|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
7-472 |
0e+00 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 767.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 7 QYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQ 86
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 87 AITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERRGDDLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSP 166
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 167 VVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLEL 246
Cdd:cd07138 161 VVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 247 GGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQ 326
Cdd:cd07138 241 GGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 327 FDQVQNYINKGIEEGAELFYGGPGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYG 406
Cdd:cd07138 321 FDRVQGYIQKGIEEGARLVAGGPGRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYG 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88196026 407 LAGYVIGKDKETLHKVARSIEAGTVEINEAGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSIAG 472
Cdd:cd07138 401 LAGYVWSADPERARAVARRLRAGQVHINGAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQG 466
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
5-471 |
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: 609.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 5 TKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDI 84
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 85 VQAITDELGAPLSLSeRVHYQMGLNHFVAARDALDNYEFEERRGDD-----LVVKEAIGVSGLITPWNFPTNQTSLKLAA 159
Cdd:COG1012 86 AALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDApgtraYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 160 AFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDF 239
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 240 KKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVG 319
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 320 PIISKKQFDQVQNYINKGIEEGAELFYGgpGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQI 399
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGAELLTG--GRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIAL 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88196026 400 ANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE--AGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSIA 471
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDgtTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVT 476
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
13-470 |
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: 595.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 13 WVESNSnETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDEL 92
Cdd:pfam00171 1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 93 GAPLSLSeRVHYQMGLNHFVAARDALDNYEFEERRGDD----LVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVV 168
Cdd:pfam00171 80 GKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPgrlaYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 169 LKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGG 248
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 249 KSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFD 328
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 329 QVQNYINKGIEEGAELFYGGpgkPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLA 408
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGG---EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88196026 409 GYVIGKDKETLHKVARSIEAGTVEINE--AGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:pfam00171 396 AGVFTSDLERALRVARRLEAGMVWINDytTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
8-470 |
0e+00 |
|
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: 535.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLE--FRHTSVKERQALLDKIVKEYENRKDDIV 85
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 86 QAITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERR-----GDDLVVKEAIGVSGLITPWNFPTNQTSLKLAAA 160
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRpgsggGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 161 FAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDgAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFK 240
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD-REVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 241 KVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGP 320
Cdd:cd07139 241 RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 321 IISKKQFDQVQNYINKGIEEGAELFYGGpGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIA 400
Cdd:cd07139 321 LASARQRERVEGYIAKGRAEGARLVTGG-GRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 401 NDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07139 400 NDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
24-471 |
0e+00 |
|
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: 527.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 24 VINPATEEVIGKVAKGNKADVDKAVEAADDVYLEF-RHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSERV 102
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 103 HYQMGLNHFVAARDALDNYEFEERRGDD---------LVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSE 173
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPalrggpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 174 ETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYI 253
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 254 VLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNY 333
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 334 INKGIEEGAELFYGGpGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIG 413
Cdd:cd07089 321 IARGRDEGARLVTGG-GRPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 88196026 414 KDKETLHKVARSIEAGTVEINEAG-RKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSIA 471
Cdd:cd07089 400 ADVDRAYRVARRIRTGSVGINGGGgYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIA 458
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
45-470 |
3.75e-172 |
|
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: 490.57 E-value: 3.75e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 45 DKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSlSERVHYQMGLNHFVAARDALDNYEFE 124
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 125 ERRGDDL-----VVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLV 199
Cdd:cd07078 80 VIPSPDPgelaiVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 200 NGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAK-ATTGKVVNNtGQV 278
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKgAVFGAFGNA-GQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 279 CTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGgpGKPEGLEKG 358
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCG--GKRLEGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 359 YFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE--A 436
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDysV 396
|
410 420 430
....*....|....*....|....*....|....
gi 88196026 437 GRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07078 397 GAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTV 430
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
24-471 |
6.32e-172 |
|
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: 490.79 E-value: 6.32e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 24 VINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPL--SLSEr 101
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLaeARGE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 102 VHYqmglnhfvAArDALDNYEFEERR--GD----------DLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVL 169
Cdd:cd07103 80 VDY--------AA-SFLEWFAEEARRiyGRtipspapgkrILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 170 KPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGK 249
Cdd:cd07103 151 KPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 250 SPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQ 329
Cdd:cd07103 231 APFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 330 VQNYINKGIEEGAELFYGGPGKPEGlekGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAG 409
Cdd:cd07103 311 VEALVEDAVAKGAKVLTGGKRLGLG---GYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196026 410 YVIGKDKETLHKVARSIEAGTVEINEAG-RKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSIA 471
Cdd:cd07103 388 YVFTRDLARAWRVAEALEAGMVGINTGLiSDAEAPFGGVKESGLGREGGKEGLEEYLETKYVS 450
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
24-471 |
3.95e-169 |
|
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: 483.99 E-value: 3.95e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 24 VINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSERVH 103
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 104 Y---------------QMGLNHFVAARDALdNYefeerrgddlVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVV 168
Cdd:cd07093 81 IpraaanfrffadyilQLDGESYPQDGGAL-NY----------VLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 169 LKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGG 248
Cdd:cd07093 150 LKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 249 KSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFD 328
Cdd:cd07093 230 KNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 329 QVQNYINKGIEEGAELFYGGPGKPE-GLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGL 407
Cdd:cd07093 310 KVLGYVELARAEGATILTGGGRPELpDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88196026 408 AGYVIGKDKETLHKVARSIEAGTVEIN-EAGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSIA 471
Cdd:cd07093 390 AAYVWTRDLGRAHRVARRLEAGTVWVNcWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
5-470 |
5.43e-169 |
|
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: 484.41 E-value: 5.43e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 5 TKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVY--LEFRHTSVKERQALLDKIVKEYENRKD 82
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFetGWWRKMDPRERGRLLNKLADLIERDRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 83 DIVQAITDELGAPLSLSERVHYQMGLNH---FVAARDALDNYEFE-ERRGDDLVVKEAIGVSGLITPWNFPTNQTSLKLA 158
Cdd:cd07091 84 ELAALESLDNGKPLEESAKGDVALSIKClryYAGWADKIQGKTIPiDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 159 AAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAK- 237
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKs 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 238 DFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQ 317
Cdd:cd07091 244 NLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 318 VGPIISKKQFDQVQNYINKGIEEGAELFYGG--PGKpegleKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDE 395
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGerHGS-----KGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88196026 396 AIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGR-KPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07091 399 VIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVfDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
8-470 |
2.21e-161 |
|
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: 465.25 E-value: 2.21e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYL--EFRHTSVKERQALLDKIVKEYENRKDDIV 85
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDsgEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 86 QAITDELGAPLSLSER--------VHYQMGLnhfvAARDALDNYEfeerRGDD---LVVKEAIGVSGLITPWNFPTNQTS 154
Cdd:cd07119 81 RLETLNTGKTLRESEIdiddvancFRYYAGL----ATKETGEVYD----VPPHvisRTVREPVGVCGLITPWNYPLLQAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 155 LKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEK 234
Cdd:cd07119 153 WKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 235 AAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPRED 314
Cdd:cd07119 233 AAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 315 GTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGpGKPEG--LEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYND 392
Cdd:cd07119 313 DTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGG-KRPTGdeLAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDT 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 88196026 393 LDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRK-PDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07119 392 EEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYfAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
8-470 |
9.37e-159 |
|
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: 457.88 E-value: 9.37e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQA 87
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 88 ITDELGAPLSL-SERVHYQMGLNHFVA--ARdaldNYEFE----ERRGDDLVV-KEAIGVSGLITPWNFPTNQTSLKLAA 159
Cdd:cd07088 81 IVEEQGKTLSLaRVEVEFTADYIDYMAewAR----RIEGEiipsDRPNENIFIfKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 160 AFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDF 239
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 240 KKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVG 319
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 320 PIISKKQFDQVQNYINKGIEEGAELFYGgpGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQI 399
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTG--GKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIEL 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88196026 400 ANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKPDLPF-GGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07088 395 ANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFhAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
24-470 |
2.12e-155 |
|
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: 449.11 E-value: 2.12e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 24 VINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPL------- 96
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLdeaawdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 97 -----------SLSERvhyqmgLNHFVAARDALDNYEFEERrgddlVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGS 165
Cdd:cd07110 81 ddvagcfeyyaDLAEQ------LDAKAERAVPLPSEDFKAR-----VRREPVGVVGLITPWNFPLLMAAWKVAPALAAGC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 166 PVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLE 245
Cdd:cd07110 150 TVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 246 LGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKK 325
Cdd:cd07110 230 LGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 326 QFDQVQNYINKGIEEGAELFYGGpGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKY 405
Cdd:cd07110 310 QYEKVLSFIARGKEEGARLLCGG-RRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEY 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88196026 406 GLAGYVIGKDKETLHKVARSIEAGTVEIN-EAGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07110 389 GLAAAVISRDAERCDRVAEALEAGIVWINcSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
24-470 |
8.17e-153 |
|
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: 442.38 E-value: 8.17e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 24 VINPATEEVIGKVAKGNKADVDKAVEAADDVYL--EFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPL----- 96
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIretra 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 97 ---SLSERVHYqmglnhFVAARDALDNYEFEERRGDDLV--VKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKP 171
Cdd:cd07114 81 qvrYLAEWYRY------YAGLADKIEGAVIPVDKGDYLNftRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 172 SEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSP 251
Cdd:cd07114 155 SEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 252 YIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQ 331
Cdd:cd07114 235 NIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 332 NYINKGIEEGAELFYGG-PGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGY 410
Cdd:cd07114 315 RYVARAREEGARVLTGGeRPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196026 411 VIGKDKETLHKVARSIEAGTVEINEAGR-KPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07114 395 IWTRDLARAHRVARAIEAGTVWVNTYRAlSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-470 |
8.44e-153 |
|
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: 443.23 E-value: 8.44e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 6 KQYINGEWVESNSneTIEVINPA-TEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDI 84
Cdd:cd07097 2 RNYIDGEWVAGGD--GEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 85 VQAITDELGAPLSLSE-RVHYQMGLNHFVAA---RDALDNYEFEERRGDDLVVKEAIGVSGLITPWNFPTNQTSLKLAAA 160
Cdd:cd07097 80 ARLLTREEGKTLPEARgEVTRAGQIFRYYAGealRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 161 FAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFK 240
Cdd:cd07097 160 LAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 241 KVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGP 320
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 321 IISKKQFDQVQNYINKGIEEGAELFYGGpGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIA 400
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGG-ERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88196026 401 NDTKYGL-AGYVIGKDKETLHKVARSiEAGTVEINE--AGRKPDLPFGGYKQSGLG-REWGDYGIEEFLEVKSI 470
Cdd:cd07097 399 NDTEFGLsAGIVTTSLKHATHFKRRV-EAGVVMVNLptAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
5-470 |
2.14e-149 |
|
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: 434.91 E-value: 2.14e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 5 TKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLE-FRHTSVKERQALLDKIVKEYENRKDD 83
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 84 IVQAITDELGAPLSLSERVHYQMGLN---HFVAARDALDNYEFE-ERRGDDLVVKEAIGVSGLITPWNFPTNQTSLKLAA 159
Cdd:cd07144 88 LAAIEALDSGKPYHSNALGDLDEIIAvirYYAGWADKIQGKTIPtSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 160 AFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDF 239
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 240 KKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQV-RVGNPREDGTQV 318
Cdd:cd07144 248 KAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDTVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 319 GPIISKKQFDQVQNYINKGIEEGAELFYGGPGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQ 398
Cdd:cd07144 328 GPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIK 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196026 399 IANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAG-RKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07144 408 KANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNdSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
8-468 |
1.05e-148 |
|
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: 432.31 E-value: 1.05e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQA 87
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 88 ITDELGAPLSLSERVHYQMGLN--HFVAARDALDNYEFEERRGDDL--VVKEAIGVSGLITPWNFPTNQTSLKLAAAFAA 163
Cdd:TIGR01804 81 ETLDTGKTLQETIVADMDSGADvfEFFAGLAPALNGEIIPLGGPSFayTIREPLGVCVGIGAWNYPLQIASWKIAPALAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 164 GSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVS 243
Cdd:TIGR01804 161 GNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 244 LELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIIS 323
Cdd:TIGR01804 241 MELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLIS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 324 KKQFDQVQNYINKGIEEGAELFYGGpGKPE--GLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIAN 401
Cdd:TIGR01804 321 AAHRDKVLSYIEKGKAEGATLATGG-GRPEnvGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARAN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196026 402 DTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKP-DLPFGGYKQSGLGREWGDYGIEEFLEVK 468
Cdd:TIGR01804 400 DTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPaEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
6-473 |
9.35e-148 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 431.46 E-value: 9.35e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 6 KQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFR-----HTSVKERQALLDKIVKEYENR 80
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRNKgkdwaRTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 81 KDDIVQAITDELGAPLSLSErvhYQM----GLNHFVAAR-DALDNY----------EFEERrgddlVVKEAIGVSGLITP 145
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAA---WDMddvaGCFEYYADLaEALDAKqkapvslpmeTFKGY-----VLKEPLGVVGLITP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 146 WNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSG 225
Cdd:PLN02467 161 WNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 226 PTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQ 305
Cdd:PLN02467 241 ATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 306 VRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGpGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVM 385
Cdd:PLN02467 321 IKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGG-KRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 386 SVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAgrKP---DLPFGGYKQSGLGREWGDYGIE 462
Cdd:PLN02467 400 CVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCS--QPcfcQAPWGGIKRSGFGRELGEWGLE 477
|
490
....*....|.
gi 88196026 463 EFLEVKSIAGY 473
Cdd:PLN02467 478 NYLSVKQVTKY 488
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
25-470 |
2.07e-146 |
|
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: 425.98 E-value: 2.07e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 25 INPATEEVIGKVAKGNKADVDKAVEAADDVYLE--FRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSE-R 101
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARgE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 102 VHYQMGLNHFVA--AR----DALDNYefeerrGDD---LVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPS 172
Cdd:cd07118 82 IEGAADLWRYAAslARtlhgDSYNNL------GDDmlgLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 173 EETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPY 252
Cdd:cd07118 156 EFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 253 IVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQN 332
Cdd:cd07118 236 IVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 333 YINKGIEEGAELFYGGPGKPEGleKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVI 412
Cdd:cd07118 316 YVDAGRAEGATLLLGGERLASA--AGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVW 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196026 413 GKDKETLHKVARSIEAGTVEIN---EAGrkPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07118 394 SKDIDTALTVARRIRAGTVWVNtflDGS--PELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-470 |
6.55e-146 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 426.22 E-value: 6.55e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 1 MRDYTKQ--YINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYE 78
Cdd:PRK13252 1 MSRQPLQslYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 79 NRKDDIVQAITDELGAPLSLSERVHYQMG---LNHFVAARDALdNYEFEERRGDDLV--VKEAIGVSGLITPWNFPTNQT 153
Cdd:PRK13252 81 ERNDELAALETLDTGKPIQETSVVDIVTGadvLEYYAGLAPAL-EGEQIPLRGGSFVytRREPLGVCAGIGAWNYPIQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 154 SLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAgVGNPLSEHPKVRMMSFTGSGPTGSKIME 233
Cdd:PRK13252 160 CWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 234 KAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATtgkVVNN---TGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGN 310
Cdd:PRK13252 239 AAAASLKEVTMELGGKSPLIVFDDADLDRAADIA---MLANfysSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 311 PREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPG-KPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVIT 389
Cdd:PRK13252 316 PMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERlTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 390 YNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKP-DLPFGGYKQSGLGREWGDYGIEEFLEVK 468
Cdd:PRK13252 396 FDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPaEMPVGGYKQSGIGRENGIATLEHYTQIK 475
|
..
gi 88196026 469 SI 470
Cdd:PRK13252 476 SV 477
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
8-455 |
2.49e-145 |
|
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: 424.45 E-value: 2.49e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQA 87
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 88 ITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERRGDD----LVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAA 163
Cdd:cd07559 84 ETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEdtlsYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 164 GSPVVLKPSEETPFAAVILAEIFDKVgVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVS 243
Cdd:cd07559 164 GNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIPVT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 244 LELGGKSPYIVLDDVDIKEAA---KATTGKV--VNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQV 318
Cdd:cd07559 243 LELGGKSPNIFFDDAMDADDDfddKAEEGQLgfAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 319 GPIISKKQFDQVQNYINKGIEEGAELFYGGPGKPE-GLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAI 397
Cdd:cd07559 323 GAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAI 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 88196026 398 QIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKPD-LPFGGYKQSGLGRE 455
Cdd:cd07559 403 AIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAhAPFGGYKKSGIGRE 461
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
24-470 |
8.45e-144 |
|
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: 419.24 E-value: 8.45e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 24 VINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSER-V 102
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFeV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 103 HYQMGLNHFVAARDALDNYEFEERRGDDLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVIL 182
Cdd:cd07106 81 GGAVAWLRYTASLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 183 AEIFDKVgVPKGVFNLVNGDGAgVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKE 262
Cdd:cd07106 161 GELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 263 AAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGA 342
Cdd:cd07106 239 VAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 343 ELFYGGPgKPEGleKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKV 422
Cdd:cd07106 319 KVLAGGE-PLDG--PGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAV 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 88196026 423 ARSIEAGTVEINEAGR-KPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07106 396 ARRLEAGTVWINTHGAlDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
24-470 |
9.53e-141 |
|
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: 411.70 E-value: 9.53e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 24 VINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSeRVH 103
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA-RVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 104 YQMGLNHF-----VAARDALDNYEFeerRGDDLVV--KEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETP 176
Cdd:cd07090 80 IDSSADCLeyyagLAPTLSGEHVPL---PGGSFAYtrREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 177 FAAVILAEIFDKVGVPKGVFNLVNGDGAgVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLD 256
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 257 DVDIKEAAkatTGKVVNN---TGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNY 333
Cdd:cd07090 236 DADLENAV---NGAMMANflsQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 334 INKGIEEGAELFYGGPGKP--EGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYV 411
Cdd:cd07090 313 IESAKQEGAKVLCGGERVVpeDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 412 IGKDKETLHKVARSIEAGTVEINEAGRKP-DLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07090 393 FTRDLQRAHRVIAQLQAGTCWINTYNISPvEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
19-470 |
1.37e-140 |
|
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: 411.61 E-value: 1.37e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 19 NETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLE--FRHTSVKERQALLDKIVKEYENRKDDIvqAITDEL--GA 94
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDEL--ALLETLdmGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 95 PLSLSERVHYQMGLNHFVAARDALDN-YEFEERRGDD---LVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLK 170
Cdd:cd07112 79 PISDALAVDVPSAANTFRWYAEAIDKvYGEVAPTGPDalaLITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 171 PSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAK-DFKKVSLELGGK 249
Cdd:cd07112 159 PAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 250 SPYIVLDDV-DIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFD 328
Cdd:cd07112 239 SPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 329 QVQNYINKGIEEGAELFYGG-PGKPEGleKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGL 407
Cdd:cd07112 319 KVLGYIESGKAEGARLVAGGkRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88196026 408 AGYVIGKDKETLHKVARSIEAGTVEIN--EAGrkpDL--PFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07112 397 AASVWTSDLSRAHRVARRLRAGTVWVNcfDEG---DIttPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
4-470 |
5.28e-140 |
|
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: 410.59 E-value: 5.28e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 4 YTKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVY---LEFRHTSVKERQALLDKIVKEYENR 80
Cdd:cd07141 6 YTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 81 KDDIVQAITDELGAPLSLSERVHYQMGLN---HFVAARDA-------LDNYEFEERRgddlvvKEAIGVSGLITPWNFPT 150
Cdd:cd07141 86 RAYLASLETLDNGKPFSKSYLVDLPGAIKvlrYYAGWADKihgktipMDGDFFTYTR------HEPVGVCGQIIPWNFPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 151 NQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSK 230
Cdd:cd07141 160 LMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 231 IMEKAAK-DFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVG 309
Cdd:cd07141 240 IQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 310 NPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGgpGKPEGlEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVIT 389
Cdd:cd07141 320 NPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECG--GKRHG-DKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 390 YNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGR-KPDLPFGGYKQSGLGREWGDYGIEEFLEVK 468
Cdd:cd07141 397 FKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVvSPQAPFGGYKMSGNGRELGEYGLQEYTEVK 476
|
..
gi 88196026 469 SI 470
Cdd:cd07141 477 TV 478
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
24-470 |
5.33e-139 |
|
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: 407.21 E-value: 5.33e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 24 VINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSERVH 103
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 104 yqmglnhFVAARDALDNY---------EFEERRGDDL--VVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPS 172
Cdd:cd07115 81 -------VPRAADTFRYYagwadkiegEVIPVRGPFLnyTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 173 EETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPY 252
Cdd:cd07115 154 ELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 253 IVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQN 332
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 333 YINKGIEEGAELFYGgpGKPEGlEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVI 412
Cdd:cd07115 314 YVDVGREEGARLLTG--GKRPG-ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVW 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 88196026 413 GKDKETLHKVARSIEAGTVEINEAGR-KPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07115 391 TRDLGRAHRVAAALKAGTVWINTYNRfDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
24-470 |
3.17e-138 |
|
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: 405.21 E-value: 3.17e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 24 VINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSERVH 103
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 104 YQMGLNHF-----VAARDALDNYEFeerrGDDLV---VKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEET 175
Cdd:cd07108 81 AAVLADLFryfggLAGELKGETLPF----GPDVLtytVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 176 PFAAVILAEIFDKVgVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVL 255
Cdd:cd07108 157 PLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 256 DDVDIKEAAK-ATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYI 334
Cdd:cd07108 236 PDADLDDAVDgAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 335 NKGIEE-GAELFYGGPGKPEG-LEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVI 412
Cdd:cd07108 316 DLGLSTsGATVLRGGPLPGEGpLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 413 GKDKETLHKVARSIEAGTVEINEA-GRKPDLPFGGYKQSGLGREWGDYG-IEEFLEVKSI 470
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGgGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
8-470 |
6.55e-136 |
|
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: 400.18 E-value: 6.55e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNSNETIEVINPA-TEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQ 86
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 87 AITDELGAPLSlservhyqMGLNHFVAARDALDNYEFEERR--GD----DLVVKEA------IGVSGLITPWNFPTNQTS 154
Cdd:cd07131 82 LVTREMGKPLA--------EGRGDVQEAIDMAQYAAGEGRRlfGEtvpsELPNKDAmtrrqpIGVVALITPWNFPVAIPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 155 LKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEK 234
Cdd:cd07131 154 WKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 235 AAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPRED 314
Cdd:cd07131 234 CARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 315 GTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPGKPEG-LEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDL 393
Cdd:cd07131 314 ETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGgYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 394 DEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEA--GRKPDLPFGGYKQSGLG-REWGDYGIEEFLEVKSI 470
Cdd:cd07131 394 EEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPtiGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
24-471 |
7.17e-135 |
|
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: 396.60 E-value: 7.17e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 24 VINPATEEVIGKVAKGNKADVDKAVEAADDVYLE-FRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSErv 102
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 103 hyqmglNHFVAARDALDNY--EFEERRGD---------DLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKP 171
Cdd:cd07109 79 ------ADVEAAARYFEYYggAADKLHGEtiplgpgyfVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 172 SEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSP 251
Cdd:cd07109 153 AEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 252 YIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGnPREDGTQVGPIISKKQFDQVQ 331
Cdd:cd07109 233 QIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 332 NYINKGIEEGAELFYGGPGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYV 411
Cdd:cd07109 312 GFVARARARGARIVAGGRIAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88196026 412 IGKDKETLHKVARSIEAGTVEINE--AGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSIA 471
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNygAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
6-470 |
8.41e-134 |
|
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: 394.90 E-value: 8.41e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 6 KQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIV 85
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 86 QAITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERRGDD----LVVKEAIGVSGLITPWNFPTNQTSLKLAAAF 161
Cdd:cd07117 82 MVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEdtlsIVLREPIGVVGQIIPWNFPFLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 162 AAGSPVVLKPSEETPFAAVILAEIFDKVgVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKK 241
Cdd:cd07117 162 AAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 242 VSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPI 321
Cdd:cd07117 241 ATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 322 ISKKQFDQVQNYINKGIEEGAELFYGGPGKPE-GLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIA 400
Cdd:cd07117 321 VNKDQLDKILSYVDIAKEEGAKILTGGHRLTEnGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196026 401 NDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKPD-LPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07117 401 NDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAgAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
5-468 |
2.73e-133 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 394.06 E-value: 2.73e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 5 TKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDI 84
Cdd:PLN02278 25 TQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 85 VQAITDELGAPL--SLSErVHYQMGLNHFVAA---RDALDNYEFEERRGDDLVVKEAIGVSGLITPWNFPTNQTSLKLAA 159
Cdd:PLN02278 105 AQLMTLEQGKPLkeAIGE-VAYGASFLEYFAEeakRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 160 AFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDF 239
Cdd:PLN02278 184 ALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 240 KKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVG 319
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 320 PIISKKQFDQVQNYINKGIEEGAELFYGgpGKPEGLeKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQI 399
Cdd:PLN02278 344 PLINEAAVQKVESHVQDAVSKGAKVLLG--GKRHSL-GGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAI 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196026 400 ANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEaGRKPD--LPFGGYKQSGLGREWGDYGIEEFLEVK 468
Cdd:PLN02278 421 ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNE-GLISTevAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
11-470 |
4.86e-132 |
|
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: 389.74 E-value: 4.86e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 11 GEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITD 90
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 91 ELGAPLSLSE-RVHYQMG-------LNHFVAARDALDNYEFEERRgddlVVKEAIGVSGLITPWNFPTNQTSLKLAAAFA 162
Cdd:cd07151 81 ESGSTRIKANiEWGAAMAitreaatFPLRMEGRILPSDVPGKENR----VYREPLGVVGVISPWNFPLHLSMRSVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 163 AGSPVVLKPSEETPF-AAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKK 241
Cdd:cd07151 157 LGNAVVLKPASDTPItGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 242 VSLELGGKSPYIVLDDVDIKEAAKATT-GKVVNNtGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGP 320
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVfGKFLHQ-GQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 321 IISKKQFDQVQNYINKGIEEGAELFYGGPgkPEGLekgyFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIA 400
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEGATLLVGGE--AEGN----VLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELA 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88196026 401 NDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE--AGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07151 390 NDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDqpVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
24-470 |
1.53e-131 |
|
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: 388.22 E-value: 1.53e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 24 VINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSERVH 103
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 104 YQMGLNHF----VAARDA--------LDNYEFEERRgddlvvkEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKP 171
Cdd:cd07092 81 LPGAVDNFrffaGAARTLegpaageyLPGHTSMIRR-------EPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 172 SEETPFAAVILAEIFDKVgVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSP 251
Cdd:cd07092 154 SETTPLTTLLLAELAAEV-LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 252 YIVLDDVDIKEAA-KATTGKVVnNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQV 330
Cdd:cd07092 233 VIVFDDADLDAAVaGIATAGYY-NAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 331 QNYINKgIEEGAELFYGGpGKPEGleKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGY 410
Cdd:cd07092 312 AGFVER-APAHARVLTGG-RRAEG--PGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196026 411 VIGKDKETLHKVARSIEAGTVEINEAGR-KPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPlAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
24-468 |
3.55e-131 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 387.17 E-value: 3.55e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 24 VINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSE-RV 102
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKgEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 103 HYQMGLnhfvaardaLDNYEFEERR--GDD----------LVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLK 170
Cdd:TIGR01780 81 LYAASF---------LEWFAEEAKRvyGDTipspqsdkrlIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 171 PSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAG-VGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGK 249
Cdd:TIGR01780 152 PAEQTPLSALALARLAEQAGIPKGVLNVITGSRAKeVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 250 SPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQ 329
Cdd:TIGR01780 232 APFIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 330 VQNYINKGIEEGAELFYGGPGKPEGlekGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAG 409
Cdd:TIGR01780 312 VEKHIADAVEKGAKVVTGGKRHELG---GNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 410 YVIGKDKETLHKVARSIEAGTVEINEAG-RKPDLPFGGYKQSGLGREWGDYGIEEFLEVK 468
Cdd:TIGR01780 389 YFFSRDLSRIWRVAEALEYGMVGINTGLiSNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
43-470 |
3.74e-131 |
|
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: 386.50 E-value: 3.74e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 43 DVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPlslservhYQMGLNHFVAARDALDNYE 122
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGST--------RPKAAFEVGAAIAILREAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 123 FEERR--GDDL----------VVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFA-AVILAEIFDKV 189
Cdd:cd07104 73 GLPRRpeGEILpsdvpgkesmVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 190 GVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTG 269
Cdd:cd07104 153 GLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 270 KVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGgp 349
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTG-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 350 GKPEGLekgyFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAG 429
Cdd:cd07104 311 GTYEGL----FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETG 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 88196026 430 TVEINE--AGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07104 387 MVHINDqtVNDEPHVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
4-470 |
1.59e-130 |
|
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: 386.46 E-value: 1.59e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 4 YTKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLE--FRHTSVKERQALLDKIVKEYENRK 81
Cdd:cd07142 3 HTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 82 DDIVQAITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERRGDD----LVVKEAIGVSGLITPWNFPTNQTSLKL 157
Cdd:cd07142 83 DELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGphhvYTLHEPIGVVGQIIPWNFPLLMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 158 AAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAK 237
Cdd:cd07142 163 GPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 238 -DFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGT 316
Cdd:cd07142 243 sNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 317 QVGPIISKKQFDQVQNYINKGIEEGAELFYGgpGKPEGlEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEA 396
Cdd:cd07142 323 EQGPQVDKEQFEKILSYIEHGKEEGATLITG--GDRIG-SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88196026 397 IQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEIN-EAGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
8-470 |
2.31e-130 |
|
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: 386.11 E-value: 2.31e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEF--RHTSVKERQALLDKIVKEYENRKDDIV 85
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDwgLKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 86 QAITDELGAPLSLSERVHYQMGLNHFV-----AARDALDNYEFEERRGDdLVVKEAIGVSGLITPWNFPTNQTSLKLAAA 160
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFRyyggwADKIHGQVIETDIKKLT-YTRHEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 161 FAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAK-DF 239
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKsNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 240 KKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVG 319
Cdd:cd07143 249 KKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 320 PIISKKQFDQVQNYINKGIEEGAELFYGgpGKPEGlEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQI 399
Cdd:cd07143 329 PQVSQIQYERIMSYIESGKAEGATVETG--GKRHG-NEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKR 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88196026 400 ANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGR-KPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07143 406 ANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLlHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
4-470 |
5.25e-130 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 386.10 E-value: 5.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 4 YTKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVyleFRH-----TSVKERQALLDKIVKEYE 78
Cdd:PLN02766 20 FTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREA---FDHgpwprMSGFERGRIMMKFADLIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 79 NRKDDIVQAITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFE----ERRGDDLVVKEAIGVSGLITPWNFPTNQTS 154
Cdd:PLN02766 97 EHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGEtlkmSRQLQGYTLKEPIGVVGHIIPWNFPSTMFF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 155 LKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEK 234
Cdd:PLN02766 177 MKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 235 AAK-DFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPRE 313
Cdd:PLN02766 257 AATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 314 DGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGgpGKPEGlEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDL 393
Cdd:PLN02766 337 PRARQGPQVDKQQFEKILSYIEHGKREGATLLTG--GKPCG-DKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196026 394 DEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEIN-EAGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNcYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
23-471 |
5.19e-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: 381.68 E-value: 5.19e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 23 EVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPlslserv 102
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGST------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 103 hYQMGLNHFVAARDALDNYEFEERR--GDDL----------VVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLK 170
Cdd:cd07150 75 -YGKAWFETTFTPELLRAAAGECRRvrGETLpsdspgtvsmSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 171 PSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKS 250
Cdd:cd07150 154 PSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 251 PYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQV 330
Cdd:cd07150 234 PLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 331 QNYINKGIEEGAELFYGGPgkpeglEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGY 410
Cdd:cd07150 314 KRQVEDAVAKGAKLLTGGK------YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196026 411 VIGKDKETLHKVARSIEAGTVEINEAG--RKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSIA 471
Cdd:cd07150 388 ILTNDLQRAFKLAERLESGMVHINDPTilDEAHVPFGGVKASGFGREGGEWSMEEFTELKWIT 450
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
5-470 |
8.59e-129 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 381.95 E-value: 8.59e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 5 TKQYINGEWVESnSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDI 84
Cdd:PRK13473 3 TKLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 85 VQAITDELGAPLSLServhyqmgLNHFVAArdALDNYEF-------------EERRGD--DLVVKEAIGVSGLITPWNFP 149
Cdd:PRK13473 82 ARLESLNCGKPLHLA--------LNDEIPA--IVDVFRFfagaarclegkaaGEYLEGhtSMIRRDPVGVVASIAPWNYP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 150 TNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVgVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGS 229
Cdd:PRK13473 152 LMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 230 KIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAA-KATTGKVVnNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRV 308
Cdd:PRK13473 231 HVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVeGIRTFGYY-NAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 309 GNPREDGTQVGPIISKKQFDQVQNYINKGIEEG-AELFYGGpGKPEGleKGYFARPTIFINVDNQMTIAQEEIFGPVMSV 387
Cdd:PRK13473 310 GDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGG-EAPDG--KGYYYEPTLLAGARQDDEIVQREVFGPVVSV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 388 ITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEIN-------EagrkpdLPFGGYKQSGLGREWGDYG 460
Cdd:PRK13473 387 TPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNthfmlvsE------MPHGGQKQSGYGKDMSLYG 460
|
490
....*....|
gi 88196026 461 IEEFLEVKSI 470
Cdd:PRK13473 461 LEDYTVVRHV 470
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
22-471 |
3.02e-127 |
|
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: 377.46 E-value: 3.02e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 22 IEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSeR 101
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 102 VHYQMGLNHF-VAARDA---------LDNYEFEERRGDdLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKP 171
Cdd:cd07145 80 VEVERTIRLFkLAAEEAkvlrgetipVDAYEYNERRIA-FTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 172 SEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSP 251
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 252 YIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQ 331
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 332 NYINKGIEEGAELFYGGPGkpeglEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYV 411
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKR-----DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88196026 412 IGKDKETLHKVARSIEAGTVEINEAG--RKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSIA 471
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTrfRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIV 455
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
5-471 |
2.69e-126 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 375.64 E-value: 2.69e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 5 TKQYINGEWVESNSNeTIEVINPATEEVIGKVAKGNKADVDKAVEAADDVY--------LEFRHTSVKE-RQALLDKIvk 75
Cdd:TIGR04284 1 SRLLIDGKLVAGSAG-TFPTVNPATEEVLGVAADATAADMDAAIAAARRAFdetdwsrdTALRVRCLRQlRDALRAHV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 76 eyenrkDDIVQAITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERRG---------DDLVVKEAIGVSGLITPW 146
Cdd:TIGR04284 78 ------EELRELTIAEVGAPRMLTAGAQLEGPVDDLGFAADLAESYAWTTDLGvaspmgiptRRTLRREAVGVVGAITPW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 147 NFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAE-IFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSG 225
Cdd:TIGR04284 152 NFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAVLGElIAEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGST 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 226 PTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQ 305
Cdd:TIGR04284 232 ATGRAVMADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 306 VRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGpGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVM 385
Cdd:TIGR04284 312 IKPGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGG-GRPADRDRGFFVEPTVIAGLDNNARVAREEIFGPVL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 386 SVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINeAG--RKPDLPFGGYKQSGLGREWGDYGIEE 463
Cdd:TIGR04284 391 TVIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVN-GGvwYSADAPFGGYKQSGIGREMGVAGFEE 469
|
....*...
gi 88196026 464 FLEVKSIA 471
Cdd:TIGR04284 470 YLETKLIA 477
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
22-470 |
7.41e-126 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 373.47 E-value: 7.41e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 22 IEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSeR 101
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 102 VHYQMGLNHF-VAARDA---------LDNYEFEERR-GddLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLK 170
Cdd:cd07149 80 KEVDRAIETLrLSAEEAkrlagetipFDASPGGEGRiG--FTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 171 PSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKdfKKVSLELGGKS 250
Cdd:cd07149 158 PASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGL--KKVTLELGSNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 251 PYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQV 330
Cdd:cd07149 236 AVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 331 QNYINKGIEEGAELFYGgpGKPEGlekGYFArPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGY 410
Cdd:cd07149 316 EEWVEEAVEGGARLLTG--GKRDG---AILE-PTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88196026 411 VIGKDKETLHKVARSIEAGTVEINEAG--RKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07149 390 VFTNDLQKALKAARELEVGGVMINDSStfRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
49-470 |
2.79e-125 |
|
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: 368.87 E-value: 2.79e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 49 EAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSeRVHYQMGLNHF-VAARDALDNYEFEERR 127
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEA-LGEVARAIDTFrYAAGLADKLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 128 GDD----LVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDG 203
Cdd:cd06534 80 PDPggeaYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 204 AGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAK-ATTGKVVNNtGQVCTAG 282
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEgAVFGAFFNA-GQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 283 TRVLVPNKIKDAFLAELKeqfsqvrvgnpredgtqvgpiiskkqfdqvqnyinkgieegaelfyggpgkpeglekgyfar 362
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV-------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 363 pTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE--AGRKP 440
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDssIGVGP 335
|
410 420 430
....*....|....*....|....*....|
gi 88196026 441 DLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTV 365
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
25-470 |
4.08e-125 |
|
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: 371.68 E-value: 4.08e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 25 INPATEEVIGKVAKGNKADVDKAVEAADDVyleFRHT----SVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSe 100
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRA---FDETdwahDPRLRARVLLELADAFEANAERLARLLALENGKILGEA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 101 RVHYQMG---LNHFVAARDALDNYEFEERRGD-DLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETP 176
Cdd:cd07120 78 RFEISGAiseLRYYAGLARTEAGRMIEPEPGSfSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 177 FAAVILAEIFDKV-GVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVL 255
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 256 DDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYIN 335
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 336 KGIEEGAE-LFYGGPGkPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGK 414
Cdd:cd07120 318 RAIAAGAEvVLRGGPV-TEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 88196026 415 DKETLHKVARSIEAGTVEINEAGR-KPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKlFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
24-470 |
1.96e-124 |
|
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: 370.17 E-value: 1.96e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 24 VINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPlslservh 103
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 104 YQMGLNHFVAARDALDNYE--FEERRGDDL---------VVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPS 172
Cdd:cd07107 73 VSAMLGDVMVAAALLDYFAglVTELKGETIpvggrnlhyTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 173 EETPFAAVILAEIFDKVgVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPY 252
Cdd:cd07107 153 EQAPLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 253 IVLDDVDIKEAAK-ATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQ 331
Cdd:cd07107 232 IVFPDADPEAAADaAVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 332 NYINKGIEEGAELFYGGpGKPEG--LEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAG 409
Cdd:cd07107 312 HYIDSAKREGARLVTGG-GRPEGpaLEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88196026 410 YVIGKDKETLHKVARSIEAGTVEINEAGRK-PDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07107 391 AIWTNDISQAHRTARRVEAGYVWINGSSRHfLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
44-470 |
6.84e-124 |
|
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: 367.56 E-value: 6.84e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 44 VDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLS----ERVhyQMGLNHFVA-ARDAL 118
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEAraevEKC--AWICRYYAEnAEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 119 DNYEFEERRGDDLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNL 198
Cdd:cd07100 79 ADEPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 199 VNGDGAGVGNpLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAK-ATTGKVVNNtGQ 277
Cdd:cd07100 159 LLIDSDQVEA-IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKtAVKGRLQNA-GQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 278 VCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPgKPEGleK 357
Cdd:cd07100 237 SCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGK-RPDG--P 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 358 GYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAG 437
Cdd:cd07100 314 GAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMV 393
|
410 420 430
....*....|....*....|....*....|....
gi 88196026 438 R-KPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07100 394 KsDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
8-468 |
1.84e-121 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 363.46 E-value: 1.84e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQA 87
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 88 ITDELGAPLSLSE-RVHYQMGLNHFVAAR------DALDNYEFEERRgddLVVKEAIGVSGLITPWNFPTNQTSLKLAAA 160
Cdd:PRK11241 94 MTLEQGKPLAEAKgEISYAASFIEWFAEEgkriygDTIPGHQADKRL---IVIKQPIGVTAAITPWNFPAAMITRKAGPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 161 FAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFK 240
Cdd:PRK11241 171 LAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 241 KVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGP 320
Cdd:PRK11241 251 KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 321 IISKKQFDQVQNYINKGIEEGAELFYGgpGKPEGLEkGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIA 400
Cdd:PRK11241 331 LIDEKAVAKVEEHIADALEKGARVVCG--GKAHELG-GNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 88196026 401 NDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKPDL-PFGGYKQSGLGREWGDYGIEEFLEVK 468
Cdd:PRK11241 408 NDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVaPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
8-474 |
2.46e-121 |
|
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: 364.24 E-value: 2.46e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNsnETIEVINPA-TEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQ 86
Cdd:cd07124 36 VIGGKEVRTE--EKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 87 AITDELGAPLS-----LSERVHYqmgLNHFVAARDALDNYEFEERRG-DDLVVKEAIGVSGLITPWNFPTNQTSLKLAAA 160
Cdd:cd07124 114 WMVLEVGKNWAeadadVAEAIDF---LEYYAREMLRLRGFPVEMVPGeDNRYVYRPLGVGAVISPWNFPLAILAGMTTAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 161 FAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKD-- 238
Cdd:cd07124 191 LVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqp 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 239 ----FKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPRED 314
Cdd:cd07124 271 gqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 315 GTQVGPIISKKQFDQVQNYINKGIEEGaELFYGGPGkPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLD 394
Cdd:cd07124 351 EVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEV-LELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 395 EAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE------AGRKpdlPFGGYKQSGLGREWG--DYgIEEFLE 466
Cdd:cd07124 429 EALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRkitgalVGRQ---PFGGFKMSGTGSKAGgpDY-LLQFMQ 504
|
....*...
gi 88196026 467 VKSIAGYF 474
Cdd:cd07124 505 PKTVTENF 512
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
8-457 |
7.38e-121 |
|
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: 361.50 E-value: 7.38e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESnSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQA 87
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 88 ITDELGAPLS-----LSERVH---YQMGL--------------NHFVaardaldnyeFEERRgddlvvkeAIGVSGLITP 145
Cdd:cd07086 81 VSLEMGKILPeglgeVQEMIDicdYAVGLsrmlygltipserpGHRL----------MEQWN--------PLGVVGVITA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 146 WNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKV----GVPKGVFNLVNGdGAGVGNPLSEHPKVRMMSF 221
Cdd:cd07086 143 FNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 222 TGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKE 301
Cdd:cd07086 222 TGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 302 QFSQVRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGpGKPEGLEKGYFARPTIFINVDNQMTIAQEEIF 381
Cdd:cd07086 302 AYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGG-KRIDGGEPGNYVEPTIVTGVTDDARIVQEETF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 382 GPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKV--ARSIEAGTVEIN------EAGrkpdLPFGGYKQSGLG 453
Cdd:cd07086 381 APILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNiptsgaEIG----GAFGGEKETGGG 456
|
....
gi 88196026 454 REWG 457
Cdd:cd07086 457 RESG 460
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
5-470 |
2.86e-117 |
|
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: 352.95 E-value: 2.86e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 5 TKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYL--EFRHTSVKERQALLDKIVKEYENRKD 82
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFEngEWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 83 DIVQAITDELGAPLSLSERVHYQMGLNHF--------------VAARDALDNyefeerRGDDLVVKEAIGVSGLITPWNF 148
Cdd:cd07140 86 ELATIESLDSGAVYTLALKTHVGMSIQTFryfagwcdkiqgktIPINQARPN------RNLTLTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 149 PTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTG 228
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 229 SKIMEKAAK-DFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVR 307
Cdd:cd07140 240 KHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 308 VGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPGKPeglEKGYFARPTIFINVDNQMTIAQEEIFGPVMSV 387
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVD---RPGFFFEPTVFTDVEDHMFIAKEESFGPIMII 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 388 ITYN--DLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAgRKPDL--PFGGYKQSGLGREWGDYGIEE 463
Cdd:cd07140 397 SKFDdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTY-NKTDVaaPFGGFKQSGFGKDLGEEALNE 475
|
....*..
gi 88196026 464 FLEVKSI 470
Cdd:cd07140 476 YLKTKTV 482
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
3-470 |
9.17e-116 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 350.65 E-value: 9.17e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 3 DYTKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLE--FRHTSVKERQALLDKIVKEYENR 80
Cdd:PLN02466 56 SYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 81 KDDIVQAITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERRGDDL----VVKEAIGVSGLITPWNFPTNQTSLK 156
Cdd:PLN02466 136 NDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPhhvqTLHEPIGVAGQIIPWNFPLLMFAWK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 157 LAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAA 236
Cdd:PLN02466 216 VGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 237 K-DFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDG 315
Cdd:PLN02466 296 KsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 316 TQVGPIISKKQFDQVQNYINKGIEEGAELFYGGP--GKpegleKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDL 393
Cdd:PLN02466 376 VEQGPQIDSEQFEKILRYIKSGVESGATLECGGDrfGS-----KGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 394 DEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEIN-----EAGrkpdLPFGGYKQSGLGREWGDYGIEEFLEVK 468
Cdd:PLN02466 451 DEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfDAA----IPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
..
gi 88196026 469 SI 470
Cdd:PLN02466 527 AV 528
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
6-471 |
3.43e-115 |
|
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: 346.87 E-value: 3.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 6 KQYINGEWVESnSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHT-SVKERQALLDKIVKEYENRKDDI 84
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 85 VQAITDELGAPL--SLSErvhyqmglnhFVAA----RDALDNYEFEER---RGDD---------LVVKEAIGVSGLITPW 146
Cdd:cd07082 82 ANLLMWEIGKTLkdALKE----------VDRTidyiRDTIEELKRLDGdslPGDWfpgtkgkiaQVRREPLGVVLAIGPF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 147 NFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGP 226
Cdd:cd07082 152 NYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 227 TGSKIMEKAAKdfKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQV 306
Cdd:cd07082 232 VGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 307 RVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGpgkpEGLEKGYFaRPTIFINVDNQMTIAQEEIFGPVMS 386
Cdd:cd07082 310 KVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG----GREGGNLI-YPTLLDPVTPDMRLAWEEPFGPVLP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 387 VITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEA-GRKPD-LPFGGYKQSGLGREWGDYGIEEF 464
Cdd:cd07082 385 IIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcQRGPDhFPFLGRKDSGIGTQGIGDALRSM 464
|
....*..
gi 88196026 465 LEVKSIA 471
Cdd:cd07082 465 TRRKGIV 471
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
22-470 |
8.12e-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: 345.57 E-value: 8.12e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 22 IEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSlSER 101
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIK-DAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 102 VHYQMGLNHF-VAARDALDNY----EFEERRGDD----LVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPS 172
Cdd:cd07094 80 VEVDRAIDTLrLAAEEAERIRgeeiPLDATQGSDnrlaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 173 EETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAkdFKKVSLELGGKSPY 252
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 253 IVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQN 332
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 333 YINKGIEEGAELFYGgpGKPEGLekgyFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVI 412
Cdd:cd07094 318 WVEEAVEAGARLLCG--GERDGA----LFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 413 GKDKETLHKVARSIEAGTVEINE--AGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNDssAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
25-471 |
1.23e-114 |
|
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: 344.98 E-value: 1.23e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 25 INPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPL--SLSERV 102
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRadAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 103 hyqMGLNHF-VAARDALDNYEFEERRGDDL-------VVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEE 174
Cdd:cd07099 81 ---LALEAIdWAARNAPRVLAPRKVPTGLLmpnkkatVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 175 TPFAAVILAEIFDKVGVPKGVFNLVNGDGAgVGNPLSEHpKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIV 254
Cdd:cd07099 158 TPLVGELLAEAWAAAGPPQGVLQVVTGDGA-TGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 255 LDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYI 334
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 335 NKGIEEGAELFYGGPgkpEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGK 414
Cdd:cd07099 316 DDAVAKGAKALTGGA---RSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 415 DKETLHKVARSIEAGTVEINEA---GRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSIA 471
Cdd:cd07099 393 DLARAEAIARRLEAGAVSINDVlltAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
8-466 |
4.71e-113 |
|
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: 341.68 E-value: 4.71e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIvqA 87
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLF--A 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 88 ITDEL--GAPLSLSERVHYQMGLNHFV--AARDALDNYEFEERrgddlvvkEAIGVSGLITPWNFPTNQTSLKLAAAFAA 163
Cdd:cd07111 103 VLESLdnGKPIRESRDCDIPLVARHFYhhAGWAQLLDTELAGW--------KPVGVVGQIVPWNFPLLMLAWKICPALAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 164 GSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAgVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVS 243
Cdd:cd07111 175 GNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 244 LELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIIS 323
Cdd:cd07111 254 LELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 324 KKQFDQVQNYINKGIEEGAELFYGGPGKPeglEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDT 403
Cdd:cd07111 334 PAQLKRIRELVEEGRAEGADVFQPGADLP---SKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNT 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88196026 404 KYGLAGYVIGKDKETLHKVARSIEAGTVEINEAG-RKPDLPFGGYKQSGLGREWGDYGIEEFLE 466
Cdd:cd07111 411 PYGLAASVWSENLSLALEVALSLKAGVVWINGHNlFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
7-470 |
5.81e-112 |
|
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: 339.03 E-value: 5.81e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 7 QYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYL-EFRHTSVKERQALLDKIVKEYENRKDDIV 85
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 86 QAITDELGAPLSLSERVHYQMGLN--HFVAARDALDNYE--------FEERRGDDLVVKEAIGVSGLITPWNFPTNQTSL 155
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANflRYFAGWATKINGEtlapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 156 KLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGaGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKA 235
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 236 AKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDG 315
Cdd:cd07113 241 ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 316 TQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPGKPeglEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDE 395
Cdd:cd07113 321 VMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA---GEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88196026 396 AIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEIN-EAGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07113 398 LIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
22-470 |
7.23e-111 |
|
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: 335.10 E-value: 7.23e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 22 IEVINPATEEVIGKVAKGNKADVDKAVEAAddvyLEFR-HTSVKERQALLDKIVKEYENRKDDIVQAITDELGapLSLSE 100
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALALA----ASYRsTLTRYQRSAILNKAAALLEARREEFARLITLESG--LCLKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 101 RVhYQMG--LNHFVAA-----RD-----ALDNYE-FEERRGddLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPV 167
Cdd:cd07146 75 TR-YEVGraADVLRFAaaealRDdgesfSCDLTAnGKARKI--FTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 168 VLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAkdFKKVSLELG 247
Cdd:cd07146 152 VLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 248 GKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQF 327
Cdd:cd07146 230 GNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 328 DQVQNYINKGIEEGAELFYGGPgkpeglEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGL 407
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQ------RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGL 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88196026 408 AGYVIGKDKETLHKVARSIEAGTVEINEAG--RKPDLPFGGYKQSGLG-REWGDYGIEEFLEVKSI 470
Cdd:cd07146 384 SSGVCTNDLDTIKRLVERLDVGTVNVNEVPgfRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
5-470 |
7.07e-109 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 331.48 E-value: 7.07e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 5 TKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYL--EFRHTSVKERQALLDKIVKEYENRKD 82
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 83 DIVQAITDELGAPLSLSERVHYQMGLNHFVAARDALDNY--EFEERRGDDL--VVKEAIGVSGLITPWNFPTNQTSLKLA 158
Cdd:PRK09847 100 ELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVygEVATTSSHELamIVREPVGVIAAIVPWNFPLLLTCWKLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 159 AAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAK- 237
Cdd:PRK09847 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDs 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 238 DFKKVSLELGGKSPYIVLDDV-DIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGT 316
Cdd:PRK09847 260 NMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPAT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 317 QVGPIISKKQFDQVQNYINKGIEEGaELFYGGPGKPEGLEKGyfarPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEA 396
Cdd:PRK09847 340 TMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAAIG----PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88196026 397 IQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKP-DLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:PRK09847 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDmTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
70-468 |
7.22e-109 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 328.62 E-value: 7.22e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 70 LDKIVKEYENRKDDIVQAITDELGAPLSLSE-RVHYQMGLNHFVA--ARdaldNYEFE----ERRGDD-LVVKEAIGVSG 141
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEvEVAFTADYIDYMAewAR----RYEGEiiqsDRPGENiLLFKRALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 142 LITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSF 221
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 222 TGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKE 301
Cdd:PRK10090 157 TGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 302 QFSQVRVGNP-REDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGgpGKPEGlEKGYFARPTIFINVDNQMTIAQEEI 380
Cdd:PRK10090 237 AMQAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGARVALG--GKAVE-GKGYYYPPTLLLDVRQEMSIMHEET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 381 FGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKPDLPF-GGYKQSGLGREWGDY 459
Cdd:PRK10090 314 FGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFhAGWRKSGIGGADGKH 393
|
....*....
gi 88196026 460 GIEEFLEVK 468
Cdd:PRK10090 394 GLHEYLQTQ 402
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
5-453 |
3.56e-108 |
|
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: 329.09 E-value: 3.56e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 5 TKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDI 84
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 85 VQAITDELGAPLSLSE----RV-----------HYQMGLNHFVAARDaLDNYefeerrgddlVVKEAIGVSGLITPWNFP 149
Cdd:cd07085 81 ARLITLEHGKTLADARgdvlRGlevvefacsipHLLKGEYLENVARG-IDTY----------SYRQPLGVVAGITPFNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 150 TNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVgNPLSEHPKVRMMSFTGSGPTGS 229
Cdd:cd07085 150 AMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 230 KIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVG 309
Cdd:cd07085 229 YIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 310 NPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPG-KPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVI 388
Cdd:cd07085 309 AGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGvKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIV 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88196026 389 TYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE--AGRKPDLPFGGYKQSGLG 453
Cdd:cd07085 389 RVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVpiPVPLAFFSFGGWKGSFFG 455
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
8-455 |
7.84e-108 |
|
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: 328.26 E-value: 7.84e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQA 87
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 88 ITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERRGDDLVVK----EAIGVSGLITPWNFPTNQTSLKLAAAFAA 163
Cdd:cd07116 84 ETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAyhfhEPLGVVGQIIPWNFPLLMATWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 164 GSPVVLKPSEETPFAAVILAEIFDKVgVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVS 243
Cdd:cd07116 164 GNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 244 LELGGKSPYIVLDDVDIKEAA---KATTGKVVN--NTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQV 318
Cdd:cd07116 243 LELGGKSPNIFFADVMDADDAffdKALEGFVMFalNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 319 GPIISKKQFDQVQNYINKGIEEGAELFYGGP-GKPEGLEKGYFARPTIFINvDNQMTIAQEEIFGPVMSVITYNDLDEAI 397
Cdd:cd07116 323 GAQASLEQLEKILSYIDIGKEEGAEVLTGGErNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 88196026 398 QIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKP-DLPFGGYKQSGLGRE 455
Cdd:cd07116 402 EIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPaHAAFGGYKQSGIGRE 460
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
8-471 |
3.43e-107 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 327.66 E-value: 3.43e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNsnETIEVINPA-TEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQ 86
Cdd:PRK03137 40 IIGGERITTE--DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 87 AITDELGAPLSLSErVHYQMGLNHF-VAARDALD--------NYEFEERRgddlVVKEAIGVSGLITPWNFPTNQTSLKL 157
Cdd:PRK03137 118 WLVKEAGKPWAEAD-ADTAEAIDFLeYYARQMLKladgkpveSRPGEHNR----YFYIPLGVGVVISPWNFPFAIMAGMT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 158 AAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAK 237
Cdd:PRK03137 193 LAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 238 D------FKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNP 311
Cdd:PRK03137 273 VqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 312 rEDGTQVGPIISKKQFDQVQNYINKGIEEGaELFYGGPGkpeGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYN 391
Cdd:PRK03137 353 -EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEG---DDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAK 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 392 DLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINeagRKPD------LPFGGYKQSGLGREWG--DYgIEE 463
Cdd:PRK03137 428 DFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN---RGCTgaivgyHPFGGFNMSGTDSKAGgpDY-LLL 503
|
....*...
gi 88196026 464 FLEVKSIA 471
Cdd:PRK03137 504 FLQAKTVS 511
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
22-469 |
6.46e-107 |
|
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: 324.97 E-value: 6.46e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 22 IEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSeR 101
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 102 VHYQMGLNHF-VAARDALDNY-EF---------EERRGddLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLK 170
Cdd:cd07147 80 GEVARAIDTFrIAAEEATRIYgEVlpldisargEGRQG--LVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 171 PSEETPFAAVILAEIFDKVGVPKGVFNLV--NGDGAgvgNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKdfKKVSLELGG 248
Cdd:cd07147 158 PASRTPLSALILGEVLAETGLPKGAFSVLpcSRDDA---DLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 249 KSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFD 328
Cdd:cd07147 233 NAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 329 QVQNYINKGIEEGAELFYGGPgkpeglEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLA 408
Cdd:cd07147 313 RVEGWVNEAVDAGAKLLTGGK------RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQ 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196026 409 GYVIGKDKETLHKVARSIEAGTVEINE--AGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKS 469
Cdd:cd07147 387 AGVFTRDLEKALRAWDELEVGGVVINDvpTFRVDHMPYGGVKDSGIGREGVRYAIEEMTEPRL 449
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
14-471 |
4.02e-104 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 320.29 E-value: 4.02e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 14 VESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKE-YENRKD--DIVQAIT- 89
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLvLENREEllDLVQLETg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 90 -------DELgAPLSLSERvHYqmglnhfvaARDALDNYEFEERRG------DDLVVKEAIGVSGLITPWNFPtnqtsLK 156
Cdd:PRK09407 106 karrhafEEV-LDVALTAR-YY---------ARRAPKLLAPRRRAGalpvltKTTELRQPKGVVGVISPWNYP-----LT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 157 LA-----AAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHpkVRMMSFTGSGPTGSKI 231
Cdd:PRK09407 170 LAvsdaiPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 232 MEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNP 311
Cdd:PRK09407 248 AEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 312 REDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPGKPE-GlekGYFARPTIFINVDNQMTIAQEEIFGPVMSVITY 390
Cdd:PRK09407 328 YDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDlG---PLFYEPTVLTGVTPDMELAREETFGPVVSVYPV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 391 NDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEA-----GRKpDLPFGGYKQSGLGREWGDYGIEEFL 465
Cdd:PRK09407 405 ADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGyaaawGSV-DAPMGGMKDSGLGRRHGAEGLLKYT 483
|
....*.
gi 88196026 466 EVKSIA 471
Cdd:PRK09407 484 ESQTIA 489
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
43-470 |
6.29e-101 |
|
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: 309.12 E-value: 6.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 43 DVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLServhyqmGLNHFVAA---RDA-- 117
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWA-------GFNVDLAAgmlREAas 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 118 LDNYEFEE----RRGDDL--VVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGV 191
Cdd:cd07105 74 LITQIIGGsipsDKPGTLamVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 192 PKGVFNLVN---GDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATT 268
Cdd:cd07105 154 PKGVLNVVThspEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 269 GKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGnpredGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGG 348
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 349 PgkPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEA 428
Cdd:cd07105 309 L--ADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIES 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 88196026 429 GTVEIN------EAGrkpdLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07105 387 GAVHINgmtvhdEPT----LPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
8-474 |
1.19e-99 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 308.33 E-value: 1.19e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNSNetIEVINPA-TEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQ 86
Cdd:TIGR01237 36 VINGERVETENK--IVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 87 AITDELGAPLS-----LSERV----HYQMGLNHFVAARDALDnYEFEERRgddlVVKEAIGVSGLITPWNFPTNQTSLKL 157
Cdd:TIGR01237 114 LLVKEVGKPWNeadaeVAEAIdfmeYYARQMIELAKGKPVNS-REGETNQ----YVYTPTGVTVVISPWNFPFAIMVGMT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 158 AAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAK 237
Cdd:TIGR01237 189 VAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 238 ------DFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNP 311
Cdd:TIGR01237 269 vqpgqkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPP 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 312 REDGTQVGPIISKKQFDQVQNYINKGIEEGaELFYGGPGKPEgleKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYN 391
Cdd:TIGR01237 349 DSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDS---KGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRAS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 392 DLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE------AGRKpdlPFGGYKQSGLGREWG--DYgIEE 463
Cdd:TIGR01237 425 DFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRnitgaiVGYQ---PFGGFKMSGTDSKAGgpDY-LAL 500
|
490
....*....|.
gi 88196026 464 FLEVKSIAGYF 474
Cdd:TIGR01237 501 FMQAKTVTEMF 511
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
31-466 |
6.53e-97 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 299.21 E-value: 6.53e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 31 EVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSER-VHYQMGLN 109
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFeVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 110 HFVAARDALDNYE-FEERRGD-DLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAA-VILAEIF 186
Cdd:cd07152 82 HEAAGLPTQPQGEiLPSAPGRlSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 187 DKVGVPKGVFNLVNGdGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKA 266
Cdd:cd07152 162 EEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 267 TTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFY 346
Cdd:cd07152 241 GAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 347 GGPgkpeglEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSI 426
Cdd:cd07152 321 GGT------YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 88196026 427 EAGTVEINE--AGRKPDLPFGGYKQSGLG-REWGDYGIEEFLE 466
Cdd:cd07152 395 RTGMLHINDqtVNDEPHNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
25-471 |
2.18e-95 |
|
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: 295.37 E-value: 2.18e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 25 INPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDK---IVKEYENRKDDIVQAITDELGApLSLSER 101
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRfhdLVLERRDELLDLIQLETGKARR-HAFEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 102 VHYQMGLNHFvaARDALDNYEFEERRG------DDLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEET 175
Cdd:cd07101 80 LDVAIVARYY--ARRAERLLKPRRRRGaipvltRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 176 PFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMmsFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVL 255
Cdd:cd07101 158 ALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADYVM--FTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 256 DDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYIN 335
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 336 KGIEEGAELFYGGPGKPE-GlekGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGK 414
Cdd:cd07101 316 DAVAKGATVLAGGRARPDlG---PYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196026 415 DKETLHKVARSIEAGTVEINEAGRKP----DLPFGGYKQSGLGREWGDYGIEEFLEVKSIA 471
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNEGYAAAwasiDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
26-471 |
3.65e-93 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 289.97 E-value: 3.65e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 26 NPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLslserVHYQ 105
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTM-----VDAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 106 MG--LNHFVAARDALDNYEF----EERRGDDL-------VVKEAIGVSGLITPWNFP-TNQTSLKLAAAFAaGSPVVLKP 171
Cdd:cd07098 77 LGeiLVTCEKIRWTLKHGEKalrpESRPGGLLmfykrarVEYEPLGVVGAIVSWNYPfHNLLGPIIAALFA-GNAIVVKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 172 SEETPFAAV----ILAEIFDKVGVPKGVFNLVNGDGaGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELG 247
Cdd:cd07098 156 SEQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 248 GKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQF 327
Cdd:cd07098 235 GKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 328 DQVQNYINKGIEEGAELFYGGPGKPEGLE-KGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYG 406
Cdd:cd07098 315 DRLEELVADAVEKGARLLAGGKRYPHPEYpQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196026 407 LAGYVIGKDKETLHKVARSIEAGTVEINEAGRK---PDLPFGGYKQSGLGREWGDYGIEEFLEVKSIA 471
Cdd:cd07098 395 LGASVFGKDIKRARRIASQLETGMVAINDFGVNyyvQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
25-470 |
4.26e-93 |
|
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: 289.53 E-value: 4.26e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 25 INPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLS----- 99
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAggeir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 100 ---ERVHYQMGLNHFVAARDALDNYE-FEERrgddlVVKEAIGVSGLITPWNFP----TNqtslKLAAAFAAGSPVVLKP 171
Cdd:cd07102 81 gmlERARYMISIAEEALADIRVPEKDgFERY-----IRREPLGVVLIIAPWNYPyltaVN----AVIPALLAGNAVILKH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 172 SEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAgVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSP 251
Cdd:cd07102 152 SPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 252 YIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQ 331
Cdd:cd07102 231 AYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 332 NYINKGIEEGAELFYGGPGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYV 411
Cdd:cd07102 311 AQIADAIAKGARALIDGALFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 412 IGKDKETLHKVARSIEAGTVEINEAGR-KPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMNRCDYlDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
22-470 |
4.84e-87 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 273.92 E-value: 4.84e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 22 IEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSlSER 101
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLA-SAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 102 V----------HYQMGLNHFVAARDAlDNYEFEERRGddLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKP 171
Cdd:PRK09406 82 AealkcakgfrYYAEHAEALLADEPA-DAAAVGASRA--YVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 172 SEETPFAAVILAEIFDKVGVPKGVF-NLVNGDGAgVGNPLSEhPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKS 250
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFqTLLVGSGA-VEAILRD-PRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 251 PYIVLDDVDIKEAAK-ATTGKVVNNtGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQ 329
Cdd:PRK09406 237 PFIVMPSADLDRAAEtAVTARVQNN-GQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 330 VQNYINKGIEEGAELFYGGPgKPEGleKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAG 409
Cdd:PRK09406 316 VEKQVDDAVAAGATILCGGK-RPDG--PGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88196026 410 YVIGKDKETLHKVARSIEAGTVEIN-EAGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFINgMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
62-470 |
1.24e-84 |
|
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: 266.70 E-value: 1.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 62 SVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERRGDDL--------VV 133
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRVSVPLllqpakayVI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 134 KEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVgVPKGVFNLVNGDGAgVGNPLSEH 213
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE-VATALLAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 214 PKVRMMsFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAK-ATTGKVVNNtGQVCTAGTRVLVPNKIK 292
Cdd:cd07087 176 PFDHIF-FTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARrIAWGKFLNA-GQTCIAPDYVLVHESIK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 293 DAFLAELKEQFSQVRVGNPREDgTQVGPIISKKQFDQVQNYINKGieegaELFYGGPGKPEGLekgYFArPTIFINVDNQ 372
Cdd:cd07087 254 DELIEELKKAIKEFYGEDPKES-PDYGRIINERHFDRLASLLDDG-----KVVIGGQVDKEER---YIA-PTILDDVSPD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 373 MTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE----AGrKPDLPFGGYK 448
Cdd:cd07087 324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDvllhAA-IPNLPFGGVG 402
|
410 420
....*....|....*....|..
gi 88196026 449 QSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07087 403 NSGMGAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
56-464 |
2.09e-84 |
|
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: 266.40 E-value: 2.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 56 LEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLS---LSERVHYQMGLNHfvaARDALDNYEFEERRGDDL- 131
Cdd:cd07134 12 LALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAevdLTEILPVLSEINH---AIKHLKKWMKPKRVRTPLl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 132 -------VVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETP----FAAVILAEIFDkvgvPKGVFnLVN 200
Cdd:cd07134 89 lfgtkskIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPhtsaVIAKIIREAFD----EDEVA-VFE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 201 GDgAGVGNPLSEHPkVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATT-GKVVNNtGQVC 279
Cdd:cd07134 164 GD-AEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAwGKFLNA-GQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 280 TAGTRVLVPNKIKDAFLAELKEQFSQVrVGnpREDGTQVGP----IISKKQFDQVQNYINKGIEEGAELFYGGPGKPEGL 355
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLKAEIEKF-YG--KDAARKASPdlarIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 356 ekgYFArPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE 435
Cdd:cd07134 318 ---YIA-PTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVND 393
|
410 420 430
....*....|....*....|....*....|..
gi 88196026 436 AGRK---PDLPFGGYKQSGLGREWGDYGIEEF 464
Cdd:cd07134 394 VVLHflnPNLPFGGVNNSGIGSYHGVYGFKAF 425
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
55-470 |
1.50e-82 |
|
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: 261.65 E-value: 1.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 55 YLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAplslseRVHYQ----------MGLNHfvaARDALDNYEFE 124
Cdd:cd07133 11 FLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGH------RSRHEtllaeilpsiAGIKH---ARKHLKKWMKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 125 ERRGDDL--------VVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETP-FAAVI---LAEIF--DKVG 190
Cdd:cd07133 82 SRRHVGLlflpakaeVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPrTSALLaelLAEYFdeDEVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 191 VpkgvfnlVNGdGAGVGNPLSEHPKVRMMsFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKA-TTG 269
Cdd:cd07133 162 V-------VTG-GADVAAAFSSLPFDHLL-FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERiAFG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 270 KVVNNtGQVCTAGTRVLVPNKIKDAFLAELKEQFSQV---RVGNPreDGTqvgPIISKKQFDQVQNYINKGIEEGAELFY 346
Cdd:cd07133 233 KLLNA-GQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNP--DYT---SIINERHYARLQGLLEDARAKGARVIE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 347 GGPGKPEGLEKGYFArPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSI 426
Cdd:cd07133 307 LNPAGEDFAATRKLP-PTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRT 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 88196026 427 EAGTVEINEAG---RKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07133 386 HSGGVTINDTLlhvAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
6-470 |
6.44e-81 |
|
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: 258.66 E-value: 6.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 6 KQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIV 85
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 86 QAITDELGAPLSLS--------ERVHYQMGLNHFVAArdalDNYEFEERRGDDLVVKEAIGVSGLITPWNFPTNQTSLKL 157
Cdd:TIGR01722 82 ELITAEHGKTHSDAlgdvarglEVVEHACGVNSLLKG----ETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 158 AAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVgNPLSEHPKVRMMSFTGSGPTGSKIMEKAAK 237
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAV-DRLLEHPDVKAVSFVGSTPIGRYIHTTGSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 238 DFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDaFLAELKEQFSQVRVGNPREDGTQ 317
Cdd:TIGR01722 237 HGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAADE-WVPEIRERAEKIRIGPGDDPGAE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 318 VGPIISKKQFDQVQNYINKGIEEGAELFYGGPG-KPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEA 396
Cdd:TIGR01722 316 MGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGyKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 88196026 397 IQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKPdLP---FGGYKQSGLG--REWGDYGIEEFLEVKSI 470
Cdd:TIGR01722 396 IALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVP-LPyfsFTGWKDSFFGdhHIYGKQGTHFYTRGKTV 473
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
43-454 |
7.25e-80 |
|
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: 254.50 E-value: 7.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 43 DVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPL--SLSErvhyqmglnhfVAAR----- 115
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLweAQTE-----------VAAMagkid 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 116 ---DALDNYEFEERR----GDDLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDK 188
Cdd:cd07095 70 isiKAYHERTGERATpmaqGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 189 VGVPKGVFNLVNGDGAgVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKV-SLELGGKSPYIVLDDVDIKEAAKAT 267
Cdd:cd07095 150 AGLPPGVLNLVQGGRE-TGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKIlALEMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 268 TGKVVNNTGQVCTAGTRVLVPNKIK-DAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFy 346
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 347 ggpGKPEGL-EKGYFARPTIfINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARS 425
Cdd:cd07095 308 ---LAMERLvAGTAFLSPGI-IDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLAR 383
|
410 420 430
....*....|....*....|....*....|.
gi 88196026 426 IEAGTVEINE--AGRKPDLPFGGYKQSGLGR 454
Cdd:cd07095 384 IRAGIVNWNRptTGASSTAPFGGVGLSGNHR 414
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
25-470 |
1.90e-77 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 249.39 E-value: 1.90e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 25 INPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSE-RVH 103
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARaEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 104 YQMGLNHFVAARD-ALDNYEFEERRGDDLVVK-EAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVI 181
Cdd:PRK13968 92 KSANLCDWYAEHGpAMLKAEPTLVENQQAVIEyRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 182 LAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEhPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIK 261
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 262 EAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEG 341
Cdd:PRK13968 251 LAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 342 AELFYGGPgKPEGleKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHK 421
Cdd:PRK13968 331 ARLLLGGE-KIAG--AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQ 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 88196026 422 VARSIEAGTVEINE-AGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:PRK13968 408 MAARLECGGVFINGyCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
8-457 |
2.22e-77 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 249.43 E-value: 2.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNsnETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQA 87
Cdd:cd07130 2 VYDGEWGGGG--GVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 88 ITDELGAPLS-----LSERV---HYQMGLNHfvaardALDNYEF-EERRGDDLVvkEA---IGVSGLITPWNFPTNQTSL 155
Cdd:cd07130 80 VSLEMGKILPeglgeVQEMIdicDFAVGLSR------QLYGLTIpSERPGHRMM--EQwnpLGVVGVITAFNFPVAVWGW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 156 KLAAAFAAGSPVVLKPSEETPFAAV----ILAEIFDKVGVPKGVFNLVNGDGAgVGNPLSEHPKVRMMSFTGSGPTGSKI 231
Cdd:cd07130 152 NAAIALVCGNVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 232 MEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNP 311
Cdd:cd07130 231 GQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 312 REDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPGKPEGlekGYFARPTIfINVDNQMTIAQEEIFGPVMSVITYN 391
Cdd:cd07130 311 LDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGP---GNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFD 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88196026 392 DLDEAIQIANDTKYGLAGYVIGKDKETLHKV--ARSIEAGTVEIN------EAGRKpdlpFGGYKQSGLGREWG 457
Cdd:cd07130 387 TLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNigtsgaEIGGA----FGGEKETGGGRESG 456
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
9-453 |
4.42e-77 |
|
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: 249.81 E-value: 4.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 9 INGEwvESNSNETIEVINPA-TEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQA 87
Cdd:cd07125 37 INGE--ETETGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 88 ITDELGAPLS-----LSERVHYqmgLNHFVA-ARDALDNYEFEERRG-DDLVVKEAIGVSGLITPWNFP----TNQTslk 156
Cdd:cd07125 115 AAAEAGKTLAdadaeVREAIDF---CRYYAAqARELFSDPELPGPTGeLNGLELHGRGVFVCISPWNFPlaifTGQI--- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 157 lAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEK-A 235
Cdd:cd07125 189 -AAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRAlA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 236 AKDFKKVSL--ELGGKSPYIVLDDVDIKEAAKattgKVV----NNTGQVCTAgTRVL-VPNKIKDAFLAELKEQFSQVRV 308
Cdd:cd07125 268 ERDGPILPLiaETGGKNAMIVDSTALPEQAVK----DVVqsafGSAGQRCSA-LRLLyLQEEIAERFIEMLKGAMASLKV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 309 GNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELfyggPGKPEGLEKGYFARPTIfINVDNQMTIaQEEIFGPVMSVI 388
Cdd:cd07125 343 GDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLI----APAPLDDGNGYFVAPGI-IEIVGIFDL-TTEVFGPILHVI 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196026 389 TY--NDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEA------GRKpdlPFGGYKQSGLG 453
Cdd:cd07125 417 RFkaEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNitgaivGRQ---PFGGWGLSGTG 486
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
8-471 |
4.82e-77 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 249.42 E-value: 4.82e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNSNETIevINP-ATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQ 86
Cdd:cd07083 22 VIGGEWVDTKERMVS--VSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 87 AITDELGAplslservHYQMGLNhfvAARDALDNYEFEERRGDDLVVKEAI----------------GVSGLITPWNFPT 150
Cdd:cd07083 100 TLTYEVGK--------NWVEAID---DVAEAIDFIRYYARAALRLRYPAVEvvpypgednesfyvglGAGVVISPWNFPV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 151 NQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSK 230
Cdd:cd07083 169 AIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 231 IMEKAAKD------FKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFS 304
Cdd:cd07083 249 IYEAAARLapgqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 305 QVRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGaELFYGGPgKPEGleKGYFARPTIFINVDNQMTIAQEEIFGPV 384
Cdd:cd07083 329 RLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGK-RLEG--EGYFVAPTVVEEVPPKARIAQEEIFGPV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 385 MSVITY--NDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE------AGRKpdlPFGGYKQSGLGREW 456
Cdd:cd07083 405 LSVIRYkdDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRkitgalVGVQ---PFGGFKLSGTNAKT 481
|
490
....*....|....*..
gi 88196026 457 G--DYgIEEFLEVKSIA 471
Cdd:cd07083 482 GgpHY-LRRFLEMKAVA 497
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
62-470 |
3.86e-69 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 228.37 E-value: 3.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 62 SVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSERVHYQMGLNHFVAARDALDNY--------EFEERRGDDLVV 133
Cdd:PTZ00381 27 PLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYlkpekvdtVGVFGPGKSYII 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 134 KEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVgVPKGVFNLVNGdGAGVGNPLSEH 213
Cdd:PTZ00381 107 PEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLKE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 214 PkVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATT-GKVVNNtGQVCTAGTRVLVPNKIK 292
Cdd:PTZ00381 185 P-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAwGKFLNA-GQTCVAPDYVLVHRSIK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 293 DAFLAELKEQFSQVRVGNPREDGTqVGPIISKKQFDQVQNYINkgiEEGAELFYGGPGkpeGLEKGYFArPTIFINVDNQ 372
Cdd:PTZ00381 263 DKFIEALKEAIKEFFGEDPKKSED-YSRIVNEFHTKRLAELIK---DHGGKVVYGGEV---DIENKYVA-PTIIVNPDLD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 373 MTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEA---GRKPDLPFGGYKQ 449
Cdd:PTZ00381 335 SPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCvfhLLNPNLPFGGVGN 414
|
410 420
....*....|....*....|.
gi 88196026 450 SGLGREWGDYGIEEFLEVKSI 470
Cdd:PTZ00381 415 SGMGAYHGKYGFDTFSHPKPV 435
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
56-470 |
9.27e-69 |
|
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: 226.23 E-value: 9.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 56 LEFRHTSVKerqaLLDKIVKEYENrkdDIVQAITDELGAP----------LSLSErvhyqmgLNHfvaARDALDNYEFEE 125
Cdd:cd07136 19 VEFRIEQLK----KLKQAIKKYEN---EILEALKKDLGKSefeaymteigFVLSE-------INY---AIKHLKKWMKPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 126 RRGDDL--------VVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVgVPKGVFN 197
Cdd:cd07136 82 RVKTPLlnfpsksyIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 198 LVNGDGAGVGNPLSEhpKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATT-GKVVNnTG 276
Cdd:cd07136 161 VVEGGVEENQELLDQ--KFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVwGKFLN-AG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 277 QVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTqVGPIISKKQFDQVQNYInkgieEGAELFYGGPGKPEGLe 356
Cdd:cd07136 238 QTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPD-YGRIINEKHFDRLAGLL-----DNGKIVFGGNTDRETL- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 357 kgYFArPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE- 435
Cdd:cd07136 311 --YIE-PTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDt 387
|
410 420 430
....*....|....*....|....*....|....*....
gi 88196026 436 ----AgrKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07136 388 imhlA--NPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
7-451 |
1.18e-68 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 227.15 E-value: 1.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 7 QYINGEWVESNSnETIEVINPATEEVI--GKVAkgNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDI 84
Cdd:PRK09457 3 LWINGDWIAGQG-EAFESRNPVSGEVLwqGNDA--TAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 85 VQAITDELGAPL--SLSERVHyqmglnhfVAARDALDNYEFEERRG---DDLVVKEAI------GVSGLITPWNFPTNQT 153
Cdd:PRK09457 80 AEVIARETGKPLweAATEVTA--------MINKIAISIQAYHERTGekrSEMADGAAVlrhrphGVVAVFGPYNFPGHLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 154 SLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGdGAGVGNPLSEHPKVRMMSFTGSGPTGSKIME 233
Cdd:PRK09457 152 NGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 234 KAAKDFKKV-SLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIK-DAFLAELKEQFSQVRVGNP 311
Cdd:PRK09457 231 QFAGQPEKIlALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 312 REDGTQ-VGPIISKKQFDQV----QNYINKGIEEGAELFYGGPGKPeglekgyFARPTIfINVDNQMTIAQEEIFGPVMS 386
Cdd:PRK09457 311 DAEPQPfMGAVISEQAAQGLvaaqAQLLALGGKSLLEMTQLQAGTG-------LLTPGI-IDVTGVAELPDEEYFGPLLQ 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88196026 387 VITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE--AGRKPDLPFGGYKQSG 451
Cdd:PRK09457 383 VVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKplTGASSAAPFGGVGASG 449
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
42-464 |
1.88e-68 |
|
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: 225.18 E-value: 1.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 42 ADVDKAVEAADDVYLEFRHTSVKERQALLDKI---VKEYENRkddIVQAITDELGAPLSLSERVHYQMGLNHFVAARDAL 118
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLywaVKDNEEA---IVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 119 DNYEFEERRGDDLVV---------KEAIGVSGLITPWNFPTnQTSLK-LAAAFAAGSPVVLKPSEETPFAAVILAEIFDK 188
Cdd:cd07135 82 KKWAKDEKVKDGPLAfmfgkprirKEPLGVVLIIGPWNYPV-LLALSpLVGAIAAGCTVVLKPSELTPHTAALLAELVPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 189 vGVPKGVFNLVNGDGAGVGNPLSEhpKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATT 268
Cdd:cd07135 161 -YLDPDAFQVVQGGVPETTALLEQ--KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 269 -GKVvNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDgTQVGPIISKKQFDQVQNYINKgieEGAELFYG 347
Cdd:cd07135 238 wGKF-GNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANAS-PDYTRIVNPRHFNRLKSLLDT---TKGKVVIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 348 GPGKPEGLekgyFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIE 427
Cdd:cd07135 313 GEMDEATR----FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTR 388
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 88196026 428 AGTVEINE---AGRKPDLPFGGYKQSGLGREWGDYGIEEF 464
Cdd:cd07135 389 SGGVVINDtliHVGVDNAPFGGVGDSGYGAYHGKYGFDTF 428
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
3-469 |
2.97e-68 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 226.18 E-value: 2.97e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 3 DYTKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDK---IVKEYen 79
Cdd:PLN00412 14 DVYKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKaaaILKEH-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 80 rKDDIVQAITDELGAPL--SLSERVHYQMGLNHfvAARDAL-----------DNYEFEERRGDDLVVKEAIGVSGLITPW 146
Cdd:PLN00412 92 -KAPIAECLVKEIAKPAkdAVTEVVRSGDLISY--TAEEGVrilgegkflvsDSFPGNERNKYCLTSKIPLGVVLAIPPF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 147 NFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGsGP 226
Cdd:PLN00412 169 NYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTG-GD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 227 TGSKIMEKAAkdFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQV 306
Cdd:PLN00412 248 TGIAISKKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 307 RVGNPrEDGTQVGPIISKKQFDQVQNYINKGIEEGAELfyggpgKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMS 386
Cdd:PLN00412 326 TVGPP-EDDCDITPVVSESSANFIEGLVMDAKEKGATF------CQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 387 VITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEA-GRKPD-LPFGGYKQSGLGREWGDYGIEEF 464
Cdd:PLN00412 399 VIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDhFPFQGLKDSGIGSQGITNSINMM 478
|
....*
gi 88196026 465 LEVKS 469
Cdd:PLN00412 479 TKVKS 483
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
22-453 |
4.30e-66 |
|
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: 219.60 E-value: 4.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 22 IEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEF-RHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSe 100
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRnNWLPAHERIAILERLADLMEERADELALLIAREGGKPLVDA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 101 RVHYQMGLNHFVAARDALDNYEFEE-----------RRGddLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVL 169
Cdd:cd07148 80 KVEVTRAIDGVELAADELGQLGGREipmgltpasagRIA--FTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 170 KPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAgVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDfKKVSLELGGK 249
Cdd:cd07148 158 KPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 250 SPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQ 329
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 330 VQNYINKGIEEGAELFYGgpGKPegLEKGYFArPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAG 409
Cdd:cd07148 316 VEEWVNEAVAAGARLLCG--GKR--LSDTTYA-PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 88196026 410 YVIGKDKETLHKVARSIEAGTVEINE--AGRKPDLPFGGYKQSGLG 453
Cdd:cd07148 391 AVFTKDLDVALKAVRRLDATAVMVNDhtAFRVDWMPFAGRRQSGYG 436
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
9-475 |
2.66e-63 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 215.77 E-value: 2.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 9 INGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAI 88
Cdd:PLN02419 118 IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 89 TDELGAPLSLS--------ERVHYQMGLnhfvaARDALDNYEFEERRG-DDLVVKEAIGVSGLITPWNFPTNQTSLKLAA 159
Cdd:PLN02419 198 TTEQGKTLKDShgdifrglEVVEHACGM-----ATLQMGEYLPNVSNGvDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 160 AFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVgNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDF 239
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 240 KKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKdAFLAELKEQFSQVRVGNPREDGTQVG 319
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAK-SWEDKLVERAKALKVTCGSEPDADLG 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 320 PIISKKQFDQVQNYINKGIEEGAELFYGGPG-KPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQ 398
Cdd:PLN02419 431 PVISKQAKERICRLIQSGVDDGAKLLLDGRDiVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAIS 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 399 IANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKPdLP---FGGYKQSGLG--REWGDYGIEEFLEVKSIAGY 473
Cdd:PLN02419 511 IINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVP-LPffsFTGNKASFAGdlNFYGKAGVDFFTQIKLVTQK 589
|
..
gi 88196026 474 FK 475
Cdd:PLN02419 590 QK 591
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
46-470 |
1.27e-59 |
|
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: 202.07 E-value: 1.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 46 KAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSERVHYQMGLNHFVAARDALDNY---E 122
Cdd:cd07132 2 EAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWmkpE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 123 FEERR----GDDLVV-KEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVgVPKGVFN 197
Cdd:cd07132 82 PVKKNlatlLDDVYIyKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKY-LDKECYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 198 LVNGdGAGVGNPLSEHpKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATT-GKVVNnTG 276
Cdd:cd07132 161 VVLG-GVEETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAwGKFIN-AG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 277 QVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDgTQVGPIISKKQFDQVQNYInkgieEGAELFYGGpgkpEGLE 356
Cdd:cd07132 238 QTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKES-PDYGRIINDRHFQRLKKLL-----SGGKVAIGG----QTDE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 357 KGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEA 436
Cdd:cd07132 308 KERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDT 387
|
410 420 430
....*....|....*....|....*....|....*..
gi 88196026 437 ---GRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07132 388 imhYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSC 424
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
59-470 |
2.61e-56 |
|
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: 193.01 E-value: 2.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 59 RHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERRGDDL------- 131
Cdd:cd07137 16 RTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPEKVKTPLttfpaka 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 132 -VVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVfNLVNGdGAGVGNPL 210
Cdd:cd07137 96 eIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAI-KVIEG-GVPETTAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 211 SEHpKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAK-ATTGKVVNNTGQVCTAGTRVLVPN 289
Cdd:cd07137 174 LEQ-KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRrIAGGKWGCNNGQACIAPDYVLVEE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 290 ----KIKDAFLAELKEQFSQvrvgNPREDGtQVGPIISKKQFDQVQNYINKGIEEgAELFYGGpgkpEGLEKGYFARPTI 365
Cdd:cd07137 253 sfapTLIDALKNTLEKFFGE----NPKESK-DLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGG----ERDEKNLYIEPTI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 366 FINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRK---PDL 442
Cdd:cd07137 323 LLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQyaiDTL 402
|
410 420
....*....|....*....|....*...
gi 88196026 443 PFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:cd07137 403 PFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
8-451 |
9.95e-53 |
|
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: 185.48 E-value: 9.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNsnETIEVINPAT-EEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALL----DKIVKEYENRKD 82
Cdd:cd07123 36 VIGGKEVRTG--NTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFlkaaDLLSGKYRYELN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 83 ---------DIVQAITD---EL----------------GAPLSLSE----RVHYQmGLNHFVAArdaldnyefeerrgdd 130
Cdd:cd07123 114 aatmlgqgkNVWQAEIDaacELidflrfnvkyaeelyaQQPLSSPAgvwnRLEYR-PLEGFVYA---------------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 131 lvvkeaigvsglITPWNFptnqTSL--KLAAAFA-AGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVG 207
Cdd:cd07123 177 ------------VSPFNF----TAIggNLAGAPAlMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 208 NPLSEHPKVRMMSFTGSGPTGSKIMEKAA------KDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTA 281
Cdd:cd07123 241 DTVLASPHLAGLHFTGSTPTFKSLWKQIGenldryRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 282 GTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEE-GAELFYGgpGKPEGlEKGYF 360
Cdd:cd07123 321 ASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAG--GKCDD-SVGYF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 361 ARPTIFINVDNQMTIAQEEIFGPVMSVITY--NDLDEAIQIANDT-KYGLAGYVIGKDK---ETLHKVARSiEAGTVEIN 434
Cdd:cd07123 398 VEPTVIETTDPKHKLMTEEIFGPVLTVYVYpdSDFEETLELVDTTsPYALTGAIFAQDRkaiREATDALRN-AAGNFYIN 476
|
490 500
....*....|....*....|...
gi 88196026 435 EagrKP------DLPFGGYKQSG 451
Cdd:cd07123 477 D---KPtgavvgQQPFGGARASG 496
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
9-451 |
1.31e-52 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 185.37 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 9 INGEWVESnSNETIEVINPATEE-VIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALL----DKIVKEYenrKDD 83
Cdd:TIGR01236 36 IGGEEVYD-SNERIPQVNPHNHQaVLAKATNATEEDAMKAVEAALDAKKDWSNLPFYDRAAIFlkaaDLLSGPY---RYE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 84 IVQAITdelgapLSLSERVhYQMGLNhfvAARDALDNYEFEERRGDDLVVKEAIGVSGL---------------ITPWNF 148
Cdd:TIGR01236 112 ILAATM------LGQSKTV-YQAEID---AVAELIDFFRFNVKYARELYAQQPISAPGEwnrteyrplegfvyaISPFNF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 149 PTNQTSLKLAAAFAaGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTG 228
Cdd:TIGR01236 182 TAIAGNLAGAPALM-GNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 229 SKIMEKAA------KDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQ 302
Cdd:TIGR01236 261 KHLWKKVAqnldryHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 303 FSQVRVGNPREDGTQVGPIISKKQFDQVQNYIN--KGIEEGAELFYGGPGKPEgleKGYFARPTIFINVDNQMTIAQEEI 380
Cdd:TIGR01236 341 LQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEdaKKDPEALTILYGGKYDDS---QGYFVEPTVVESKDPDHPLMSEEI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 381 FGPVMSVITYND--LDEAIQIA-NDTKYGLAGYVIGKDKETLHKVARSIE--AGTVEINE------AGRKpdlPFGGYKQ 449
Cdd:TIGR01236 418 FGPVLTVYVYPDdkYKEILDLVdSTSQYGLTGAVFAKDRKAILEADKKLRfaAGNFYINDkctgavVGQQ---PFGGARM 494
|
..
gi 88196026 450 SG 451
Cdd:TIGR01236 495 SG 496
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
15-453 |
5.33e-51 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 186.61 E-value: 5.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 15 ESNSNETIEVINPA-TEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELG 93
Cdd:PRK11905 562 GDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 94 --APLSLSErvhyqmglnhfvaARDALD---NYEFEERRGDDLVVKEAIGVSGLITPWNFP----TNQtslkLAAAFAAG 164
Cdd:PRK11905 642 ktLANAIAE-------------VREAVDflrYYAAQARRLLNGPGHKPLGPVVCISPWNFPlaifTGQ----IAAALVAG 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 165 SPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGsKIMEK--AAKDFKKV 242
Cdd:PRK11905 705 NTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVA-RLIQRtlAKRSGPPV 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 243 SL--ELGGKSPYIVlDDVDIKEAAkatTGKVVN----NTGQVCTAgTRVL-VPNKIKDAFLAELKEQFSQVRVGNPREDG 315
Cdd:PRK11905 784 PLiaETGGQNAMIV-DSSALPEQV---VADVIAsafdSAGQRCSA-LRVLcLQEDVADRVLTMLKGAMDELRIGDPWRLS 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 316 TQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPgkPEGLEKGYFARPTIfINVDNqmtIAQ--EEIFGPVMSVITY--N 391
Cdd:PRK11905 859 TDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPL--PAETEKGTFVAPTL-IEIDS---ISDleREVFGPVLHVVRFkaD 932
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196026 392 DLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE------AGRKpdlPFGGYKQSGLG 453
Cdd:PRK11905 933 ELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRniigavVGVQ---PFGGEGLSGTG 997
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
16-453 |
1.03e-50 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 185.40 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 16 SNSNETIEVINPA-TEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGA 94
Cdd:PRK11904 558 NGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGK 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 95 PL--SLSE--------RVHYQMGLNHFvAARDAL------DNYEFEERRGddlvvkeaigVSGLITPWNFP----TNQts 154
Cdd:PRK11904 638 TLqdAIAEvreavdfcRYYAAQARRLF-GAPEKLpgptgeSNELRLHGRG----------VFVCISPWNFPlaifLGQ-- 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 155 lkLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKI-ME 233
Cdd:PRK11904 705 --VAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInRT 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 234 KAAKDFKKVSL--ELGGKSPYI---------VLDDVdIKEAAKAttgkvvnnTGQVCTAgTRVL-VPNKIKDAFLAELKE 301
Cdd:PRK11904 783 LAARDGPIVPLiaETGGQNAMIvdstalpeqVVDDV-VTSAFRS--------AGQRCSA-LRVLfVQEDIADRVIEMLKG 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 302 QFSQVRVGNPREDGTQVGPIISKKQFDQVQNYINKgIEEGAELFYGGPgKPEGLEKGYFARPTIFiNVDNqmtIAQ--EE 379
Cdd:PRK11904 853 AMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIER-MKREARLLAQLP-LPAGTENGHFVAPTAF-EIDS---ISQleRE 926
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 380 IFGPVMSVITYN--DLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE------AGRKpdlPFGGYKQSG 451
Cdd:PRK11904 927 VFGPILHVIRYKasDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRnqigavVGVQ---PFGGQGLSG 1003
|
..
gi 88196026 452 LG 453
Cdd:PRK11904 1004 TG 1005
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
15-434 |
3.08e-50 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 184.37 E-value: 3.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 15 ESNSNETIEVINPA-TEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELG 93
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAG 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 94 --APLSLSErvhyqmglnhfVaaRDALDnyeF-------EERRGDDLVVKEAIGVSGLITPWNFP----TNQTslklAAA 160
Cdd:COG4230 645 ktLPDAIAE-----------V--REAVD---FcryyaaqARRLFAAPTVLRGRGVFVCISPWNFPlaifTGQV----AAA 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 161 FAAGSPVVLKPSEETP---FAAVilaEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGsKIMEK--A 235
Cdd:COG4230 705 LAAGNTVLAKPAEQTPliaARAV---RLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETA-RLINRtlA 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 236 AKDFKKVSL--ELGGKSPYIVlDdvdikeaAKATTGKVV--------NNTGQVCTAgTRVL-VPNKIKDAFLAELKEQFS 304
Cdd:COG4230 781 ARDGPIVPLiaETGGQNAMIV-D-------SSALPEQVVddvlasafDSAGQRCSA-LRVLcVQEDIADRVLEMLKGAMA 851
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 305 QVRVGNPREDGTQVGPIISKKQFDQVQNYINKgIEEGAELFYGGPgKPEGLEKGYFARPTIF-INVDNQMtiaQEEIFGP 383
Cdd:COG4230 852 ELRVGDPADLSTDVGPVIDAEARANLEAHIER-MRAEGRLVHQLP-LPEECANGTFVAPTLIeIDSISDL---EREVFGP 926
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 88196026 384 VMSVITY--NDLDEAI-QIaNDTKYGLAGYV---IgkdKETLHKVARSIEAGTVEIN 434
Cdd:COG4230 927 VLHVVRYkaDELDKVIdAI-NATGYGLTLGVhsrI---DETIDRVAARARVGNVYVN 979
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
9-457 |
1.06e-48 |
|
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: 174.33 E-value: 1.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 9 INGEWVESNSNETieVINPAT-EEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQA 87
Cdd:TIGR01238 42 IGHSYKADGEAQP--VTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 88 ITDELGAPLSLS-ERVHYQMGLNHFVA--ARDALDNYEfeerrgddlvvKEAIGVSGLITPWNFPTNQTSLKLAAAFAAG 164
Cdd:TIGR01238 120 CVREAGKTIHNAiAEVREAVDFCRYYAkqVRDVLGEFS-----------VESRGVFVCISPWNFPLAIFTGQISAALAAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 165 SPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDF-KKVS 243
Cdd:TIGR01238 189 NTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdAPVP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 244 L--ELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAgTRVL-VPNKIKDAFLAELKEQFSQVRVGNPREDGTQVGP 320
Cdd:TIGR01238 269 LiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSA-LRVLcVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 321 IISKKQFDQVQNYINKGIEEGAELFYGGPGKPEGLEKGYFARPTIFiNVDNqMTIAQEEIFGPVMSVITY--NDLDEAIQ 398
Cdd:TIGR01238 348 VIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACQHGTFVAPTLF-ELDD-IAELSEEVFGPVLHVVRYkaRELDQIVD 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88196026 399 IANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE------AGRKpdlPFGGYKQSGLGREWG 457
Cdd:TIGR01238 426 QINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRnqvgavVGVQ---PFGGQGLSGTGPKAG 487
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
8-457 |
2.01e-46 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 168.47 E-value: 2.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWveSNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQA 87
Cdd:PLN02315 24 YVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 88 ITDELGAPLS--------LSERVHYQMGLNHfvaardALDNYEFEERRGDDLV--VKEAIGVSGLITPWNFPTNQTSLKL 157
Cdd:PLN02315 102 VSLEMGKILAegigevqeIIDMCDFAVGLSR------QLNGSIIPSERPNHMMmeVWNPLGIVGVITAFNFPCAVLGWNA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 158 AAAFAAGSPVVLKPSEETPFAAV----ILAEIFDKVGVPKGVFNLVNGdGAGVGNPLSEHPKVRMMSFTGSGPTGSKIME 233
Cdd:PLN02315 176 CIALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 234 KAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPRE 313
Cdd:PLN02315 255 TVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 314 DGTQVGPI---ISKKQFDqvqnyinKGIE----EGAELFYGGPGKPEGlekGYFARPTIfINVDNQMTIAQEEIFGPVMS 386
Cdd:PLN02315 335 KGTLLGPLhtpESKKNFE-------KGIEiiksQGGKILTGGSAIESE---GNFVQPTI-VEISPDADVVKEELFGPVLY 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88196026 387 VITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKV--ARSIEAGTVEIN--EAGRKPDLPFGGYKQSGLGREWG 457
Cdd:PLN02315 404 VMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWigPLGSDCGIVNVNipTNGAEIGGAFGGEKATGGGREAG 478
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
37-470 |
3.26e-45 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 164.51 E-value: 3.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 37 AKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSERVHYQMGLNHFVAARD 116
Cdd:PLN02203 1 EEAPGETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 117 ALDNYEFEERR--------GDDLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDK 188
Cdd:PLN02203 81 NLKKWMAPKKAklplvafpATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 189 VGVPKGVfNLVNGdGAGVGNPLSEHPKVRMMsFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVlDDVDIKEAAKATT 268
Cdd:PLN02203 161 YLDSKAV-KVIEG-GPAVGEQLLQHKWDKIF-FTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIV-DSLSSSRDTKVAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 269 GKVVNN-----TGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTqVGPIISKKQFDQVQNYInKGIEEGAE 343
Cdd:PLN02203 237 NRIVGGkwgscAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLL-KDPRVAAS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 344 LFYGGPGKPEGLekgyFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVA 423
Cdd:PLN02203 315 IVHGGSIDEKKL----FIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRIL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 88196026 424 RSIEAGTVEINEAGRK---PDLPFGGYKQSGLGREWGDYGIEEFLEVKSI 470
Cdd:PLN02203 391 SETSSGSVTFNDAIIQyacDSLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
8-426 |
1.49e-40 |
|
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: 152.04 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVeSNSNETIEVINPATEEVIGKVAkGNKADVDKAVEAADDVYLE-FRHTSVKERQALLDKIVKEYENRKDDIVQ 86
Cdd:cd07128 4 YVAGQWH-AGTGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAREKGGPaLRALTFHERAAMLKALAKYLMERKEDLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 87 A--------------ITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERRGDDLVVKEAiGVSGLITPWNFPTNQ 152
Cdd:cd07128 82 LsaatgatrrdswidIDGGIGTLFAYASLGRRELPNAHFLVEGDVEPLSKDGTFVGQHILTPRR-GVAVHINAFNFPVWG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 153 TSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGV-PKGVFNLVNGDGAGVGNPLSEHPKVrmmSFTGSGPTGSK- 230
Cdd:cd07128 161 MLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHLGEQDVV---AFTGSAATAAKl 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 231 -----IMEKAAK-----DfkkvSLELGGKSPYIVLD----DVDIKEAAKATTGKvvnnTGQVCTAGTRVLVPNKIKDAFL 296
Cdd:cd07128 238 rahpnIVARSIRfnaeaD----SLNAAILGPDATPGtpefDLFVKEVAREMTVK----AGQKCTAIRRAFVPEARVDAVI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 297 AELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYINKgIEEGAELFYGGPGKPEGL----EKGYFARPTIFI--NVD 370
Cdd:cd07128 310 EALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDRFEVVgadaEKGAFFPPTLLLcdDPD 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 88196026 371 NQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSI 426
Cdd:cd07128 389 AATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
15-453 |
4.31e-40 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 154.36 E-value: 4.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 15 ESNSNETIEVINPA-TEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELG 93
Cdd:PRK11809 654 PVAAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAG 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 94 APLS-----LSERVHYqmgLNHFVA-ARDALDNyefEERRgddlvvkeAIGVSGLITPWNFP----TNQtslkLAAAFAA 163
Cdd:PRK11809 734 KTFSnaiaeVREAVDF---LRYYAGqVRDDFDN---DTHR--------PLGPVVCISPWNFPlaifTGQ----VAAALAA 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 164 GSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAK----DF 239
Cdd:PRK11809 796 GNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGrldpQG 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 240 KKVSL--ELGGKSPYIVlDdvdikeaAKATTGKVVNN--------TGQVCTAgTRVL-VPNKIKDAFLAELKEQFSQVRV 308
Cdd:PRK11809 876 RPIPLiaETGGQNAMIV-D-------SSALTEQVVADvlasafdsAGQRCSA-LRVLcLQDDVADRTLKMLRGAMAECRM 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 309 GNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPGKPEGLEKGYFARPTIfINVDNqmtIA--QEEIFGPVMS 386
Cdd:PRK11809 947 GNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEDWQSGTFVPPTL-IELDS---FDelKREVFGPVLH 1022
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88196026 387 VITY--NDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINE------AGRKpdlPFGGYKQSGLG 453
Cdd:PRK11809 1023 VVRYnrNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRnmvgavVGVQ---PFGGEGLSGTG 1094
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
44-396 |
6.29e-37 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 140.84 E-value: 6.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 44 VDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSE---RVHYQMGLNHFVAA----RD 116
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAEnicGDQVQLRARAFVIYsyriPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 117 ALDNYEFEERRGDDLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVG-VPKGV 195
Cdd:cd07084 81 EPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 196 FNLVNGDGAgVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAkdFKKVSLELGGKSPYIVLDDVDIKEA-AKATTGKVVNN 274
Cdd:cd07084 161 VTLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDAK--QARIYLELAGFNWKVLGPDAQAVDYvAWQCVQDMTAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 275 TGQVCTAGTRVLVPNKI-KDAFLAELKEQFSQVRVGnpredGTQVGPIISkkqFDQVQNYINKGIEEGAELFYGGPGKPE 353
Cdd:cd07084 238 SGQKCTAQSMLFVPENWsKTPLVEKLKALLARRKLE-----DLLLGPVQT---FTTLAMIAHMENLLGSVLLFSGKELKN 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 88196026 354 GLEKGYFA---RPTIFINVD--NQMTIA-QEEIFGPVMSVITYNDLDEA 396
Cdd:cd07084 310 HSIPSIYGacvASALFVPIDeiLKTYELvTEEIFGPFAIVVEYKKDQLA 358
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
79-470 |
3.04e-36 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 139.80 E-value: 3.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 79 NRKDDIVQAITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERRGDDL--------VVKEAIGVSGLITPWNFPT 150
Cdd:PLN02174 47 NHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSLttfpasaeIVSEPLGVVLVISAWNYPF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 151 NQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVfNLVNGDGAGVGNPLSEhpKVRMMSFTGSGPTGSK 230
Cdd:PLN02174 127 LLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAV-RVVEGAVTETTALLEQ--KWDKIFYTGSSKIGRV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 231 IMEKAAKDFKKVSLELGGKSPYIVLDDVDIK-EAAKATTGKVVNNTGQVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVG 309
Cdd:PLN02174 204 IMAAAAKHLTPVVLELGGKSPVVVDSDTDLKvTVRRIIAGKWGCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 310 NPREDgTQVGPIISKKQFDQVQNYINKGiEEGAELFYGGPGKPEGLEKGyfarPTIFINVDNQMTIAQEEIFGPVMSVIT 389
Cdd:PLN02174 284 NPMES-KDMSRIVNSTHFDRLSKLLDEK-EVSDKIVYGGEKDRENLKIA----PTILLDVPLDSLIMSEEIFGPLLPILT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 390 YNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRK---PDLPFGGYKQSGLGREWGDYGIEEFLE 466
Cdd:PLN02174 358 LNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHlalHTLPFGGVGESGMGAYHGKFSFDAFSH 437
|
....
gi 88196026 467 VKSI 470
Cdd:PLN02174 438 KKAV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
6-423 |
8.07e-35 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 136.37 E-value: 8.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 6 KQYINGEWVESnSNETIEVINPATEEVIGKVAkGNKADVDKAVE-AADDVYLEFRHTSVKERQALLDKIVKEYENRKDDI 84
Cdd:PRK11903 6 ANYVAGRWQAG-SGAGTPLFDPVTGEELVRVS-ATGLDLAAAFAfAREQGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 85 VQAIT------------DELGAPLSLSE--RVHYQMGLNHFVA-------ARDALdnyeFEERRgddlVVKEAIGVSGLI 143
Cdd:PRK11903 84 YDIATansgttrndsavDIDGGIFTLGYyaKLGAALGDARLLRdgeavqlGKDPA----FQGQH----VLVPTRGVALFI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 144 TPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGV-PKGVFNLVNGDGAGVGNPLSEHPKVrmmSFT 222
Cdd:PRK11903 156 NAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFDVV---SFT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 223 GSGPTGSKIMEKAA--KDFKKVSLELGGKSPYIVLDDVD---------IKEAAKATTGKvvnnTGQVCTAGTRVLVPNKI 291
Cdd:PRK11903 233 GSAETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAApgseafdlfVKEVVREMTVK----SGQKCTAIRRIFVPEAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 292 KDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQnyinKGIE---EGAELFYGGPGKP---EGLEKGYFARPTI 365
Cdd:PRK11903 309 YDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVR----AGLAalrAQAEVLFDGGGFAlvdADPAVAACVGPTL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 366 FI--NVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVA 423
Cdd:PRK11903 385 LGasDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
44-401 |
1.00e-30 |
|
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: 123.81 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 44 VDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSE----RVHYQMGLnhfvAArDALD 119
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQgelgRTTGQLRL----FA-DLVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 120 NYEFEERRGD------------DLV-VKEAIGVSGLITPWNFP---------TnqtslklAAAFAAGSPVVLKPSEETPF 177
Cdd:cd07129 76 EGSWLDARIDpadpdrqplprpDLRrMLVPLGPVAVFGASNFPlafsvaggdT-------ASALAAGCPVVVKAHPAHPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 178 AAVILAEIFDKV----GVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAK--DFKKVSLELGGKSP 251
Cdd:cd07129 149 TSELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 252 YIVLDD---VDIKEAAKATTGKVVNNTGQVCTAGTRVLVP-NKIKDAFLAELKEQFSQVrvgnprEDGTQVGPIIskkqf 327
Cdd:cd07129 229 VFILPGalaERGEAIAQGFVGSLTLGAGQFCTNPGLVLVPaGPAGDAFIAALAEALAAA------PAQTMLTPGI----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 328 dqVQNYiNKGIEE-----GAELFYGGPGKPEGLEkgyfARPTIFInVDNQMTIA----QEEIFGPVMSVITYNDLDEAIQ 398
Cdd:cd07129 298 --AEAY-RQGVEAlaaapGVRVLAGGAAAEGGNQ----AAPTLFK-VDAAAFLAdpalQEEVFGPASLVVRYDDAAELLA 369
|
...
gi 88196026 399 IAN 401
Cdd:cd07129 370 VAE 372
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
8-430 |
4.65e-14 |
|
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: 74.07 E-value: 4.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 8 YINGEWVESNsnETIEVINPATEEVIGKVAKGNKADVDKAVEAADDVYLEFRHTSVK--ERQALLDkivkeyenrkdDIV 85
Cdd:cd07126 2 LVAGKWKGAS--NYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKnpERYLLYG-----------DVS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 86 QAITDELGAP------LSLSERV---HYQMGLNHFVAARDALDNYEFEERR---------GDDLVVKEA-----IGVSGL 142
Cdd:cd07126 69 HRVAHELRKPevedffARLIQRVapkSDAQALGEVVVTRKFLENFAGDQVRflarsfnvpGDHQGQQSSgyrwpYGPVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 143 ITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEhPKVRMMSFT 222
Cdd:cd07126 149 ITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-ANPRMTLFT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 223 GSgptgSKIMEKAAKDFK-KVSLELGGKSPYIVLDDV-DIKEAAKATTGKVVNNTGQVCTAGTRVLV-PNKIKDAFLAEL 299
Cdd:cd07126 228 GS----SKVAERLALELHgKVKLEDAGFDWKILGPDVsDVDYVAWQCDQDAYACSGQKCSAQSILFAhENWVQAGILDKL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 300 KEQFSQVRVgnprEDGTqVGPIISKKQfDQVQNYINKGIE-EGAELFYGG-PGKPEGLEKGYFA-RPT-IF-----INVD 370
Cdd:cd07126 304 KALAEQRKL----EDLT-IGPVLTWTT-ERILDHVDKLLAiPGAKVLFGGkPLTNHSIPSIYGAyEPTaVFvpleeIAIE 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88196026 371 NQMTIAQEEIFGPVMSVITY--NDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGT 430
Cdd:cd07126 378 ENFELVTTEVFGPFQVVTEYkdEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGT 439
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
44-400 |
7.56e-11 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 63.82 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 44 VDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAplslsERVHYQMGLNHFvAARDALDNYEF 123
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGM-----GRVEDKVIKNHF-AAEYIYNVYKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 124 EER----RGDD----LVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKP----SEETPFAAVILAEIFDKVGV 191
Cdd:cd07081 75 EKTcgvlTGDEnggtLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 192 PKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGsGPTgskiMEKAAKDFKKVSLELG-GKSPYIVLDDVDIKEAAKATTGK 270
Cdd:cd07081 155 PENLIGWIDNPSIELAQRLMKFPGIGLLLATG-GPA----VVKAAYSSGKPAIGVGaGNTPVVIDETADIKRAVQSIVKS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 271 VVNNTGQVCTAGTRVLVPNKIKDaflaELKEQFSqvrvgnpredgTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPG 350
Cdd:cd07081 230 KTFDNGVICASEQSVIVVDSVYD----EVMRLFE-----------GQGAYKLTAEELQQVQPVILKNGDVNRDIVGQDAY 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 88196026 351 KPEGLeKGYFARPTIFINVDNQMTIAQEEIFG-----PVMSVITYNDLDEAIQIA 400
Cdd:cd07081 295 KIAAA-AGLKVPQETRILIGEVTSLAEHEPFAheklsPVLAMYRAANFADADAKA 348
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
42-427 |
3.39e-10 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 61.87 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 42 ADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAplslsERVHYQMGLNHFVAARD-ALDN 120
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGM-----GRVEDKIAKNHLAAEKTpGTED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 121 YEFEERRGDD-LVVKEA--IGVSGLITPWNFPT-----NQTSLklaaaFAAGSPVVLKPSeetPFAAVILAEIFD----- 187
Cdd:cd07121 79 LTTTAWSGDNgLTLVEYapFGVIGAITPSTNPTetiinNSISM-----LAAGNAVVFNPH---PGAKKVSAYAVElinka 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 188 --KVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGsgptGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAK 265
Cdd:cd07121 151 iaEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTG----GPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 266 AttgkVV------NNTgqVCTAGTRVLVPNKIKDAFLAELKEQFSQVRVGNPREDGTQV------GPIISKKQFDQVQNY 333
Cdd:cd07121 227 D----IVqgasfdNNL--PCIAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQAEQLLEVvlltnkGATPNKKWVGKDASK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 334 INK--GIEEGAELfyggpgkpeglekgyfarPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGL--AG 409
Cdd:cd07121 301 ILKaaGIEVPADI------------------RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTA 362
|
410
....*....|....*...
gi 88196026 410 YVIGKDKETLHKVARSIE 427
Cdd:cd07121 363 IIHSKNVENLTKMARAMQ 380
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
138-400 |
9.64e-10 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 60.57 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 138 GVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEET--PFAAV------ILAEI-FDkvgvPKGVFNLVNGDGAGVGN 208
Cdd:cd07127 195 GVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAilPLAITvqvareVLAEAgFD----PNLVTLAADTPEEPIAQ 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 209 PLSEHPKVRMMSFTGSGPTGSKiMEKAAKDfKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVP 288
Cdd:cd07127 271 TLATRPEVRIIDFTGSNAFGDW-LEANARQ-AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVP 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 289 N---------KIKDAFLAELKEQFSQVrVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPGKPEGLekgy 359
Cdd:cd07127 349 RdgiqtddgrKSFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPDAR---- 423
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 88196026 360 fARPTIFINVDNQMTIA-QEEIFGPVMSVITYNDLDEAIQIA 400
Cdd:cd07127 424 -VRTPLLLKLDASDEAAyAEERFGPIAFVVATDSTDHSIELA 464
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
42-400 |
2.74e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 56.06 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 42 ADVDKAVEAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGaplslservhyqMG------LNHFVAAR 115
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETG------------MGrvedkiAKNVAAAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 116 D--ALDNYEFEERRGDD-LVVKE--AIGVSGLITPWNFPT-----NQTSLklaaaFAAGSPVVLKPSeetPFAAVI---- 181
Cdd:PRK15398 104 KtpGVEDLTTEALTGDNgLTLIEyaPFGVIGAVTPSTNPTetiinNAISM-----LAAGNSVVFSPH---PGAKKVslra 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 182 ---LAEIFDKVGvpkGVFNLVngdgAGVGNP-------LSEHPKVRMMSFTGsgptGSKIMEKAAKDFKKVSLELGGKSP 251
Cdd:PRK15398 176 ielLNEAIVAAG---GPENLV----VTVAEPtietaqrLMKHPGIALLVVTG----GPAVVKAAMKSGKKAIGAGAGNPP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 252 YIVLDDVDIKEAAKAttgkVV------NNTgqVCTAGTRVLVPNKIKDAFLAELKeqfsqvrvgnpREDGTQvgpiISKK 325
Cdd:PRK15398 245 VVVDETADIEKAARD----IVkgasfdNNL--PCIAEKEVIVVDSVADELMRLME-----------KNGAVL----LTAE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 326 QFDQVQNYINKGIEEGAELFYggpGKPEG--LEKGYFARPT----IFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQI 399
Cdd:PRK15398 304 QAEKLQKVVLKNGGTVNKKWV---GKDAAkiLEAAGINVPKdtrlLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIAL 380
|
.
gi 88196026 400 A 400
Cdd:PRK15398 381 A 381
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
44-434 |
1.78e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 53.26 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 44 VDKAVEAADdvylEFRHTSvkerQALLDKIVKE-----YENRKDdIVQAITDELGaplslservhyqMGL-------NHF 111
Cdd:cd07122 5 VERARKAQR----EFATFS----QEQVDKIVEAvawaaADAAEE-LAKMAVEETG------------MGVvedkvikNHF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 112 vAARDALDNY----------EFEERRgddlVVK--EAIGVSGLITPwnfPTNQTS---LKLAAAFAAGSPVVLKPSE--- 173
Cdd:cd07122 64 -ASEYVYNDIkdmktvgvieEDEEKG----IVEiaEPVGVIAALIP---STNPTStaiFKALIALKTRNAIIFSPHPrak 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 174 ETPFAAV-ILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPtgskiMEKAAKDFKKVSLELG-GKSP 251
Cdd:cd07122 136 KCSIEAAkIMREAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGGPG-----MVKAAYSSGKPAIGVGpGNVP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 252 YIVLDDVDIKEAAKAT-TGKVVNNtGQVCTAGTRVLVPNKIKDAFLAELKEQfsqvrvgnpredGTQvgpIISKKQFDQV 330
Cdd:cd07122 211 AYIDETADIKRAVKDIiLSKTFDN-GTICASEQSVIVDDEIYDEVRAELKRR------------GAY---FLNEEEKEKL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 331 QNYInkgIEEGAELFYGGPGKPEGL--EKGYFARP--TIFINVDNQMTIAQE----EIFGPVMSVITYNDLDEAIQIAND 402
Cdd:cd07122 275 EKAL---FDDGGTLNPDIVGKSAQKiaELAGIEVPedTKVLVAEETGVGPEEplsrEKLSPVLAFYRAEDFEEALEKARE 351
|
410 420 430
....*....|....*....|....*....|....*.
gi 88196026 403 -TKYGLAGY--VI-GKDKETLHKVARSIEAGTVEIN 434
Cdd:cd07122 352 lLEYGGAGHtaVIhSNDEEVIEEFALRMPVSRILVN 387
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
49-303 |
2.91e-07 |
|
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: 52.61 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 49 EAADDVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPL-SLSERVHYQMGL-------NHF----VAARD 116
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIrSLIANWIAMMGCsesklykNIDtergITASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 117 ALDNYEFEERRGDDLVVKEAIGVSGLITPWNFPTNQTSlKLAAAFAAGSPVVLKPSEETPFAAVILAEIF---DKVGVPK 193
Cdd:cd07077 81 GHIQDVLLPDNGETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFqaaDAAHGPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196026 194 GVFNLVNGDGAGVGNPLSEHPKVRMMSFTGsGPTGSKIMEKAAKdfKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVN 273
Cdd:cd07077 160 ILVLYVPHPSDELAEELLSHPKIDLIVATG-GRDAVDAAVKHSP--HIPVIGFGAGNSPVVVDETADEERASGSVHDSKF 236
|
250 260 270
....*....|....*....|....*....|
gi 88196026 274 NTGQVCtAGTRVLVpnkIKDAFLAELKEQF 303
Cdd:cd07077 237 FDQNAC-ASEQNLY---VVDDVLDPLYEEF 262
|
|
| |
