|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
7-450 |
2.16e-149 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 431.14 E-value: 2.16e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 7 FPLADTAEGLTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTIDVDPDGKA 86
Cdd:PRK11856 5 FKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 87 APAAAPSKEEEPAEEEmkplvgygskavvthrrarkgaapaaaptaptapAAPVAAPVAAAPAPAPAKPKGGYVPLAKPP 166
Cdd:PRK11856 85 AAAAEAAPEAPAPEPA----------------------------------PAAAAAAAAAPAAAAAPAAPAAAAAKASPA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 167 VRKLAKDLGVDLHALTGTADGGVITRDDVQ--AAANGSAAPAPVQSVVDSGYDPATRERRVPIKGVRKATAAAMVQSAYT 244
Cdd:PRK11856 131 VRKLARELGVDLSTVKGSGPGGRITKEDVEaaAAAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKRE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 245 APHVTEFLTVDVTPMMEFREKLKKsrefAGVKVTPLTFAAKAVCLAAKRTPDVNAVWDEAAqeIVYKDYVHLGIAAATPR 324
Cdd:PRK11856 211 IPHFTLTDEVDVTALLALRKQLKA----IGVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 325 GLVVPKVRDADSMSLKELAIALTELTDVAREGKTTPAAMLGGTITITNVGVFGVDTGTPIINPGESAILCLGAIKDTPWV 404
Cdd:PRK11856 285 GLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVV 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1039680235 405 VDGEIKVRKVLQLSLSFDHRVVDGQQGSEFLADVGALLADPAVAIT 450
Cdd:PRK11856 365 VDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
15-446 |
2.68e-106 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 325.62 E-value: 2.68e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 15 GLTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTIDVDPDGKAApaaapsk 94
Cdd:PRK11855 129 EITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAA------- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 95 eeepaeeemkplvgygskavvthrrARKGAAPAAAPTAPTAPAAPVAAPVAAAPAPAPAKPKGGYVPLAKPPVRKLAKDL 174
Cdd:PRK11855 202 -------------------------AAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLAREL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 175 GVDLHALTGTADGGVITRDDVQAAANGSAAPAPVQSVVDSGYDPAT---------------RERRVPIKGVRKATAAAMV 239
Cdd:PRK11855 257 GVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAAAAAGGGGlgllpwpkvdfskfgEIETKPLSRIKKISAANLH 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 240 QSAYTAPHVTEFLTVDVTPMMEFREKLKKSREFAGVKVTPLTFAAKAVCLAAKRTPDVNAVWDEAAQEIVYKDYVHLGIA 319
Cdd:PRK11855 337 RSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFA 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 320 AATPRGLVVPKVRDADSMSLKELAIALTELTDVAREGKTTPAAMLGGTITITNVGVFGVDTGTPIINPGESAILCLGAIK 399
Cdd:PRK11855 417 VDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQ 496
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1039680235 400 DTPWVVDGEIKVRKVLQLSLSFDHRVVDGQQGSEFLADVGALLADPA 446
Cdd:PRK11855 497 MKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPR 543
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
238-446 |
1.98e-94 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 283.67 E-value: 1.98e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 238 MVQSAYTAPHVTEFLTVDVTPMMEFREKLKKSREFAGVKVTPLTFAAKAVCLAAKRTPDVNAVWDEAAQEIVYKDYVHLG 317
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 318 IAAATPRGLVVPKVRDADSMSLKELAIALTELTDVAREGKTTPAAMLGGTITITNVGVFGVDTGTPIINPGESAILCLGA 397
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039680235 398 IKDTPWVVDGEIKVRKVLQLSLSFDHRVVDGQQGSEFLADVGALLADPA 446
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPE 209
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
13-446 |
1.52e-82 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 260.15 E-value: 1.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 13 AEGLTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTIDVdpdgkaapaaap 92
Cdd:PRK05704 11 PESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDE------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 93 skeeepaeeemkplvgyGSKAVvthrrarkgaapaaaptAPTAPAAPVAAPVAAAPAPAPAKPKGGYVPLAKPPVRKLAK 172
Cdd:PRK05704 79 -----------------GAAAG-----------------AAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 173 DLGVDLHALTGTADGGVITRDDVQAAANGSAAPA----PVQSVVDSGYDPATRERRVPIKGVRKATAAAMVQSAYTAPHV 248
Cdd:PRK05704 125 ENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPaapaAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAML 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 249 TEFLTVDVTPMMEFREKLKKSREFA-GVKVTPLTFAAKAVCLAAKRTPDVNAVWDeaAQEIVYKDYVHLGIAAATPRGLV 327
Cdd:PRK05704 205 TTFNEVDMTPVMDLRKQYKDAFEKKhGVKLGFMSFFVKAVVEALKRYPEVNASID--GDDIVYHNYYDIGIAVGTPRGLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 328 VPKVRDADSMSLKELAIALTELTDVAREGKTTPAAMLGGTITITNVGVFGVDTGTPIINPGESAILCLGAIKDTPWVVDG 407
Cdd:PRK05704 283 VPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNG 362
|
410 420 430
....*....|....*....|....*....|....*....
gi 1039680235 408 EIKVRKVLQLSLSFDHRVVDGQQGSEFLADVGALLADPA 446
Cdd:PRK05704 363 QIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPE 401
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
11-447 |
1.99e-81 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 256.97 E-value: 1.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 11 DTAEGLTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTI--DVDPDGKAAP 88
Cdd:TIGR01347 7 ELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILeeGNDATAAPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 89 AAAPSKEEEPAEEEMKplvgygSKAVVTHRrarkgaapaaaptaptapaapvaapvaaapapapakpkggyvPLAKPPVR 168
Cdd:TIGR01347 87 KSGEEKEETPAASAAA------APTAAANR------------------------------------------PSLSPAAR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 169 KLAKDLGVDLHALTGTADGGVITRDDV--QAAANGSAAPAPVQSVVDSGYDPATRERRVPIKGVRKATAAAMVQSAYTAP 246
Cdd:TIGR01347 119 RLAKEHGIDLSAVPGTGVTGRVTKEDIikKTEAPASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 247 HVTEFLTVDVTPMMEFREKLKKSREFA-GVKVTPLTFAAKAVCLAAKRTPDVNAVWDeaAQEIVYKDYVHLGIAAATPRG 325
Cdd:TIGR01347 199 MLTTFNEVDMSAVMELRKRYKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEID--GDDIVYKDYYDISVAVSTDRG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 326 LVVPKVRDADSMSLKELAIALTELTDVAREGKTTPAAMLGGTITITNVGVFGVDTGTPIINPGESAILCLGAIKDTPWVV 405
Cdd:TIGR01347 277 LVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAV 356
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1039680235 406 DGEIKVRKVLQLSLSFDHRVVDGQQGSEFLADVGALLADPAV 447
Cdd:TIGR01347 357 NGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRR 398
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
15-444 |
7.43e-77 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 251.46 E-value: 7.43e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 15 GLTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTIDVDpdgkaapaaapsk 94
Cdd:PRK11854 215 GGDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVE------------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 95 eeepaeeemkplvgyGSKAVvthrrARKGAAPAAAPTAPTAPAAPVAAPVAAAPAPAPAKPKGGYVPLAKPPVRKLAKDL 174
Cdd:PRK11854 282 ---------------GAAPA-----AAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREF 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 175 GVDLHALTGTADGGVITRDDVQAAANGSAAPAPVQSVVDSG------------YDPATRERR--VPIKGVRKATAAAMVQ 240
Cdd:PRK11854 342 GVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAAAAAggggpgllpwpkVDFSKFGEIeeVELGRIQKISGANLHR 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 241 SAYTAPHVTEFLTVDVTPMMEFReKLKKSREFA---GVKVTPLTFAAKAVCLAAKRTPDVNAVWDEAAQEIVYKDYVHLG 317
Cdd:PRK11854 422 NWVMIPHVTQFDKADITELEAFR-KQQNAEAEKrklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIG 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 318 IAAATPRGLVVPKVRDADSMSLKELAIALTELTDVAREGKTTPAAMLGGTITITNVGVFGVDTGTPIINPGESAILCLGA 397
Cdd:PRK11854 501 IAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSK 580
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1039680235 398 IKDTPwVVDG-EIKVRKVLQLSLSFDHRVVDGQQGSEFLADVGALLAD 444
Cdd:PRK11854 581 SAMEP-VWNGkEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
13-447 |
2.17e-73 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 236.50 E-value: 2.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 13 AEGLTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTIDVDPDGKAAPAAAP 92
Cdd:PTZ00144 53 GDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAAPAAA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 93 SKEEEPAEEEMKPlvgygskavvthrrarkgaapaaaptaptapaapvaapvaaAPAPAPAKPKGGYVPLAKPPVRKLAK 172
Cdd:PTZ00144 133 AAAKAEKTTPEKP-----------------------------------------KAAAPTPEPPAASKPTPPAAAKPPEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 173 dlgvdlhaltgtadggvitrddvqaaangSAAPAPVQSVVDSGyDPatRERRVPIKGVRKATAAAMVQSAYTAPHVTEFL 252
Cdd:PTZ00144 172 -----------------------------APAAKPPPTPVARA-DP--RETRVPMSRMRQRIAERLKASQNTCAMLTTFN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 253 TVDVTPMMEFREKLKKS-REFAGVKVTPLTFAAKAVCLAAKRTPDVNAVWDEaaQEIVYKDYVHLGIAAATPRGLVVPKV 331
Cdd:PTZ00144 220 ECDMSALMELRKEYKDDfQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDG--DEIVYRNYVDISVAVATPTGLVVPVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 332 RDADSMSLKELAIALTELTDVAREGKTTPAAMLGGTITITNVGVFGVDTGTPIINPGESAILCLGAIKDTPWVVDGEIKV 411
Cdd:PTZ00144 298 RNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVI 377
|
410 420 430
....*....|....*....|....*....|....*.
gi 1039680235 412 RKVLQLSLSFDHRVVDGQQGSEFLADVGALLADPAV 447
Cdd:PTZ00144 378 RPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPAR 413
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
15-445 |
3.49e-73 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 239.78 E-value: 3.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 15 GLTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTIDVDPDGKAAPAAAPSK 94
Cdd:TIGR01348 126 DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPATAPAPASA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 95 EEEPAEEEMKPLVGYGSKAvvthrrarkgaapaaaptaptapaapvAAPVAAAPAPAPAKPKGGYVPLAKPPVRKLAKDL 174
Cdd:TIGR01348 206 QPAAQSPAATQPEPAAAPA---------------------------AAKAQAPAPQQAGTQNPAKVDHAAPAVRRLAREF 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 175 GVDLHALTGTADGGVITRDDVQAAANGSAAPAPVQSVVDSGYDPATRE------------RRVPIKGVRKATAAAMVQSA 242
Cdd:TIGR01348 259 GVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALPwpnvdfskfgevEEVDMSRIRKISGANLTRNW 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 243 YTAPHVTEFLTVDVTPMMEFREKLKKSREFAGVKVTPLTFAAKAVCLAAKRTPDVNAVWDEAAQEIVYKDYVHLGIAAAT 322
Cdd:TIGR01348 339 TMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDT 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 323 PRGLVVPKVRDADSMSLKELAIALTELTDVAREGKTTPAAMLGGTITITNVGVFGVDTGTPIINPGESAILCLGAIKDTP 402
Cdd:TIGR01348 419 PNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEP 498
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1039680235 403 wVVDG-EIKVRKVLQLSLSFDHRVVDGQQGSEFLADVGALLADP 445
Cdd:TIGR01348 499 -VWNGkEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADI 541
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
7-428 |
2.46e-62 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 207.65 E-value: 2.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 7 FPLADTAEGLTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTIDVDPDGKA 86
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 87 APAAAPSKEEEPAEEEMKPLVGYGSkavvTHRRArkgaapaaaptaptapaapvaapvaaapapapakpkggyvpLAKPP 166
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGS----NLSGV-----------------------------------------LSTPA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 167 VRKLAKDLGVDLHALTGTADGGVITRDDV----------QAAANGSAAPAPVQSVVDSGYDPAT----RERRVPIKGVRK 232
Cdd:PLN02528 116 VRHLAKQYGIDLNDILGTGKDGRVLKEDVlkyaaqkgvvKDSSSAEEATIAEQEEFSTSVSTPTeqsyEDKTIPLRGFQR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 233 ATAAAMVQSAyTAPHVTEFLTVDVTPMMEFREKLKKSREFAGVKVTPLTFAAKAVCLAAKRTPDVNAVWDEAAQEIVYKD 312
Cdd:PLN02528 196 AMVKTMTAAA-KVPHFHYVEEINVDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 313 YVHLGIAAATPRGLVVPKVRDADSMSLKELAIALTELTDVAREGKTTPAAMLGGTITITNVGVFGVDTGTPIINPGESAI 392
Cdd:PLN02528 275 SHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAI 354
|
410 420 430
....*....|....*....|....*....|....*..
gi 1039680235 393 LCLGAIKDTPWVVD-GEIKVRKVLQLSLSFDHRVVDG 428
Cdd:PLN02528 355 IALGRIQKVPRFVDdGNVYPASIMTVTIGADHRVLDG 391
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
165-445 |
4.26e-52 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 178.95 E-value: 4.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 165 PPVRKLAKDLGVDLHALTGTADGGVITRDDVQAAANGSAAPAPVQS--------VVDSGYDPATRERRVPIKGVRKATAA 236
Cdd:PRK14843 53 PLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSpaqiekveEVPDNVTPYGEIERIPMTPMRKVIAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 237 AMVQSAYTAPHVTEFLTVDVTPMMEFREK-LKKSREFAGVKVTPLTFAAKAVCLAAKRTPDVNAVWDEAAQEIVYKDYVH 315
Cdd:PRK14843 133 RMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 316 LGIAAATPRGLVVPKVRDADSMSLKELAIALTELTDVAREGKTTPAAMLGGTITITNVGVFGVDTGTPIINPGESAILCL 395
Cdd:PRK14843 213 LAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGV 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1039680235 396 GAIKDTPWVVDGEIKVRKVLQLSLSFDHRVVDGQQGSEFLADVGALLADP 445
Cdd:PRK14843 293 SSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETP 342
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
162-447 |
3.93e-50 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 172.29 E-value: 3.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 162 LAKPPVRKLAKDLGVDLHALTGTADGGVITRDDVQ--------AAANGSAAPAPVQSVVDSGYDPA-----TRERRVPIK 228
Cdd:PRK11857 3 LATPIARALAKKLGIDISLLKGSGRDGKILAEDVEnfikslksAPTPAEAASVSSAQQAAKTAAPAaappkLEGKREKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 229 GVRKATAAAMVQSAYTAPHVTEFLTVDVTPMMEFREKLKKS-REFAGVKVTPLTFAAKAVCLAAKRTPDVNAVWDEAAQE 307
Cdd:PRK11857 83 PIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEATSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 308 IVYKDYVHLGIAAATPRGLVVPKVRDADSMSLKELAIALTELTDVAREGKTTPAAMLGGTITITNVGVFGVDTGTPIINP 387
Cdd:PRK11857 163 LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINY 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 388 GESAILCLGAIKDTPWVVDGEIKVRKVLQLSLSFDHRVVDGQQGSEFLADVGALLADPAV 447
Cdd:PRK11857 243 PELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEI 302
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
13-445 |
2.83e-49 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 174.56 E-value: 2.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 13 AEGLTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTIDVDPDGKAAPAAAP 92
Cdd:PLN02226 100 GESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQVTPSQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 93 SKEEEPAEEEMKPLVGYGSKAVVTHRRARKgaapaaaptaptapaapvaapvaaapapapakPKGgyvPLAKPPvrklak 172
Cdd:PLN02226 180 KIPETTDPKPSPPAEDKQKPKVESAPVAEK--------------------------------PKA---PSSPPP------ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 173 dlgvdlhaltgtadggvitrddvqaaangsaapaPVQSVVDSGYDPATRERRVPIKGVRKATAAAMVQSAYTAPHVTEFL 252
Cdd:PLN02226 219 ----------------------------------PKQSAKEPQLPPKERERRVPMTRLRKRVATRLKDSQNTFALLTTFN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 253 TVDVTPMMEFREKLKKS-REFAGVKVTPLTFAAKAVCLAAKRTPDVNAVWDeaAQEIVYKDYVHLGIAAATPRGLVVPKV 331
Cdd:PLN02226 265 EVDMTNLMKLRSQYKDAfYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVID--GDDIIYRDYVDISIAVGTSKGLVVPVI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 332 RDADSMSLKELAIALTELTDVAREGKTTPAAMLGGTITITNVGVFGVDTGTPIINPGESAILCLGAIKDTPWVVDGEIKV 411
Cdd:PLN02226 343 RGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVP 422
|
410 420 430
....*....|....*....|....*....|....
gi 1039680235 412 RKVLQLSLSFDHRVVDGQQGSEFLADVGALLADP 445
Cdd:PLN02226 423 RPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDP 456
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
16-445 |
6.28e-42 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 155.78 E-value: 6.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 16 LTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPG-QTVEVGAPI-LTIDVDPDGKAAPAAAPS 93
Cdd:PLN02744 124 MTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIaITVEEEEDIGKFKDYKPS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 94 KEEEPAEEEMKPlvgygskavvthrrarkgaapaAAPTAPTAPAAPVAAPVAAAPAPAPAKPKGGYVPLAKPPVRKLAKD 173
Cdd:PLN02744 204 SSAAPAAPKAKP----------------------SPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAED 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 174 LGVDLHALTGTADGGVITRDDVQAAANGSAAPAPVQSVVDSGYdPATRERRVPIKGVRKATAAAMVQSAYTAPHVteFLT 253
Cdd:PLN02744 262 NNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKA-PALDYTDIPNTQIRKVTASRLLQSKQTIPHY--YLT 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 254 VD--VTPMMEFREKLKKSREFAGVKVTPLT-FAAKAVCLAAKRTPDVNAVW-DEAAQEivYKDyVHLGIAAATPRGLVVP 329
Cdd:PLN02744 339 VDtrVDKLMALRSQLNSLQEASGGKKISVNdLVIKAAALALRKVPQCNSSWtDDYIRQ--YHN-VNINVAVQTENGLYVP 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 330 KVRDADSMSLKELAIALTELTDVAREGKTTPAAMLGGTITITNV-GVFGVDTGTPIINPGESAILCLGAIKD--TPWVVD 406
Cdd:PLN02744 416 VVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKrvIPGSGP 495
|
410 420 430
....*....|....*....|....*....|....*....
gi 1039680235 407 GEIKVRKVLQLSLSFDHRVVDGQQGSEFLADVGALLADP 445
Cdd:PLN02744 496 DQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENP 534
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
14-78 |
5.73e-22 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 89.36 E-value: 5.73e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039680235 14 EGLTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTI 78
Cdd:COG0508 12 ESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
7-78 |
3.50e-21 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 87.07 E-value: 3.50e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039680235 7 FPLADTAEGLTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTI 78
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
217-442 |
1.09e-19 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 92.26 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 217 DPATRERRVPIKGVRKATAAAMVQSaYTAPHVTEFLTVDVTPMMEFR----EKLKKSRefaGVKVTPLTFAAKAVCLAAK 292
Cdd:PRK12270 110 AAAVEDEVTPLRGAAAAVAKNMDAS-LEVPTATSVRAVPAKLLIDNRivinNHLKRTR---GGKVSFTHLIGYALVQALK 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 293 RTPDVNAVWDEAA--QEIVYKDYVHLGIAAATP-----RGLVVPKVRDADSMSLKELAIALTELTDVAREGKTTPAAMLG 365
Cdd:PRK12270 186 AFPNMNRHYAEVDgkPTLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 366 GTITITNVGVFGVDTGTPIINPGESAILCLGAIkDTPWVVDG-------EIKVRKVLQLSLSFDHRVVDGQQGSEFLADV 438
Cdd:PRK12270 266 TTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGaseerlaELGISKVMTLTSTYDHRIIQGAESGEFLRTI 344
|
....
gi 1039680235 439 GALL 442
Cdd:PRK12270 345 HQLL 348
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
5-78 |
2.25e-13 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 64.93 E-value: 2.25e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039680235 5 KHFPLADTAEGLTEAdIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTI 78
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
15-84 |
3.28e-13 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 71.57 E-value: 3.28e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 15 GLTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTIDVDPDG 84
Cdd:PRK11854 11 GADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGA 80
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
17-75 |
1.76e-11 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 65.35 E-value: 1.76e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039680235 17 TEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPI 75
Cdd:PRK14875 15 TEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
161-196 |
3.76e-10 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 54.61 E-value: 3.76e-10
10 20 30
....*....|....*....|....*....|....*.
gi 1039680235 161 PLAKPPVRKLAKDLGVDLHALTGTADGGVITRDDVQ 196
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
21-78 |
1.59e-09 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 53.96 E-value: 1.59e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 21 IIAWQVKPGDTVTVNQIVVEVETAKaaVELPI--PWAGVVTELLVEPGQTVEVGAPILTI 78
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMK--MENEVtaPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
26-79 |
2.16e-08 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 52.59 E-value: 2.16e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1039680235 26 VKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTID 79
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
8-78 |
1.02e-07 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 48.98 E-value: 1.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039680235 8 PLADTAEGLTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTI 78
Cdd:cd06663 3 LIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
26-78 |
4.99e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 48.69 E-value: 4.99e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1039680235 26 VKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTI 78
Cdd:PRK09282 538 VKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
26-78 |
2.87e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 43.65 E-value: 2.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1039680235 26 VKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTI 78
Cdd:PRK06549 77 VAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITI 129
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
16-78 |
1.26e-04 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 44.14 E-value: 1.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039680235 16 LTEADIIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPG-QTVEVGAPILTI 78
Cdd:PRK11892 14 MEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVL 77
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
26-78 |
3.01e-04 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 43.00 E-value: 3.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1039680235 26 VKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTI 78
Cdd:PRK14040 540 VTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
26-72 |
1.03e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 41.60 E-value: 1.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1039680235 26 VKPGDTVTVNQIVVEVETAK--AAVELPIpwAGVVTELLVEPGQTVEVG 72
Cdd:COG1038 1092 VKEGDEVKKGDPLLTIEAMKmeTTITAPR--DGTVKEVLVKEGDQVEAG 1138
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
26-78 |
1.15e-03 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 39.46 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1039680235 26 VKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTI 78
Cdd:PRK05641 100 VREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
21-80 |
2.64e-03 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 40.09 E-value: 2.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039680235 21 IIAWQVKPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTIDV 80
Cdd:PRK14042 536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVEV 595
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
27-60 |
4.84e-03 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 37.03 E-value: 4.84e-03
10 20 30
....*....|....*....|....*....|....
gi 1039680235 27 KPGDTVTVNQIVVEVETAKAAVELPIPWAGVVTE 60
Cdd:COG0509 46 EVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVE 79
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
20-72 |
6.10e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 39.35 E-value: 6.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1039680235 20 DIIAWQVKPGDTVTVNQIVVEVETAK--AAVELPIpwAGVVTELLVEPGQTVEVG 72
Cdd:PRK12999 1086 SVVTVLVKEGDEVKAGDPLAVIEAMKmeTTITAPV--DGTVKRVLVKAGDQVEAG 1138
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
29-79 |
6.94e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 35.37 E-value: 6.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1039680235 29 GDTVTVNQIVVEVETAKAAVELPIPWAGVVTELLVEPGQTVEVGAPILTID 79
Cdd:PRK07051 29 GDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| |
