ERREELAALLTLETGKPLAEARG-EVDRAADFLRYYAGEAR-RLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 185 LSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVA 264
Cdd:COG1012 158 AAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 265 AAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPS 344
Cdd:COG1012 238 AAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 345 NDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPClpkEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFE 424
Cdd:COG1012 318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRP---DGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 425 AEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTW-LHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMN 503
Cdd:COG1012 395 DEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGtTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKT 474
|
....*
gi 663513266 504 ICLKH 508
Cdd:COG1012 475 VTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
50-504 |
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: 535.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAvD 129
Cdd:pfam00171 11 VINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARG-E 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 130 AYRSVANFRFFAGLIREKADspnEIFEMD-NATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTP 208
Cdd:pfam00171 90 VDRAIDVLRYYAGLARRLDG---ETLPSDpGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 209 MTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFD 288
Cdd:pfam00171 167 LTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 289 DCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVAL 368
Cdd:pfam00171 247 DADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVED 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 369 AQEEGGEVLTGGHPCLpkefEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGD 448
Cdd:pfam00171 327 AKEEGAKLLTGGEAGL----DNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSD 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 663513266 449 LDKGRRVAESIDTGMVWVNTWLHRDLR-VPFGGVKDSGVGREGGRWSLGFFSEPMNI 504
Cdd:pfam00171 403 LERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
26-507 |
0e+00 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 525.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 26 LLNYIGGEFVGHSGNEADENnwlnvlePATGYRFARVPLSGPDDVDAAVIAA-RAAAPDWGALDFAERADWLDRIADALE 104
Cdd:TIGR03216 1 IRNFINGAFVESGKTFANIN-------PVDGRVIARVHEAGAAEVDAAVAAArAALKGPWGKMTVAERADLLYAVADEIE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 105 TKYEDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIRekaDSPNEIFEMD-----NATNVVVSKPVGVAALITPWN 179
Cdd:TIGR03216 74 RRFDDFLAAEVADTGKPRSLASHLDIPRGAANFRVFADVVK---NAPTECFEMAtpdgkGALNYAVRKPLGVVGVISPWN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 180 LPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGP-LTTHSDVDLVSFTGGTD 258
Cdd:TIGR03216 151 LPLLLMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPDSAGEfLTRHPGVDAITFTGETR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 259 TGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESM 338
Cdd:TIGR03216 231 TGSAIMKAAADGVKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 339 RIGDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGH-PCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPV 417
Cdd:TIGR03216 311 KIGVPDDPATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGGvPDFGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPC 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 418 VTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGF 497
Cdd:TIGR03216 391 CHIAPFDSEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEF 470
|
490
....*....|
gi 663513266 498 FSEPMNICLK 507
Cdd:TIGR03216 471 YTELTNVCIK 480
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
82-506 |
6.38e-168 |
|
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: 481.32 E-value: 6.38e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 82 PDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAvDAYRSVANFRFFAGLIReKADSPNEIFEMDNAT 161
Cdd:cd07078 12 KAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLAR-RLHGEVIPSPDPGEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 162 NVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGP 241
Cdd:cd07078 90 AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 242 LTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQS 321
Cdd:cd07078 170 LASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 322 GIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHpclPKEFEHGNWLAPTVIAG 401
Cdd:cd07078 250 SIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGK---RLEGGKGYFVPPTVLTD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 402 LSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWL-HRDLRVPFGG 480
Cdd:cd07078 327 VDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSvGAEPSAPFGG 406
|
410 420
....*....|....*....|....*.
gi 663513266 481 VKDSGVGREGGRWSLGFFSEPMNICL 506
Cdd:cd07078 407 VKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
29-508 |
8.10e-167 |
|
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: 480.27 E-value: 8.10e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAA--APDWGALDFAERADWLDRIADALETK 106
Cdd:cd07119 1 YIDGEWV-----EAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIRED 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 107 YEDIAALESRDTGKPIALARAvDAYRSVANFRFFAGLIREKADSPNEIfeMDNATNVVVSKPVGVAALITPWNLPLYLLS 186
Cdd:cd07119 76 AEELARLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDV--PPHVISRTVREPVGVCGLITPWNYPLLQAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 187 WKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAA 266
Cdd:cd07119 153 WKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 267 AAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSND 346
Cdd:cd07119 233 AAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 347 ETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAE 426
Cdd:cd07119 313 DTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 427 EEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEpmnicL 506
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQE-----T 467
|
..
gi 663513266 507 KH 508
Cdd:cd07119 468 KH 469
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
26-509 |
1.46e-166 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 480.07 E-value: 1.46e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 26 LLNYIGGEFVGHSGNEADENnwlnvLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALET 105
Cdd:TIGR02299 1 IGHFIDGEFVPSESGETFET-----LSPATNEVLGSVARGGAADVDRAAKAAKEAFKRWAELKAAERKRYLHKIADLIEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 106 KYEDIAALESRDTGKPIALARAVdAYRSVANFRFFAGLIREKADspNEIFEMDNATNVVVSKPVGVAALITPWNLPLYLL 185
Cdd:TIGR02299 76 HADEIAVLECLDCGQPLRQTRQQ-VIRAAENFRFFADKCEEAMD--GRTYPVDTHLNYTVRVPVGPVGLITPWNAPFMLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 186 SWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAA 265
Cdd:TIGR02299 153 TWKIAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 266 AAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSN 345
Cdd:TIGR02299 233 NGADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 346 DETELGALISPDHLAKVEGYVALAQEEGGEVLTGGH---PCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHR 422
Cdd:TIGR02299 313 PETEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGErapTFRGEDLGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 423 FEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPM 502
Cdd:TIGR02299 393 FKDEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETK 472
|
....*..
gi 663513266 503 NICLKHD 509
Cdd:TIGR02299 473 NVALALG 479
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
28-501 |
4.75e-164 |
|
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: 472.76 E-value: 4.75e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 28 NYIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKY 107
Cdd:cd07138 1 FYIDGAWV-----APAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 108 EDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIREKAdspneiFEMDNATNVVVSKPVGVAALITPWNLPLYLLSW 187
Cdd:cd07138 76 DELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFE------FEERRGNSLVVREPIGVCGLITPWNWPLNQIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 188 KVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAA 267
Cdd:cd07138 150 KVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 268 APQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDE 347
Cdd:cd07138 230 ADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 348 TELGALISPDHLAKVEGYVALAQEEGGEVLTGGhPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEE 427
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG-PGRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDED 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663513266 428 EAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHrDLRVPFGGVKDSGVGREGGRWSLGFFSEP 501
Cdd:cd07138 389 EAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAF-NPGAPFGGYKQSGNGREWGRYGLEEFLEV 461
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
50-504 |
1.71e-161 |
|
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: 465.87 E-value: 1.71e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARA--AAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARA 127
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAafEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 128 vdAYRSVAN-FRFFAGLIrEKADSPNEIFEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSEL 206
Cdd:cd07114 81 --QVRYLAEwYRYYAGLA-DKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 207 TPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASII 286
Cdd:cd07114 158 TPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 287 FDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYV 366
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 367 ALAQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWT 446
Cdd:cd07114 318 ARAREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 447 GDLDKGRRVAESIDTGMVWVNTwlHRDLR--VPFGGVKDSGVGREGGRWSLGFFSEPMNI 504
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNT--YRALSpsSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
50-506 |
4.69e-153 |
|
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: 444.19 E-value: 4.69e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAVD 129
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 130 AYRSVANFRFFAGLIREKADS--PNEifemDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELT 207
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEviPVR----GPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 208 PMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIF 287
Cdd:cd07115 157 PLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 288 DDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVA 367
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 368 LAQEEGGEVLTGGHpclpKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTG 447
Cdd:cd07115 317 VGREEGARLLTGGK----RPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 663513266 448 DLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNICL 506
Cdd:cd07115 393 DLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
50-506 |
3.79e-151 |
|
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: 439.17 E-value: 3.79e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARA-V 128
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGeV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 129 DayRSVANFRFFAGLIR----EKADSPNeifemDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPS 204
Cdd:cd07103 81 D--YAASFLEWFAEEARriygRTIPSPA-----PGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 205 ELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGkNAS 284
Cdd:cd07103 154 EETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG-NAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 285 -IIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVE 363
Cdd:cd07103 233 fIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 364 GYVALAQEEGGEVLTGGHPCLPKefehGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGS 443
Cdd:cd07103 313 ALVEDAVAKGAKVLTGGKRLGLG----GYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAY 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663513266 444 VWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNICL 506
Cdd:cd07103 389 VFTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
28-504 |
8.08e-150 |
|
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: 437.16 E-value: 8.08e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 28 NYIGGEFVGHSGNEadennWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKY 107
Cdd:cd07559 3 NFINGEWVAPSKGE-----YFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 108 EDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIREKADSPNEIFEmdNATNVVVSKPVGVAALITPWNLPLYLLSW 187
Cdd:cd07559 78 ELLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDE--DTLSYHFHEPLGVVGQIIPWNFPLLMAAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 188 KVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVgLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAA 267
Cdd:cd07559 156 KLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 268 APQFKKLSLELGGKNASIIFDD-----CDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGD 342
Cdd:cd07559 235 AENLIPVTLELGGKSPNIFFDDamdadDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 343 PSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHR 422
Cdd:cd07559 315 PLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVIT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 423 FEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPM 502
Cdd:cd07559 395 FKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
..
gi 663513266 503 NI 504
Cdd:cd07559 475 NI 476
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
50-505 |
4.26e-149 |
|
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: 434.42 E-value: 4.26e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARaVD 129
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 130 AYRSVANFRFFAGLIrekADSPNEIFEMDNATNVVVSK-PVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTP 208
Cdd:cd07090 80 IDSSADCLEYYAGLA---PTLSGEHVPLPGGSFAYTRRePLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 209 MTANLLMETIDEVGLPAGVVNLVHGNGAgAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFD 288
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 289 DCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVAL 368
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 369 AQEEGGEVLTGGHPCLPKE-FEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTG 447
Cdd:cd07090 316 AKQEGAKVLCGGERVVPEDgLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 663513266 448 DLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNIC 505
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
29-504 |
7.36e-149 |
|
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: 434.31 E-value: 7.36e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVGHSGNEadennWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPD--WGALDFAERADWLDRIADALETK 106
Cdd:cd07139 2 FIGGRWVAPSGSE-----TIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 107 YEDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIREKAdspneiFE-----MDNATNVVVSKPVGVAALITPWNLP 181
Cdd:cd07139 77 ADELARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFP------FEerrpgSGGGHVLVRREPVGVVAAIVPWNAP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 182 LYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGnGAGAGGPLTTHSDVDLVSFTGGTDTGA 261
Cdd:cd07139 151 LFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 262 KVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIG 341
Cdd:cd07139 230 RIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 342 DPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPclPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIH 421
Cdd:cd07139 310 DPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 422 RFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNtWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEP 501
Cdd:cd07139 388 PYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLET 466
|
...
gi 663513266 502 MNI 504
Cdd:cd07139 467 KSI 469
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
29-495 |
1.48e-146 |
|
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: 428.55 E-value: 1.48e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPD--WGALDFAERADWLDRIADALETK 106
Cdd:cd07091 7 FINNEFV-----DSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 107 YEDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLirekADSPN-EIFEMD-NATNVVVSKPVGVAALITPWNLPLYL 184
Cdd:cd07091 82 RDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGW----ADKIQgKTIPIDgNFLAYTRREPIGVCGQIIPWNFPLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 185 LSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVA 264
Cdd:cd07091 158 LAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 265 AA-AAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDP 343
Cdd:cd07091 238 EAaAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 344 SNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKefehGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRF 423
Cdd:cd07091 318 FDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSK----GYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKF 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663513266 424 EAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSL 495
Cdd:cd07091 394 KTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGL 465
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
50-508 |
1.53e-145 |
|
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: 425.20 E-value: 1.53e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAVD 129
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 130 AYRSVANFRFFAGLIRE-KADSPNEIFEmdNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTP 208
Cdd:cd07092 81 LPGAVDNFRFFAGAARTlEGPAAGEYLP--GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 209 MTANLLMETIDEVgLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFD 288
Cdd:cd07092 159 LTTLLLAELAAEV-LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 289 DCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVAL 368
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 369 AQeEGGEVLTGGHPCLPKefehGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGD 448
Cdd:cd07092 318 AP-AHARVLTGGRRAEGP----GYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 449 LDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSepmniCLKH 508
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYT-----RIKH 447
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
50-501 |
7.21e-143 |
|
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: 418.09 E-value: 7.21e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAvD 129
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 130 AYRSVANFRFFAGLirekaDSPNE-IFEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTP 208
Cdd:cd07106 80 VGGAVAWLRYTASL-----DLPDEvIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 209 MTANLLMETIDEVgLPAGVVNLVHGnGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFD 288
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 289 DCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVAL 368
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 369 AQEEGGEVLTGGHPclpkEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGD 448
Cdd:cd07106 313 AKAKGAKVLAGGEP----LDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSD 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 663513266 449 LDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEP 501
Cdd:cd07106 389 LERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQT 441
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
50-504 |
9.61e-143 |
|
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: 418.18 E-value: 9.61e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWG-ALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAV 128
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 129 DAYRSVANFRFFAGLIREKADS---PNEIFEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSE 205
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEfdlPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 206 LTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASI 285
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 286 IFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGY 365
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 366 VALAQEEGGEVLTGGHPclPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVW 445
Cdd:cd07089 321 IARGRDEGARLVTGGGR--PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 663513266 446 TGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNI 504
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
28-488 |
9.40e-140 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 411.23 E-value: 9.40e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 28 NYIGGEFVGHSGNEADennwlnVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKY 107
Cdd:PRK13473 5 LLINGELVAGEGEKQP------VYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 108 EDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIRE-KADSPNEIfeMDNATNVVVSKPVGVAALITPWNLPLYLLS 186
Cdd:PRK13473 79 DEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARClEGKAAGEY--LEGHTSMIRRDPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 187 WKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVgLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAA 266
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 267 AAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSND 346
Cdd:PRK13473 236 AADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 347 ETELGALISPDHLAKVEGYVALAQEEG-GEVLTGGHPCLPKefehGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEA 425
Cdd:PRK13473 316 DTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGK----GYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDD 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663513266 426 EEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTwlHRDL--RVPFGGVKDSGVGR 488
Cdd:PRK13473 392 EDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT--HFMLvsEMPHGGQKQSGYGK 454
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
29-504 |
1.96e-139 |
|
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: 410.31 E-value: 1.96e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVGHSGNEAdennwLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYE 108
Cdd:cd07117 4 FINGEWVKGSSGET-----IDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 109 DIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIREKADSPNEIFEmdNATNVVVSKPVGVAALITPWNLPLYLLSWK 188
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDE--DTLSIVLREPIGVVGQIIPWNFPFLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 189 VAPAIGMGNTVVCKPSELTPMTANLLMETIDEVgLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAA 268
Cdd:cd07117 157 LAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 269 PQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDET 348
Cdd:cd07117 236 KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 349 ELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEE 428
Cdd:cd07117 316 QMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663513266 429 AVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNI 504
Cdd:cd07117 396 VIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
53-500 |
7.96e-139 |
|
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: 407.88 E-value: 7.96e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 53 PATGYRFARVPLSGPDDVDAAVIAARAAAPD--WGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARA-VD 129
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGeIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 130 AyrSVANFRFFAGLIRE-KADSPNEIfeMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTP 208
Cdd:cd07118 84 G--AADLWRYAASLARTlHGDSYNNL--GDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 209 MTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFD 288
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 289 DCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVAL 368
Cdd:cd07118 240 DADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 369 AQEEGGEVLTGGHPClpkEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGD 448
Cdd:cd07118 320 GRAEGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 663513266 449 LDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSE 500
Cdd:cd07118 397 IDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTE 448
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
53-504 |
1.06e-138 |
|
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: 408.14 E-value: 1.06e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 53 PATGYRFARVPLSGPDDVDAAVIAARAAAPD--WGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAVDA 130
Cdd:cd07112 9 PATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAVDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 131 YRSVANFRFFAGLIR----EKADSPNeifemdNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSEL 206
Cdd:cd07112 89 PSAANTFRWYAEAIDkvygEVAPTGP------DALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 207 TPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAK-VAAAAAPQFKKLSLELGGKNASI 285
Cdd:cd07112 163 SPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRfLEYSGQSNLKRVWLECGGKSPNI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 286 IFDDC-DLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEG 364
Cdd:cd07112 243 VFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 365 YVALAQEEGGEVLTGGHPCLPKEfeHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSV 444
Cdd:cd07112 323 YIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 445 WTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNI 504
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
50-500 |
3.72e-137 |
|
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: 404.04 E-value: 3.72e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALArAVD 129
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 130 AYRSVANFRFFAGL---IREKADSPNEIfEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSEL 206
Cdd:cd07110 80 VDDVAGCFEYYADLaeqLDAKAERAVPL-PSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 207 TPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASII 286
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 287 FDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYV 366
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 367 ALAQEEGGEVLTGGHpcLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWT 446
Cdd:cd07110 319 ARGKEEGARLLCGGR--RPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 663513266 447 GDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSE 500
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLE 450
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
27-499 |
7.86e-134 |
|
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: 395.85 E-value: 7.86e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 27 LNYIGGEFVGhsGNEADENnwlnvLEPA-TGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALET 105
Cdd:cd07097 2 RNYIDGEWVA--GGDGEEN-----RNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 106 KYEDIAALESRDTGKPIALARAvDAYRSVANFRFFAGLIRekaDSPNEIFEMDNA-TNVVVSK-PVGVAALITPWNLPLY 183
Cdd:cd07097 75 RKEELARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEAL---RLSGETLPSTRPgVEVETTRePLGVVGLITPWNFPIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 184 LLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKV 263
Cdd:cd07097 151 IPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 264 AAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDP 343
Cdd:cd07097 231 AAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 344 SNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPcLPKEfEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRF 423
Cdd:cd07097 311 LDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGER-LKRP-DEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRV 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663513266 424 EAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVN-TWLHRDLRVPFGGVKDSGVG-REGGRWSLGFFS 499
Cdd:cd07097 389 RDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSSYGpREQGEAALEFYT 466
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
28-500 |
8.44e-134 |
|
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: 395.95 E-value: 8.44e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 28 NYIGGEFVGHSGNEADENnwlnvLEPATGYRF-ARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETK 106
Cdd:cd07131 1 NYIGGEWVDSASGETFDS-----RNPADLEEVvGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 107 YEDIAALESRDTGKPIALARAvDAYRSVANFRFFAGLIRE-KADS-PNEIFEMDNATnvvVSKPVGVAALITPWNLPLYL 184
Cdd:cd07131 76 KEELARLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRlFGETvPSELPNKDAMT---RRQPIGVVALITPWNFPVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 185 LSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVA 264
Cdd:cd07131 152 PSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 265 AAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPS 344
Cdd:cd07131 232 ETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 345 NDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFE 424
Cdd:cd07131 312 DEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVS 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663513266 425 AEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVN-TWLHRDLRVPFGGVKDSGVG-REGGRWSLGFFSE 500
Cdd:cd07131 392 SLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNaPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTE 469
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
82-500 |
6.74e-133 |
|
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: 391.89 E-value: 6.74e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 82 PDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALAravdayrsVANFRFFAGLIREKADSPNEIF------ 155
Cdd:cd07104 14 KAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKA--------AFEVGAAIAILREAAGLPRRPEgeilps 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 156 EMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLM-ETIDEVGLPAGVVNLVHGN 234
Cdd:cd07104 86 DVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGVLNVVPGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 235 GAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCG 314
Cdd:cd07104 166 GSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 315 SRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHpclpkefEHGNWL 394
Cdd:cd07104 246 GRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT-------YEGLFY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 395 APTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVN-TWLHRD 473
Cdd:cd07104 319 QPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINdQTVNDE 398
|
410 420
....*....|....*....|....*..
gi 663513266 474 LRVPFGGVKDSGVGREGGRWSLGFFSE 500
Cdd:cd07104 399 PHVPFGGVKASGGGRFGGPASLEEFTE 425
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
29-500 |
1.22e-131 |
|
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: 390.32 E-value: 1.22e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYE 108
Cdd:TIGR01804 1 FIDGEYV-----EDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 109 DIAALESRDTGKPIALARAVDAYRSVANFRFFAGLirekADSPN-EIFEMDNATNVVVSK-PVGVAALITPWNLPLYLLS 186
Cdd:TIGR01804 76 ELAKLETLDTGKTLQETIVADMDSGADVFEFFAGL----APALNgEIIPLGGPSFAYTIRePLGVCVGIGAWNYPLQIAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 187 WKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAA 266
Cdd:TIGR01804 152 WKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 267 AAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSND 346
Cdd:TIGR01804 232 AAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 347 ETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAE 426
Cdd:TIGR01804 312 ATEMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDE 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663513266 427 EEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSE 500
Cdd:TIGR01804 392 DEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTE 465
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
50-500 |
2.01e-129 |
|
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: 383.99 E-value: 2.01e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALAravd 129
Cdd:cd07150 3 DLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 130 ayrsVANFRFFAGLIREKADSP----NEIFEMDNATNV--VVSKPVGVAALITPWNLPLyLLSWK-VAPAIGMGNTVVCK 202
Cdd:cd07150 79 ----WFETTFTPELLRAAAGECrrvrGETLPSDSPGTVsmSVRRPLGVVAGITPFNYPL-ILATKkVAFALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 203 PSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKN 282
Cdd:cd07150 154 PSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 283 ASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKV 362
Cdd:cd07150 234 PLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 363 EGYVALAQEEGGEVLTGGHpclpkefEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAG 442
Cdd:cd07150 314 KRQVEDAVAKGAKLLTGGK-------YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 663513266 443 SVWTGDLDKGRRVAESIDTGMVWVN-TWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSE 500
Cdd:cd07150 387 AILTNDLQRAFKLAERLESGMVHINdPTILDEAHVPFGGVKASGFGREGGEWSMEEFTE 445
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
28-500 |
2.64e-128 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 382.31 E-value: 2.64e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 28 NYIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKY 107
Cdd:PRK13252 9 LYIDGAYV-----EATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 108 EDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIreKADSPNEIFEMDNATNVVVSKPVGVAALITPWNLPLYLLSW 187
Cdd:PRK13252 84 DELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLA--PALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 188 KVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAgAGGPLTTHSDVDLVSFTGGTDTGAKVAAAA 267
Cdd:PRK13252 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 268 APQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDE 347
Cdd:PRK13252 241 AASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 348 TELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEE 427
Cdd:PRK13252 321 TNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDED 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663513266 428 EAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSE 500
Cdd:PRK13252 401 EVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQ 473
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
82-506 |
2.89e-128 |
|
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: 377.73 E-value: 2.89e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 82 PDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAvDAYRSVANFRFFAGLIReKADSPNEIFEMDNAT 161
Cdd:cd06534 8 KAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLAD-KLGGPELPSPDPGGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 162 NVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGP 241
Cdd:cd06534 86 AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 242 LTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQS 321
Cdd:cd06534 166 LLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 322 GIYDEFVERFVdsvesmrigdpsndetelgalispdhlakvegyvalaqeeggevltgghpclpkefehgnwlapTVIAG 401
Cdd:cd06534 246 SIYDEFVEKLV----------------------------------------------------------------TVLVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 402 LSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTW-LHRDLRVPFGG 480
Cdd:cd06534 262 VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSsIGVGPEAPFGG 341
|
410 420
....*....|....*....|....*.
gi 663513266 481 VKDSGVGREGGRWSLGFFSEPMNICL 506
Cdd:cd06534 342 VKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
29-492 |
5.64e-128 |
|
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: 380.84 E-value: 5.64e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVGHSGNEadennWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYE 108
Cdd:cd07088 1 YINGEFVPSSSGE-----TIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 109 DIAALESRDTGKPIALARaVDAYRSVANFRFFAGLIRE------KADSPNE-IFemdnatnvVVSKPVGVAALITPWNLP 181
Cdd:cd07088 76 ELAKLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRiegeiiPSDRPNEnIF--------IFKVPIGVVAGILPWNFP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 182 LYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGA 261
Cdd:cd07088 147 FFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 262 KVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIG 341
Cdd:cd07088 227 KIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 342 DPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHpclPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIH 421
Cdd:cd07088 307 DPFDAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGK---RPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVV 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663513266 422 RFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNtwlhrdlRVPF-------GGVKDSGVGREGGR 492
Cdd:cd07088 384 KFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYIN-------RENFeamqgfhAGWKKSGLGGADGK 454
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
50-491 |
7.12e-128 |
|
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: 380.04 E-value: 7.12e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAP-DWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAv 128
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFEsGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 129 DAYRSVANFRFFAGLirekADS--PNEIFEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSEL 206
Cdd:cd07109 80 DVEAAARYFEYYGGA----ADKlhGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 207 TPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASII 286
Cdd:cd07109 156 APLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 287 FDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGdPSNDETELGALISPDHLAKVEGYV 366
Cdd:cd07109 236 FADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 367 ALAQEEGGEVLTGGHPcLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWT 446
Cdd:cd07109 315 ARARARGARIVAGGRI-AEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWT 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 663513266 447 GDLDKGRRVAESIDTGMVWVNTWLHR-DLRVPFGGVKDSGVGREGG 491
Cdd:cd07109 394 RDGDRALRVARRLRAGQVFVNNYGAGgGIELPFGGVKKSGHGREKG 439
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
29-492 |
8.96e-126 |
|
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: 375.58 E-value: 8.96e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYE 108
Cdd:cd07111 25 FINGKWV-----KPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 109 DIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIrEKADSpneifEMDNatnvvvSKPVGVAALITPWNLPLYLLSWK 188
Cdd:cd07111 100 LFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWA-QLLDT-----ELAG------WKPVGVVGQIVPWNFPLLMLAWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 189 VAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAgAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAA 268
Cdd:cd07111 168 ICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 269 PQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDET 348
Cdd:cd07111 247 GTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 349 ELGALISPDHLAKVEGYVALAQEEGGEVLTGGhPCLPKEfehGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEE 428
Cdd:cd07111 327 DMGAIVDPAQLKRIRELVEEGRAEGADVFQPG-ADLPSK---GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKE 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663513266 429 AVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGR 492
Cdd:cd07111 403 AVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGK 466
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
50-489 |
3.41e-125 |
|
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: 373.23 E-value: 3.41e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAVD 129
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 130 AYRSVANFRFFAGLIRE-KADSpneIFEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTP 208
Cdd:cd07108 81 AAVLADLFRYFGGLAGElKGET---LPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 209 MTANLLMETIDEVgLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFD 288
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 289 DCDLEKTVPGV---TRaaFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGY 365
Cdd:cd07108 237 DADLDDAVDGAiagMR--FTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 366 VALAQEE-GGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSV 444
Cdd:cd07108 315 IDLGLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 663513266 445 WTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGRE 489
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGRE 439
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
30-506 |
1.58e-124 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 373.26 E-value: 1.58e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 30 IGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYED 109
Cdd:PLN02278 29 IGGKWT-----DAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 110 IAALESRDTGKPIALARAVDAYrsVANF-RFFAglirEKADSPN-EIFEMDNATN--VVVSKPVGVAALITPWNLPLYLL 185
Cdd:PLN02278 104 LAQLMTLEQGKPLKEAIGEVAY--GASFlEYFA----EEAKRVYgDIIPSPFPDRrlLVLKQPVGVVGAITPWNFPLAMI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 186 SWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAA 265
Cdd:PLN02278 178 TRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 266 AAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSN 345
Cdd:PLN02278 258 GAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 346 DETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPclpkEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEA 425
Cdd:PLN02278 338 EGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKR----HSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 426 EEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNIC 505
Cdd:PLN02278 414 EEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVC 493
|
.
gi 663513266 506 L 506
Cdd:PLN02278 494 L 494
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
50-506 |
7.40e-123 |
|
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: 367.31 E-value: 7.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARA-V 128
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKeV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 129 DayRSVANFRFFAglirEKADSPN-EIFEMDNATNV------VVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVC 201
Cdd:cd07149 83 D--RAIETLRLSA----EEAKRLAgETIPFDASPGGegrigfTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 202 KPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAApqFKKLSLELGGK 281
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 282 NASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAK 361
Cdd:cd07149 235 AAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 362 VEGYVALAQEEGGEVLTGGHPclpkefeHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLA 441
Cdd:cd07149 315 IEEWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663513266 442 GSVWTGDLDKGRRVAESIDTGMVWVNTwlHRDLRV---PFGGVKDSGVGREGGRWSLGFFSEPMNICL 506
Cdd:cd07149 388 AGVFTNDLQKALKAARELEVGGVMIND--SSTFRVdhmPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
23-495 |
2.57e-122 |
|
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: 367.12 E-value: 2.57e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 23 PLDLlnYIGGEFVGHSGNEAdennwLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPD-WGALDFAERADWLDRIAD 101
Cdd:cd07144 7 PTGL--FINNEFVKSSDGET-----IKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 102 ALETKYEDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLirekADSPN-EIFEMDNATNV-VVSKPVGVAALITPWN 179
Cdd:cd07144 80 LVEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGW----ADKIQgKTIPTSPNKLAyTLHEPYGVCGQIIPWN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 180 LPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDT 259
Cdd:cd07144 156 YPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 260 GAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSV-ESM 338
Cdd:cd07144 236 GRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 339 RIGDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPcLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVV 418
Cdd:cd07144 316 KVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK-APEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVV 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663513266 419 TIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSL 495
Cdd:cd07144 395 VISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGL 471
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
50-500 |
4.51e-122 |
|
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: 365.13 E-value: 4.51e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARaVD 129
Cdd:cd07145 3 VRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR-VE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 130 AYRSVANFRFFAGLIREKADspnEIFEMDNATN----VVVSK--PVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKP 203
Cdd:cd07145 82 VERTIRLFKLAAEEAKVLRG---ETIPVDAYEYnerrIAFTVrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 204 SELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNA 283
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 284 SIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVE 363
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 364 GYVALAQEEGGEVLTGGhpclpkEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGS 443
Cdd:cd07145 319 NLVNDAVEKGGKILYGG------KRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 663513266 444 VWTGDLDKGRRVAESIDTGMVWVN--TWLHRDlRVPFGGVKDSGVGREGGRWSLGFFSE 500
Cdd:cd07145 393 VFTNDINRALKVARELEAGGVVINdsTRFRWD-NLPFGGFKKSGIGREGVRYTMLEMTE 450
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
29-495 |
5.88e-122 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 366.75 E-value: 5.88e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIA-----ARAAAPDWGALDFAERADWLDRIADAL 103
Cdd:PLN02467 11 FIGGEWR-----EPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAarkafKRNKGKDWARTTGAVRAKYLRAIAAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 104 ETKYEDIAALESRDTGKPIALArAVDAYRSVANFRFFAGL---IREKADSPNEIfEMDNATNVVVSKPVGVAALITPWNL 180
Cdd:PLN02467 86 TERKSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLaeaLDAKQKAPVSL-PMETFKGYVLKEPLGVVGLITPWNY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 181 PLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTG 260
Cdd:PLN02467 164 PLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 261 AKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRI 340
Cdd:PLN02467 244 RKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 341 GDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGhpCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTI 420
Cdd:PLN02467 324 SDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGG--KRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCV 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663513266 421 HRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSL 495
Cdd:PLN02467 402 KTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGL 476
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
28-504 |
2.23e-119 |
|
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: 359.07 E-value: 2.23e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 28 NYIGGEFVGHSGNEADENnwlnvLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKY 107
Cdd:cd07116 3 NFIGGEWVAPVKGEYFDN-----ITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 108 EDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIREKADSPNEIFEmdNATNVVVSKPVGVAALITPWNLPLYLLSW 187
Cdd:cd07116 78 EMLAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDE--NTVAYHFHEPLGVVGQIIPWNFPLLMATW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 188 KVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVgLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAA 267
Cdd:cd07116 156 KLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 268 APQFKKLSLELGGKNASIIF------DDCDLEKTVPGVTRAAFlNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIG 341
Cdd:cd07116 235 SENIIPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 342 DPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGlSPDARCSTEEIFGPVVTIH 421
Cdd:cd07116 314 NPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 422 RFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEP 501
Cdd:cd07116 393 TFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQT 472
|
...
gi 663513266 502 MNI 504
Cdd:cd07116 473 KNL 475
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
45-507 |
2.93e-119 |
|
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: 358.97 E-value: 2.93e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 45 NNWLN--------VLEPATGYRFARVPLSGPDDVDAAVIAARA---AAPDWGALDFAERADWLDRIADALETKYEDIAAL 113
Cdd:cd07141 13 NEWHDsvsgktfpTINPATGEKICEVQEGDKADVDKAVKAARAafkLGSPWRTMDASERGRLLNKLADLIERDRAYLASL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 114 ESRDTGKPIALARAVDAYRSVANFRFFAGlireKADS-PNEIFEMD-NATNVVVSKPVGVAALITPWNLPLYLLSWKVAP 191
Cdd:cd07141 93 ETLDNGKPFSKSYLVDLPGAIKVLRYYAG----WADKiHGKTIPMDgDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 192 AIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAA-APQ 270
Cdd:cd07141 169 ALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAgKSN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 271 FKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETEL 350
Cdd:cd07141 249 LKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 351 GALISPDHLAKVEGYVALAQEEGGEVLTGGHPclpkefeHGN---WLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEE 427
Cdd:cd07141 329 GPQIDEEQFKKILELIESGKKEGAKLECGGKR-------HGDkgyFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 428 EAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNICLK 507
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
29-500 |
8.22e-119 |
|
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: 357.99 E-value: 8.22e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAA-APDWG-ALDFAERADWLDRIADALETK 106
Cdd:cd07143 10 FINGEFV-----DSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 107 YEDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLirekADSP-NEIFEMDNAT-NVVVSKPVGVAALITPWNLPLYL 184
Cdd:cd07143 85 LDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGW----ADKIhGQVIETDIKKlTYTRHEPIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 185 LSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKV- 263
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVm 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 264 AAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDP 343
Cdd:cd07143 241 EAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 344 SNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHpclpkefEHGN---WLAPTVIAGLSPDARCSTEEIFGPVVTI 420
Cdd:cd07143 321 FAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGK-------RHGNegyFIEPTIFTDVTEDMKIVKEEIFGPVVAV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 421 HRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSE 500
Cdd:cd07143 394 IKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQ 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
51-506 |
8.45e-118 |
|
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: 354.34 E-value: 8.45e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 51 LEPATGYRFARVPLSGPDDVDAAVIAARA--AAPDWgALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARaV 128
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRafDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEAR-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 129 DAYRSVANFRFFAGLIREKADSPNEIfEMDNATnVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTP 208
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEP-EPGSFS-LVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 209 MTANLLMETIDEV-GLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIF 287
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 288 DDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGdPSNDET-ELGALISPDHLAKVEGYV 366
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVG-PGLDPAsDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 367 ALAQEEGGEVLTGGHPcLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWT 446
Cdd:cd07120 317 ERAIAAGAEVVLRGGP-VTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 447 GDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNICL 506
Cdd:cd07120 396 RDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
53-491 |
4.67e-117 |
|
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: 352.29 E-value: 4.67e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 53 PATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAvDAYR 132
Cdd:cd07099 3 PATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL-EVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 133 SVANFRFFAG-----LIREKADSPNEifeMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELT 207
Cdd:cd07099 82 ALEAIDWAARnaprvLAPRKVPTGLL---MPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 208 PMTANLLMETIDEVGLPAGVVNLVHGngAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIF 287
Cdd:cd07099 159 PLVGELLAEAWAAAGPPQGVLQVVTG--DGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 288 DDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVA 367
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 368 LAQEEGGEVLTGGHPclpkEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTG 447
Cdd:cd07099 317 DAVAKGAKALTGGAR----SNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 663513266 448 DLDKGRRVAESIDTGMVWVN----TWLHRDLrvPFGGVKDSGVGREGG 491
Cdd:cd07099 393 DLARAEAIARRLEAGAVSINdvllTAGIPAL--PFGGVKDSGGGRRHG 438
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
50-504 |
6.24e-117 |
|
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: 352.06 E-value: 6.24e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAvD 129
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 130 AYRSVANFRFFAGLIRE-KADSpneIFEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTP 208
Cdd:cd07107 80 VMVAAALLDYFAGLVTElKGET---IPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 209 MTANLLMETIDEVgLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFD 288
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 289 DCDLEKTVPGVTRAA-FLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVA 367
Cdd:cd07107 236 DADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 368 LAQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTG 447
Cdd:cd07107 316 SAKREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 663513266 448 DLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNI 504
Cdd:cd07107 396 DISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
28-500 |
7.04e-117 |
|
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: 352.64 E-value: 7.04e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 28 NYIGGEFVGHSGNEadennwLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKY 107
Cdd:cd07086 1 GVIGGEWVGSGGET------FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 108 EDIAALESRDTGKPIALARA-VDAYRSVANF-----RFFAGLIrekadSPNEI-----FEMDNatnvvvskPVGVAALIT 176
Cdd:cd07086 75 EALGRLVSLEMGKILPEGLGeVQEMIDICDYavglsRMLYGLT-----IPSERpghrlMEQWN--------PLGVVGVIT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 177 PWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEV----GLPAGVVNLVHGngAGAGGPLTTHSD-VDLV 251
Cdd:cd07086 142 AFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG--GGDGGELLVHDPrVPLV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 252 SFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERF 331
Cdd:cd07086 220 SFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 332 VDSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPclPKEFEHGNWLAPTVIAGLSPDARCSTE 411
Cdd:cd07086 300 VKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKR--IDGGEPGNYVEPTIVTGVTDDARIVQE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 412 EIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRV--AESIDTGMVWVNT-----WLHrdlrVPFGGVKDS 484
Cdd:cd07086 378 ETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIptsgaEIG----GAFGGEKET 453
|
490
....*....|....*.
gi 663513266 485 GVGREGGRWSLGFFSE 500
Cdd:cd07086 454 GGGRESGSDAWKQYMR 469
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
32-508 |
1.28e-115 |
|
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: 349.43 E-value: 1.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 32 GEFVGHSGNEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAA-APDWGALDFAERADWLDRIADALETKYEDI 110
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 111 AALESRDTGKPIALARAVDAYRSVANFRFFAGL---IREKADSPNeIFEMDNA--TNVVVSKPVGVAALITPWNLPLYLL 185
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWatkINGETLAPS-IPSMQGEryTAFTRREPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 186 SWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGaGAGGPLTTHSDVDLVSFTGGTDTGAKVAA 265
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 266 AAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSN 345
Cdd:cd07113 239 QAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 346 DETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHpCLPKEfehGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEA 425
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGE-ALAGE---GYFVQPTLVLARSADSRLMREETFGPVVSFVPYED 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 426 EEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNIC 505
Cdd:cd07113 395 EEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
...
gi 663513266 506 LKH 508
Cdd:cd07113 475 IRY 477
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
48-506 |
9.77e-115 |
|
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: 346.34 E-value: 9.77e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 48 LNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARa 127
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 128 VDAYRSVANFRFFAGLIREKADspnEIFEMDNATN------VVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVC 201
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRG---EEIPLDATQGsdnrlaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 202 KPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAApqFKKLSLELGGK 281
Cdd:cd07094 157 KPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 282 NASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAK 361
Cdd:cd07094 235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 362 VEGYVALAQEEGGEVLTGGHPclpkefeHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLA 441
Cdd:cd07094 315 VERWVEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663513266 442 GSVWTGDLDKGRRVAESIDTGMVWVNTwlHRDLRV---PFGGVKDSGVGREGGRWSLGFFSEPMNICL 506
Cdd:cd07094 388 AGIFTRDLNVAFKAAEKLEVGGVMVND--SSAFRTdwmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
29-495 |
1.38e-114 |
|
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: 346.79 E-value: 1.38e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPD--WGALDFAERADWLDRIADALETK 106
Cdd:cd07142 7 FINGQFV-----DAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 107 YEDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIRE------KADSPNEIFEMdnatnvvvSKPVGVAALITPWNL 180
Cdd:cd07142 82 ADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKihgmtlPADGPHHVYTL--------HEPIGVVGQIIPWNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 181 PLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTG 260
Cdd:cd07142 154 PLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 261 AKV-AAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMR 339
Cdd:cd07142 234 KIImQLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 340 IGDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKefehGNWLAPTVIAGLSPDARCSTEEIFGPVVT 419
Cdd:cd07142 314 VGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSK----GYYIQPTIFSDVKDDMKIARDEIFGPVQS 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663513266 420 IHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSL 495
Cdd:cd07142 390 ILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYAL 465
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
48-508 |
9.92e-113 |
|
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: 341.59 E-value: 9.92e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 48 LNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIAlara 127
Cdd:cd07151 12 IDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRI---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 128 vdayRSVANFRFFAGLIREKADSPNEI------FEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVC 201
Cdd:cd07151 88 ----KANIEWGAAMAITREAATFPLRMegrilpSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 202 KPSELTPMTANLLMETI-DEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGG 280
Cdd:cd07151 164 KPASDTPITGGLLLAKIfEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 281 KNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLA 360
Cdd:cd07151 244 NNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 361 KVEGYVALAQEEGGEVLTGGHPclpkefeHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGL 440
Cdd:cd07151 324 GLLDKIEQAVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663513266 441 AGSVWTGDLDKGRRVAESIDTGMVWVN-TWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNICLKH 508
Cdd:cd07151 397 SGAVFTSDLERGVQFARRIDAGMTHINdQPVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQH 465
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
82-504 |
5.85e-110 |
|
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: 333.27 E-value: 5.85e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 82 PDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARA-VDayRSVANFRFFAglirEKADS--PNEIFEMD 158
Cdd:cd07100 13 LAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVE--KCAWICRYYA----ENAEAflADEPIETD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 159 NATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGV-VNLVHGNGAG 237
Cdd:cd07100 87 AGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVfQNLLIDSDQV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 238 AGgpLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRI 317
Cdd:cd07100 167 EA--IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 318 LVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPcLPKEfehGNWLAPT 397
Cdd:cd07100 245 IVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKR-PDGP---GAFYPPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 398 VIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVP 477
Cdd:cd07100 321 VLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLP 400
|
410 420
....*....|....*....|....*..
gi 663513266 478 FGGVKDSGVGREGGRWSLGFFsepMNI 504
Cdd:cd07100 401 FGGVKRSGYGRELGRFGIREF---VNI 424
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
50-504 |
4.91e-108 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 331.46 E-value: 4.91e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYE---DIAALEsrdTGKpialAR 126
Cdd:PRK09407 36 VTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREellDLVQLE---TGK----AR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 127 AvDAYRSVA----NFRFFA----GLIREKaDSPNEIFEMDNATnvVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNT 198
Cdd:PRK09407 109 R-HAFEEVLdvalTARYYArrapKLLAPR-RRAGALPVLTKTT--ELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 199 VVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHsdVDLVSFTGGTDTGAKVAAAAAPQFKKLSLEL 278
Cdd:PRK09407 185 VVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGFSLEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 279 GGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDH 358
Cdd:PRK09407 263 GGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 359 LAKVEGYVALAQEEGGEVLTGGH--PCL-PKEFEhgnwlaPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANN 435
Cdd:PRK09407 343 LETVSAHVDDAVAKGATVLAGGKarPDLgPLFYE------PTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAND 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663513266 436 TRYGLAGSVWTGDLDKGRRVAESIDTGMVWVN-----TWLHRDlrVPFGGVKDSGVGREGGRWSLGFFSEPMNI 504
Cdd:PRK09407 417 TPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVD--APMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
29-491 |
3.48e-107 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 328.70 E-value: 3.48e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPD--WGALDFAERADWLDRIADALETK 106
Cdd:PLN02766 24 FINGEFV-----DAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 107 YEDIAALESRDTGKPIALARAVDAYRSVANFRFFAGlireKADSPN-EIFEMDNATN-VVVSKPVGVAALITPWNLPLYL 184
Cdd:PLN02766 99 IEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAG----AADKIHgETLKMSRQLQgYTLKEPIGVVGHIIPWNFPSTM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 185 LSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKV- 263
Cdd:PLN02766 175 FFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIm 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 264 AAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDP 343
Cdd:PLN02766 255 QAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 344 SNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPClpkeFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRF 423
Cdd:PLN02766 335 FDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPC----GDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKF 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663513266 424 EAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGG 491
Cdd:PLN02766 411 KTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQG 478
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
52-504 |
2.81e-106 |
|
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: 324.65 E-value: 2.81e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 52 EPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKpiALARAVDAY 131
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGK--ARRHAFEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 132 RSVA-NFRFFAG-----LIREKADSPneifeMDNATNVVVSK-PVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPS 204
Cdd:cd07101 80 LDVAiVARYYARraerlLKPRRRRGA-----IPVLTRTTVNRrPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 205 ELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDvdLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNAS 284
Cdd:cd07101 155 SQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD--YVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 285 IIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEG 364
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 365 YVALAQEEGGEVLTGGH--PCL-PKEFEhgnwlaPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLA 441
Cdd:cd07101 313 HVDDAVAKGATVLAGGRarPDLgPYFYE------PTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLN 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663513266 442 GSVWTGDLDKGRRVAESIDTGMVWVN-----TWLHRDlrVPFGGVKDSGVGREGGRWSLGFFSEPMNI 504
Cdd:cd07101 387 ASVWTRDGARGRRIAARLRAGTVNVNegyaaAWASID--APMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
29-505 |
2.40e-104 |
|
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: 321.48 E-value: 2.40e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVGHSGNeadennwLNVLEPA-TGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKY 107
Cdd:cd07124 36 VIGGKEVRTEEK-------IESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 108 EDIAALESRDTGKPIALARAvDAYRSVANFRFFAGLIREKADSPNEifEMDNATNVVVSKPVGVAALITPWNLPLYLLSW 187
Cdd:cd07124 109 FELAAWMVLEVGKNWAEADA-DVAEAIDFLEYYAREMLRLRGFPVE--MVPGEDNRYVYRPLGVGAVISPWNFPLAILAG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 188 KVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTG------A 261
Cdd:cd07124 186 MTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGlriyerA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 262 KVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIG 341
Cdd:cd07124 266 AKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 342 DPSNDETELGALISPDHLAKVEGYVALAQEEgGEVLTGGHPclPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIH 421
Cdd:cd07124 346 DPEDPEVYMGPVIDKGARDRIRRYIEIGKSE-GRLLLGGEV--LELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 422 RFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGmvwvNTWLHRDL------RVPFGGVKDSGVG-REGGRWS 494
Cdd:cd07124 423 KAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVG----NLYANRKItgalvgRQPFGGFKMSGTGsKAGGPDY 498
|
490
....*....|.
gi 663513266 495 LGFFSEPMNIC 505
Cdd:cd07124 499 LLQFMQPKTVT 509
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
56-500 |
3.85e-101 |
|
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: 311.15 E-value: 3.85e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 56 GYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKpIALARAVDAYRSVA 135
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGS-IRPKAGFEVGAAIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 136 NFRFFAGLirekADSPN-EIFEMDNA-TNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANL 213
Cdd:cd07152 80 ELHEAAGL----PTQPQgEILPSAPGrLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 214 LMETI-DEVGLPAGVVNLVHGnGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDL 292
Cdd:cd07152 156 VIARLfEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 293 EKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQEE 372
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 373 GGEVLTGGHpclpkefEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKG 452
Cdd:cd07152 315 GARLEAGGT-------YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 663513266 453 RRVAESIDTGMVWVN--TWLHrDLRVPFGGVKDSGVG-REGGRWSLGFFSE 500
Cdd:cd07152 388 MALADRLRTGMLHINdqTVND-EPHNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
30-495 |
5.65e-101 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 313.67 E-value: 5.65e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 30 IGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPD--WGALDFAERADWLDRIADALETKY 107
Cdd:PLN02466 62 INGQFV-----DAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 108 EDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIRE------KADSPNEIfemdnatnVVVSKPVGVAALITPWNLP 181
Cdd:PLN02466 137 DELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKihgltvPADGPHHV--------QTLHEPIGVAGQIIPWNFP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 182 LYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGA 261
Cdd:PLN02466 209 LLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 262 KV-AAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRI 340
Cdd:PLN02466 289 IVlELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 341 GDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKefehGNWLAPTVIAGLSPDARCSTEEIFGPVVTI 420
Cdd:PLN02466 369 GDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSK----GYYIQPTVFSNVQDDMLIAQDEIFGPVQSI 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663513266 421 HRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSL 495
Cdd:PLN02466 445 LKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSL 519
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
48-501 |
1.16e-100 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 310.33 E-value: 1.16e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 48 LNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARA 127
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 128 -VDayRSVANFRFFAGlirEKADSPNEIFEMDNATN------VVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVV 200
Cdd:cd07147 81 eVA--RAIDTFRIAAE---EATRIYGEVLPLDISARgegrqgLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 201 CKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGgPLTTHSDVDLVSFTGGTDTGAKVAAAAAPqfKKLSLELGG 280
Cdd:cd07147 156 LKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDAD-LLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 281 KNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLA 360
Cdd:cd07147 233 NAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 361 KVEGYVALAQEEGGEVLTGGHpclpkefEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGL 440
Cdd:cd07147 313 RVEGWVNEAVDAGAKLLTGGK-------RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663513266 441 AGSVWTGDLDKGRRVAESIDTGMVWVN---TWlhrdlRV---PFGGVKDSGVGREGGRWSLGFFSEP 501
Cdd:cd07147 386 QAGVFTRDLEKALRAWDELEVGGVVINdvpTF-----RVdhmPYGGVKDSGIGREGVRYAIEEMTEP 447
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
29-506 |
1.12e-99 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 308.76 E-value: 1.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYE 108
Cdd:PRK11241 14 LINGEWL-----DANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 109 DIAALESRDTGKPIALARAVDAYRsvanfrffAGLIREKADSPNEIF------EMDNATNVVVSKPVGVAALITPWNLPL 182
Cdd:PRK11241 89 DLARLMTLEQGKPLAEAKGEISYA--------ASFIEWFAEEGKRIYgdtipgHQADKRLIVIKQPIGVTAAITPWNFPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 183 YLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAK 262
Cdd:PRK11241 161 AMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 263 VAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGD 342
Cdd:PRK11241 241 LMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 343 PSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPclpkEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHR 422
Cdd:PRK11241 321 GLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKA----HELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 423 FEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFSEPM 502
Cdd:PRK11241 397 FKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
....
gi 663513266 503 NICL 506
Cdd:PRK11241 477 YMCI 480
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
29-495 |
1.57e-99 |
|
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: 308.27 E-value: 1.57e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVGhsgneADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAA--APDWGALDFAERADWLDRIADALETK 106
Cdd:cd07140 9 FINGEFVD-----AEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 107 YEDIAALESRDTGKPIALARAVDAYRSVANFRFFAGL---IREKADSPNEIFEMDNATnVVVSKPVGVAALITPWNLPLY 183
Cdd:cd07140 84 QEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWcdkIQGKTIPINQARPNRNLT-LTKREPIGVCGIVIPWNYPLM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 184 LLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKV 263
Cdd:cd07140 163 MLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 264 AAA-AAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGD 342
Cdd:cd07140 243 MKScAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 343 PSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPClPKEfehGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHR 422
Cdd:cd07140 323 PLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQV-DRP---GFFFEPTVFTDVEDHMFIAKEESFGPIMIISK 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663513266 423 FEAE--EEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSL 495
Cdd:cd07140 399 FDDGdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEAL 473
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
29-500 |
1.25e-98 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 306.44 E-value: 1.25e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFvghsgNEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAP--DWGALDFAERADWLDRIADALETK 106
Cdd:PRK09847 23 FINGEY-----TAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 107 YEDIAALESRDTGKPIALARAVDAYRSVANFRFFAglirEKADSP-NEIFEMDNAT-NVVVSKPVGVAALITPWNLPLYL 184
Cdd:PRK09847 98 AEELALLETLDTGKPIRHSLRDDIPGAARAIRWYA----EAIDKVyGEVATTSSHElAMIVREPVGVIAAIVPWNFPLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 185 LSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKV- 263
Cdd:PRK09847 174 TCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLl 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 264 AAAAAPQFKKLSLELGGKNASIIFDDC-DLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGD 342
Cdd:PRK09847 254 KDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 343 PSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTG---GHPClpkefehgnWLAPTVIAGLSPDARCSTEEIFGPVVT 419
Cdd:PRK09847 334 PLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGrnaGLAA---------AIGPTIFVDVDPNASLSREEIFGPVLV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 420 IHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFFS 499
Cdd:PRK09847 405 VTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFT 484
|
.
gi 663513266 500 E 500
Cdd:PRK09847 485 E 485
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
82-500 |
1.32e-98 |
|
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: 304.11 E-value: 1.32e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 82 PDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAvdayrsvaNFRFFAGLIREKADSPNEIFE----- 156
Cdd:cd07105 14 PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGF--------NVDLAAGMLREAASLITQIIGgsips 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 157 -MDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVH--- 232
Cdd:cd07105 86 dKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVThsp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 233 GNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCL 312
Cdd:cd07105 166 EDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICM 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 313 CGSRILVQSGIYDEFVERFVDSVESMRIGDpsndeTELGALISPDHLAKVEGYVALAQEEGGEVLTGGHpclPKEFEHGN 392
Cdd:cd07105 246 STERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGL---ADESPSGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 393 WLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVN-TWLH 471
Cdd:cd07105 318 SMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINgMTVH 397
|
410 420
....*....|....*....|....*....
gi 663513266 472 RDLRVPFGGVKDSGVGREGGRWSLGFFSE 500
Cdd:cd07105 398 DEPTLPHGGVKSSGYGRFNGKWGIDEFTE 426
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
53-487 |
9.71e-98 |
|
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: 302.63 E-value: 9.71e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 53 PATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARA-VDAY 131
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGeIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 132 RSVAnfRFFAGlIREKADSPNEIFEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTA 211
Cdd:cd07102 83 LERA--RYMIS-IAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 212 NLLMETIDEVGLPAGVVNLVHGNGAgAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCD 291
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 292 LEKTVPGVTRAAFLNQGQVClCG-SRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQ 370
Cdd:cd07102 239 LDAAAESLVDGAFFNSGQSC-CSiERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 371 EEGGEVLTGGHPcLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLD 450
Cdd:cd07102 318 AKGARALIDGAL-FPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 663513266 451 KGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVG 487
Cdd:cd07102 397 RAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRG 433
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
48-499 |
4.19e-97 |
|
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: 300.81 E-value: 4.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 48 LNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPdwgALDFAERADWLDRIADALETKYEDIAALESRDTGKPIA---- 123
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKdtry 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 124 -LARAVDAYRSVANfrffaglirEKADSPNEIFEMDNATN------VVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMG 196
Cdd:cd07146 78 eVGRAADVLRFAAA---------EALRDDGESFSCDLTANgkarkiFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAAN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 197 NTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAApqFKKLSL 276
Cdd:cd07146 149 NRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 277 ELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISP 356
Cdd:cd07146 227 ELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 357 DHLAKVEGYVALAQEEGGEVLTGGHpclpkefEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNT 436
Cdd:cd07146 307 EAAIQIENRVEEAIAQGARVLLGNQ-------RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNST 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663513266 437 RYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLR-VPFGGVKDSG-VGREGGRWSLGFFS 499
Cdd:cd07146 380 AYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGlGGKEGVREAMKEMT 444
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
28-487 |
1.18e-93 |
|
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: 292.88 E-value: 1.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 28 NYIGGEFVGHSGNEadennWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKY 107
Cdd:cd07085 3 LFINGEWVESKTTE-----WLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 108 EDIAALESRDTGKPIALARAvDAYRSVANFRFFAGLIRE-KADSPNEI-FEMDNATnvvVSKPVGVAALITPWNLPLYLL 185
Cdd:cd07085 78 DELARLITLEHGKTLADARG-DVLRGLEVVEFACSIPHLlKGEYLENVaRGIDTYS---YRQPLGVVAGITPFNFPAMIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 186 SWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAgAGGPLTTHSDVDLVSFTGGTDTGAKVAA 265
Cdd:cd07085 154 LWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKE-AVNALLDHPDIKAVSFVGSTPVGEYIYE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 266 AAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSN 345
Cdd:cd07085 233 RAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 346 DETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEA 425
Cdd:cd07085 313 PGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDT 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663513266 426 EEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNtwlhrdlrVP---------FGGVKDSGVG 487
Cdd:cd07085 393 LDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN--------VPipvplaffsFGGWKGSFFG 455
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
28-499 |
2.69e-93 |
|
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: 291.78 E-value: 2.69e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 28 NYIGGEFVGHSGNeadennWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAP-DWGALDFAERADWLDRIADALETK 106
Cdd:cd07082 4 YLINGEWKESSGK------TIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRgWWPTMPLEERIDCLHKFADLLKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 107 YEDIAALESRDTGKPIALARA-VDayRSVANFRF--FAGLIREKADSPNEIFEMDNATNVVVSK-PVGVAALITPWNLPL 182
Cdd:cd07082 78 KEEVANLLMWEIGKTLKDALKeVD--RTIDYIRDtiEELKRLDGDSLPGDWFPGTKGKIAQVRRePLGVVLAIGPFNYPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 183 YLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAK 262
Cdd:cd07082 156 NLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 263 VAAAAApqFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGD 342
Cdd:cd07082 236 LKKQHP--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 343 PSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHpclpkeFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHR 422
Cdd:cd07082 314 PWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG------REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIR 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663513266 423 FEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRV-PFGGVKDSGVGREGGRWSLGFFS 499
Cdd:cd07082 388 VNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQGIGDALRSMT 465
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
52-505 |
2.34e-88 |
|
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: 278.80 E-value: 2.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 52 EPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIalaraVDA- 130
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTM-----VDAs 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 131 ----YRSVANFRFfagLIR--EKADSPNEI---FEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVC 201
Cdd:cd07098 77 lgeiLVTCEKIRW---TLKhgEKALRPESRpggLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 202 KPSELTPMTA----NLLMETIDEVGLPAGVVNLVHGNGaGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLE 277
Cdd:cd07098 154 KVSEQVAWSSgfflSIIRECLAACGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 278 LGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPD 357
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 358 HLAKVEGYVALAQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTR 437
Cdd:cd07098 313 RFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663513266 438 YGLAGSVWTGDLDKGRRVAESIDTGMVWVN----TWLHRDLrvPFGGVKDSGVGREGGRWSLGFFSEPMNIC 505
Cdd:cd07098 393 YGLGASVFGKDIKRARRIASQLETGMVAINdfgvNYYVQQL--PFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
96-498 |
5.42e-86 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 270.84 E-value: 5.42e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 96 LDRIADALETKYEDIAALESRDTGKPIALAR-----AVDAYRSVANF-RFFAGLIREkADSPNEifemdnatNVVVSK-P 168
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEvevafTADYIDYMAEWaRRYEGEIIQ-SDRPGE--------NILLFKrA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 169 VGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDV 248
Cdd:PRK10090 72 LGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 249 DLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFV 328
Cdd:PRK10090 152 AMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 329 ERFVDSVESMRIGDP-SNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPclpkEFEHGNWLAPTVIAGLSPDAR 407
Cdd:PRK10090 232 NRLGEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKA----VEGKGYYYPPTLLLDVRQEMS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 408 CSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVG 487
Cdd:PRK10090 308 IMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIG 387
|
410
....*....|.
gi 663513266 488 REGGRWSLGFF 498
Cdd:PRK10090 388 GADGKHGLHEY 398
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
29-485 |
8.66e-80 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 257.94 E-value: 8.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVghsgnEADENnwLNVLEPA-TGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKY 107
Cdd:PRK03137 40 IIGGERI-----TTEDK--IVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 108 EDIAALESRDTGKPIALARAvDAYRSVANFRFFA-GLIREKADSPneIFEMDNATNVVVSKPVGVAALITPWNLPLYLLS 186
Cdd:PRK03137 113 HEFSAWLVKEAGKPWAEADA-DTAEAIDFLEYYArQMLKLADGKP--VESRPGEHNRYFYIPLGVGVVISPWNFPFAIMA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 187 WKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTG------ 260
Cdd:PRK03137 190 GMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlriyer 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 261 -AKVAAAaapQ--FKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVES 337
Cdd:PRK03137 270 aAKVQPG---QiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 338 MRIGDPSnDETELGALISPDHLAKVEGYVALAQEEgGEVLTGGHpCLPKEfehGNWLAPTVIAGLSPDARCSTEEIFGPV 417
Cdd:PRK03137 347 LTVGNPE-DNAYMGPVINQASFDKIMSYIEIGKEE-GRLVLGGE-GDDSK---GYFIQPTIFADVDPKARIMQEEIFGPV 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663513266 418 VTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGmvwvNTWLHRDLR------VPFGGVKDSG 485
Cdd:PRK03137 421 VAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVG----NLYFNRGCTgaivgyHPFGGFNMSG 490
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
53-489 |
3.88e-77 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 249.27 E-value: 3.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 53 PATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAvDAYR 132
Cdd:PRK09406 8 PATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA-EALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 133 SVANFRFFAGLIREK-ADSPNEIFEMDNATNVVVSKPVGVAALITPWNLPLyllsWKV----APAIGMGNTVVCKPSELT 207
Cdd:PRK09406 87 CAKGFRYYAEHAEALlADEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNVGLLKHASNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 208 PMTANLLMETIDEVGLPAGVVN--LVhgnGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASI 285
Cdd:PRK09406 163 PQTALYLADLFRRAGFPDGCFQtlLV---GSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 286 IFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGY 365
Cdd:PRK09406 240 VMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 366 VALAQEEGGEVLTGGH-PCLPkefehGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSV 444
Cdd:PRK09406 320 VDDAVAAGATILCGGKrPDGP-----GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNA 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 663513266 445 WTGDLDKGRRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGRE 489
Cdd:PRK09406 395 WTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRE 439
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
82-502 |
1.59e-74 |
|
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: 241.79 E-value: 1.59e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 82 PDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARA-VDAYRSVANFRFFAGLIRekadSPNEIFEMDNA 160
Cdd:cd07095 14 PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTeVAAMAGKIDISIKAYHER----TGERATPMAQG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 161 TNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAgAGG 240
Cdd:cd07095 90 RAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRE-TGE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 241 PLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKK-LSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILV 319
Cdd:cd07095 169 ALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 320 QSGIY-DEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLtgghpcLPKEF--EHGNWLAP 396
Cdd:cd07095 249 PDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL------LAMERlvAGTAFLSP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 397 TVI----AGLSPDarcstEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNtwlhR 472
Cdd:cd07095 323 GIIdvtdAADVPD-----EEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWN----R 393
|
410 420 430
....*....|....*....|....*....|....*
gi 663513266 473 DL-----RVPFGGVKDSGVGREGGRWSLGFFSEPM 502
Cdd:cd07095 394 PTtgassTAPFGGVGLSGNHRPSAYYAADYCAYPV 428
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
53-498 |
1.57e-70 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 232.44 E-value: 1.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 53 PATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAvDAYR 132
Cdd:PRK13968 14 PATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-EVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 133 SVANFRFFAGliREKADSPNEIFEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTAN 212
Cdd:PRK13968 93 SANLCDWYAE--HGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 213 LLMETIDEVGLPAGVVNLVHGNGAGAGgPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDL 292
Cdd:PRK13968 171 LIAQVFKDAGIPQGVYGWLNADNDGVS-QMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 293 EKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQEE 372
Cdd:PRK13968 250 ELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 373 GGEVLTGGHpclpKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKG 452
Cdd:PRK13968 330 GARLLLGGE----KIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQA 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 663513266 453 RRVAESIDTGMVWVNTWLHRDLRVPFGGVKDSGVGREGGRWSLGFF 498
Cdd:PRK13968 406 RQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
37-491 |
4.27e-70 |
|
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: 232.86 E-value: 4.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 37 HSGNEADENNWLNVLEPATGYR-FARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALES 115
Cdd:cd07125 37 INGEETETGEGAPVIDPADHERtIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 116 RDTGKpiALARAVDAYRSVANF-RFFAGLIREKADSPnEIFEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIG 194
Cdd:cd07125 117 AEAGK--TLADADAEVREAIDFcRYYAAQARELFSDP-ELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 195 MGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTgAKVAAAAAPQFK-- 272
Cdd:cd07125 194 AGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTET-AKLINRALAERDgp 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 273 --KLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETEL 350
Cdd:cd07125 273 ilPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 351 GALISPDHLAKVEGYVALAQEEGGEVltggHPC-LPKEFehGNWLAPTVIAGLSPDarCSTEEIFGPVVTIHRFEAE--E 427
Cdd:cd07125 353 GPLIDKPAGKLLRAHTELMRGEAWLI----APApLDDGN--GYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFKAEdlD 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 428 EAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNtwlhRD------LRVPFGGVKDSGVGREGG 491
Cdd:cd07125 425 EAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN----RNitgaivGRQPFGGWGLSGTGPKAG 490
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
48-491 |
1.52e-68 |
|
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: 227.47 E-value: 1.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 48 LNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARA 127
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 128 -VDAYRSVANF-----RFFAGLIrekadSPNE-----IFEMDNatnvvvskPVGVAALITPWNLPLYLLSWKVAPAIGMG 196
Cdd:cd07130 94 eVQEMIDICDFavglsRQLYGLT-----IPSErpghrMMEQWN--------PLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 197 NTVVCKPSELTPMTA----NLLMETIDEVGLPAGVVNLVHGnGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFK 272
Cdd:cd07130 161 NVVVWKPSPTTPLTAiavtKIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 273 KLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGA 352
Cdd:cd07130 240 RSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 353 LISPDHLAKVEGYVALAQEEGGEVLTGGHpclpKEFEHGNWLAPTVIAGLsPDARCSTEEIFGPVVTIHRFEAEEEAVAI 432
Cdd:cd07130 320 LHTKAAVDNYLAAIEEAKSQGGTVLFGGK----VIDGPGNYVEPTIVEGL-SDAPIVKEETFAPILYVLKFDTLEEAIAW 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663513266 433 ANNTRYGLAGSVWTGDLdkgRRVAESI-----DTGMVWVNtwlhrdlrVP---------FGGVKDSGVGREGG 491
Cdd:cd07130 395 NNEVPQGLSSSIFTTDL---RNAFRWLgpkgsDCGIVNVN--------IGtsgaeiggaFGGEKETGGGRESG 456
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
29-487 |
6.29e-66 |
|
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: 220.52 E-value: 6.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYE 108
Cdd:TIGR01722 4 WIGGKFA-----EGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 109 DIAALESRDTGKPIALARAvDAYRSVAnfrffaglIREKADSPNEIFEMDNATNVV-------VSKPVGVAALITPWNLP 181
Cdd:TIGR01722 79 EIAELITAEHGKTHSDALG-DVARGLE--------VVEHACGVNSLLKGETSTQVAtrvdvysIRQPLGVCAGITPFNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 182 LYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGnGAGAGGPLTTHSDVDLVSFTGGTDTGA 261
Cdd:TIGR01722 150 AMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 262 KVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSrILVQSGIYDEFVERFVDSVESMRIG 341
Cdd:TIGR01722 229 YIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS-AAVLVGAADEWVPEIRERAEKIRIG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 342 DPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIH 421
Cdd:TIGR01722 308 PGDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVL 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663513266 422 RFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTwlhrDLRVP-----FGGVKDSGVG 487
Cdd:TIGR01722 388 EADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV----PIPVPlpyfsFTGWKDSFFG 454
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
29-485 |
4.05e-64 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 215.98 E-value: 4.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEFVGHSGNEadennwLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYE 108
Cdd:PRK09457 4 WINGDWIAGQGEA------FESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 109 DIAALESRDTGKPI--------ALARAVDAyrSVANFRFFAGlirEKADspneifEMDNATNVVVSKPVGVAALITPWNL 180
Cdd:PRK09457 78 ELAEVIARETGKPLweaatevtAMINKIAI--SIQAYHERTG---EKRS------EMADGAAVLRHRPHGVVAVFGPYNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 181 PLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGnGAGAGGPLTTHSDVDLVSFTGGTDTG 260
Cdd:PRK09457 147 PGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 261 AKVAAaaapQF-----KKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIY-DEFVERFVDS 334
Cdd:PRK09457 226 YLLHR----QFagqpeKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 335 VESMRIGDPsNDETE--LGALISpdhLAKVEGYVAlAQEE----GGEVLTggHPCLPKEfEHGnWLAP-----TVIAGLs 403
Cdd:PRK09457 302 AKRLTVGRW-DAEPQpfMGAVIS---EQAAQGLVA-AQAQllalGGKSLL--EMTQLQA-GTG-LLTPgiidvTGVAEL- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 404 PDarcstEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVwvnTWlHRDLR-----VPF 478
Cdd:PRK09457 372 PD-----EEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIV---NW-NKPLTgassaAPF 442
|
....*..
gi 663513266 479 GGVKDSG 485
Cdd:PRK09457 443 GGVGASG 449
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
84-508 |
1.29e-59 |
|
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: 204.35 E-value: 1.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 84 WGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIAlaRAVDAYRSVANF-RFFAGLIREKADSPNEIFEMDNATN 162
Cdd:cd07083 71 WKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWV--EAIDDVAEAIDFiRYYARAALRLRYPAVEVVPYPGEDN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 163 VVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPL 242
Cdd:cd07083 149 ESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 243 TTHSDVDLVSFTGGTDTGAKV------AAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSR 316
Cdd:cd07083 229 TEHERIRGINFTGSLETGKKIyeaaarLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 317 ILVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQEEgGEVLTGGHpCLPKEfehGNWLAP 396
Cdd:cd07083 309 LILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNE-GQLVLGGK-RLEGE---GYFVAP 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 397 TVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVA--IANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHRDL 474
Cdd:cd07083 384 TVVEEVPPKARIAQEEIFGPVLSVIRYKDDDFAEAleVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGAL 463
|
410 420 430
....*....|....*....|....*....|....*..
gi 663513266 475 --RVPFGGVKDSGVG-REGGRWSLGFFSEPMNICLKH 508
Cdd:cd07083 464 vgVQPFGGFKLSGTNaKTGGPHYLRRFLEMKAVAERF 500
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
48-490 |
1.72e-56 |
|
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: 194.94 E-value: 1.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 48 LNVLEPATGYRFARVPLSGPDDVDaaviaaraaapdwGALD-----FAERADW---------LDRIADALETKYEDIAAL 113
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAID-------------KALDtahalFLDRNNWlpaheriaiLERLADLMEERADELALL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 114 ESRDTGKPIALARaVDAYRSVANFRFFAGLIREKADSpnEIfEMD------NATNVVVSKPVGVAALITPWNLPLYLLSW 187
Cdd:cd07148 68 IAREGGKPLVDAK-VEVTRAIDGVELAADELGQLGGR--EI-PMGltpasaGRIAFTTREPIGVVVAISAFNHPLNLIVH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 188 KVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGgPLTTHSDVDLVSFTGGTDTGAKVAAAA 267
Cdd:cd07148 144 QVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAE-KLVTDPRVAFFSFIGSARVGWMLRSKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 268 APQfKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDE 347
Cdd:cd07148 223 APG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 348 TELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKEFehgnwlAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEE 427
Cdd:cd07148 302 TEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY------APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663513266 428 EAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTwlHRDLRV---PFGGVKDSGVGREG 490
Cdd:cd07148 376 EAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND--HTAFRVdwmPFAGRRQSGYGTGG 439
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
164-499 |
1.19e-54 |
|
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: 189.27 E-value: 1.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 164 VVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVgLPAGVVNLVHGnGAGAGGPLT 243
Cdd:cd07087 96 VIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-GVEVATALL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 244 THSdVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGI 323
Cdd:cd07087 174 AEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 324 YDEFVERFVDSVESMrIGDPSNDETELGALISPDHLAKVEGYValaqeEGGEVLTGGhpclpkEFEHGN-WLAPTVIAGL 402
Cdd:cd07087 253 KDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGG------QVDKEErYIAPTILDDV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 403 SPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVN-TWLH---RDLrvPF 478
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdVLLHaaiPNL--PF 398
|
330 340
....*....|....*....|.
gi 663513266 479 GGVKDSGVGREGGRWSLGFFS 499
Cdd:cd07087 399 GGVGNSGMGAYHGKAGFDTFS 419
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
90-499 |
2.50e-51 |
|
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: 180.50 E-value: 2.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 90 AERADWLDRIADALETKYEDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIRE-----KADSPNEIFemdNATNVV 164
Cdd:cd07134 20 AERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKwmkpkRVRTPLLLF---GTKSKI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 165 VSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVgLPAGVVNLVHGNGAGAGGPLTT 244
Cdd:cd07134 97 RYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEGDAEVAQALLEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 245 hsDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIY 324
Cdd:cd07134 176 --PFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 325 DEFVERFVDSVESMRIGDPSNDETE-LGALISPDHLAKVEGYVALAQEEGGEVLTGGhpclpkEF-EHGNWLAPTVIAGL 402
Cdd:cd07134 254 DAFVEHLKAEIEKFYGKDAARKASPdLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG------QFdAAQRYIAPTVLTNV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 403 SPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTW----LHRDLrvPF 478
Cdd:cd07134 328 TPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVvlhfLNPNL--PF 405
|
410 420
....*....|....*....|...
gi 663513266 479 GGVKDSGVGREGGRWslGF--FS 499
Cdd:cd07134 406 GGVNNSGIGSYHGVY--GFkaFS 426
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
29-495 |
8.35e-51 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 180.72 E-value: 8.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 29 YIGGEF-VGHSGNEadennwLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKY 107
Cdd:PLN00412 19 YADGEWrTSSSGKS------VAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 108 EDIAALESRDTGKPIALAR-------------AVDAYRSVANFRF-----FAGLIREKAdspneifemdnatnVVVSK-P 168
Cdd:PLN00412 93 APIAECLVKEIAKPAKDAVtevvrsgdlisytAEEGVRILGEGKFlvsdsFPGNERNKY--------------CLTSKiP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 169 VGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDV 248
Cdd:PLN00412 159 LGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 249 DLVSFTGGtDTGAKVAaaaapqfKK-----LSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGI 323
Cdd:PLN00412 239 NCISFTGG-DTGIAIS-------KKagmvpLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 324 YDEFVERFVDSVESMRIGDPsNDETELGALISPDHLAKVEGYVALAQEEGGEVLTgghpclpkEFE-HGNWLAPTVIAGL 402
Cdd:PLN00412 311 ADALVEKVNAKVAKLTVGPP-EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQ--------EWKrEGNLIWPLLLDNV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 403 SPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTWLHR--DlRVPFGG 480
Cdd:PLN00412 382 RPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARgpD-HFPFQG 460
|
490
....*....|....*
gi 663513266 481 VKDSGVGREGGRWSL 495
Cdd:PLN00412 461 LKDSGIGSQGITNSI 475
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
21-485 |
3.57e-50 |
|
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: 179.70 E-value: 3.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 21 AAPLDLLNYIGGEfvghsgnEADENNWLNVLEPAT-GYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRI 99
Cdd:cd07123 28 SLTVEIPLVIGGK-------EVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 100 ADALETKY-EDIAALESRDTGKPIALARaVDAYRSVANF-RF---FAGLIreKADSPNEIFEmdNATNVVVSKPV-GVAA 173
Cdd:cd07123 101 ADLLSGKYrYELNAATMLGQGKNVWQAE-IDAACELIDFlRFnvkYAEEL--YAQQPLSSPA--GVWNRLEYRPLeGFVY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 174 LITPWN-------LPLyllswkvAPAIgMGNTVVCKPSElTPMTAN-LLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTH 245
Cdd:cd07123 176 AVSPFNftaiggnLAG-------APAL-MGNVVLWKPSD-TAVLSNyLVYKILEEAGLPPGVINFVPGDGPVVGDTVLAS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 246 SDVDLVSFTGGTDT--------GAKVAAAAapQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRI 317
Cdd:cd07123 247 PHLAGLHFTGSTPTfkslwkqiGENLDRYR--TYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 318 LVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQEEGG-EVLTGGHpCLPKEfehGNWLAP 396
Cdd:cd07123 325 YVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEaEIIAGGK-CDDSV---GYFVEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 397 TVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIA---NNTRYGLAGSVWTGD-------LDKGRRVAesidtGMVWV 466
Cdd:cd07123 401 TVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLElvdTTSPYALTGAIFAQDrkaireaTDALRNAA-----GNFYI 475
|
490 500
....*....|....*....|....*.
gi 663513266 467 NtwlhrDL-------RVPFGGVKDSG 485
Cdd:cd07123 476 N-----DKptgavvgQQPFGGARASG 496
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
87-499 |
4.02e-49 |
|
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: 174.72 E-value: 4.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 87 LDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIR-----EKADSPNEIFEMDNAT 161
Cdd:cd07135 24 KDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKkwakdEKVKDGPLAFMFGKPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 162 nvVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEvGLPAGVVNLVHGngagaGGP 241
Cdd:cd07135 104 --IRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPK-YLDPDAFQVVQG-----GVP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 242 LTT---HSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRIL 318
Cdd:cd07135 176 ETTallEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 319 VQSGIYDEFVERFVDSVESMRIGDPsNDETELGALISPDHLAKVEGyvaLAQEEGGEVLTGGHPCLPKEFehgnwLAPTV 398
Cdd:cd07135 256 VDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKS---LLDTTKGKVVIGGEMDEATRF-----IPPTI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 399 IAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVN-TWLHRDLR-V 476
Cdd:cd07135 327 VSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdTLIHVGVDnA 406
|
410 420
....*....|....*....|...
gi 663513266 477 PFGGVKDSGVGREGGRWSLGFFS 499
Cdd:cd07135 407 PFGGVGDSGYGAYHGKYGFDTFT 429
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
15-500 |
9.45e-48 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 174.55 E-value: 9.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 15 ERDRDGAAPLDLLNYIGGEFVghsgnEADENNWLNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERAD 94
Cdd:PLN02419 103 EQSTQPQMPPRVPNLIGGSFV-----ESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 95 WLDRIADALETKYEDIAALESRDTGKPIALARAvDAYRSVANFRFFAGLIREKADS--PNEIFEMDNATnvvVSKPVGVA 172
Cdd:PLN02419 178 VMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEylPNVSNGVDTYS---IREPLGVC 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 173 ALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGpLTTHSDVDLVS 252
Cdd:PLN02419 254 AGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVS 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 253 FTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRIlVQSGIYDEFVERFV 332
Cdd:PLN02419 333 FVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV-VFVGDAKSWEDKLV 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 333 DSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKEFEHGNWLAPTVIAGLSPDARCSTEE 412
Cdd:PLN02419 412 ERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEE 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 413 IFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNTwlhrDLRVP-----FGGVKDSGVG 487
Cdd:PLN02419 492 IFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV----PIPVPlpffsFTGNKASFAG 567
|
490
....*....|....*
gi 663513266 488 REG--GRWSLGFFSE 500
Cdd:PLN02419 568 DLNfyGKAGVDFFTQ 582
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
145-508 |
1.12e-47 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 172.14 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 145 REKADSPNEIFEmdnATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVgLP 224
Cdd:PTZ00381 89 PEKVDTVGVFGP---GKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 225 AGVVNLVHGnGAGAGGPLTTHSdVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAF 304
Cdd:PTZ00381 165 PSYVRVIEG-GVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKF 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 305 LNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNdETELGALISPDHLAKVEGyvaLAQEEGGEVLTGGhpcl 384
Cdd:PTZ00381 243 LNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKK-SEDYSRIVNEFHTKRLAE---LIKDHGGKVVYGG---- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 385 pkEFEHGN-WLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGM 463
Cdd:PTZ00381 315 --EVDIENkYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGA 392
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 663513266 464 VWVN-TWLH-RDLRVPFGGVKDSGVGREGGRWSLGFFSEPMNICLKH 508
Cdd:PTZ00381 393 VVINdCVFHlLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKS 439
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
20-491 |
1.15e-46 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 169.63 E-value: 1.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 20 GAAPLDLLNYIGGEFvGHSGNEADENNwlnvlePATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRI 99
Cdd:PLN02315 15 GLSSRNLGCYVGGEW-RANGPLVSSVN------PANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 100 ADALETKYEDIAALESRDTGKpiALARAVDAYRSVANFRFFA-GLIREKADS--PNEifeMDNATNVVVSKPVGVAALIT 176
Cdd:PLN02315 88 GDALRAKLDYLGRLVSLEMGK--ILAEGIGEVQEIIDMCDFAvGLSRQLNGSiiPSE---RPNHMMMEVWNPLGIVGVIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 177 PWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPM----TANLLMETIDEVGLPAGVVNLVHGnGAGAGGPLTTHSDVDLVS 252
Cdd:PLN02315 163 AFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLitiaMTKLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 253 FTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFV 332
Cdd:PLN02315 242 FTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 333 DSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPCLPKefehGNWLAPTVIAgLSPDARCSTEE 412
Cdd:PLN02315 322 TVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESE----GNFVQPTIVE-ISPDADVVKEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 413 IFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTgdldkgrRVAESI---------DTGMVWVNTWLH-RDLRVPFGGVK 482
Cdd:PLN02315 397 LFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFT-------RNPETIfkwigplgsDCGIVNVNIPTNgAEIGGAFGGEK 469
|
....*....
gi 663513266 483 DSGVGREGG 491
Cdd:PLN02315 470 ATGGGREAG 478
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
82-491 |
3.92e-46 |
|
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: 168.17 E-value: 3.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 82 PDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKpiALARAVDAYRSVANF-RFFAGLIREkaDSPNEifemdna 160
Cdd:TIGR01238 88 PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGK--TIHNAIAEVREAVDFcRYYAKQVRD--VLGEF------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 161 tnvvVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGG 240
Cdd:TIGR01238 157 ----SVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 241 PLTTHSDVDLVSFTGGTDTGAKVAAAAAPQFK---KLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRI 317
Cdd:TIGR01238 233 ALTSDPRIAGVAFTGSTEVAQLINQTLAQREDapvPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 318 LVQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQEEG---GEVLTGGhpclPKEFEHGNWL 394
Cdd:TIGR01238 313 CVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDD----SRACQHGTFV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 395 APTVIAGLSPDARcsTEEIFGPVVTIHRFEAEEEAVAIA--NNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNtwlhR 472
Cdd:TIGR01238 389 APTLFELDDIAEL--SEEVFGPVLHVVRYKARELDQIVDqiNQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN----R 462
|
410 420
....*....|....*....|....*
gi 663513266 473 DL------RVPFGGVKDSGVGREGG 491
Cdd:TIGR01238 463 NQvgavvgVQPFGGQGLSGTGPKAG 487
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
39-480 |
9.66e-46 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 172.04 E-value: 9.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 39 GNEADENNWLNVLEPATGYRFA-RVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRD 117
Cdd:COG4230 563 AGEAASGEARPVRNPADHSDVVgTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVRE 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 118 TGK--PIALA--R-AVDayrsvanF-RFFAGLIREkadspneifEMDNATnvvVSKPVGVAALITPWNLPLYLLSWKVAP 191
Cdd:COG4230 643 AGKtlPDAIAevReAVD-------FcRYYAAQARR---------LFAAPT---VLRGRGVFVCISPWNFPLAIFTGQVAA 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 192 AIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTG-------AKVA 264
Cdd:COG4230 704 ALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETArlinrtlAARD 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 265 AAAAPqfkkLSLELGGKNASIIfddcD----LEKTVPGVTRAAFLNQGQVClcgS--RIL-VQSGIYDEFVERFVDSVES 337
Cdd:COG4230 784 GPIVP----LIAETGGQNAMIV----DssalPEQVVDDVLASAFDSAGQRC---SalRVLcVQEDIADRVLEMLKGAMAE 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 338 MRIGDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGhpcLPKEFEHGNWLAPTVIAGLSPDARcsTEEIFGPV 417
Cdd:COG4230 853 LRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLP---LPEECANGTFVAPTLIEIDSISDL--EREVFGPV 927
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663513266 418 VTIHRFEAEEEAV--AIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNtwlhRDL---RV---PFGG 480
Cdd:COG4230 928 LHVVRYKADELDKviDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN----RNIigaVVgvqPFGG 994
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
88-499 |
2.57e-45 |
|
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: 164.20 E-value: 2.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 88 DFAERADWLDRIADALetkyediaaLESRDtgkpiALARAVDA---YRSVANFRF--FAGLIREKADSpneifeMDN--- 159
Cdd:cd07133 18 SLEERRDRLDRLKALL---------LDNQD-----ALAEAISAdfgHRSRHETLLaeILPSIAGIKHA------RKHlkk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 160 ---------------ATNVVVSKPVGVAALITPWNLPLYLLswkVAPAIGM---GNTVVCKPSELTPMTANLLMETIDEV 221
Cdd:cd07133 78 wmkpsrrhvgllflpAKAEVEYQPLGVVGIIVPWNYPLYLA---LGPLIAAlaaGNRVMIKPSEFTPRTSALLAELLAEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 222 gLPAGVVNLVHGnGAGAGGPLTT----HsdvdLVsFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVP 297
Cdd:cd07133 155 -FDEDEVAVVTG-GADVAAAFSSlpfdH----LL-FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 298 GVTRAAFLNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDetELGALISPDHLAKVEGYVALAQEEGGEVl 377
Cdd:cd07133 228 RIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNP--DYTSIINERHYARLQGLLEDARAKGARV- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 378 tggHPCLPK--EFEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRV 455
Cdd:cd07133 305 ---IELNPAgeDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRV 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 663513266 456 AESIDTGMVWVNTWL-H---RDLrvPFGGVKDSGVGREGGRWslGF--FS 499
Cdd:cd07133 382 LRRTHSGGVTINDTLlHvaqDDL--PFGGVGASGMGAYHGKE--GFltFS 427
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
50-487 |
3.30e-44 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 167.35 E-value: 3.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPA-TGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKpiALARAV 128
Cdd:PRK11905 571 VLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGK--TLANAI 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 129 DAYRSVANF-RFFAGLIREKADSPneifemdnatnvvVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELT 207
Cdd:PRK11905 649 AEVREAVDFlRYYAAQARRLLNGP-------------GHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQT 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 208 PMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTG-------AKVAAAAAPqfkkLSLELGG 280
Cdd:PRK11905 716 PLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVArliqrtlAKRSGPPVP----LIAETGG 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 281 KNASIIfDDCDL-EKTVPGVTRAAFLNQGQVClcgS--RIL-VQSGIYDEFVERFVDSVESMRIGDPSNDETELGALISP 356
Cdd:PRK11905 792 QNAMIV-DSSALpEQVVADVIASAFDSAGQRC---SalRVLcLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDA 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 357 DHLAKVEGYVALAQEEGGEVltggHPC-LPKEFEHGNWLAPTVI--AGLSPDARcsteEIFGPVVTIHRFEAEEEAV--A 431
Cdd:PRK11905 868 EAQANIEAHIEAMRAAGRLV----HQLpLPAETEKGTFVAPTLIeiDSISDLER----EVFGPVLHVVRFKADELDRviD 939
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663513266 432 IANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNtwlhrdlR------V---PFGGVKDSGVG 487
Cdd:PRK11905 940 DINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN-------RniigavVgvqPFGGEGLSGTG 997
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
50-487 |
1.57e-43 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 165.37 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 50 VLEPATGYRFA-RVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKpiALARAV 128
Cdd:PRK11904 566 VVSPADRRRVVgEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGK--TLQDAI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 129 DAYRSVANF-RFFAGLIREKADSPNEIFEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELT 207
Cdd:PRK11904 644 AEVREAVDFcRYYAAQARRLFGAPEKLPGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQT 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 208 PMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDT------------GAKVaaaaaPqfkkLS 275
Cdd:PRK11904 724 PLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETariinrtlaardGPIV-----P----LI 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 276 LELGGKNASIIfDDCDL-EKTVPGVTRAAFLNQGQVClcgS--RIL-VQSGIYDEFVERFVDSVESMRIGDPSNDETELG 351
Cdd:PRK11904 795 AETGGQNAMIV-DSTALpEQVVDDVVTSAFRSAGQRC---SalRVLfVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVG 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 352 ALISPDHLAKVEGYVALAQEEGGEVLTGGhpcLPKEFEHGNWLAPTVIAglSPDARCSTEEIFGPVVTIHRFEAEEEAV- 430
Cdd:PRK11904 871 PVIDAEAKANLDAHIERMKREARLLAQLP---LPAGTENGHFVAPTAFE--IDSISQLEREVFGPILHVIRYKASDLDKv 945
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663513266 431 -AIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNtwlhRDL--RV----PFGGVKDSGVG 487
Cdd:PRK11904 946 iDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN----RNQigAVvgvqPFGGQGLSGTG 1005
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
164-499 |
1.38e-42 |
|
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: 157.28 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 164 VVSKPVGVAALITPWNLPLYLLswkVAPAIGM---GNTVVCKPSELTPMTANLLMETIDEVgLPAGVVNLVHGngagaGG 240
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFQLA---LAPLIGAiaaGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-----GV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 241 PLTT---HSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRI 317
Cdd:cd07136 167 EENQellDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 318 LVQSGIYDEFVERFVDSVESMRIGDPSNDEtELGALISPDHLAKVEGYValaqeEGGEVLTGGhpclpKEFEHGNWLAPT 397
Cdd:cd07136 247 LVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLL-----DNGKIVFGG-----NTDRETLYIEPT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 398 VIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVN-TWLH-RDLR 475
Cdd:cd07136 316 ILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdTIMHlANPY 395
|
330 340
....*....|....*....|....
gi 663513266 476 VPFGGVKDSGVGREGGRWSLGFFS 499
Cdd:cd07136 396 LPFGGVGNSGMGSYHGKYSFDTFS 419
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
82-420 |
3.17e-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: 3.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 82 PDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALAraVDAYRSVANFRFFAGLI------REKADSPNEIF 155
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA--ENICGDQVQLRARAFVIysyripHEPGNHLGQGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 156 EMDNATNVVvskPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVG-LPAGVVNLVHGN 234
Cdd:cd07084 91 KQQSHGYRW---PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 235 GAgAGGPLTTHSDVDLVSFTGGTDTGAKVaaAAAPQFKKLSLELGGKNASIIFDDCDLEKTVP-GVTRAAFLNQGQVCLC 313
Cdd:cd07084 168 GK-TMQALLLHPNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQAVDYVAwQCVQDMTACSGQKCTA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 314 GSRILVQSgiyDEFVERFVDSVESMrIGDPSNDETELGALISPDHLAKVEGyvalAQEEGGEVLTGGHPCLPKEFEHGNW 393
Cdd:cd07084 245 QSMLFVPE---NWSKTPLVEKLKAL-LARRKLEDLLLGPVQTFTTLAMIAH----MENLLGSVLLFSGKELKNHSIPSIY 316
|
330 340 350
....*....|....*....|....*....|...
gi 663513266 394 ---LAPTVIAGLSPDARCS---TEEIFGPVVTI 420
Cdd:cd07084 317 gacVASALFVPIDEILKTYelvTEEIFGPFAIV 349
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
39-491 |
1.98e-38 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 150.12 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 39 GNEADENNWLNVLEPAT-----GYrfarVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAAL 113
Cdd:PRK11809 652 EDPVAAGEMSPVINPADprdivGY----VREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGL 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 114 ESRDTGKpiALARAVDAYRSVANF-RFFAGLIREkadspneifEMDNATNvvvsKPVGVAALITPWNLPLYLLSWKVAPA 192
Cdd:PRK11809 728 LVREAGK--TFSNAIAEVREAVDFlRYYAGQVRD---------DFDNDTH----RPLGPVVCISPWNFPLAIFTGQVAAA 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 193 IGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGA----KVAAAAA 268
Cdd:PRK11809 793 LAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARllqrNLAGRLD 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 269 PQFKKLSL--ELGGKNASIIfDDCDL-EKTVPGVTRAAFLNQGQVC-----LCgsrilVQSGIYDEFVERFVDSVESMRI 340
Cdd:PRK11809 873 PQGRPIPLiaETGGQNAMIV-DSSALtEQVVADVLASAFDSAGQRCsalrvLC-----LQDDVADRTLKMLRGAMAECRM 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 341 GDPSNDETELGALISPDHLAKVEGYVALAQEEGGEVLTGGHPClPKEFEHGNWLAPTVIAGLSPDARcsTEEIFGPVVTI 420
Cdd:PRK11809 947 GNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAAREN-SEDWQSGTFVPPTLIELDSFDEL--KREVFGPVLHV 1023
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 421 HRFEAEEEAVAIA--NNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVNtwlhRDLrV-------PFGGVKDSGVGREGG 491
Cdd:PRK11809 1024 VRYNRNQLDELIEqiNASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN----RNM-VgavvgvqPFGGEGLSGTGPKAG 1098
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
157-499 |
3.95e-36 |
|
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: 139.28 E-value: 3.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 157 MDNAtnVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETI----DEVGLPagVVNlvh 232
Cdd:cd07132 91 LDDV--YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkylDKECYP--VVL--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 233 gngagAGGPLTT---HSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQ 309
Cdd:cd07132 164 -----GGVEETTellKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 310 VCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSNDEtELGALISPDHLAKVEGYValaqeEGGEVLTGGHpCLPKEfe 389
Cdd:cd07132 239 TCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESP-DYGRIINDRHFQRLKKLL-----SGGKVAIGGQ-TDEKE-- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 390 hgNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMVWVN-T 468
Cdd:cd07132 310 --RYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdT 387
|
330 340 350
....*....|....*....|....*....|..
gi 663513266 469 WLHRDLRV-PFGGVKDSGVGREGGRWSLGFFS 499
Cdd:cd07132 388 IMHYTLDSlPFGGVGNSGMGAYHGKYSFDTFS 419
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
146-499 |
1.48e-31 |
|
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: 126.37 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 146 EKADSPNEIFEmdnATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVgLPA 225
Cdd:cd07137 82 EKVKTPLTTFP---AKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 226 GVVNLVHGngagaGGPLTTH---SDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRA 302
Cdd:cd07137 158 KAIKVIEG-----GVPETTAlleQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 303 AF-LNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMrIGDPSNDETELGALISPDHLAKVEGY-----VALAQEEGGEV 376
Cdd:cd07137 233 KWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLlddpsVADKIVHGGER 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 377 LtgghpclpkefEHGNWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVA 456
Cdd:cd07137 312 D-----------EKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIV 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 663513266 457 ESIDTGMVWVN-TWLHRDLR-VPFGGVKDSGVGREGGRWSLGFFS 499
Cdd:cd07137 381 AETSSGGVTFNdTVVQYAIDtLPFGGVGESGFGAYHGKFSFDAFS 425
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
26-456 |
5.27e-27 |
|
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: 113.90 E-value: 5.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 26 LLNYIGGEFVGHSGNEAdennwlNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALET 105
Cdd:cd07128 1 LQSYVAGQWHAGTGDGR------TLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLME 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 106 KYEDIAALeSRDTGkpiALAR--AVDAYRSVANFRFFAGLIREKADSPNEIFEMD----------NATNVVVSKPvGVAA 173
Cdd:cd07128 75 RKEDLYAL-SAATG---ATRRdsWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDveplskdgtfVGQHILTPRR-GVAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 174 LITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVG-LPAGVVNLVhgngAGAGGPLTTH-SDVDLV 251
Cdd:cd07128 150 HINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLI----CGSVGDLLDHlGEQDVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 252 SFTGGTDTGAKVAAAaaPQFKK----LSLELGGKNASII-----FDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQSG 322
Cdd:cd07128 226 AFTGSAATAAKLRAH--PNIVArsirFNAEADSLNAAILgpdatPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 323 IYDEFVERFVDSVESMRIGDPSNDETELGALISPDHLAKVEGYVALAQEEgGEVLTGGHPCLPKEFEH---GNWLAPTVI 399
Cdd:cd07128 304 RVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGPDRFEVVGADaekGAFFPPTLL 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 663513266 400 AGLSPDARCSTEEI--FGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVA 456
Cdd:cd07128 383 LCDDPDAATAVHDVeaFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
146-499 |
5.29e-25 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 107.82 E-value: 5.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 146 EKADSPNEIFEmdnATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVgLPA 225
Cdd:PLN02174 93 EKAKTSLTTFP---ASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 226 GVVNLVHGNGAGAGGPLttHSDVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAF- 304
Cdd:PLN02174 169 SAVRVVEGAVTETTALL--EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWg 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 305 LNQGQVCLCGSRILVQSGIYDEFVERFVDSVESMRIGDPSnDETELGALISPDHLAKVEGYVAlAQEEGGEVLTGGHpcl 384
Cdd:PLN02174 247 CNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPM-ESKDMSRIVNSTHFDRLSKLLD-EKEVSDKIVYGGE--- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 385 pKEFEHGNwLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESIDTGMV 464
Cdd:PLN02174 322 -KDRENLK-IAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGI 399
|
330 340 350
....*....|....*....|....*....|....*..
gi 663513266 465 WVN-TWLHRDLR-VPFGGVKDSGVGREGGRWSLGFFS 499
Cdd:PLN02174 400 VVNdIAVHLALHtLPFGGVGESGMGAYHGKFSFDAFS 436
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
146-499 |
6.54e-25 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 107.50 E-value: 6.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 146 EKADSPNEIFEmdnATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVgLPA 225
Cdd:PLN02203 89 KKAKLPLVAFP---ATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 226 GVVNLVHGnGAGAGGPLTTHSdVDLVSFTGGTDTGAKVAAAAAPQFKKLSLELGGKNASIIfdDC-----DLEKTVPGVT 300
Cdd:PLN02203 165 KAVKVIEG-GPAVGEQLLQHK-WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIV--DSlsssrDTKVAVNRIV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 301 RAAFLN-QGQVCLCGSRILVQSGIYDEFVERFVDSVESMrIGDPSNDETELGALISPDHLAKVEGYVALAQEEgGEVLTG 379
Cdd:PLN02203 241 GGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKF-FGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 380 GHpCLPKEFehgnWLAPTVIAGLSPDARCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVAESI 459
Cdd:PLN02203 319 GS-IDEKKL----FIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSET 393
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 663513266 460 DTGMVWVNTWLHRDL--RVPFGGVKDSGVGREGGRWSLGFFS 499
Cdd:PLN02203 394 SSGSVTFNDAIIQYAcdSLPFGGVGESGFGRYHGKYSFDTFS 435
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
26-456 |
1.15e-24 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 107.10 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 26 LLNYIGGEFVGHSGNEAdennwlNVLEPATGYRFARVPLSGPDDVDAAVIAARAAAPDWGALDFAERADWLDRIADALET 105
Cdd:PRK11903 5 LANYVAGRWQAGSGAGT------PLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 106 KYEDIAALESRDTGKpIALARAVDAYRSVANFRFFA------GLIREKADSPNEIFEMDNA---TNVVVSKPvGVAALIT 176
Cdd:PRK11903 79 NRDAYYDIATANSGT-TRNDSAVDIDGGIFTLGYYAklgaalGDARLLRDGEAVQLGKDPAfqgQHVLVPTR-GVALFIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 177 PWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVG-LPAGVVNLVHGNGAGaggpLTTH-SDVDLVSFT 254
Cdd:PRK11903 157 AFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAG----LLDHlQPFDVVSFT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 255 GGTDTGAKVAA--AAAPQFKKLSLELGGKNASIIFDDCD-----LEKTVPGVTRAAFLNQGQVCLCGSRILVQSGIYDEF 327
Cdd:PRK11903 233 GSAETAAVLRShpAVVQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 328 VERFVDSVESMRIGDPSNDETELGALISPDHLAKV-EGYVALAQEegGEVLTGG--HPCLPKEFEHGNWLAPTVIAGLSP 404
Cdd:PRK11903 313 AEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVrAGLAALRAQ--AEVLFDGggFALVDADPAVAACVGPTLLGASDP 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 663513266 405 DA--RCSTEEIFGPVVTIHRFEAEEEAVAIANNTRYGLAGSVWTGDLDKGRRVA 456
Cdd:PRK11903 391 DAatAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
82-417 |
1.89e-18 |
|
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: 87.60 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 82 PDWGALDFAERADWLDRIADALETKYEDIAALESRDTGKPIALARaVDAYRSVANFRFFAGLIREKA------DSPNEIF 155
Cdd:cd07129 13 ESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQ-GELGRTTGQLRLFADLVREGSwldariDPADPDR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 156 EMDNATNVVVSK-PVGVAALITPWNLPlylLSWKV-----APAIGMGNTVVCKPSELTPMTANLLMETIDEV----GLPA 225
Cdd:cd07129 92 QPLPRPDLRRMLvPLGPVAVFGASNFP---LAFSVaggdtASALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 226 GVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGT-------DTGAKvaaaaAPQFKKLSLELGGKNASIIFddcdlektvPG 298
Cdd:cd07129 169 GVFSLLQGGGREVGVALVKHPAIKAVGFTGSRrggralfDAAAA-----RPEPIPFYAELGSVNPVFIL---------PG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 299 VTRA-------AF-----LNQGQVCLC-GSRILVQSGIYDEFVERFVDSVEsmrigdpsndETELGALISPD-HLAKVEG 364
Cdd:cd07129 235 ALAErgeaiaqGFvgsltLGAGQFCTNpGLVLVPAGPAGDAFIAALAEALA----------AAPAQTMLTPGiAEAYRQG 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 663513266 365 YVALAQEEGGEVLTGGHpclpkEFEHGNWLAPTViagLSPDARCST------EEIFGPV 417
Cdd:cd07129 305 VEALAAAPGVRVLAGGA-----AAEGGNQAAPTL---FKVDAAAFLadpalqEEVFGPA 355
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
69-417 |
6.96e-13 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 70.97 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 69 DVDAAVIAARAAAPDWGALDFAERADWLDRIADALETKYEDIAALESRDTGK----------PIALARAVDA--YRSVAN 136
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQafmmafqaggPHAQDRGLEAvaYAWREM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 137 FRFFAGLIREKADSPNEIFEMDNATNVVvskPVGVAALITPWNLPlyllSWKVAP----AIGMGNTVVCKPSELT----P 208
Cdd:cd07127 165 SRIPPTAEWEKPQGKHDPLAMEKTFTVV---PRGVALVIGCSTFP----TWNGYPglfaSLATGNPVIVKPHPAAilplA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 209 MTANLLMETIDEVGLPAGVVNLV-HGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPqfKKLSLELGGKNASIIF 287
Cdd:cd07127 238 ITVQVAREVLAEAGFDPNLVTLAaDTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVVD 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 288 DDCDLEKTVPGVTRAAFLNQGQVCLCGSRILV-QSGI--------YDEFVERFVDSVESMrIGDPSNDETELGALISPDH 358
Cdd:cd07127 316 STDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDT 394
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663513266 359 LAKVE-----GYVALAQEEggevltGGHPCLPKEFEHgnwlAPTVIAGLSPDARCSTEEIFGPV 417
Cdd:cd07127 395 LARIAearqlGEVLLASEA------VAHPEFPDARVR----TPLLLKLDASDEAAYAEERFGPI 448
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
90-333 |
4.80e-08 |
|
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: 55.31 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 90 AERADWLDRIADALETKYEDIAALESRDTGKPIALARAVDAYRSVANFRFFAGLIREKADSPN------EIFEMDNATNV 163
Cdd:cd07077 16 EQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGITAsvghiqDVLLPDNGETY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 164 VVSKPVGVAALITPWNLPLYLLSwKVAPAIGMGNTVVCKPSELTPMTA---NLLMETIDEVGLPAGVVNLVHGNGAGAGG 240
Cdd:cd07077 96 VRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNralALLFQAADAAHGPKILVLYVPHPSDELAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 241 PLTTHSDVDLVSFTGGTDTgakVAAAAAPQFKKLSLELGGKNASIIFDDCDLEKTVPGVTRAAFLNQGQVCLCGSRILVQ 320
Cdd:cd07077 175 ELLSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQNACASEQNLYVV 251
|
250
....*....|...
gi 663513266 321 SGIYDEFVERFVD 333
Cdd:cd07077 252 DDVLDPLYEEFKL 264
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
150-331 |
8.40e-06 |
|
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: 48.03 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 150 SPNEIFEMDNATNVVVSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKP----SELTPMTANLLMETIDEVGLPA 225
Cdd:cd07081 77 TCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 226 GVVNLVHGNGAGAGGPLTTHSDVDLVSFTGGTDTGAKVAAAAAPqfkklSLELGGKNASIIFDD-CDLEKTVPGVTRAAF 304
Cdd:cd07081 157 NLIGWIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGKP-----AIGVGAGNTPVVIDEtADIKRAVQSIVKSKT 231
|
170 180
....*....|....*....|....*..
gi 663513266 305 LNQGQVCLCGSRILVQSGIYDEFVERF 331
Cdd:cd07081 232 FDNGVICASEQSVIVVDSVYDEVMRLF 258
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
168-281 |
1.20e-04 |
|
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: 44.41 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 168 PVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPSELTPMTANLLMETIDEVGLPAGVVNLVHGNGAgAGGPLTTHSD 247
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGP-TMNKILLEAN 220
|
90 100 110
....*....|....*....|....*....|....
gi 663513266 248 VDLVSFTGGTdtgaKVAaaaapqfKKLSLELGGK 281
Cdd:cd07126 221 PRMTLFTGSS----KVA-------ERLALELHGK 243
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
96-331 |
9.64e-03 |
|
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: 38.24 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 96 LDRI----ADALETKYEDIAALESRDTG------KPIALARAVDA-YRSVANFRFfAGLIREkadspneifemDNATNVV 164
Cdd:cd07122 23 VDKIveavAWAAADAAEELAKMAVEETGmgvvedKVIKNHFASEYvYNDIKDMKT-VGVIEE-----------DEEKGIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 165 -VSKPVGVAALITPWNLPLYLLSWKVAPAIGMGNTVVCKPS----ELTPMTANLLMETIDEVGLPAGVVNLVHGNGAGAG 239
Cdd:cd07122 91 eIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHprakKCSIEAAKIMREAAVAAGAPEGLIQWIEEPSIELT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513266 240 GPLTTHSDVDLVSFTGGT-------DTGakvaaaaapqfkKLSLELGGKNASIIFD-DCDLEKTVPG-VTRAAFLNqGQV 310
Cdd:cd07122 171 QELMKHPDVDLILATGGPgmvkaaySSG------------KPAIGVGPGNVPAYIDeTADIKRAVKDiILSKTFDN-GTI 237
|
250 260
....*....|....*....|.
gi 663513266 311 CLCGSRILVQSGIYDEFVERF 331
Cdd:cd07122 238 CASEQSVIVDDEIYDEVRAEL 258
|
|
| |
