|
Name |
Accession |
Description |
Interval |
E-value |
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
4-484 |
0e+00 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 962.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 4 IHNFINGEFVATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGPWGRMTVAERVDLLNAVADGINRRFDDFL 83
Cdd:TIGR03216 1 IRNFINGAFVESGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAALKGPWGKMTVAERADLLYAVADEIERRFDDFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPKSLASHIDIPRGAANFKVFADVIKSVPTEFFEMATPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKV 163
Cdd:TIGR03216 81 AAEVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTECFEMATPDGKGALNYAVRKPLGVVGVISPWNLPLLLMTWKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 164 GPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAA 243
Cdd:TIGR03216 161 GPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPDSAGEFLTRHPGVDAITFTGETRTGSAIMKAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 244 DGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDAST 323
Cdd:TIGR03216 241 DGVKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDPAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 324 GMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAED 403
Cdd:TIGR03216 321 NMGPLISAEHRDKVLSYYALAVEEGATVVTGGGVPDFGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFDSEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 404 EVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICIK 483
Cdd:TIGR03216 401 EVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNVCIK 480
|
.
gi 500090152 484 L 484
Cdd:TIGR03216 481 L 481
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
22-482 |
0e+00 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 745.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 22 CSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGPWgRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLASHID 101
Cdd:cd07093 2 FNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWS-RMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 102 IPRGAANFKVFADVIKSVPTEFFEMAtpdgRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEET 181
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQD----GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 182 PQTATLLGEVMNEVGMPKGVYNVVHGFGPGsAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIV 261
Cdd:cd07093 157 PLTAWLLAELANEAGLPPGVVNVVHGFGPE-AGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 262 FADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYY 341
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 342 NKARELGATVVTGGGVPQMPGeLANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVW 421
Cdd:cd07093 316 ELARAEGATILTGGGRPELPD-LEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500090152 422 TKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07093 395 TRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
2-484 |
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: 599.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 2 KQIHNFINGEFV--ATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRF 79
Cdd:COG1012 4 PEYPLFIGGEWVaaASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPA-WAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 80 DDFLAAECADTGKPKSLAsHIDIPRGAANFKVFADVIKSVPTEFFEMATPDGRgalNYALRRPVGVVGVICPWNLPLLLM 159
Cdd:COG1012 83 EELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDAPGTR---AYVRREPLGVVGAITPWNFPLALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 160 TWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIM 239
Cdd:COG1012 159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGS-EVGAALVAHPDVDKISFTGSTAVGRRIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 240 KAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPD 319
Cdd:COG1012 238 AAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 320 DASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPqmpgELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPF 399
Cdd:COG1012 318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRP----DGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 400 DAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFL-RDLRTPFGGAKQSGIGREGGVHSLEFYTEQK 478
Cdd:COG1012 394 DDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTETK 473
|
....*.
gi 500090152 479 NICIKL 484
Cdd:COG1012 474 TVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
14-480 |
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: 533.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 14 ATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKP 93
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA-WRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 94 KSLASHiDIPRGAANFKVFADVIKSVPTEFFEMAtpdgRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTV 173
Cdd:pfam00171 83 LAEARG-EVDRAIDVLRYYAGLARRLDGETLPSD----PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 174 VVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEM 253
Cdd:pfam00171 158 VLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGA-EVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 254 GGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEH 333
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 334 KNKVLSYYNKARELGATVVTGGgvpqmPGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTD 413
Cdd:pfam00171 317 LERVLKYVEDAKEEGAKLLTGG-----EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500090152 414 YGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRT-PFGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:pfam00171 392 YGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
56-482 |
3.56e-176 |
|
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: 501.35 E-value: 3.56e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSlASHIDIPRGAANFKVFADVIKSVPtefFEMATPDGRGAL 135
Cdd:cd07078 14 WAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLH---GEVIPSPDPGEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 136 NYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGE 215
Cdd:cd07078 90 AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGD-EVGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 216 FVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVE 295
Cdd:cd07078 169 ALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 296 RPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPqmpgELANGAWVQPTIW 375
Cdd:cd07078 249 ESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRL----EGGKGYFVPPTVL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 376 TGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSW-FLRDLRTPF 454
Cdd:cd07078 325 TDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYsVGAEPSAPF 404
|
410 420
....*....|....*....|....*...
gi 500090152 455 GGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07078 405 GGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
4-484 |
1.56e-170 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 489.32 E-value: 1.56e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 4 IHNFINGEFVATAKP--FDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDD 81
Cdd:TIGR02299 1 IGHFIDGEFVPSESGetFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKR-WAELKAAERKRYLHKIADLIEQHADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 82 FLAAECADTGKPKSLASHIdIPRGAANFKVFADVIK------SVPTEFFematpdgrgaLNYALRRPVGVVGVICPWNLP 155
Cdd:TIGR02299 80 IAVLECLDCGQPLRQTRQQ-VIRAAENFRFFADKCEeamdgrTYPVDTH----------LNYTVRVPVGPVGLITPWNAP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 156 LLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTG 235
Cdd:TIGR02299 149 FMLSTWKIAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGE-EAGKALVAHPDVKAVSFTGETATG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 236 AAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKL 315
Cdd:TIGR02299 228 SIIMRNGADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 316 GVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGV--PQMPGELANGAWVQPTIWTGLDDNSPIAREEIFGPC 393
Cdd:TIGR02299 308 GHPLDPETEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERapTFRGEDLGRGNYVLPTVFTGADNHMRIAQEEIFGPV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 394 TLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEF 473
Cdd:TIGR02299 388 LTVIPFKDEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDF 467
|
490
....*....|.
gi 500090152 474 YTEQKNICIKL 484
Cdd:TIGR02299 468 YTETKNVALAL 478
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
7-480 |
3.02e-170 |
|
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: 487.87 E-value: 3.02e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFV--ATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALK-GPWGRMTVAERVDLLNAVADGINRRFDDFL 83
Cdd:cd07091 7 FINNEFVdsVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFEtGWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPKSLASHIDIPRGAANFKVFA---DVI--KSVPTeffematpdGRGALNYALRRPVGVVGVICPWNLPLLL 158
Cdd:cd07091 87 ALESLDNGKPLEESAKGDVALSIKCLRYYAgwaDKIqgKTIPI---------DGNFLAYTRREPIGVCGQIIPWNFPLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 159 MTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAI 238
Cdd:cd07091 158 LAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGP-TAGAAISSHMDVDKIAFTGSTAVGRTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 239 MKAAAD-GARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGV 317
Cdd:cd07091 237 MEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 318 PDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQmpgelANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQ 397
Cdd:cd07091 317 PFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHG-----SKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTIL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 398 PFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQ 477
Cdd:cd07091 392 KFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQV 471
|
...
gi 500090152 478 KNI 480
Cdd:cd07091 472 KAV 474
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
7-484 |
6.52e-165 |
|
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: 474.49 E-value: 6.52e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFV--ATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAAL-KGPWGRMTVAERVDLLNAVADGINRRFDDFL 83
Cdd:cd07119 1 YIDGEWVeaASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPksLA-SHIDIPRGAANFKVFADVIKSvPTEFFEMATPDgrgALNYALRRPVGVVGVICPWNLPLLLMTWK 162
Cdd:cd07119 81 RLETLNTGKT--LReSEIDIDDVANCFRYYAGLATK-ETGEVYDVPPH---VISRTVREPVGVCGLITPWNYPLLQAAWK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 163 VGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIMKAA 242
Cdd:cd07119 155 LAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGA-TVGAELAESPDVDLVSFTGGTATGRSIMRAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 243 ADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDAS 322
Cdd:cd07119 234 AGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDAD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 323 TGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQmPGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAE 402
Cdd:cd07119 314 TEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPT-GDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 403 DEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
..
gi 500090152 483 KL 484
Cdd:cd07119 473 NL 474
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
24-482 |
2.14e-164 |
|
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: 472.42 E-value: 2.14e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 24 PLDNRRIALVHEAGKTEVDAAVAAAQAALK-GPWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKP----KSLAS 98
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAAARAAFEgGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLiretRAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 99 HIdiprgAANFKVFADVIKSVPTEFFEMATPDgrgALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPS 178
Cdd:cd07114 84 YL-----AEWYRYYAGLADKIEGAVIPVDKGD---YLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 179 EETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNP 258
Cdd:cd07114 156 EHTPASTLELAKLAEEAGFPPGVVNVVTGFGP-ETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 259 AIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVL 338
Cdd:cd07114 235 NIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 339 SYYNKARELGATVVTGGGVPQmPGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLAC 418
Cdd:cd07114 315 RYVARAREEGARVLTGGERPS-GADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500090152 419 SVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07114 394 GIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
17-482 |
1.59e-162 |
|
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: 467.85 E-value: 1.59e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 17 KPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALK-GPWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKS 95
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 96 LASHIDIPRGAANFKVFADVIKSVpteFFEMAtPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVV 175
Cdd:cd07112 82 DALAVDVPSAANTFRWYAEAIDKV---YGEVA-PTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 176 KPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADG-ARPVSLEMG 254
Cdd:cd07112 158 KPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGH-TAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 255 GKNPAIVFADC-DFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEH 333
Cdd:cd07112 237 GKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 334 KNKVLSYYNKARELGATVVTGGGVPQmpgELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTD 413
Cdd:cd07112 317 FDKVLGYIESGKAEGARLVAGGKRVL---TETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500090152 414 YGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07112 394 YGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
6-480 |
4.08e-161 |
|
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: 464.28 E-value: 4.08e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 6 NFINGEFVATAKP--FDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFL 83
Cdd:cd07138 1 FYIDGAWVAPAGTetIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA-WSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPKSLASHIDIPRGAANFKVFADVIKSvptefFEMATPDGRGALnyaLRRPVGVVGVICPWNLPLLLMTWKV 163
Cdd:cd07138 80 QAITLEMGAPITLARAAQVGLGIGHLRAAADALKD-----FEFEERRGNSLV---VREPIGVCGLITPWNWPLNQIVLKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 164 GPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPGsAGEFVTTHPKVNAITFTGETRTGAAIMKAAA 243
Cdd:cd07138 152 APALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPV-VGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 244 DGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDAST 323
Cdd:cd07138 231 DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 324 GMGPLISQEHKNKVLSYYNKARELGATVVTGGgvPQMPGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAED 403
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGG--PGRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDED 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500090152 404 EVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLrDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:cd07138 389 EAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAF-NPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
24-482 |
3.89e-160 |
|
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: 461.39 E-value: 3.89e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 24 PLDNRRIALVHEAGKTEVDAAVAAAQAALKgPWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAShIDIP 103
Cdd:cd07090 4 PATGEVLATVHCAGAEDVDLAVKSAKAAQK-EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VDID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 104 RGAANFKVFADVIKSVPTEFFEMatpdGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQ 183
Cdd:cd07090 82 SSADCLEYYAGLAPTLSGEHVPL----PGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 184 TATLLGEVMNEVGMPKGVYNVVHGfgPGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFA 263
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQG--GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 264 DCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNK 343
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 344 ARELGATVVTGGGVPQMPGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTK 423
Cdd:cd07090 316 AKQEGAKVLCGGERVVPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 500090152 424 DLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
6-484 |
2.86e-155 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 450.10 E-value: 2.86e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 6 NFINGEFVA--TAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKgPWGRMTVAERVDLLNAVADGINRRFDDFL 83
Cdd:PRK13252 9 LYIDGAYVEatSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK-IWAAMTAMERSRILRRAVDILRERNDELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPKSLASHIDIPRGAANFKVFADVIKSVPTEFfemaTPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKV 163
Cdd:PRK13252 88 ALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQ----IPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 164 GPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGfgPGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAA 243
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQG--DGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 244 DGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDAST 323
Cdd:PRK13252 242 ASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPAT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 324 GMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQmPGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAED 403
Cdd:PRK13252 322 NFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLT-EGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDED 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 404 EVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICIK 483
Cdd:PRK13252 401 EVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVE 480
|
.
gi 500090152 484 L 484
Cdd:PRK13252 481 M 481
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
22-484 |
3.27e-154 |
|
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: 446.50 E-value: 3.27e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 22 CSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGPWGrMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLASHID 101
Cdd:cd07115 2 LNPATGELIARVAQASAEDVDAAVAAARAAFEAWSA-MDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 102 IPRGAANFKVFADVIKSVPTEffemATPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEET 181
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGE----VIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 182 PQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIV 261
Cdd:cd07115 157 PLSALRIAELMAEAGFPAGVLNVVTGFGE-VAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 262 FADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYY 341
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 342 NKARELGATVVTGGgvpQMPGelANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVW 421
Cdd:cd07115 316 DVGREEGARLLTGG---KRPG--ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVW 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500090152 422 TKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICIKL 484
Cdd:cd07115 391 TRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
7-478 |
5.25e-154 |
|
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: 446.18 E-value: 5.25e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFV--ATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAAlKGPWGRMTVAERVDLLNAVADGINRRFDDFLA 84
Cdd:TIGR01804 1 FIDGEYVedSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRA-QGEWAAMSPMERGRILRRAADLIRERNEELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 85 AECADTGKPKSLASHIDIPRGAANFKVFADVIKSVPTEFFEMATPDgrgaLNYALRRPVGVVGVICPWNLPLLLMTWKVG 164
Cdd:TIGR01804 80 LETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPS----FAYTIREPLGVCVGIGAWNYPLQIASWKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 165 PALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGpGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAAD 244
Cdd:TIGR01804 156 PALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDG-AEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 245 GARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTG 324
Cdd:TIGR01804 235 HLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 325 MGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPGeLANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDE 404
Cdd:TIGR01804 315 MGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVG-LQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500090152 405 VIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQK 478
Cdd:TIGR01804 394 VIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
7-480 |
4.03e-150 |
|
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: 436.62 E-value: 4.03e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVA--TAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAAL-KGPWGRMTVAERVDLLNAVADGINRRFDDFL 83
Cdd:cd07139 2 FIGGRWVApsGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPKSLASHIDIPRGAANFKVFADVIKSVPtefFEMATPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKV 163
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFP---FEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 164 GPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVhgfgPG--SAGEFVTTHPKVNAITFTGETRTGAAIMKA 241
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVV----PAdrEVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 242 AADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDA 321
Cdd:cd07139 235 CGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 322 STGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQmpgELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDA 401
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPA---GLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDD 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500090152 402 EDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNsWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:cd07139 392 EDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
7-484 |
3.75e-148 |
|
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: 431.83 E-value: 3.75e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVATA--KPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGPWGRMTVAERVDLLNAVADGINRRFDDFLA 84
Cdd:cd07144 11 FINNEFVKSSdgETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 85 AECADTGKPKSLASHIDIPRGAANFKVF---ADVI--KSVPTEFFEMAtpdgrgalnYALRRPVGVVGVICPWNLPLLLM 159
Cdd:cd07144 91 IEALDSGKPYHSNALGDLDEIIAVIRYYagwADKIqgKTIPTSPNKLA---------YTLHEPYGVCGQIIPWNYPLAMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 160 TWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIM 239
Cdd:cd07144 162 AWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGA-VAGSALAEHPDVDKIAFTGSTATGRLVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 240 KAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGA-EGLKLGVP 318
Cdd:cd07144 241 KAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 319 DDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVpqMPGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQP 398
Cdd:cd07144 321 FDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK--APEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 399 FDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQK 478
Cdd:cd07144 399 FKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
....*.
gi 500090152 479 NICIKL 484
Cdd:cd07144 479 AVHINL 484
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
3-484 |
8.17e-148 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 430.87 E-value: 8.17e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 3 QIHNFINGEFVA-TAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDD 81
Cdd:PRK13473 2 QTKLLINGELVAgEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE-WSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 82 FLAAECADTGKPKSLASHIDIPRGAANFKVFADVIKSVPteffematpdGRGALNYA------LRR-PVGVVGVICPWNL 154
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLE----------GKAAGEYLeghtsmIRRdPVGVVASIAPWNY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 155 PLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVgMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRT 234
Cdd:PRK13473 151 PLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGA-TVGDALVGHPKVRMVSLTGSIAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 235 GAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLK 314
Cdd:PRK13473 229 GKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 315 LGVPDDASTGMGPLISQEHKNKVLSYYNKARELG-ATVVTGGGVPQmpgelANGAWVQPTIWTGLDDNSPIAREEIFGPC 393
Cdd:PRK13473 309 VGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPD-----GKGYYYEPTLLAGARQDDEIVQREVFGPV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 394 TLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEF 473
Cdd:PRK13473 384 VSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLED 463
|
490
....*....|.
gi 500090152 474 YTEQKNICIKL 484
Cdd:PRK13473 464 YTVVRHVMVKH 474
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
24-482 |
1.47e-147 |
|
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: 429.16 E-value: 1.47e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 24 PLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPksLA-SHIDI 102
Cdd:cd07103 4 PATGEVIGEVPDAGAADADAAIDAAAAAFKT-WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKP--LAeARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 103 PRGAANFKVFADVIKSVPTEFFEMATPDGRgalNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETP 182
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKR---ILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 183 QTATLLGEVMNEVGMPKGVYNVVHGfGPGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVF 262
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTG-SPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 263 ADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYN 342
Cdd:cd07103 237 DDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 343 KARELGATVVTGGGVPQMPGelangAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWT 422
Cdd:cd07103 317 DAVAKGAKVLTGGKRLGLGG-----YFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 423 KDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07103 392 RDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
6-484 |
6.32e-147 |
|
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: 428.69 E-value: 6.32e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 6 NFINGEFVATAKP--FDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFL 83
Cdd:cd07559 3 NFINGEWVAPSKGeyFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT-WGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPKSLASHIDIPRGAANFKVFADVIKSvptEFFEMATPDGRgALNYALRRPVGVVGVICPWNLPLLLMTWKV 163
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRA---QEGSLSEIDED-TLSYHFHEPLGVVGQIIPWNFPLLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 164 GPALACGNTVVVKPSEETPQTATLLGEVMNEVgMPKGVYNVVHGFGpGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAA 243
Cdd:cd07559 158 APALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFG-SEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 244 DGARPVSLEMGGKNPAIVFADCD------FDAAIEGTMRSVFaNCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGV 317
Cdd:cd07559 236 ENLIPVTLELGGKSPNIFFDDAMdadddfDDKAEEGQLGFAF-NQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 318 PDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPGeLANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQ 397
Cdd:cd07559 315 PLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGG-LDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 398 PFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQ 477
Cdd:cd07559 394 TFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQT 473
|
....*..
gi 500090152 478 KNICIKL 484
Cdd:cd07559 474 KNILVSY 480
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
23-480 |
3.87e-145 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 422.89 E-value: 3.87e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 23 SPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLASHIDI 102
Cdd:cd07092 3 DPATGEEIATVPDASAADVDAAVAAAHAAFPS-WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 103 PRGAANFKVFADVIKSVPTEffeMATPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETP 182
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGP---AAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 183 QTATLLGEVMNEVgMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVF 262
Cdd:cd07092 159 LTTLLLAELAAEV-LPPGVVNVVCGGGA-SAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 263 ADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYN 342
Cdd:cd07092 237 DDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 343 KARElGATVVTGGGVPQmpgelANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWT 422
Cdd:cd07092 317 RAPA-HARVLTGGRRAE-----GPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWT 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 500090152 423 KDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:cd07092 391 RDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
54-480 |
4.05e-144 |
|
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: 420.88 E-value: 4.05e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 54 GPWgRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLASHIDIPRGAANFKVFADVIKSVPTEF-FEMATPDGR 132
Cdd:cd07089 35 GDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADSFPWEFdLPVPALRGG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 133 GALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPGs 212
Cdd:cd07089 114 PGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNA- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 213 AGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERV 292
Cdd:cd07089 193 VGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 293 YVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQmpgELANGAWVQP 372
Cdd:cd07089 273 LVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGRPA---GLDKGFYVEP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 373 TIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRT 452
Cdd:cd07089 350 TLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDA 429
|
410 420
....*....|....*....|....*...
gi 500090152 453 PFGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:cd07089 430 PFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
24-482 |
5.52e-143 |
|
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: 417.79 E-value: 5.52e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 24 PLDNRRIALVHEAGKTEVDAAVAAAQAALKGPWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAsHIDIP 103
Cdd:cd07109 4 PSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA-RADVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 104 RGAANFKVFADVIKSVPTEFFematPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQ 183
Cdd:cd07109 83 AAARYFEYYGGAADKLHGETI----PLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 184 TATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFA 263
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGA-EAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 264 DCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGvPDDASTGMGPLISQEHKNKVLSYYNK 343
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 344 ARELGATVVTGGGVPQmpGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTK 423
Cdd:cd07109 317 ARARGARIVAGGRIAE--GAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 424 DLARAHRVAGQIEAGLVWVNSWFLR-DLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07109 395 DGDRALRVARRLRAGQVFVNNYGAGgGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
30-480 |
3.51e-142 |
|
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: 415.39 E-value: 3.51e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 30 IALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDF---LAAECadtGKPKSLAsHIDIPRGA 106
Cdd:cd07106 10 FASAPVASEAQLDQAVAAAKAAFPG-WSATPLEERRAALLAIADAIEANAEELarlLTLEQ---GKPLAEA-QFEVGGAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 107 ANFKVFADVikSVPTEFFEmATPDGRGALnyaLRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTAT 186
Cdd:cd07106 85 AWLRYTASL--DLPDEVIE-DDDTRRVEL---RRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 187 LLGEVMNEVgMPKGVYNVVHGfgPGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCD 266
Cdd:cd07106 159 KLGELAQEV-LPPGVLNVVSG--GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 267 FDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARE 346
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 347 LGATVVTGGGVPQMPGelangAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLA 426
Cdd:cd07106 316 KGAKVLAGGEPLDGPG-----YFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLE 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 500090152 427 RAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:cd07106 391 RAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
7-483 |
8.05e-141 |
|
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: 413.28 E-value: 8.05e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFV--ATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALK--GPWGRMTVAERVDLLNAVADGINRRFDDF 82
Cdd:cd07141 10 FINNEWHdsVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgSPWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 83 LAAECADTGKPKSLASHIDIPRGAANFKVFA---DVI--KSVPTeffematpDGRgALNYALRRPVGVVGVICPWNLPLL 157
Cdd:cd07141 90 ASLETLDNGKPFSKSYLVDLPGAIKVLRYYAgwaDKIhgKTIPM--------DGD-FFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 158 LMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAA 237
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGP-TAGAAISSHPDIDKVAFTGSTEVGKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 238 IMKAAADGA-RPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLG 316
Cdd:cd07141 240 IQQAAGKSNlKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 317 VPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGvpqMPGElaNGAWVQPTIWTGLDDNSPIAREEIFGPCTLI 396
Cdd:cd07141 320 NPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGK---RHGD--KGYFIQPTVFSDVTDDMRIAKEEIFGPVQQI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 397 QPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTE 476
Cdd:cd07141 395 FKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTE 474
|
....*..
gi 500090152 477 QKNICIK 483
Cdd:cd07141 475 VKTVTIK 481
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
24-480 |
9.40e-140 |
|
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: 409.43 E-value: 9.40e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 24 PLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAShIDIP 103
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPR-WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA-WDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 104 RGAANFKVFADVIKSVPT---EFFEMATPDGRGalnYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEE 180
Cdd:cd07110 82 DVAGCFEYYADLAEQLDAkaeRAVPLPSEDFKA---RVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 181 TPQTATLLGEVMNEVGMPKGVYNVVHGFGPGsAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAI 260
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDE-AGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 261 VFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSY 340
Cdd:cd07110 238 VFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 341 YNKARELGATVVTGGGVPQMPGElanGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSV 420
Cdd:cd07110 318 IARGKEEGARLLCGGRRPAHLEK---GYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 421 WTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:cd07110 395 ISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
7-484 |
1.47e-137 |
|
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: 404.99 E-value: 1.47e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVATAK--PFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGPWGR-MTVAERVDLLNAVADGINRRFDDFL 83
Cdd:cd07143 10 FINGEFVDSVHggTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLkVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPKSLASHIDIPRGAANF--------KVFADVIKSVPTEffematpdgrgaLNYALRRPVGVVGVICPWNLP 155
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFryyggwadKIHGQVIETDIKK------------LTYTRHEPIGVCGQIIPWNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 156 LLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTG 235
Cdd:cd07143 158 LLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGR-TCGNAISSHMDIDKVAFTGSTLVG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 236 AAIMKAAA-DGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLK 314
Cdd:cd07143 237 RKVMEAAAkSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 315 LGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGgvpQMPGELanGAWVQPTIWTGLDDNSPIAREEIFGPCT 394
Cdd:cd07143 317 VGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGG---KRHGNE--GYFIEPTIFTDVTEDMKIVKEEIFGPVV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 395 LIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFY 474
Cdd:cd07143 392 AVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENY 471
|
490
....*....|
gi 500090152 475 TEQKNICIKL 484
Cdd:cd07143 472 TQIKAVHINL 481
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
23-482 |
6.22e-137 |
|
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: 402.10 E-value: 6.22e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 23 SPLDNRRIALVHEAGKTEVDAAVAAAQAAL-KGPWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAsHID 101
Cdd:cd07118 3 SPAHGVVVARYAEGTVEDVDAAVAAARKAFdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 102 IPRGAANFKVFADVIKSVPTEFFEMAtpdGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEET 181
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNL---GDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 182 PQTATLLGEVMNEVGMPKGVYNVVHGFGpGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIV 261
Cdd:cd07118 159 SGTTLMLAELLIEAGLPAGVVNIVTGYG-ATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 262 FADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYY 341
Cdd:cd07118 238 FADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 342 NKARELGATVVTGGGVpqmpGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVW 421
Cdd:cd07118 318 DAGRAEGATLLLGGER----LASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVW 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500090152 422 TKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07118 394 SKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
7-480 |
1.25e-136 |
|
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: 402.26 E-value: 1.25e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFV--ATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAAL-KGPWGRMTVAERVDLLNAVADGINRRFDDFL 83
Cdd:cd07142 7 FINGQFVdaASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFdEGPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPKSLASHIDIPRGAANFKVFA---DVI--KSVPTEFFEMAtpdgrgalnYALRRPVGVVGVICPWNLPLLL 158
Cdd:cd07142 87 ALETWDNGKPYEQARYAEVPLAARLFRYYAgwaDKIhgMTLPADGPHHV---------YTLHEPIGVVGQIIPWNFPLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 159 MTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAI 238
Cdd:cd07142 158 FAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGP-TAGAAIASHMDVDKVAFTGSTEVGKII 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 239 MKAAADGA-RPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGV 317
Cdd:cd07142 237 MQLAAKSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 318 PDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGvpqmpgELAN-GAWVQPTIWTGLDDNSPIAREEIFGPCTLI 396
Cdd:cd07142 317 PFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGD------RIGSkGYYIQPTIFSDVKDDMKIARDEIFGPVQSI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 397 QPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTE 476
Cdd:cd07142 391 LKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
|
....
gi 500090152 477 QKNI 480
Cdd:cd07142 471 VKAV 474
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
56-482 |
1.22e-134 |
|
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: 393.13 E-value: 1.22e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAShIDIPRGAANFKVFADVIKSVPTEffeMATPDGRGAL 135
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGP---ELPSPDPGGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 136 NYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGE 215
Cdd:cd06534 86 AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD-EVGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 216 FVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVE 295
Cdd:cd06534 165 ALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 296 RPIFDRFVAALKagaeglklgvpddastgmgplisqehknkvlsyynkarelgatvvtgggvpqmpgelangawvqpTIW 375
Cdd:cd06534 245 ESIYDEFVEKLV-----------------------------------------------------------------TVL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 376 TGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSW-FLRDLRTPF 454
Cdd:cd06534 260 VDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSsIGVGPEAPF 339
|
410 420
....*....|....*....|....*...
gi 500090152 455 GGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd06534 340 GGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
23-482 |
2.76e-132 |
|
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: 390.57 E-value: 2.76e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 23 SPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLASHIDI 102
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPE-WAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 103 PRGAANFKVFADVIKSVPTEffemATPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETP 182
Cdd:cd07108 82 AVLADLFRYFGGLAGELKGE----TLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 183 QTATLLGEVMNEVgMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVF 262
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGE-ECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 263 ADCDFDAAIEGTMRSV-FANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYY 341
Cdd:cd07108 236 PDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 342 NKAREL-GATVVTGGGVPQmPGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSV 420
Cdd:cd07108 316 DLGLSTsGATVLRGGPLPG-EGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500090152 421 WTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHS-LEFYTEQKNICI 482
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTVNI 457
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
7-484 |
5.79e-131 |
|
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: 387.97 E-value: 5.79e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVATA--KPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKgPWGRMTVAERVDLLNAVADGINRRFDDFLA 84
Cdd:cd07117 4 FINGEWVKGSsgETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK-TWRKTTVAERANILNKIADIIDENKELLAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 85 AECADTGKPKSLASHIDIPRGAANFKVFADVIKSVPTEffemATPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVG 164
Cdd:cd07117 83 VETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGS----ANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 165 PALACGNTVVVKPSEETPQTATLLGEVMNEVgMPKGVYNVVHGFGPGSaGEFVTTHPKVNAITFTGETRTGAAIMKAAAD 244
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKS-GEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 245 GARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTG 324
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 325 MGPLISQEHKNKVLSYYNKARELGATVVTGGGvPQMPGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDE 404
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGH-RLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 405 VIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICIKL 484
Cdd:cd07117 396 VIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
7-480 |
1.48e-130 |
|
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: 386.62 E-value: 1.48e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFV--ATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLA 84
Cdd:cd07088 1 YINGEFVpsSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA-WERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 85 AECADTGKPKSLAS-----HIDIPRGAANF--KVFADVIKSvpteffemaTPDGRGALNYalRRPVGVVGVICPWNLPLL 157
Cdd:cd07088 80 LIVEEQGKTLSLARvevefTADYIDYMAEWarRIEGEIIPS---------DRPNENIFIF--KVPIGVVAGILPWNFPFF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 158 LMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPGsAGEFVTTHPKVNAITFTGETRTGAA 237
Cdd:cd07088 149 LIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSV-VGDALVAHPKVGMISLTGSTEAGQK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 238 IMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGV 317
Cdd:cd07088 228 IMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 318 PDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPqmpgELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQ 397
Cdd:cd07088 308 PFDAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRP----EGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 398 PFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNswflrdlRTPF-------GGAKQSGIGREGGVHS 470
Cdd:cd07088 384 KFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYIN-------RENFeamqgfhAGWKKSGLGGADGKHG 456
|
490
....*....|
gi 500090152 471 LEFYTEQKNI 480
Cdd:cd07088 457 LEEYLQTKVV 466
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
23-484 |
9.68e-130 |
|
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: 384.03 E-value: 9.68e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 23 SPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSlASHIDI 102
Cdd:cd07107 3 NPATGQVLARVPAASAADVDRAVAAARAAFPE-WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 103 PRGAANFKVFADVIksvpTEFFEMATPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETP 182
Cdd:cd07107 81 MVAAALLDYFAGLV----TELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 183 QTATLLGEVMNEVgMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVF 262
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGA-TAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 263 ADCDFDAAIEGTMRSV-FANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYY 341
Cdd:cd07107 235 PDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 342 NKARELGATVVTGGGVPQMPgELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVW 421
Cdd:cd07107 315 DSAKREGARLVTGGGRPEGP-ALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIW 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500090152 422 TKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICIKL 484
Cdd:cd07107 394 TNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
19-482 |
1.00e-129 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 383.60 E-value: 1.00e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 19 FDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKgPWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAS 98
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP-AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 99 H-----IDIPRGAAN--FKVFADVIKSvpteffematpDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGN 171
Cdd:cd07150 80 FettftPELLRAAAGecRRVRGETLPS-----------DSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 172 TVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGfGPGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSL 251
Cdd:cd07150 149 TVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTG-GGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 252 EMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQ 331
Cdd:cd07150 228 ELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 332 EHKNKVLSYYNKARELGATVVTGGGVpqmpgelaNGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRAND 411
Cdd:cd07150 308 RQVERIKRQVEDAVAKGAKLLTGGKY--------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELAND 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500090152 412 TDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRT-PFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07150 380 TEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTILDEAHvPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
56-482 |
5.30e-129 |
|
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: 381.11 E-value: 5.30e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDF---LAAECADTgKPKS---LASHIDIPRGAANFkvfadviksvPTEFF-EMAT 128
Cdd:cd07104 16 WAATPPQERAAILRKAAEILEERRDEIadwLIRESGST-RPKAafeVGAAIAILREAAGL----------PRRPEgEILP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 129 PDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETP-QTATLLGEVMNEVGMPKGVYNVVHG 207
Cdd:cd07104 85 SDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvTGGLLIAEIFEEAGLPKGVLNVVPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 208 fGPGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCL 287
Cdd:cd07104 165 -GGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 288 GTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGvpqmpgelANG 367
Cdd:cd07104 244 AAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT--------YEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 368 AWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFL 447
Cdd:cd07104 316 LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTV 395
|
410 420 430
....*....|....*....|....*....|....*.
gi 500090152 448 RDLRT-PFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07104 396 NDEPHvPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
7-480 |
6.36e-129 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 383.40 E-value: 6.36e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFV--ATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALK-GPWGRMTVAERVDLLNAVADGINRRFDDFL 83
Cdd:PLN02766 24 FINGEFVdaASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhGPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPKSLASHIDIPRGAANFKVFADVIKSVPTEFFEMAtpdgRGALNYALRRPVGVVGVICPWNLPLLLMTWKV 163
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMS----RQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 164 GPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIMKAAA 243
Cdd:PLN02766 180 APALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGP-TAGAAIASHMDVDKVSFTGSTEVGRKIMQAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 244 -DGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDAS 322
Cdd:PLN02766 259 tSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 323 TGMGPLISQEHKNKVLSYYNKARELGATVVTGGgvpQMPGElaNGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAE 402
Cdd:PLN02766 339 ARQGPQVDKQQFEKILSYIEHGKREGATLLTGG---KPCGD--KGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500090152 403 DEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
7-483 |
8.28e-129 |
|
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: 382.56 E-value: 8.28e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVATA--KPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGPWGRMTVAERVDLLNAVADGINRRFDDFLA 84
Cdd:cd07113 3 FIDGRPVAGQseKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 85 AECADTGKPKSLASHIDIPRGAANFKVFADVIKSVPTEFFEMATPDGRGA--LNYALRRPVGVVGVICPWNLPLLLMTWK 162
Cdd:cd07113 83 LETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIPSMQGEryTAFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 163 VGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGfgPGSAGEFVTTHPKVNAITFTGETRTGAAIMKAA 242
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNG--KGAVGAQLISHPDVAKVSFTGSVATGKKIGRQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 243 ADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDAS 322
Cdd:cd07113 241 ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 323 TGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPqmPGElanGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAE 402
Cdd:cd07113 321 VMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEAL--AGE---GYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 403 DEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07113 396 EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
.
gi 500090152 483 K 483
Cdd:cd07113 476 R 476
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
7-484 |
2.12e-124 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 371.92 E-value: 2.12e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVATA--KPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAAL-KGPWGRMTVAERVDLLNAVADGINRRFDDFL 83
Cdd:PRK09847 23 FINGEYTAAAenETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFeRGDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPKSLASHIDIPRGAANFKVFADVIKSVpteFFEMAtPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKV 163
Cdd:PRK09847 103 LLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKV---YGEVA-TTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 164 GPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGpGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAA 243
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFG-HEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 244 DG-ARPVSLEMGGKNPAIVFADC-DFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDA 321
Cdd:PRK09847 258 DSnMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 322 STGMGPLISQEHKNKVLSYYNKARELGATVVTGGgvpqmpgELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDA 401
Cdd:PRK09847 338 ATTMGTLIDCAHADSVHSFIREGESKGQLLLDGR-------NAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 402 EDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNIC 481
Cdd:PRK09847 411 EEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIW 490
|
...
gi 500090152 482 IKL 484
Cdd:PRK09847 491 ISL 493
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
7-480 |
2.65e-124 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 371.76 E-value: 2.65e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVA--TAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGP----WGRMTVAERVDLLNAVADGINRRFD 80
Cdd:PLN02467 11 FIGGEWREpvLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRNkgkdWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 81 DFLAAECADTGKPKSLASHiDIPRGAANFKVFADVIK----------SVPTEFFEmatpdgrgalNYALRRPVGVVGVIC 150
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAW-DMDDVAGCFEYYADLAEaldakqkapvSLPMETFK----------GYVLKEPLGVVGLIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 151 PWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTG 230
Cdd:PLN02467 160 PWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGT-EAGAPLASHPGVDKIAFTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 231 ETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGA 310
Cdd:PLN02467 239 STATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 311 EGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQmpgELANGAWVQPTIWTGLDDNSPIAREEIF 390
Cdd:PLN02467 319 KNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPE---HLKKGFFIEPTIITDVTTSMQIWREEVF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 391 GPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHS 470
Cdd:PLN02467 396 GPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWG 475
|
490
....*....|
gi 500090152 471 LEFYTEQKNI 480
Cdd:PLN02467 476 LENYLSVKQV 485
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-478 |
4.77e-124 |
|
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: 370.04 E-value: 4.77e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 6 NFINGEFVATAKPFDKCSPLDNRRI-ALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLA 84
Cdd:cd07097 3 NYIDGEWVAGGDGEENRNPSDTSDVvGKYARASAEDADAAIAAAAAAFPA-WRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 85 AECADTGKPksLASHID-IPRGAANFKVFADVIKSVPTEFFEMATPdgrGALNYALRRPVGVVGVICPWNLPLLLMTWKV 163
Cdd:cd07097 82 LLTREEGKT--LPEARGeVTRAGQIFRYYAGEALRLSGETLPSTRP---GVEVETTREPLGVVGLITPWNFPIAIPAWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 164 GPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVhgFGPGSA-GEFVTTHPKVNAITFTGETRTGAAIMKAA 242
Cdd:cd07097 157 APALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLV--MGSGSEvGQALVEHPDVDAVSFTGSTAVGRRIAAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 243 ADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDAS 322
Cdd:cd07097 235 AARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 323 TGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPGElanGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAE 402
Cdd:cd07097 315 VDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDE---GYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 403 DEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNswfLR----DLRTPFGGAKQSGIG-REGGVHSLEFYTEQ 477
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVN---LPtagvDYHVPFGGRKGSSYGpREQGEAALEFYTTI 468
|
.
gi 500090152 478 K 478
Cdd:cd07097 469 K 469
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
6-482 |
5.27e-122 |
|
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: 365.24 E-value: 5.27e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 6 NFINGEFVATAKP--FDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFL 83
Cdd:cd07116 3 NFIGGEWVAPVKGeyFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA-WGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPKSLASHIDIPRGAANFKVFADVIKSvptEFFEMATPDGRgALNYALRRPVGVVGVICPWNLPLLLMTWKV 163
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRA---QEGSISEIDEN-TVAYHFHEPLGVVGQIIPWNFPLLMATWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 164 GPALACGNTVVVKPSEETPQTATLLGEVMNEVgMPKGVYNVVHGFGpGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAA 243
Cdd:cd07116 158 APALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFG-LEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 244 DGARPVSLEMGGKNPAIVFADCD------FDAAIEGTMrsVFA-NCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLG 316
Cdd:cd07116 236 ENIIPVTLELGGKSPNIFFADVMdaddafFDKALEGFV--MFAlNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 317 VPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPGELANGAWVQPTIWTGldDNSPIAREEIFGPCTLI 396
Cdd:cd07116 314 NPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKGG--NKMRIFQEEIFGPVLAV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 397 QPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTE 476
Cdd:cd07116 392 TTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQ 471
|
....*.
gi 500090152 477 QKNICI 482
Cdd:cd07116 472 TKNLLV 477
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
6-478 |
1.09e-121 |
|
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: 364.36 E-value: 1.09e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 6 NFINGEFV--ATAKPFDKCSPLDNRR-IALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDF 82
Cdd:cd07131 1 NYIGGEWVdsASGETFDSRNPADLEEvVGTFPLSTASDVDAAVEAAREAFPE-WRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 83 ---LAAECadtGKPKS-----LASHIDIPRGAAN--FKVFADVIKSvpteffEMATPDgrgalNYALRRPVGVVGVICPW 152
Cdd:cd07131 80 arlVTREM---GKPLAegrgdVQEAIDMAQYAAGegRRLFGETVPS------ELPNKD-----AMTRRQPIGVVALITPW 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 153 NLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGpGSAGEFVTTHPKVNAITFTGET 232
Cdd:cd07131 146 NFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRG-EEVGEALVEHPDVDVVSFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 233 RTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEG 312
Cdd:cd07131 225 EVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 313 LKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQmPGELANGAWVQPTIWTGLDDNSPIAREEIFGP 392
Cdd:cd07131 305 LRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLT-GGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 393 CTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVN-SWFLRDLRTPFGGAKQSGIG-REGGVHS 470
Cdd:cd07131 384 VVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNaPTIGAEVHLPFGGVKKSGNGhREAGTTA 463
|
....*...
gi 500090152 471 LEFYTEQK 478
Cdd:cd07131 464 LDAFTEWK 471
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
7-478 |
1.50e-121 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 366.05 E-value: 1.50e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFV--ATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAAL-KGPWGRMTVAERVDLLNAVADGINRRFDDFL 83
Cdd:PLN02466 61 LINGQFVdaASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFdEGPWPKMTAYERSRILLRFADLLEKHNDELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPKSLASHIDIPRGAANFKVF---ADVIK--SVPTeffematpDGRGALNyALRRPVGVVGVICPWNLPLLL 158
Cdd:PLN02466 141 ALETWDNGKPYEQSAKAELPMFARLFRYYagwADKIHglTVPA--------DGPHHVQ-TLHEPIGVAGQIIPWNFPLLM 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 159 MTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAI 238
Cdd:PLN02466 212 FAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGP-TAGAALASHMDVDKLAFTGSTDTGKIV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 239 MKAAA-DGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAalKAGAEGLKLGV 317
Cdd:PLN02466 291 LELAAkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVE--KAKARALKRVV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 318 PDDASTGM--GPLISQEHKNKVLSYYNKARELGATVVTGGGVPQmpgelANGAWVQPTIWTGLDDNSPIAREEIFGPCTL 395
Cdd:PLN02466 369 GDPFKKGVeqGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG-----SKGYYIQPTVFSNVQDDMLIAQDEIFGPVQS 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 396 IQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYT 475
Cdd:PLN02466 444 ILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYL 523
|
...
gi 500090152 476 EQK 478
Cdd:PLN02466 524 QVK 526
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
22-482 |
4.09e-119 |
|
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: 356.52 E-value: 4.09e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 22 CSPLDNRRIALVHEAGKTEVDAAVAAAQAALKgPWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAShID 101
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAK-EMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR-KE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 102 IPRGAANFKVFADVIKSVPTEFFEM-ATPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEE 180
Cdd:cd07149 82 VDRAIETLRLSAEEAKRLAGETIPFdASPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 181 TPQTATLLGEVMNEVGMPKGVYNVVHGFGpGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAadGARPVSLEMGGKNPAI 260
Cdd:cd07149 162 TPLSALKLAELLLEAGLPKGALNVVTGSG-ETVGDALVTDPRVRMISFTGSPAVGEAIARKA--GLKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 261 VFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSY 340
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 341 YNKARELGATVVTGGGVpqmpgelaNGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSV 420
Cdd:cd07149 319 VEEAVEGGARLLTGGKR--------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500090152 421 WTKDLARAHRVAGQIEAGLVWVN--SWFLRDlRTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMINdsSTFRVD-HMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-482 |
6.15e-119 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 357.85 E-value: 6.15e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVAT--AKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKgPWGRMTVAERVDLLNAVADGINRRFDDFLA 84
Cdd:PLN02278 28 LIGGKWTDAydGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP-SWSKLTASERSKILRRWYDLIIANKEDLAQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 85 AECADTGKPksLA-SHIDIPRGAANFKVFADVIKSVPTEFFEMATPDGRgalNYALRRPVGVVGVICPWNLPLLLMTWKV 163
Cdd:PLN02278 107 LMTLEQGKP--LKeAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRR---LLVLKQPVGVVGAITPWNFPLAMITRKV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 164 GPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIMKAAA 243
Cdd:PLN02278 182 GPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAP-EIGDALLASPKVRKITFTGSTAVGKKLMAGAA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 244 DGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDAST 323
Cdd:PLN02278 261 ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 324 GMGPLISQEHKNKVLSYYNKARELGATVVTGGGvPQMPGelanGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAED 403
Cdd:PLN02278 341 TQGPLINEAAVQKVESHVQDAVSKGAKVLLGGK-RHSLG----GTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500090152 404 EVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:PLN02278 416 EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
23-482 |
7.05e-118 |
|
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: 353.58 E-value: 7.05e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 23 SPLDNRRIALVHEAGKTEVDAAVAAAQAAlKGPWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKP-KSlaSHID 101
Cdd:cd07145 5 NPANGEVIDTVPSLSREEVREAIEVAEKA-KDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPiKQ--SRVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 102 IPRGAANFKVFADVIKSVPTEFFEM-ATPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEE 180
Cdd:cd07145 82 VERTIRLFKLAAEEAKVLRGETIPVdAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 181 TPQTATLLGEVMNEVGMPKGVYNVVHGFGPGSAGEFVTtHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAI 260
Cdd:cd07145 162 TPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVT-NPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 261 VFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSY 340
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 341 YNKARELGATVVTGGGVPQmpgelanGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSV 420
Cdd:cd07145 321 VNDAVEKGGKILYGGKRDE-------GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500090152 421 WTKDLARAHRVAGQIEAGLVWVN-SWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
23-481 |
3.51e-117 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 351.65 E-value: 3.51e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 23 SPLDNRRIALVHEAGKTEVDAAVAAAQAALKGPWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAsHIDI 102
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-RFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 103 PRGAANFKVFADVIKSVPTEFFEMATpdgrGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETP 182
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPEP----GSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 183 QTATLLGEVMNEV-GMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIV 261
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGS-EGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 262 FADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYY 341
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 342 NKARELGATVVTGGGVPqmPGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVW 421
Cdd:cd07120 317 ERAIAAGAEVVLRGGPV--TEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 422 TKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNIC 481
Cdd:cd07120 395 TRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
56-480 |
9.00e-117 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 350.75 E-value: 9.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSlASHIDIPRGAANFKVFADVIKSV---PTEFFEMATPDGR 132
Cdd:cd07099 34 WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRA-DAGLEVLLALEAIDWAARNAPRVlapRKVPTGLLMPNKK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 133 GALNYalrRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPGS 212
Cdd:cd07099 113 ATVEY---RPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 213 AG--EFVtthpkVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTE 290
Cdd:cd07099 190 AAliDAG-----VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 291 RVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVpqmpgELANGAWV 370
Cdd:cd07099 265 RVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGAR-----SNGGGPFY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 371 QPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDL 450
Cdd:cd07099 340 EPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAG 419
|
410 420 430
....*....|....*....|....*....|..
gi 500090152 451 --RTPFGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:cd07099 420 ipALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
7-478 |
6.41e-115 |
|
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: 347.08 E-value: 6.41e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVATA--KPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLA 84
Cdd:cd07111 25 FINGKWVKPEnrKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES-WSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 85 AECADTGKPKSLASHIDIPRGAANFKVFADVIKSVPTEFfematpdgrgalnyALRRPVGVVGVICPWNLPLLLMTWKVG 164
Cdd:cd07111 104 LESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTEL--------------AGWKPVGVVGQIVPWNFPLLMLAWKIC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 165 PALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGfgPGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAAD 244
Cdd:cd07111 170 PALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG--NGSFGSALANHPGVDKVAFTGSTEVGRALRRATAG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 245 GARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTG 324
Cdd:cd07111 248 TGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAID 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 325 MGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQmpgelANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDE 404
Cdd:cd07111 328 MGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLP-----SKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKE 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500090152 405 VIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQK 478
Cdd:cd07111 403 AVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPS 476
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
7-483 |
7.35e-115 |
|
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: 347.18 E-value: 7.35e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFV--ATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALK-GPWGRMTVAERVDLLNAVADGINRRFDDFL 83
Cdd:cd07140 9 FINGEFVdaEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFEnGEWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 84 AAECADTGKPKSLASHIDIPRGAANFKVFA---DVI--KSVPtefFEMATPDGRgaLNYALRRPVGVVGVICPWNLPLLL 158
Cdd:cd07140 89 TIESLDSGAVYTLALKTHVGMSIQTFRYFAgwcDKIqgKTIP---INQARPNRN--LTLTKREPIGVCGIVIPWNYPLMM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 159 MTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGpGSAGEFVTTHPKVNAITFTGETRTGAAI 238
Cdd:cd07140 164 LAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSG-SLVGQRLSDHPDVRKLGFTGSTPIGKHI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 239 MKAAADG-ARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGV 317
Cdd:cd07140 243 MKSCAVSnLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 318 PDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPgelanGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQ 397
Cdd:cd07140 323 PLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRP-----GFFFEPTVFTDVEDHMFIAKEESFGPIMIIS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 398 PFDAED--EVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYT 475
Cdd:cd07140 398 KFDDGDvdGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYL 477
|
....*...
gi 500090152 476 EQKNICIK 483
Cdd:cd07140 478 KTKTVTIE 485
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
56-482 |
6.38e-114 |
|
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: 342.63 E-value: 6.38e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAsHIDIPRGAANFKVFADVIKSVPTEFFEMATPdgrGAL 135
Cdd:cd07105 16 WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWA-GFNVDLAAGMLREAASLITQIIGGSIPSDKP---GTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 136 NYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHgFGPGSAGE 215
Cdd:cd07105 92 AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVT-HSPEDAPE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 216 FVTT---HPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERV 292
Cdd:cd07105 171 VVEAliaHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 293 YVERPIFDRFVAALKAGAEGLKLGvpddaSTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPGelanGAWVQP 372
Cdd:cd07105 251 IVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPS----GTSMPP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 373 TIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRT 452
Cdd:cd07105 322 TILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDEPT 401
|
410 420 430
....*....|....*....|....*....|.
gi 500090152 453 -PFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07105 402 lPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
6-482 |
2.13e-104 |
|
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: 319.89 E-value: 2.13e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 6 NFINGEFVATA-KPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLA 84
Cdd:cd07086 1 GVIGGEWVGSGgETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE-WRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 85 AECADTGKPKSLA-----SHIDIprgaANFKV------FADVIKSvpteffEMatPDGRgalNYALRRPVGVVGVICPWN 153
Cdd:cd07086 80 LVSLEMGKILPEGlgevqEMIDI----CDYAVglsrmlYGLTIPS------ER--PGHR---LMEQWNPLGVVGVITAFN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 154 LPLLLMTWKVGPALACGNTVVVKPSEETPQTAT----LLGEVMNEVGMPKGVYNVVHGFGPGsaGEFVTTHPKVNAITFT 229
Cdd:cd07086 145 FPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIavtkILAEVLEKNGLPPGVVNLVTGGGDG--GELLVHDPRVPLVSFT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 230 GETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAG 309
Cdd:cd07086 223 GSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 310 AEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQmpgELANGAWVQPTIWTGLDDNSPIAREEI 389
Cdd:cd07086 303 YKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRID---GGEPGNYVEPTIVTGVTDDARIVQEET 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 390 FGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQ--IEAGLVWVNswflrdLRT-------PFGGAKQS 460
Cdd:cd07086 380 FAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVN------IPTsgaeiggAFGGEKET 453
|
490 500
....*....|....*....|..
gi 500090152 461 GIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07086 454 GGGRESGSDAWKQYMRRSTCTI 475
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
7-481 |
2.73e-104 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 320.71 E-value: 2.73e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVATAKPFDKCSPLD-NRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLAA 85
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPT-WRRTPPEERARLLLRAAALLRRRRFELAAW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 86 ECADTGKPKSLAShidiprgaanfkvfADVIKSVptEFFEM-----------ATPDGRGALNYALRRPVGVVGVICPWNL 154
Cdd:cd07124 115 MVLEVGKNWAEAD--------------ADVAEAI--DFLEYyaremlrlrgfPVEMVPGEDNRYVYRPLGVGAVISPWNF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 155 PLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGpGSAGEFVTTHPKVNAITFTGETRT 234
Cdd:cd07124 179 PLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPG-EEVGDYLVEHPDVRFIAFTGSREV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 235 GAAIMKAAADGA------RPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKA 308
Cdd:cd07124 258 GLRIYERAAKVQpgqkwlKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 309 GAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARElGATVVTGGGVpqmPGELANGAWVQPTIWTGLDDNSPIAREE 388
Cdd:cd07124 338 RTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKS-EGRLLLGGEV---LELAAEGYFVQPTIFADVPPDHRLAQEE 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 389 IFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNswflRDL------RTPFGGAKQSGI 462
Cdd:cd07124 414 IFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYAN----RKItgalvgRQPFGGFKMSGT 489
|
490 500
....*....|....*....|
gi 500090152 463 G-REGGVHSLEFYTEQKNIC 481
Cdd:cd07124 490 GsKAGGPDYLLQFMQPKTVT 509
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
56-483 |
6.46e-104 |
|
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: 318.09 E-value: 6.46e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKS-----LASHIDIPRGAANFKVFADViKSVPTeffematpD 130
Cdd:cd07151 48 WAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIkanieWGAAMAITREAATFPLRMEG-RILPS--------D 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 131 GRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTA-TLLGEVMNEVGMPKGVYNVVHGFG 209
Cdd:cd07151 119 VPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 210 PGSAGEFVTtHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGT 289
Cdd:cd07151 199 SEIGDAFVE-HPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 290 ERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVpqmpgelaNGAW 369
Cdd:cd07151 278 NRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEA--------EGNV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 370 VQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRD 449
Cdd:cd07151 350 LEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVND 429
|
410 420 430
....*....|....*....|....*....|....*
gi 500090152 450 L-RTPFGGAKQSGIGREGGVHSLEFYTEQKNICIK 483
Cdd:cd07151 430 EpHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
56-473 |
2.63e-103 |
|
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: 315.17 E-value: 2.63e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAshidipRG-----AANFKVFAD----VIKSVPTEffem 126
Cdd:cd07100 15 WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA------RAevekcAWICRYYAEnaeaFLADEPIE---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 127 aTPDGRGALNYalrRPVGVVGVICPWNLPLllmtWKV----GPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVY 202
Cdd:cd07100 85 -TDAGKAYVRY---EPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 203 NVVhgFGPGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANC 282
Cdd:cd07100 157 QNL--LIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 283 GQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPg 362
Cdd:cd07100 235 GQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGP- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 363 elanGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWV 442
Cdd:cd07100 314 ----GAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFI 389
|
410 420 430
....*....|....*....|....*....|..
gi 500090152 443 NSWFLRDLRTPFGGAKQSGIGREGGVHSL-EF 473
Cdd:cd07100 390 NGMVKSDPRLPFGGVKRSGYGRELGRFGIrEF 421
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
56-482 |
3.64e-102 |
|
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: 313.22 E-value: 3.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAsHIDIPRGAANFKVFADVIKSVPTEFFEMATPDGRGA- 134
Cdd:cd07094 37 RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-RVEVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 135 LNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGfGPGSAG 214
Cdd:cd07094 116 LAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTG-EREVLG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 215 EFVTTHPKVNAITFTGETRTGAAIMKAAadGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYV 294
Cdd:cd07094 195 DAFAADERVAMLSFTGSAAVGEALRANA--GGKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 295 ERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGvpqmpgelANGAWVQPTI 374
Cdd:cd07094 273 HEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGE--------RDGALFKPTV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 375 WTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVN-SWFLRDLRTP 453
Cdd:cd07094 345 LEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNdSSAFRTDWMP 424
|
410 420
....*....|....*....|....*....
gi 500090152 454 FGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07094 425 FGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
19-482 |
1.84e-101 |
|
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: 311.49 E-value: 1.84e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 19 FDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKgPWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAS 98
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR-PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 99 hIDIPRGAANFKVFADVIKSVPTEFFEMAT-PDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKP 177
Cdd:cd07147 80 -GEVARAIDTFRIAAEEATRIYGEVLPLDIsARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 178 SEETPQTATLLGEVMNEVGMPKGVYNVVHGfgPGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAadGARPVSLEMGGKN 257
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLLVTDERIKLLSFTGSPAVGWDLKARA--GKKKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 258 PAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKV 337
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 338 LSYYNKARELGATVVTGGGVpqmpgelaNGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLA 417
Cdd:cd07147 315 EGWVNEAVDAGAKLLTGGKR--------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQ 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500090152 418 CSVWTKDLARAHRVAGQIEAGLVWVN---SWflRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07147 387 AGVFTRDLEKALRAWDELEVGGVVINdvpTF--RVDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
139-480 |
3.55e-100 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 310.27 E-value: 3.55e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 139 LRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPGSAGEFVt 218
Cdd:PRK09407 151 LRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALV- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 219 thPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPI 298
Cdd:PRK09407 230 --DNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 299 FDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPGELangaWVQPTIWTGL 378
Cdd:PRK09407 308 YDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGPL----FYEPTVLTGV 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 379 DDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVN-----SWFLRDlrTP 453
Cdd:PRK09407 384 TPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVD--AP 461
|
330 340
....*....|....*....|....*..
gi 500090152 454 FGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:PRK09407 462 MGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
56-480 |
7.93e-100 |
|
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: 307.31 E-value: 7.93e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAsHIDIPRGAANFKVFADVIKSVpteffeMATPDGRGAL 135
Cdd:cd07101 34 WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHA-FEEVLDVAIVARYYARRAERL------LKPRRRRGAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 136 -----NYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGP 210
Cdd:cd07101 107 pvltrTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 211 gSAGEFVTTHpkVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTE 290
Cdd:cd07101 187 -EVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 291 RVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGG-GVPQM-PgelangA 368
Cdd:cd07101 264 RIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGrARPDLgP------Y 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 369 WVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVN----- 443
Cdd:cd07101 338 FYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNegyaa 417
|
410 420 430
....*....|....*....|....*....|....*..
gi 500090152 444 SWFLRDlrTPFGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:cd07101 418 AWASID--APMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
23-463 |
3.23e-99 |
|
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: 305.71 E-value: 3.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 23 SPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDfLAAE-CADTGKPkslashid 101
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKG-WRAVPLEERKAIVTRAVELLAANTDE-IAEElTWQMGRP-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 102 IPRGAANFKVFAD----VIKSVPTEFFEMATPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKP 177
Cdd:cd07102 72 IAQAGGEIRGMLEraryMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 178 SEETPQTATLLGEVMNEVGMPKGVYNVVHGFGpgSAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKN 257
Cdd:cd07102 152 SPQTPLCGERFAAAFAEAGLPEGVFQVLHLSH--ETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 258 PAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKV 337
Cdd:cd07102 230 PAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 338 LSYYNKARELGATVVTGGGVpqMPGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLA 417
Cdd:cd07102 310 RAQIADAIAKGARALIDGAL--FPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLT 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 500090152 418 CSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIG 463
Cdd:cd07102 388 ASVWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRG 433
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
7-484 |
2.85e-95 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 296.43 E-value: 2.85e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFV--ATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLA 84
Cdd:PRK11241 14 LINGEWLdaNNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPA-WRALTAKERANILRRWFNLMMEHQDDLAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 85 AECADTGKPKSLASHiDIPRGAANFKVFADVIKSVPTEFFEMATPDGRGALnyaLRRPVGVVGVICPWNLPLLLMTWKVG 164
Cdd:PRK11241 93 LMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIV---IKQPIGVTAAITPWNFPAAMITRKAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 165 PALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGfGPGSAGEFVTTHPKVNAITFTGETRTGAAIMKAAAD 244
Cdd:PRK11241 169 PALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTG-SAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 245 GARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTG 324
Cdd:PRK11241 248 DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 325 MGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMpgelaNGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDE 404
Cdd:PRK11241 328 IGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHEL-----GGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEAD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 405 VIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREGGVHSLEFYTEQKNICIKL 484
Cdd:PRK11241 403 VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
68-474 |
2.83e-94 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 291.64 E-value: 2.83e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 68 LNAVADGINRRFDDFLAAECADTGKPKSLAShIDIPRGAANFKVFADVIKSVPTEFFEMATPdgrGALNYALRRPVGVVG 147
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAE-VEVAFTADYIDYMAEWARRYEGEIIQSDRP---GENILLFKRALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 148 VICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAIT 227
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGE-TVGQELAGNPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 228 FTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALK 307
Cdd:PRK10090 156 MTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 308 AGAEGLKLGVPDDAST-GMGPLISQEHKNKVLSYYNKARELGATVVTGGGVpqmpgELANGAWVQPTIWTGLDDNSPIAR 386
Cdd:PRK10090 236 EAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKA-----VEGKGYYYPPTLLLDVRQEMSIMH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 387 EEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPFGGAKQSGIGREG 466
Cdd:PRK10090 311 EETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGAD 390
|
....*...
gi 500090152 467 GVHSLEFY 474
Cdd:PRK10090 391 GKHGLHEY 398
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
6-483 |
1.66e-92 |
|
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: 289.09 E-value: 1.66e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 6 NFINGEFVATAKPF-DKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGPWGRMTVAERVDLLNAVADGINRRFDDFLA 84
Cdd:cd07082 4 YLINGEWKESSGKTiEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 85 AECADTGKPKSlASHIDIPRGAANFKVFADVIKSVPTEFFEM-ATPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKV 163
Cdd:cd07082 84 LLMWEIGKTLK-DALKEVDRTIDYIRDTIEELKRLDGDSLPGdWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 164 GPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVhgFGPGS-AGEFVTTHPKVNAITFTGETRTGAAIMKAA 242
Cdd:cd07082 163 IPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVV--TGRGReIGDPLVTHGRIDVISFTGSTEVGNRLKKQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 243 adGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDAS 322
Cdd:cd07082 241 --PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 323 TGMGPLISQEHKNKVLSYYNKARELGATVVTGGGvpqmpGELANgaWVQPTIwtgLDDNSP---IAREEIFGPCTLIQPF 399
Cdd:cd07082 319 VDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG-----REGGN--LIYPTL---LDPVTPdmrLAWEEPFGPVLPIIRV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 400 DAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRT-PFGGAKQSGIGREGGVHSLEFYTEQK 478
Cdd:cd07082 389 NDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQGIGDALRSMTRRK 468
|
....*
gi 500090152 479 NICIK 483
Cdd:cd07082 469 GIVIN 473
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
56-476 |
5.10e-92 |
|
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: 286.88 E-value: 5.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDF---LAAECADTGkPKSlasHIDIPRGAANFKVFAdvikSVPTEFFEMATPDGR 132
Cdd:cd07152 29 WAATPPRERAAVLRRAADLLEEHADEIadwIVRESGSIR-PKA---GFEVGAAIGELHEAA----GLPTQPQGEILPSAP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 133 GALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTA-TLLGEVMNEVGMPKGVYNVVHGfGPG 211
Cdd:cd07152 101 GRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPG-GAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 212 sAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTER 291
Cdd:cd07152 180 -AGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 292 VYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGgvpqmpgeLANGAWVQ 371
Cdd:cd07152 259 HLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGG--------TYDGLFYR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 372 PTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRD-L 450
Cdd:cd07152 331 PTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDeP 410
|
410 420
....*....|....*....|....*..
gi 500090152 451 RTPFGGAKQSGIG-REGGVHSLEFYTE 476
Cdd:cd07152 411 HNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
56-481 |
2.32e-89 |
|
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: 280.73 E-value: 2.32e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLASHIDIprgaanfKVFADVIK-------------SVPTE 122
Cdd:cd07098 34 WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI-------LVTCEKIRwtlkhgekalrpeSRPGG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 123 FFEMATpdgRGALNYalrRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTA----TLLGEVMNEVGMP 198
Cdd:cd07098 107 LLMFYK---RARVEY---EPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSgfflSIIRECLAACGHD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 199 KGVYNVVHGFGPgsAGEFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSV 278
Cdd:cd07098 181 PDLVQLVTCLPE--TAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 279 FANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVP 358
Cdd:cd07098 259 FQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 359 QMPgELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAG 438
Cdd:cd07098 339 PHP-EYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETG 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 500090152 439 LVWVNSW----FLRDLrtPFGGAKQSGIGREGGVHSLEFYTEQKNIC 481
Cdd:cd07098 418 MVAINDFgvnyYVQQL--PFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
4-480 |
7.96e-88 |
|
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: 277.09 E-value: 7.96e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 4 IHNFINGEFVA--TAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDD 81
Cdd:cd07085 1 LKLFINGEWVEskTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA-WSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 82 FLAAECADTGKpkSLA-SHIDIPRGAANfkvfADVIKSVPTEFF-EMATPDGRGALNYALRRPVGVVGVICPWNLPLLLM 159
Cdd:cd07085 80 LARLITLEHGK--TLAdARGDVLRGLEV----VEFACSIPHLLKgEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 160 TWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHgfGPGSAGEFVTTHPKVNAITFTGETRTGAAIM 239
Cdd:cd07085 154 LWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVH--GGKEAVNALLDHPDIKAVSFVGSTPVGEYIY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 240 -KAAADGARPVSLeMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVP 318
Cdd:cd07085 232 eRAAANGKRVQAL-GGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 319 DDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPGeLANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQP 398
Cdd:cd07085 311 DDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPG-YENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 399 FDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVN-------SWFlrdlrtPFGGAKQSGIGREG--GVH 469
Cdd:cd07085 390 VDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINvpipvplAFF------SFGGWKGSFFGDLHfyGKD 463
|
490
....*....|.
gi 500090152 470 SLEFYTEQKNI 480
Cdd:cd07085 464 GVRFYTQTKTV 474
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
57-482 |
1.14e-87 |
|
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: 275.78 E-value: 1.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 57 GRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKsLASHIDIPRGAANFKVFADVIKSVPTEFFEM-ATPDGRGAL 135
Cdd:cd07146 35 STLTRYQRSAILNKAAALLEARREEFARLITLESGLCL-KDTRYEVGRAADVLRFAAAEALRDDGESFSCdLTANGKARK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 136 NYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGfGPGSAGE 215
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTG-EPGEIGD 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 216 FVTTHPKVNAITFTGETRTGAAImkAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVE 295
Cdd:cd07146 193 ELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVH 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 296 RPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGvpqmpgelANGAWVQPTIW 375
Cdd:cd07146 271 ESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQ--------RQGALYAPTVL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 376 TGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLvwVNSWFLRDLRT--- 452
Cdd:cd07146 343 DHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGT--VNVNEVPGFRSels 420
|
410 420 430
....*....|....*....|....*....|.
gi 500090152 453 PFGGAKQSGIG-REGGVHSLEFYTEQKNICI 482
Cdd:cd07146 421 PFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
8-480 |
1.44e-78 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 254.09 E-value: 1.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 8 INGEFVATAKPFDKCSPLDNRR-IALVHEAGKTEVDAAVAAAQAALKgPWGRMTVAERVDLLNAVADGINRRFDDFLAAE 86
Cdd:PRK03137 41 IGGERITTEDKIVSINPANKSEvVGRVSKATKELAEKAMQAALEAFE-TWKKWSPEDRARILLRAAAIIRRRKHEFSAWL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 87 CADTGKPKSLAShidiprgaanfkvfADVIKSVptEFFE------MATPDGR------GALNYALRRPVGVVGVICPWNL 154
Cdd:PRK03137 120 VKEAGKPWAEAD--------------ADTAEAI--DFLEyyarqmLKLADGKpvesrpGEHNRYFYIPLGVGVVISPWNF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 155 PLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGfGPGSAGEFVTTHPKVNAITFTGETRT 234
Cdd:PRK03137 184 PFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPG-SGSEVGDYLVDHPKTRFITFTGSREV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 235 GAAIMKAAA---DGAR---PVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKA 308
Cdd:PRK03137 263 GLRIYERAAkvqPGQIwlkRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 309 GAEGLKLGVPDDAsTGMGPLISQEHKNKVLSYYNKARELGaTVVTGGGvpqmpGELANGAWVQPTIWTGLDDNSPIAREE 388
Cdd:PRK03137 343 LTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGE-----GDDSKGYFIQPTIFADVDPKARIMQEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 389 IFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGlvwvNSWFLRDLR------TPFGGAKQSGI 462
Cdd:PRK03137 416 IFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVG----NLYFNRGCTgaivgyHPFGGFNMSGT 491
|
490
....*....|....*....
gi 500090152 463 -GREGGVHSLEFYTEQKNI 480
Cdd:PRK03137 492 dSKAGGPDYLLLFLQAKTV 510
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
7-480 |
1.38e-75 |
|
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: 246.32 E-value: 1.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVATAKPFDKCSPLDNRRIalVHEAGKTEVDAAVAAAQAALKG--PWGRMTVAERVDLLNAVADGINRRFDDFLA 84
Cdd:TIGR01237 36 VINGERVETENKIVSINPCDKSEV--VGTVSKASQEHAEHALQAAAKAfeAWKKTDPEERAAILFKAAAIVRRRRHEFSA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 85 AECADTGKP-----KSLASHIDIPRGAAnfKVFADVIKSVPTEFFEmatpdgrGALNYALRRPVGVVGVICPWNLPLLLM 159
Cdd:TIGR01237 114 LLVKEVGKPwneadAEVAEAIDFMEYYA--RQMIELAKGKPVNSRE-------GETNQYVYTPTGVTVVISPWNFPFAIM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 160 TWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGpGSAGEFVTTHPKVNAITFTGETRTGAAIM 239
Cdd:TIGR01237 185 VGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSG-SEVGDYLVDHPKTSLITFTGSREVGTRIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 240 KAAADgARP-------VSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEG 312
Cdd:TIGR01237 264 ERAAK-VQPgqkhlkrVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITES 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 313 LKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPqmpgelANGAWVQPTIWTGLDDNSPIAREEIFGP 392
Cdd:TIGR01237 343 LKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDD------SKGYFIGPTIFADVDRKARLAQEEIFGP 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 393 CTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGlvwvNSWFLRDL------RTPFGGAKQSGIG-RE 465
Cdd:TIGR01237 417 VVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVG----NLYFNRNItgaivgYQPFGGFKMSGTDsKA 492
|
490
....*....|....*
gi 500090152 466 GGVHSLEFYTEQKNI 480
Cdd:TIGR01237 493 GGPDYLALFMQAKTV 507
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
55-467 |
2.41e-70 |
|
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: 230.24 E-value: 2.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 55 PWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKP--------KSLASHIDIPRGAANfkvfadviKSVPTEffEM 126
Cdd:cd07095 15 GWAALSLEERAAILRRFAELLKANKEELARLISRETGKPlweaqtevAAMAGKIDISIKAYH--------ERTGER--AT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 127 ATPDGRGALNYalrRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVH 206
Cdd:cd07095 85 PMAQGRAVLRH---RPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 207 GFGPgsAGEFVTTHPKVNAITFTGETRTGAAIMKAAADgaRP---VSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCG 283
Cdd:cd07095 162 GGRE--TGEALAAHEGIDGLLFTGSAATGLLLHRQFAG--RPgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 284 QVCLGTERVYVERPIF-DRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKArelgatvVTGGGVPQMPG 362
Cdd:cd07095 238 QRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDL-------LALGGEPLLAM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 363 EL--ANGAWVQPTIwtgLD--DNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAG 438
Cdd:cd07095 311 ERlvAGTAFLSPGI---IDvtDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAG 387
|
410 420 430
....*....|....*....|....*....|....
gi 500090152 439 LVWVNswflRDL-----RTPFGGAKQSGIGREGG 467
Cdd:cd07095 388 IVNWN----RPTtgassTAPFGGVGLSGNHRPSA 417
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
7-471 |
3.51e-70 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 232.09 E-value: 3.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVATAKPFDKCSPLDNRR-IALVHEAGKTEVDAAVAAAQAAlKGPWGRMTVAERVDLLNAVADGINRRFDDFLAA 85
Cdd:cd07125 36 IINGEETETGEGAPVIDPADHERtIGEVSLADAEDVDAALAIAAAA-FAGWSATPVEERAEILEKAADLLEANRGELIAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 86 ECADTGKpkSLASHIDIPRGAANF---------KVFADVIKSVPTeffematpdgrGALNYALRRPVGVVGVICPWNLPL 156
Cdd:cd07125 115 AAAEAGK--TLADADAEVREAIDFcryyaaqarELFSDPELPGPT-----------GELNGLELHGRGVFVCISPWNFPL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 157 LLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGpGSAGEFVTTHPKVNAITFTGETRTGA 236
Cdd:cd07125 182 AIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDG-EEIGEALVAHPRIDGVIFTGSTETAK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 237 AI--MKAAADGAR-PVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGL 313
Cdd:cd07125 261 LInrALAERDGPIlPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 314 KLGVPDDASTGMGPLISQEHKNKVLSYYNKARElgatvvTGGGVPQMPGELANGAWVQPTIWTGldDNSPIAREEIFGPC 393
Cdd:cd07125 341 KVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRG------EAWLIAPAPLDDGNGYFVAPGIIEI--VGIFDLTTEVFGPI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 394 TLIQPFDAE--DEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNswflRD------LRTPFGGAKQSGIGRE 465
Cdd:cd07125 413 LHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN----RNitgaivGRQPFGGWGLSGTGPK 488
|
....*..
gi 500090152 466 -GGVHSL 471
Cdd:cd07125 489 aGGPNYL 495
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
56-469 |
1.17e-69 |
|
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: 228.26 E-value: 1.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKS--LASHI-----DIPRGAANFKVFADViKSVPTEffeMAT 128
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAevDLTEIlpvlsEINHAIKHLKKWMKP-KRVRTP---LLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 129 PDGRGALNYalrRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVyNVVHGf 208
Cdd:cd07134 90 FGTKSKIRY---EPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-AVFEG- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 209 gpgsaGEFVTTH----PkVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQ 284
Cdd:cd07134 165 -----DAEVAQAllelP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 285 VCLGTERVYVERPIFDRFVAALKA------GAEGLKLGVPDdastgMGPLISQEHKNKVLSYYNKARELGATVVTGGGVP 358
Cdd:cd07134 239 TCIAPDYVFVHESVKDAFVEHLKAeiekfyGKDAARKASPD-----LARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 359 qmpgelANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAG 438
Cdd:cd07134 314 ------AAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSG 387
|
410 420 430
....*....|....*....|....*....|...
gi 500090152 439 LVWVNSWFLR--DLRTPFGGAKQSGIGREGGVH 469
Cdd:cd07134 388 GVVVNDVVLHflNPNLPFGGVNNSGIGSYHGVY 420
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
60-473 |
2.54e-67 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 223.08 E-value: 2.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 60 TVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSlASHIDIPRGAANFKVFADVIKSVPTEffEMATPDGRGALN-YA 138
Cdd:PRK09406 43 TFAQRARWANAAADLLEAEADQVAALMTLEMGKTLA-SAKAEALKCAKGFRYYAEHAEALLAD--EPADAAAVGASRaYV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 139 LRRPVGVVGVICPWNLPLllmtWKV----GPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVhgFGPGSAG 214
Cdd:PRK09406 120 RYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTL--LVGSGAV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 215 EFVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYV 294
Cdd:PRK09406 194 EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 295 ERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPgelanGAWVQPTI 374
Cdd:PRK09406 274 HADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGP-----GWFYPPTV 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 375 WTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDLRTPF 454
Cdd:PRK09406 349 ITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPF 428
|
410 420
....*....|....*....|
gi 500090152 455 GGAKQSGIGREGGVHSL-EF 473
Cdd:PRK09406 429 GGVKRSGYGRELSAHGIrEF 448
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
61-482 |
2.86e-67 |
|
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: 222.02 E-value: 2.86e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 61 VAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLA--SHIDIPRGAANF--KVFADVIK--SVPTEFfeMATPdGRGa 134
Cdd:cd07087 19 LEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylTEIAVVLGEIDHalKHLKKWMKprRVSVPL--LLQP-AKA- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 135 lnYALRRPVGVVGVICPWNLPLLLMtwkVGP---ALACGNTVVVKPSEETPQTATLLGEVMNEVgMPKGVYNVVHGFGPg 211
Cdd:cd07087 95 --YVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 212 sagefVTT--------HpkvnaITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCG 283
Cdd:cd07087 168 -----VATallaepfdH-----IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 284 QVCLGTERVYVERPIFDRFVAALKagaEGLKLGVPDD--ASTGMGPLISQEHKNKVLSYYNkarelGATVVTGGGVpqmp 361
Cdd:cd07087 238 QTCIAPDYVLVHESIKDELIEELK---KAIKEFYGEDpkESPDYGRIINERHFDRLASLLD-----DGKVVIGGQV---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 362 geLANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVW 441
Cdd:cd07087 306 --DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVC 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 500090152 442 VNSWFLR----DLrtPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07087 384 VNDVLLHaaipNL--PFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
23-482 |
3.14e-67 |
|
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: 222.68 E-value: 3.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 23 SPLDNRRIALVHEAGKTEVDAAVAAAQAALKGPWGRMTVAERVDLLNAVADGINRRFDDfLAAECADTGKPKSLASHIDI 102
Cdd:cd07148 5 NPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWLPAHERIAILERLADLMEERADE-LALLIAREGGKPLVDAKVEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 103 PRGAANFKVFADVIKSVPTEFFEMA-TPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEET 181
Cdd:cd07148 84 TRAIDGVELAADELGQLGGREIPMGlTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 182 PQTATLLGEVMNEVGMPKGVynvVHGFGPGSA-GEFVTTHPKVNAITFTGETRTGAAIMKAAADGARpVSLEMGGKNPAI 260
Cdd:cd07148 164 PLSCLAFVDLLHEAGLPEGW---CQAVPCENAvAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGTR-CALEHGGAAPVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 261 VFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSY 340
Cdd:cd07148 240 VDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 341 YNKARELGATVVTGggvpqmpGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSV 420
Cdd:cd07148 320 VNEAVAAGARLLCG-------GKRLSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500090152 421 WTKDLARAHRVAGQIEAGLVWVN--SWFLRDLrTPFGGAKQSGIGREGGVHSLEFYTEQKNICI 482
Cdd:cd07148 393 FTKDLDVALKAVRRLDATAVMVNdhTAFRVDW-MPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
132-464 |
3.30e-66 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 219.28 E-value: 3.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 132 RGALNYALRRPVGVVGVICPWNLPLLLMtwkVGP---ALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVyNVVHGf 208
Cdd:cd07133 91 LPAKAEVEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-AVVTG- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 209 GPGSAGEFvtTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLG 288
Cdd:cd07133 166 GADVAAAF--SSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 289 TERVYVERPIFDRFVAALKAGAEGL---KLGVPDDAStgmgpLISQEHKNKVLSYYNKARELGATVVTGGGVPQmpgELA 365
Cdd:cd07133 244 PDYVLVPEDKLEEFVAAAKAAVAKMyptLADNPDYTS-----IINERHYARLQGLLEDARAKGARVIELNPAGE---DFA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 366 NGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSW 445
Cdd:cd07133 316 ATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDT 395
|
330 340
....*....|....*....|...
gi 500090152 446 FLR----DLrtPFGGAKQSGIGR 464
Cdd:cd07133 396 LLHvaqdDL--PFGGVGASGMGA 416
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
1-480 |
5.02e-63 |
|
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: 212.82 E-value: 5.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 1 MKQIHNFINGEFVATAKPFDKCSPLD-NRRIALVHEAGKTEVDAAVAAAQAALKgPWGRMTVAERVDLLNAVADGINRRF 79
Cdd:cd07083 16 GRAYPLVIGGEWVDTKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFK-TWKDWPQEDRARLLLKAADLLRRRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 80 DDFLAAECADTGKpkSLASHIDIPRGAANFKVFADViKSVPTEFFEMATPDGRGALNYALRRPVGVVGVICPWNLPLLLM 159
Cdd:cd07083 95 RELIATLTYEVGK--NWVEAIDDVAEAIDFIRYYAR-AALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 160 TWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIM 239
Cdd:cd07083 172 TGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGE-EVGAYLTEHERIRGINFTGSLETGKKIY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 240 KAAADGA------RPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGL 313
Cdd:cd07083 251 EAAARLApgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 314 KLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGaTVVTGGGVPQmpgelANGAWVQPTIWTGLDDNSPIAREEIFGPC 393
Cdd:cd07083 331 SVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLE-----GEGYFVAPTVVEEVPPKARIAQEEIFGPV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 394 TLIQPFDAED--EVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDL--RTPFGGAKQSGIG-REGGV 468
Cdd:cd07083 405 LSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALvgVQPFGGFKLSGTNaKTGGP 484
|
490
....*....|..
gi 500090152 469 HSLEFYTEQKNI 480
Cdd:cd07083 485 HYLRRFLEMKAV 496
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
4-480 |
1.28e-62 |
|
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: 211.28 E-value: 1.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 4 IHNFINGEFV--ATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDD 81
Cdd:TIGR01722 1 VNHWIGGKFAegASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLT-WGQTSLAQRTSVLLRYQALLKEHRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 82 FLAAECADTGKPKSLASHiDIPRGAAnfkvFADVIKSVPTEFF-EMATPDGRGALNYALRRPVGVVGVICPWNLPLLLMT 160
Cdd:TIGR01722 80 IAELITAEHGKTHSDALG-DVARGLE----VVEHACGVNSLLKgETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 161 WKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHgfGPGSAGEFVTTHPKVNAITFTGETRTGAAIMK 240
Cdd:TIGR01722 155 WMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVH--GDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 241 AAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVyVERPIFDRFVAALKAGAEGLKLGVPDD 320
Cdd:TIGR01722 233 TGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAA-VLVGAADEWVPEIRERAEKIRIGPGDD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 321 ASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPGElANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFD 400
Cdd:TIGR01722 312 PGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGY-EEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEAD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 401 AEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSwflrDLRTP-----FGGAKQSGIGREG--GVHSLEF 473
Cdd:TIGR01722 391 TLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV----PIPVPlpyfsFTGWKDSFFGDHHiyGKQGTHF 466
|
....*..
gi 500090152 474 YTEQKNI 480
Cdd:TIGR01722 467 YTRGKTV 473
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
142-467 |
5.78e-60 |
|
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: 203.98 E-value: 5.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 142 PVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTA----TLLGEVMNEVGMPKGVYNVVhgFGPGSAGEFV 217
Cdd:cd07130 132 PLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAiavtKIVARVLEKNGLPGAIASLV--CGGADVGEAL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 218 TTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERP 297
Cdd:cd07130 210 VKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHES 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 298 IFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPGElangaWVQPTIWTG 377
Cdd:cd07130 290 IYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGN-----YVEPTIVEG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 378 LDDnSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQI--EAGLVWVNswflrdlrTP-- 453
Cdd:cd07130 365 LSD-APIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVN--------IGts 435
|
330 340
....*....|....*....|.
gi 500090152 454 -------FGGAKQSGIGREGG 467
Cdd:cd07130 436 gaeiggaFGGEKETGGGRESG 456
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
140-480 |
4.04e-59 |
|
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: 200.91 E-value: 4.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 140 RRPVGVVGVICPWNLPLLLMtwkVGP---ALACGNTVVVKPSEETPQTATLLGEVMNEvGMPKGVYNVVHGfGPGSAGEF 216
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALLAELVPK-YLDPDAFQVVQG-GVPETTAL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 217 VTThpKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVER 296
Cdd:cd07135 181 LEQ--KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 297 PIFDRFVAALKagaEGLKLGVPDDA--STGMGPLISQEHKNKVLSYYNKARelgATVVTGGgvpqmpgeLANGA--WVQP 372
Cdd:cd07135 259 SVYDEFVEELK---KVLDEFYPGGAnaSPDYTRIVNPRHFNRLKSLLDTTK---GKVVIGG--------EMDEAtrFIPP 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 373 TIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFL----R 448
Cdd:cd07135 325 TIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvgvD 404
|
330 340 350
....*....|....*....|....*....|..
gi 500090152 449 DLrtPFGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:cd07135 405 NA--PFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
56-465 |
4.25e-59 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 201.63 E-value: 4.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLAsHIDIPRGAANFKVFAD----VIKSVPTeffemATPDG 131
Cdd:PRK13968 45 WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-RAEVAKSANLCDWYAEhgpaMLKAEPT-----LVENQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 132 RGALNYalrRPVGVVGVICPWNLPLllmtWKV----GPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHG 207
Cdd:PRK13968 119 QAVIEY---RPLGTILAIMPWNFPL----WQVmrgaVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 208 FGPGSAGefVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCL 287
Cdd:PRK13968 192 DNDGVSQ--MINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 288 GTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGgvPQMPGElanG 367
Cdd:PRK13968 270 AAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLLGG--EKIAGA---G 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 368 AWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFL 447
Cdd:PRK13968 345 NYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFINGYCA 424
|
410
....*....|....*...
gi 500090152 448 RDLRTPFGGAKQSGIGRE 465
Cdd:PRK13968 425 SDARVAFGGVKKSGFGRE 442
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
117-483 |
8.35e-58 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 198.71 E-value: 8.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 117 KSVPTEFfeMATPdgrgALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVg 196
Cdd:PTZ00381 90 EKVDTVG--VFGP----GKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 197 MPKGVYNVVHGfgpgsaGEFVTTH---PKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEG 273
Cdd:PTZ00381 163 LDPSYVRVIEG------GVEVTTEllkEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARR 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 274 TMRSVFANCGQVCLGTERVYVERPIFDRFVAALKagaEGLKLGVPDDA--STGMGPLISQEHKNKVLSYYNKArelGATV 351
Cdd:PTZ00381 237 IAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALK---EAIKEFFGEDPkkSEDYSRIVNEFHTKRLAELIKDH---GGKV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 352 VTGGGVpqmpgELANgAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRV 431
Cdd:PTZ00381 311 VYGGEV-----DIEN-KYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELV 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 500090152 432 AGQIEAGLVWVNSWFLRDL--RTPFGGAKQSGIGREGGVHSLEFYTEQKNICIK 483
Cdd:PTZ00381 385 LENTSSGAVVINDCVFHLLnpNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
7-461 |
4.03e-53 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 185.93 E-value: 4.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVA-TAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLAA 85
Cdd:PRK09457 4 WINGDWIAgQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA-WARLSFEERQAIVERFAALLEENKEELAEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 86 ECADTGKP--------KSLASHIDIPRGAANfkvfadviKSVPTEffEMATPDGRGALNYalrRPVGVVGVICPWNLPLL 157
Cdd:PRK09457 83 IARETGKPlweaatevTAMINKIAISIQAYH--------ERTGEK--RSEMADGAAVLRH---RPHGVVAVFGPYNFPGH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 158 LMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGfGPgSAGEFVTTHPKVNAITFTGETRTGAA 237
Cdd:PRK09457 150 LPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GR-ETGKALAAHPDIDGLLFTGSANTGYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 238 IMKAAAdgARP---VSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIF-DRFVAALKAGAEGL 313
Cdd:PRK09457 228 LHRQFA--GQPekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 314 KLGVPD-DASTGMGPLISQEHKNKVLSYYNKARELGATVVTgggvpQMPGELANGAWVQPtiwtGLDDNSPIAR---EEI 389
Cdd:PRK09457 306 TVGRWDaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLL-----EMTQLQAGTGLLTP----GIIDVTGVAElpdEEY 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500090152 390 FGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNswflRDLR-----TPFGGAKQSG 461
Cdd:PRK09457 377 FGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWN----KPLTgassaAPFGGVGASG 449
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
61-480 |
6.53e-52 |
|
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: 181.93 E-value: 6.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 61 VAERVDLLNAVADGINRRFDDFLAAECADTGKPK--SLASHI-----DIPRGAANFKVFADViKSVPTEFFEMatpdgrG 133
Cdd:cd07136 19 VEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEfeAYMTEIgfvlsEINYAIKHLKKWMKP-KRVKTPLLNF------P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 134 ALNYALRRPVGVVGVICPWNLPLLL-MTWKVGpALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYnVVHGfGPGS 212
Cdd:cd07136 92 SKSYIYYEPYGVVLIIAPWNYPFQLaLAPLIG-AIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA-VVEG-GVEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 213 AGEfvTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEgtmRSVFA---NCGQVCLGT 289
Cdd:cd07136 169 NQE--LLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAK---RIVWGkflNAGQTCVAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 290 ERVYVERPIFDRFVAALKA------GAEGLKlgvpddaSTGMGPLISQEHKNKVLSYYNkarelGATVVTGGGVPqmpge 363
Cdd:cd07136 244 DYVLVHESVKEKFIKELKEeikkfyGEDPLE-------SPDYGRIINEKHFDRLAGLLD-----NGKIVFGGNTD----- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 364 lANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVN 443
Cdd:cd07136 307 -RETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 500090152 444 swflrD-------LRTPFGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:cd07136 386 -----DtimhlanPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
130-484 |
1.33e-51 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 182.26 E-value: 1.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 130 DGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFG 209
Cdd:PLN00412 146 NERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 210 pGSAGEFVTTHPKVNAITFTGeTRTGAAIMKAAadGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGT 289
Cdd:PLN00412 226 -SEIGDFLTMHPGVNCISFTG-GDTGIAISKKA--GMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 290 ERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTgMGPLISQEHKNKVLSYYNKARELGATVVTGGgvpQMPGELangaw 369
Cdd:PLN00412 302 KVVLVMESVADALVEKVNAKVAKLTVGPPEDDCD-ITPVVSESSANFIEGLVMDAKEKGATFCQEW---KREGNL----- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 370 vqptIWTGLDDN-SP---IAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSW 445
Cdd:PLN00412 373 ----IWPLLLDNvRPdmrIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA 448
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 500090152 446 FLR--DlRTPFGGAKQSGIGREGGVHSLEFYTEQKNICIKL 484
Cdd:PLN00412 449 PARgpD-HFPFQGLKDSGIGSQGITNSINMMTKVKSTVINL 488
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
56-463 |
8.35e-48 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 177.36 E-value: 8.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKpkSLASHIDIPRGAANF-KVFADviksvpteffematpDGRGA 134
Cdd:PRK11905 606 WSATPAAERAAILERAADLMEAHMPELFALAVREAGK--TLANAIAEVREAVDFlRYYAA---------------QARRL 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 135 LNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAG 214
Cdd:PRK11905 669 LNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGR-TVG 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 215 EFVTTHPKVNAITFTGETRTGAAIMKA-AADGARPVSL--EMGGKNPAIVfadcDFDAAIEGTMR----SVFANCGQVC- 286
Cdd:PRK11905 748 AALVADPRIAGVMFTGSTEVARLIQRTlAKRSGPPVPLiaETGGQNAMIV----DSSALPEQVVAdviaSAFDSAGQRCs 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 287 -LgteRV-YVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGggvpQMPGEL 364
Cdd:PRK11905 824 aL---RVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQL----PLPAET 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 365 ANGAWVQPTIW--TGLDDnspiAREEIFGPCTLIQPFDAE--DEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLV 440
Cdd:PRK11905 897 EKGTFVAPTLIeiDSISD----LEREVFGPVLHVVRFKADelDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNI 972
|
410 420 430
....*....|....*....|....*....|..
gi 500090152 441 WVNswflrdlRT---------PFGGAKQSGIG 463
Cdd:PRK11905 973 YVN-------RNiigavvgvqPFGGEGLSGTG 997
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
64-483 |
5.10e-47 |
|
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: 168.55 E-value: 5.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 64 RVDLLNAVADGINRRFDDFLAAECADTGKPK--SLASHIDIPRGAANFkvfadVIKSVPteffEMATPD--GRGALN--- 136
Cdd:cd07132 22 RIQQLEALLRMLEENEDEIVEALAKDLRKPKfeAVLSEILLVKNEIKY-----AISNLP----EWMKPEpvKKNLATlld 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 137 --YALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVmnevgMPKGV----YNVVHGfGP 210
Cdd:cd07132 93 dvYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLdkecYPVVLG-GV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 211 GSAGEFVTThpKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTE 290
Cdd:cd07132 167 EETTELLKQ--RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 291 RVYVERPIFDRFVAALKagaEGLK--LGVPDDASTGMGPLISQEHknkvlsyYNKAREL--GATVVTGGGVPQmpgelaN 366
Cdd:cd07132 245 YVLCTPEVQEKFVEALK---KTLKefYGEDPKESPDYGRIINDRH-------FQRLKKLlsGGKVAIGGQTDE------K 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 367 GAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNS-- 444
Cdd:cd07132 309 ERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDti 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 500090152 445 --WFLRDLrtPFGGAKQSGIGREGGVHSLEFYTEQKNICIK 483
Cdd:cd07132 389 mhYTLDSL--PFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
56-476 |
1.13e-46 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 168.94 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKpkSLASHIDIPRGAANF-KVFADVIKSVPTEFFEmatpdgrga 134
Cdd:TIGR01238 90 WNATPAKERAAKLDRLADLLELHMPELMALCVREAGK--TIHNAIAEVREAVDFcRYYAKQVRDVLGEFSV--------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 135 lnyalrRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAG 214
Cdd:TIGR01238 159 ------ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGA-DVG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 215 EFVTTHPKVNAITFTGETRTGAAIMKA-AADGARPVSL--EMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTER 291
Cdd:TIGR01238 232 AALTSDPRIAGVAFTGSTEVAQLINQTlAQREDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRV 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 292 VYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTggGVPQMPGELANGAWVQ 371
Cdd:TIGR01238 312 LCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQ--LTLDDSRACQHGTFVA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 372 PTIWTgLDDNSPIaREEIFGPCTLIQPFDAE--DEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNswflRD 449
Cdd:TIGR01238 390 PTLFE-LDDIAEL-SEEVFGPVLHVVRYKARelDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN----RN 463
|
410 420 430
....*....|....*....|....*....|....
gi 500090152 450 L------RTPFGGAKQSGIG-REGGVHSLEFYTE 476
Cdd:TIGR01238 464 QvgavvgVQPFGGQGLSGTGpKAGGPHYLYRLTQ 497
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
22-477 |
3.01e-46 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 172.69 E-value: 3.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 22 CSPLDNRR-IALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKpkSLASHI 100
Cdd:PRK11904 567 VSPADRRRvVGEVAFADAEQVEQALAAARAAFPA-WSRTPVEERAAILERAADLLEANRAELIALCVREAGK--TLQDAI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 101 DIPRGAANF---------KVFADviksvPTEFfematPDGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGN 171
Cdd:PRK11904 644 AEVREAVDFcryyaaqarRLFGA-----PEKL-----PGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGN 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 172 TVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAI--MKAAADGArPV 249
Cdd:PRK11904 714 TVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGA-TVGAALTADPRIAGVAFTGSTETARIInrTLAARDGP-IV 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 250 SL--EMGGKNPAIVfadcDFDAAIE----GTMRSVFANCGQVC--LgteRV-YVERPIFDRFVAALKAGAEGLKLGVPDD 320
Cdd:PRK11904 792 PLiaETGGQNAMIV----DSTALPEqvvdDVVTSAFRSAGQRCsaL---RVlFVQEDIADRVIEMLKGAMAELKVGDPRL 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 321 ASTGMGPLISQEHKNKVLSYYNKARELGATVVTGggvpQMPGELANGAWVQPTIW--TGLDDnspiAREEIFGPCTLIQP 398
Cdd:PRK11904 865 LSTDVGPVIDAEAKANLDAHIERMKREARLLAQL----PLPAGTENGHFVAPTAFeiDSISQ----LEREVFGPILHVIR 936
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 399 FDAE--DEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNswflrdlRT---------PFGGAKQSGIG-REG 466
Cdd:PRK11904 937 YKASdlDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-------RNqigavvgvqPFGGQGLSGTGpKAG 1009
|
490
....*....|..
gi 500090152 467 GVHSL-EFYTEQ 477
Cdd:PRK11904 1010 GPHYLlRFATEK 1021
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
8-463 |
1.98e-45 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 170.50 E-value: 1.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 8 INGEfVATAKPFDKCSPLDNRRIA-LVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRFDDFLAAE 86
Cdd:COG4230 562 IAGE-AASGEARPVRNPADHSDVVgTVVEATAADVEAALAAAQAAFPA-WSATPVEERAAILERAADLLEAHRAELMALL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 87 CADTGKpkSLASHIDIPRGAANF-KVFADVIKSVptefFEMATPdgrgalnyalRRPVGVVGVICPWNLPLLLMTWKVGP 165
Cdd:COG4230 640 VREAGK--TLPDAIAEVREAVDFcRYYAAQARRL----FAAPTV----------LRGRGVFVCISPWNFPLAIFTGQVAA 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 166 ALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGvynVVHgFGPGsAGEFV----TTHPKVNAITFTGETRTGAAIMKA 241
Cdd:COG4230 704 ALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPAD---VLQ-LLPG-DGETVgaalVADPRIAGVAFTGSTETARLINRT 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 242 -AADGARPVSL--EMGGKNPAIV---------FADCdfdaaiegtMRSVFANCGQVC--LgteRV-YVERPIFDRFVAAL 306
Cdd:COG4230 779 lAARDGPIVPLiaETGGQNAMIVdssalpeqvVDDV---------LASAFDSAGQRCsaL---RVlCVQEDIADRVLEML 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 307 KAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGggvpQMPGELANGAWVQPTIWTgLDDNSPIAR 386
Cdd:COG4230 847 KGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQL----PLPEECANGTFVAPTLIE-IDSISDLER 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 387 eEIFGPCTLIQPFDAE--DEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNswflrdlRT---------PFG 455
Cdd:COG4230 922 -EVFGPVLHVVRYKADelDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN-------RNiigavvgvqPFG 993
|
....*...
gi 500090152 456 GAKQSGIG 463
Cdd:COG4230 994 GEGLSGTG 1001
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
56-443 |
1.33e-44 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 165.30 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSlASHIDIPRGaanFKVFADVIKSVPTEFFEMATPDGRGAL 135
Cdd:PLN02419 167 WRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLK-DSHGDIFRG---LEVVEHACGMATLQMGEYLPNVSNGVD 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 136 NYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHgfGPGSAGE 215
Cdd:PLN02419 243 TYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVH--GTNDTVN 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 216 FVTTHPKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYV- 294
Cdd:PLN02419 321 AICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFv 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 295 --ERPIFDRFVAALKAgaegLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQMPGeLANGAWVQP 372
Cdd:PLN02419 401 gdAKSWEDKLVERAKA----LKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPG-YEKGNFIGP 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500090152 373 TIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVN 443
Cdd:PLN02419 476 TILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
57-480 |
2.81e-42 |
|
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: 155.65 E-value: 2.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 57 GRMTVAE-RVDLLNAVADGINRRFDDFLAAECADTGKP--KSLASHIDIPRGAANF------KVFADVIKSVPTEFFEma 127
Cdd:cd07137 15 GRTRSAEwRKSQLKGLLRLVDENEDDIFAALRQDLGKPsaESFRDEVSVLVSSCKLaikelkKWMAPEKVKTPLTTFP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 128 tpdGRGALnyaLRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVyNVVHG 207
Cdd:cd07137 93 ---AKAEI---VSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAI-KVIEG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 208 fgpgsaGEFVTTH---PKVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANC-G 283
Cdd:cd07137 166 ------GVPETTAlleQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 284 QVCLGTERVYVERPIFDRFVAALKAGAEglKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPqmpge 363
Cdd:cd07137 240 QACIAPDYVLVEESFAPTLIDALKNTLE--KFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERD----- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 364 lANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVN 443
Cdd:cd07137 313 -EKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFN 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 500090152 444 SWFLRDL--RTPFGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:cd07137 392 DTVVQYAidTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
8-461 |
4.64e-42 |
|
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: 156.59 E-value: 4.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 8 INGEFVATAKPFDKCSPLD-NRRIALVHEAGKTEVDAAVAAAQAALKGpWGRMTVAERVDLLNAVADGINRRF-DDFLAA 85
Cdd:cd07123 37 IGGKEVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKE-WARMPFEDRAAIFLKAADLLSGKYrYELNAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 86 ECADTGKP------KSLASHIDIPRGAANF--KVFADVIKSVPTeffematpdgrGALNYALRRPV-GVVGVICPWN--- 153
Cdd:cd07123 116 TMLGQGKNvwqaeiDAACELIDFLRFNVKYaeELYAQQPLSSPA-----------GVWNRLEYRPLeGFVYAVSPFNfta 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 154 ----LPLllmtwkvGPALAcGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPgSAGEFVTTHPKVNAITFT 229
Cdd:cd07123 185 iggnLAG-------APALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGP-VVGDTVLASPHLAGLHFT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 230 GETRTGAAIMKAAADG-------ARPVSlEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRF 302
Cdd:cd07123 256 GSTPTFKSLWKQIGENldryrtyPRIVG-ETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 303 VAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARE-LGATVVTGGGvpqmpGELANGAWVQPTIWTGLDDN 381
Cdd:cd07123 335 KERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSdPEAEIIAGGK-----CDDSVGYFVEPTVIETTDPK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 382 SPIAREEIFGPCTLIQPFDAED--EVIRRANDT-DYGLACSVWTKD------LARAHRVAgqieAGLVWVNswflrDLRT 452
Cdd:cd07123 410 HKLMTEEIFGPVLTVYVYPDSDfeETLELVDTTsPYALTGAIFAQDrkaireATDALRNA----AGNFYIN-----DKPT 480
|
490
....*....|....*.
gi 500090152 453 -------PFGGAKQSG 461
Cdd:cd07123 481 gavvgqqPFGGARASG 496
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
54-445 |
3.62e-38 |
|
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: 144.69 E-value: 3.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 54 GPWGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLASHIDipRGAANFKVFADVIKS--VPTEFFEmATPDG 131
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENIC--GDQVQLRARAFVIYSyrIPHEPGN-HLGQG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 132 RGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVG-MPKGVYNVVHGFGP 210
Cdd:cd07084 90 LKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 211 GSAGefVTTHPKVNAITFTGETRTGAAIMKAAADGarPVSLEMGGKNPAIVFADCD-FDAAIEGTMRSVFANCGQVCLGT 289
Cdd:cd07084 170 TMQA--LLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 290 ERVYV-ERPIFDRFVAALKAGAEGLKLGvpddastgmGPLISQEHKNKVLSYYNKARELGATVVTGGG--VPQMPGELAN 366
Cdd:cd07084 246 SMLFVpENWSKTPLVEKLKALLARRKLE---------DLLLGPVQTFTTLAMIAHMENLLGSVLLFSGkeLKNHSIPSIY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 367 GAWVQPTIWTGLDDN---SPIAREEIFGPCTLIQPF--DAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIE-AGLV 440
Cdd:cd07084 317 GACVASALFVPIDEIlktYELVTEEIFGPFAIVVEYkkDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWvAGRT 396
|
....*
gi 500090152 441 WVNSW 445
Cdd:cd07084 397 YAILR 401
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
142-480 |
6.50e-36 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 139.09 E-value: 6.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 142 PVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVyNVVHGfGPgSAGEFVTTHp 221
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV-KVIEG-GP-AVGEQLLQH- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 222 KVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVfaDC-----DFDAAIEGTMRSVFANC-GQVCLGTERVYVE 295
Cdd:PLN02203 184 KWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIV--DSlsssrDTKVAVNRIVGGKWGSCaGQACIAIDYVLVE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 296 RPIFDRFVAALKAGAEGLkLGVPDDASTGMGPLISQEHKNKvLSYYNKARELGATVVTGGGVPqmpgelANGAWVQPTIW 375
Cdd:PLN02203 262 ERFAPILIELLKSTIKKF-FGENPRESKSMARILNKKHFQR-LSNLLKDPRVAASIVHGGSID------EKKLFIEPTIL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 376 TGLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLRDL--RTP 453
Cdd:PLN02203 334 LNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdSLP 413
|
330 340
....*....|....*....|....*..
gi 500090152 454 FGGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:PLN02203 414 FGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
7-474 |
5.14e-35 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 136.89 E-value: 5.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 7 FINGEFVATAKPFDKCSPLDNRRIALVHEAGKTEVDAAVAAAQAALKgPWGRMTVAERVDLLNAVADGINRRFDDFlaae 86
Cdd:PLN02315 24 YVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAK-IWMQVPAPKRGEIVRQIGDALRAKLDYL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 87 cadtGKPKSLASHIDIPRGAANFKVFADVIK---SVPTEFFEMATPDGRGalNYALRR---PVGVVGVICPWNLPLLLMT 160
Cdd:PLN02315 99 ----GRLVSLEMGKILAEGIGEVQEIIDMCDfavGLSRQLNGSIIPSERP--NHMMMEvwnPLGIVGVITAFNFPCAVLG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 161 WKVGPALACGNTVVVKPSEETP----QTATLLGEVMNEVGMPKGVYNVVhgFGPGSAGEFVTTHPKVNAITFTGETRTGA 236
Cdd:PLN02315 173 WNACIALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIFTSF--CGGAEIGEAIAKDTRIPLVSFTGSSKVGL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 237 AIMKAAADGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLG 316
Cdd:PLN02315 251 MVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 317 VPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQmpgelANGAWVQPTIwTGLDDNSPIAREEIFGPCTLI 396
Cdd:PLN02315 331 DPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE-----SEGNFVQPTI-VEISPDADVVKEELFGPVLYV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 397 QPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQI--EAGLVWVN-SWFLRDLRTPFGGAKQSGIGREGGVHSLEF 473
Cdd:PLN02315 405 MKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLgsDCGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDSWKQ 484
|
.
gi 500090152 474 Y 474
Cdd:PLN02315 485 Y 485
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
56-445 |
3.58e-34 |
|
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: 133.44 E-value: 3.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSLASHiDIPRGAANFKVFADVIKSvpTEFFEM----ATPDG 131
Cdd:cd07129 15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQG-ELGRTTGQLRLFADLVRE--GSWLDAridpADPDR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 132 RGALNYALRR---PVGVVGVICPWNLPLLLMTwkVG----PALACGNTVVVKPSEETPQTATLLGEVMNEV----GMPKG 200
Cdd:cd07129 92 QPLPRPDLRRmlvPLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLPAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 201 VYNVVHGFGPgSAGEFVTTHPKVNAITFTGETRTGAAIMKAAAdgAR----PVSLEMGGKNPAIVFADC---DFDAAIEG 273
Cdd:cd07129 170 VFSLLQGGGR-EVGVALVKHPAIKAVGFTGSRRGGRALFDAAA--ARpepiPFYAELGSVNPVFILPGAlaeRGEAIAQG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 274 TMRSVFANCGQVCLGTERVYVER-PIFDRFVAALKAGAeglklgvpddASTGMGPLISQEhknkVLSYYNKARE-----L 347
Cdd:cd07129 247 FVGSLTLGAGQFCTNPGLVLVPAgPAGDAFIAALAEAL----------AAAPAQTMLTPG----IAEAYRQGVEalaaaP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 348 GATVVTGGGVPqmpgelANGAWVQPTIW-TGLDD--NSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVW--T 422
Cdd:cd07129 313 GVRVLAGGAAA------EGGNQAAPTLFkVDAAAflADPALQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHgeE 386
|
410 420
....*....|....*....|....*
gi 500090152 423 KDLARAHRVAGQIE--AGLVWVNSW 445
Cdd:cd07129 387 DDLALARELLPVLErkAGRLLFNGW 411
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
141-467 |
1.15e-32 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 132.40 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 141 RPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGpGSAGEFVTTH 220
Cdd:PRK11809 767 RPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRG-ETVGAALVAD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 221 PKVNAITFTGETRTGAAIMKAAAD----GARPVSL--EMGGKNPAIVfadcDFDAAIE----GTMRSVFANCGQVCLGTE 290
Cdd:PRK11809 846 ARVRGVMFTGSTEVARLLQRNLAGrldpQGRPIPLiaETGGQNAMIV----DSSALTEqvvaDVLASAFDSAGQRCSALR 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 291 RVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVtgggvpQMP----GELAN 366
Cdd:PRK11809 922 VLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVF------QAArensEDWQS 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 367 GAWVQPTIwTGLDDNSPIAReEIFGPCTLIQPF--DAEDEVIRRANDTDYGLACSVWTK-DLARAHrVAGQIEAGLVWVN 443
Cdd:PRK11809 996 GTFVPPTL-IELDSFDELKR-EVFGPVLHVVRYnrNQLDELIEQINASGYGLTLGVHTRiDETIAQ-VTGSAHVGNLYVN 1072
|
330 340 350
....*....|....*....|....*....|
gi 500090152 444 swflRDL------RTPFGGAKQSGIGREGG 467
Cdd:PRK11809 1073 ----RNMvgavvgVQPFGGEGLSGTGPKAG 1098
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
142-480 |
8.24e-29 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 118.61 E-value: 8.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 142 PVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFGPGSAgefvTTHP 221
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETTA----LLEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 222 KVNAITFTGETRTGAAIMKAAADGARPVSLEMGGKNPAIVFADCDFDAaiegTMRSVFA-----NCGQVCLGTERVYVER 296
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKV----TVRRIIAgkwgcNNGQACISPDYILTTK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 297 PIFDRFVAALKAGAEGLKLGVPDDaSTGMGPLISQEHKNKvLSYYNKARELGATVVTGGGVPQMPGELAngawvqPTIWT 376
Cdd:PLN02174 264 EYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDR-LSKLLDEKEVSDKIVYGGEKDRENLKIA------PTILL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 377 GLDDNSPIAREEIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEAGLVWVNSWFLR-DLRT-PF 454
Cdd:PLN02174 336 DVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHlALHTlPF 415
|
330 340
....*....|....*....|....*.
gi 500090152 455 GGAKQSGIGREGGVHSLEFYTEQKNI 480
Cdd:PLN02174 416 GGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
6-474 |
1.15e-24 |
|
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: 106.97 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 6 NFINGEFVA-TAKPFDKCSPLDNRRIALVHEAGkteVDAAVAAAQAALKG--PWGRMTVAERVDLLNAVADGINRRFDDF 82
Cdd:cd07128 3 SYVAGQWHAgTGDGRTLHDAVTGEVVARVSSEG---LDFAAAVAYAREKGgpALRALTFHERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 83 LAAEcADTGKPKSlASHIDIPRGAANFKVFADVIKS-VPTEFF------EMATPDGRGALNYALRRPVGVVGVICPWNLP 155
Cdd:cd07128 80 YALS-AATGATRR-DSWIDIDGGIGTLFAYASLGRReLPNAHFlvegdvEPLSKDGTFVGQHILTPRRGVAVHINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 156 LLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVG-MPKGVYNVVhgfgPGSAGEFVTTHPKVNAITFTGETRT 234
Cdd:cd07128 158 VWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLI----CGSVGDLLDHLGEQDVVAFTGSAAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 235 GAAIMKAAADGAR--PVSLEMGGKNPAIVFADC-----DFDAAIEGTMRSVFANCGQVCLGTERVYVERPIFDRFVAALK 307
Cdd:cd07128 234 AAKLRAHPNIVARsiRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 308 AGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARElGATVVTGGGVPQMP--GELANGAWVQPTIWTGLD-DNSPI 384
Cdd:cd07128 314 ARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLA-EAEVVFGGPDRFEVvgADAEKGAFFPPTLLLCDDpDAATA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 385 ARE-EIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEA--GLVWVNSwflRDLR-------TPF 454
Cdd:cd07128 393 VHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVLN---RDSAkestghgSPL 469
|
490 500
....*....|....*....|....*.
gi 500090152 455 -----GGAKQSGIGRE-GGVHSLEFY 474
Cdd:cd07128 470 pqlvhGGPGRAGGGEElGGLRGVKHY 495
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
59-474 |
2.06e-23 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 103.25 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 59 MTVAERVDLLNAVADGINRRFDDFLAAECADTGKPKSlASHIDIPRGAANFKVFADVIKSV-PTEFFEMATP-----DGR 132
Cdd:PRK11903 60 LTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRN-DSAVDIDGGIFTLGYYAKLGAALgDARLLRDGEAvqlgkDPA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 133 GALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSeeTPqTATLLGEVMNEVG----MPKGVYNVVHGf 208
Cdd:PRK11903 139 FQGQHVLVPTRGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPA--TA-TAWLTQRMVKDVVaagiLPAGALSVVCG- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 209 gpGSAGEFVTTHPkVNAITFTGETRTGAAIM---KAAADGARpVSLEMGGKNPAIVFADCD-----FDAAIEGTMRSVFA 280
Cdd:PRK11903 215 --SSAGLLDHLQP-FDVVSFTGSAETAAVLRshpAVVQRSVR-VNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 281 NCGQVCLGTERVYVERPIFDRFVAALKAGAEGLKLGVPDDASTGMGPLISQEHKNKVLSYYNKARELGATVVTGGGVPQM 360
Cdd:PRK11903 291 KSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFALV 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 361 PGELANGAWVQPTIWTGLD-DNSPIARE-EIFGPCTLIQPFDAEDEVIRRANDTDYGLACSVWTKDLARAHRVAGQIEA- 437
Cdd:PRK11903 371 DADPAVAACVGPTLLGASDpDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADs 450
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 500090152 438 -GLVWVNSWFLRDLRT------P---FGGAKQSGIGRE-GGVHSLEFY 474
Cdd:PRK11903 451 hGRVHVISPDVAALHTghgnvmPqslHGGPGRAGGGEElGGLRALAFY 498
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
142-443 |
5.69e-15 |
|
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: 77.13 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 142 PVGVVGVICPWNLPlllmTWKVGPA----LACGNTVVVKPSEET----PQTATLLGEVMNEVGM-PKGVYNVVHGFGPGS 212
Cdd:cd07127 193 PRGVALVIGCSTFP----TWNGYPGlfasLATGNPVIVKPHPAAilplAITVQVAREVLAEAGFdPNLVTLAADTPEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 213 AGEFVtTHPKVNAITFTGETRTGAAIMKAAadGARPVSLEMGGKNPAIVFADCDFDAAIEGTMRSVFANCGQVCLGTERV 292
Cdd:cd07127 269 AQTLA-TRPEVRIIDFTGSNAFGDWLEANA--RQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 293 YV---------ERPIFDRFVAALKAGAEGLkLGVPDDASTGMGPLISQEhknkVLSYYNKARELGATVVTGGGV--PQMP 361
Cdd:cd07127 346 YVprdgiqtddGRKSFDEVAADLAAAIDGL-LADPARAAALLGAIQSPD----TLARIAEARQLGEVLLASEAVahPEFP 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 362 gelanGAWVQPTIWTGLD-DNSPIAREEIFGPCTLIQPFDAEDEVIRRANDT--DYG-LACSVWTKD---LARAHRVAGQ 434
Cdd:cd07127 421 -----DARVRTPLLLKLDaSDEAAYAEERFGPIAFVVATDSTDHSIELARESvrEHGaMTVGVYSTDpevVERVQEAALD 495
|
330
....*....|....*.
gi 500090152 435 IEAGL-------VWVN 443
Cdd:cd07127 496 AGVALsinltggVFVN 511
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
130-463 |
2.25e-09 |
|
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: 59.43 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 130 DGRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVHGFG 209
Cdd:cd07126 130 DHQGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 210 PGSAGEFVTTHPKVnaITFTGETRTgaaimkaaadgARPVSLEMGGKnpaIVFADCDFDAAIEG------------TMRS 277
Cdd:cd07126 210 PTMNKILLEANPRM--TLFTGSSKV-----------AERLALELHGK---VKLEDAGFDWKILGpdvsdvdyvawqCDQD 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 278 VFANCGQVC-----LGTERVYVERPIFDRfvaaLKAGAEGLKLgvpDDAStgMGPLIS------QEHKNKVLSYYNKARE 346
Cdd:cd07126 274 AYACSGQKCsaqsiLFAHENWVQAGILDK----LKALAEQRKL---EDLT--IGPVLTwtteriLDHVDKLLAIPGAKVL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 347 LGATVVTGGGVPQMPGELANGAWVQPTIWTGLDDNSPIAREEIFGPCTLIQPFDAEDE--VIRRANDTDYGLACSVWTKD 424
Cdd:cd07126 345 FGGKPLTNHSIPSIYGAYEPTAVFVPLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSND 424
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 500090152 425 LARAHRVAGQIEAGLVWV-----------NSWFlrdlrTPFGGAKQSGIG 463
Cdd:cd07126 425 IRFLQEVLANTVNGTTYAgirarttgapqNHWF-----GPAGDPRGAGIG 469
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
60-331 |
3.25e-09 |
|
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: 58.77 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 60 TVAERVDLLNAVADGINRRFDDFLAAECADTGKP-KSLASHIDIPRGAANFKVFADVIKSVPTEFFEMATPD---GRGAL 135
Cdd:cd07077 14 HDEQRDLIINAIANALYDTRQRLASEAVSERGAYiRSLIANWIAMMGCSESKLYKNIDTERGITASVGHIQDvllPDNGE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 136 NYALRRPVGVVGVICPWNLPLLLMTwKVGPALACGNTVVVKPSEETPQTATLLGEVMNEVGMPKGVYNVVhGFGPGSAGE 215
Cdd:cd07077 94 TYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILV-LYVPHPSDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 216 FVT---THPKVNAITFTGetrtGAAIMKAA--ADGARPVsLEMGGKNPAIVFadcDFDAAIEGTMRSVFANC---GQVCL 287
Cdd:cd07077 172 LAEellSHPKIDLIVATG----GRDAVDAAvkHSPHIPV-IGFGAGNSPVVV---DETADEERASGSVHDSKffdQNACA 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500090152 288 GTERVYVER----PIFDRFvaALKAGAEGLKL-------------GVPDDASTGMGPLISQ 331
Cdd:cd07077 244 SEQNLYVVDdvldPLYEEF--KLKLVVEGLKVpqetkplskettpSFDDEALESMTPLECQ 302
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
141-308 |
3.98e-08 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 55.58 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 141 RPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMNE----VGMPKGVYNVVhgFGPGSAG-E 215
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREaavaAGAPEGLIQWI--EEPSIELtQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 216 FVTTHPKVNAITFTGetrtGAAIMKAAADGARPvSLEMG-GKNPAIVFADCDFDAAIEGTMRS-VFANcGQVCLGTERVY 293
Cdd:cd07122 172 ELMKHPDVDLILATG----GPGMVKAAYSSGKP-AIGVGpGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQSVI 245
|
170
....*....|....*
gi 500090152 294 VERPIFDRFVAALKA 308
Cdd:cd07122 246 VDDEIYDEVRAELKR 260
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
56-310 |
2.77e-03 |
|
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: 39.91 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 56 WGRMTVAERVDLLNAVADGINRRFDDFLAAECADTG----KPKSLASHIdiprgaanfkvfadVIKSVP-TEFFEMATPD 130
Cdd:cd07121 20 YRKCTLADREKIIEAIREALLSNAEELAEMAVEETGmgrvEDKIAKNHL--------------AAEKTPgTEDLTTTAWS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 131 GRGALNYALRRPVGVVGVICPWNLPLLLMTWKVGPALACGNTVVVKPSEETPQTATLLGEVMN----EVGMPKGVYNVVH 206
Cdd:cd07121 86 GDNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINkaiaEAGGPDNLVVTVE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090152 207 GFGPGSAGEFVtTHPKVNAITFTGetrtGAAIMKAA------ADGARPvslemgGKNPAIVFADCDFDAAiegtMRSVFA 280
Cdd:cd07121 166 EPTIETTNELM-AHPDINLLVVTG----GPAVVKAAlssgkkAIGAGA------GNPPVVVDETADIEKA----ARDIVQ 230
|
250 260 270
....*....|....*....|....*....|....*
gi 500090152 281 NCG----QVCLGTERVYVERPIFDRFVAAL-KAGA 310
Cdd:cd07121 231 GASfdnnLPCIAEKEVIAVDSVADYLIAAMqRNGA 265
|
|
| |
