|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-468 |
2.53e-140 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 408.80 E-value: 2.53e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTIDDGSDDQPEE 80
Cdd:PRK11856 7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAEAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 81 EPEflvghltaesgrrrrrrrgaavSAERAPEKAPqtptlktgpetdvEPVPEPVQPTQPRRQDPPRMDRAGHVLAKPPA 160
Cdd:PRK11856 87 AAE----------------------AAPEAPAPEP-------------APAAAAAAAAAPAAAAAPAAPAAAAAKASPAV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 161 RRLAADLGIDLSTVTGTGPQGAVTRSDVKAAAEAGRQAAPEPPVVGASAgdaefatlsvmsrrllggaPTEPDGHTRRVP 240
Cdd:PRK11856 132 RKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAAP-------------------PAAAAEGEERVP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 241 VRGVRKVTAKAMKDSLDTKALVTAFLTCDVTPTMDLVARLRAdrrfKGLRVSPLTIWCKAVCLAMGRTPVVNARWDDaaD 320
Cdd:PRK11856 193 LSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKA----IGVKLTVTDFLIKAVALALKKFPELNASWDD--D 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 321 QIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVFGLDAGTPVVN 400
Cdd:PRK11856 267 AIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIIN 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488475828 401 RTESAILVLGTIARRPWVVgtgdDEEVVPRWVTTMSLGFDHRLIDGEEGSTFLHDVAEILSDPASAML 468
Cdd:PRK11856 347 PPEVAILGVGAIVERPVVV----DGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1-468 |
2.28e-101 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 313.68 E-value: 2.28e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPGEgLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTIDdgsddqpee 80
Cdd:PRK11855 124 VPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE--------- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 81 epeflvghltaesgrrrrrrrgaavSAERAPEKAPQTPTLKTGPETDVEPVPEPVQPTQPRRQDPPRMDRAGHV-LAKPP 159
Cdd:PRK11855 194 -------------------------VAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKApHASPA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 160 ARRLAADLGIDLSTVTGTGPQGAVTRSDVKAAAEAGRQAAPEPPVVGASAGDAEFATLSVMSrrllggAPTEPDGHTRRV 239
Cdd:PRK11855 249 VRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAAAAAGGGGLGLLPWPK------VDFSKFGEIETK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 240 PVRGVRKVTAKAMKDSLDTKALVTAFLTCDVTPTMDLVARLRADRRFKGLRVSPLTIWCKAVCLAMGRTPVVNARWDDAA 319
Cdd:PRK11855 323 PLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDG 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 320 DQIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVFGLDAGTPVV 399
Cdd:PRK11855 403 DELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPII 482
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 400 NRTESAILVLGTIARRP-WvvgtgDDEEVVPRWVTTMSLGFDHRLIDGEEGSTFLHDVAEILSDPASAML 468
Cdd:PRK11855 483 NAPEVAILGVGKSQMKPvW-----DGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
2-468 |
9.13e-85 |
|
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: 266.21 E-value: 9.13e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 2 PDPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTIDDGSDdqpeee 81
Cdd:TIGR01347 6 PELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGND------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 82 peflvghltaesgrrrrrrRGAAVSAERAPEKApqtptlktgpetdvEPVPEPVQPTQPRRQDPPRmdraghvlAKPPAR 161
Cdd:TIGR01347 80 -------------------ATAAPPAKSGEEKE--------------ETPAASAAAAPTAAANRPS--------LSPAAR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 162 RLAADLGIDLSTVTGTGPQGAVTRSDVkaAAEAGRQAAPEPPVVGASAGDAEFATLSVmsrrllggaptepdghtRRVPV 241
Cdd:TIGR01347 119 RLAKEHGIDLSAVPGTGVTGRVTKEDI--IKKTEAPASAQPPAAAAAAAAPAAATRPE-----------------ERVKM 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 242 RGVRKVTAKAMKDSLDTKALVTAFLTCDVTPTMDLVARLRaDRRFK--GLRVSPLTIWCKAVCLAMGRTPVVNARWDDaa 319
Cdd:TIGR01347 180 TRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYK-EEFEKkhGVKLGFMSFFVKAVVAALKRFPEVNAEIDG-- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 320 DQIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVFGLDAGTPVV 399
Cdd:TIGR01347 257 DDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPII 336
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488475828 400 NRTESAILVLGTIARRPWVVgtgdDEEVVPRWVTTMSLGFDHRLIDGEEGSTFLHDVAEILSDPASAML 468
Cdd:TIGR01347 337 NPPQSAILGMHGIKERPVAV----NGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
2-468 |
2.81e-78 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 249.37 E-value: 2.81e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 2 PDPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTIDDGsddqpeee 81
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEG-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 82 peflvghltaesgrrrrrrrGAAVSAERAPEKAPQTPTlktgpetdvEPVPEPVQPTQPRRQDPprmdraghvlAKPPAR 161
Cdd:PRK05704 80 --------------------AAAGAAAAAAAAAAAAAA---------APAQAQAAAAAEQSNDA----------LSPAAR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 162 RLAADLGIDLSTVTGTGPQGAVTRSDVKAAAEAGRQAAPEPPVVGASAgdaefatlsvmSRRLLGGAPTEpdghtrRVPV 241
Cdd:PRK05704 121 KLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAAPAA-----------APAPLGARPEE------RVPM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 242 RGVRKVTAKAMKDSLDTKALVTAFLTCDVTPTMDLVARlRADRRFK--GLRVSPLTIWCKAVCLAMGRTPVVNARWDDaa 319
Cdd:PRK05704 184 TRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQ-YKDAFEKkhGVKLGFMSFFVKAVVEALKRYPEVNASIDG-- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 320 DQIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVFGLDAGTPVV 399
Cdd:PRK05704 261 DDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPII 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488475828 400 NRTESAILVLGTIARRPWVVgtgdDEEVVPRWVTTMSLGFDHRLIDGEEGSTFLHDVAEILSDPASAML 468
Cdd:PRK05704 341 NPPQSAILGMHKIKERPVAV----NGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
252-467 |
9.40e-76 |
|
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: 236.29 E-value: 9.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 252 MKDSLDTKALVTAFLTCDVTPTMDLVARLRADRRFKGLRVSPLTIWCKAVCLAMGRTPVVNARWDDAADQIVFRDQINLG 331
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 332 IAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVFGLDAGTPVVNRTESAILVLGT 411
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488475828 412 IARRPWVVgtgdDEEVVPRWVTTMSLGFDHRLIDGEEGSTFLHDVAEILSDPASAM 467
Cdd:pfam00198 161 IRKRPVVV----DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
2-464 |
2.37e-73 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 237.27 E-value: 2.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 2 PDPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTIDDGsddqpeee 81
Cdd:PTZ00144 50 PTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTG-------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 82 peflvghltaesgrrrrrrrgaavsaERAPEKAPQTPTLKTgPETDVEPVPEPVQPTQPRRQDPprmdraghvlaKPPAR 161
Cdd:PTZ00144 122 --------------------------GAPPAAAPAAAAAAK-AEKTTPEKPKAAAPTPEPPAAS-----------KPTPP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 162 RLAAdlgidlstvtgtgpqgavtrsdvkaaaeagrqaAPEPPVVGASAgdaefatLSVMSRRLlggaPTEpdghtRRVPV 241
Cdd:PTZ00144 164 AAAK---------------------------------PPEPAPAAKPP-------PTPVARAD----PRE-----TRVPM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 242 RGVRKVTAKAMKDSLDTKALVTAFLTCDVTPTMDLVARLRADRRFK-GLRVSPLTIWCKAVCLAMGRTPVVNARWDDaaD 320
Cdd:PTZ00144 195 SRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKhGVKLGFMSAFVKASTIALKKMPIVNAYIDG--D 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 321 QIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVFGLDAGTPVVN 400
Cdd:PTZ00144 273 EIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIIN 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488475828 401 RTESAILVLGTIARRPWVVGtgddEEVVPRWVTTMSLGFDHRLIDGEEGSTFLHDVAEILSDPA 464
Cdd:PTZ00144 353 PPQSAILGMHAIKKRPVVVG----NEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPA 412
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
3-468 |
7.09e-68 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 222.67 E-value: 7.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 3 DPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTIDDGSDDQPEEEP 82
Cdd:PLN02528 5 QTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRSDS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 83 eflvghltaesgrrrrrrrgaavsaerapekaPQTPTLKTGPETDVEPVPEPVQPtqprrqdpprmdraGHVLAKPPARR 162
Cdd:PLN02528 85 --------------------------------LLLPTDSSNIVSLAESDERGSNL--------------SGVLSTPAVRH 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 163 LAADLGIDLSTVTGTGPQGAVTRSDVkAAAEAGRQAAPEPPVVGASAGDAEFATLSVMSrrllggAPTEPDGHTRRVPVR 242
Cdd:PLN02528 119 LAKQYGIDLNDILGTGKDGRVLKEDV-LKYAAQKGVVKDSSSAEEATIAEQEEFSTSVS------TPTEQSYEDKTIPLR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 243 GVRKVTAKAMKDSldtkALVTAF-----LTCDVTptMDLVARLRADRRFKGLRVSPLTIWCKAVCLAMGRTPVVNARWDD 317
Cdd:PLN02528 192 GFQRAMVKTMTAA----AKVPHFhyveeINVDAL--VELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNE 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 318 AADQIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVFGLDAGTP 397
Cdd:PLN02528 266 ETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSP 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488475828 398 VVNRTESAILVLGTIARRPWVVgtgDDEEVVPRWVTTMSLGFDHRLIDGEEGSTFLHDVAEILSDPASAML 468
Cdd:PLN02528 346 VLNLPEVAIIALGRIQKVPRFV---DDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLML 413
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1-462 |
3.08e-64 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 218.72 E-value: 3.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPGegLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTIDDGsddqpee 80
Cdd:PRK11854 211 VPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVE------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 81 epeflvghltaesgrrrrrrrGAAVSAERAPEKAPQTPtlktgPETDVEPVPEPvQPTQPRRQDPPRMDRAGHVLAKPPA 160
Cdd:PRK11854 282 ---------------------GAAPAAAPAKQEAAAPA-----PAAAKAEAPAA-APAAKAEGKSEFAENDAYVHATPLV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 161 RRLAADLGIDLSTVTGTGPQGAVTRSDVKAAAEAGRQAAPEPPVVGASAGDAEfatlsvmsrRLLGGAPTEPD--GHTRR 238
Cdd:PRK11854 335 RRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAAAAAGGGGP---------GLLPWPKVDFSkfGEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 239 VPVRGVRKVTAKAMKDSLDTKALVTAFLTCDVTptmdLVARLR------ADRRFKGLRVSPLTIWCKAVCLAMGRTPVVN 312
Cdd:PRK11854 406 VELGRIQKISGANLHRNWVMIPHVTQFDKADIT----ELEAFRkqqnaeAEKRKLGVKITPLVFIMKAVAAALEQMPRFN 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 313 ARWDDAADQIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVFGL 392
Cdd:PRK11854 482 SSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGT 561
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488475828 393 DAGTPVVNRTESAILVLGTIARRP-WvvgtgDDEEVVPRWVTTMSLGFDHRLIDGEEGSTFLHDVAEILSD 462
Cdd:PRK11854 562 THFTPIVNAPEVAILGVSKSAMEPvW-----NGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1-468 |
2.05e-63 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273567 [Multi-domain] Cd Length: 436 Bit Score: 211.58 E-value: 2.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAK-LCAEPGETVAVGEPL-VTIDDGSDDqp 78
Cdd:TIGR01349 4 MPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKiLVPEGTKDVPVNKPIaVLVEEKEDV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 79 eeepEFLVGHLTAESGRRrrrrrGAAVSAERAPeKAPQTPTLKTgpetdvePVPEPVQPTQPRRQDPPRMDRAGHVLAKP 158
Cdd:TIGR01349 82 ----ADAFKNYKLESSAS-----PAPKPSEIAP-TAPPSAPKPS-------PAPQKQSPEPSSPAPLSDKESGDRIFASP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 159 PARRLAADLGIDLSTVTGTGPQGAVTRSDVKAAaeagrqaapePPVVGASAGDAEFATLSVMSRRLlggAPTEPdGHTRR 238
Cdd:TIGR01349 145 LAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESF----------VPQSPASANQQAAATTPATYPAA---APVST-GSYED 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 239 VPVRGVRKVTAKAMKDSLDTKALVTAFLTCDVTPTMDLVARLRA--DRRFKgLRVSPLTIwcKAVCLAMGRTPVVNARWD 316
Cdd:TIGR01349 211 VPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAmaSEVYK-LSVNDFII--KASALALREVPEANSSWT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 317 DaaDQIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVFGLDAGT 396
Cdd:TIGR01349 288 D--NFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFT 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488475828 397 PVVNRTESAILVLGTIARRPwVVGTGDDEEVVPRWVTTMSLGFDHRLIDGEEGSTFLHDVAEILSDPASAML 468
Cdd:TIGR01349 366 AIINPPQACILAVGAVEDVA-VVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1-463 |
2.20e-62 |
|
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: 212.04 E-value: 2.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPGeGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTIDdgsddqpee 80
Cdd:TIGR01348 121 VPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLS--------- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 81 epeflvghltaesgrrrrrRRGAAVSAERAPEKA-PQTPTlktgPETDVEPVPEPVQPTQ---PRRQDPPRMDRAGHVLA 156
Cdd:TIGR01348 191 -------------------VAGSTPATAPAPASAqPAAQS----PAATQPEPAAAPAAAKaqaPAPQQAGTQNPAKVDHA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 157 KPPARRLAADLGIDLSTVTGTGPQGAVTRSDVKAAAEAGRQAAPEPPVvGASAGDAefatlsvmsrrllgGAPTEPD--- 233
Cdd:TIGR01348 248 APAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAA-SAAGGAP--------------GALPWPNvdf 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 234 ---GHTRRVPVRGVRKVTAKAMKDSLDTKALVTAFLTCDVTPTMDLVARLRADRRFKGLRVSPLTIWCKAVCLAMGRTPV 310
Cdd:TIGR01348 313 skfGEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPK 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 311 VNARWDDAADQIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVF 390
Cdd:TIGR01348 393 FNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGI 472
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488475828 391 GLDAGTPVVNRTESAILVLGTIARRP-WvvgtgDDEEVVPRWVTTMSLGFDHRLIDGEEGSTFLHDVAEILSDP 463
Cdd:TIGR01348 473 GGTAFTPIVNAPEVAILGVSKSGMEPvW-----NGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADI 541
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
1-460 |
7.16e-58 |
|
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).
Pssm-ID: 200219 [Multi-domain] Cd Length: 579 Bit Score: 200.62 E-value: 7.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTIDDGSDD---- 76
Cdd:TIGR02927 7 MPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAIIGEPGEAgsep 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 77 -----QPEEEPE-------------------------------------------------------------------- 83
Cdd:TIGR02927 87 apaapEPEAAPEpeapapaptpaaeapapaapqaggsgeatevkmpelgesvtegtvtswlkavgdtvevdepllevstd 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 84 ------------------------FLVGHLTAESGRRRRRRRGAAVSAERAPEKAPQTPTLKTGPET-----DVEPVPEP 134
Cdd:TIGR02927 167 kvdteipspvagtlleirapeddtVEVGTVLAIIGDANAAPAEPAEEEAPAPSEAGSEPAPDPAARAphaapDPPAPAPA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 135 VQPTQPRRQDPPRMDRAGHVLAKPPARRLAADLGIDLSTVTGTGPQGAVTRSDV----KAAAEAGRQAAPEPPVVGASAG 210
Cdd:TIGR02927 247 PAKTAAPAAAAPVSSGDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVlaaaKAAEEARAAAAAPAAAAAPAAP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 211 DAEFATLSVMSRRLLGgaptepdghtRRVPVRGVRKVTAKAMKDSLDTKALVTAFLTCDVTPTMDLVARLRADRRFK-GL 289
Cdd:TIGR02927 327 AAAAKPAEPDTAKLRG----------TTQKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKnGV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 290 RVSPLTIWCKAVCLAMGRTPVVNARWDDAADQIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKE 369
Cdd:TIGR02927 397 NLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 370 GKLQPTDYTDGTFSITNVGVFGLDAGTPVVNRTESAILVLGTIARRPWVVGTGDDEEVVP-RWVTTMSLGFDHRLIDGEE 448
Cdd:TIGR02927 477 NKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEDGGESIAiRSVCYLPLTYDHRLVDGAD 556
|
570
....*....|..
gi 488475828 449 GSTFLHDVAEIL 460
Cdd:TIGR02927 557 AGRFLTTIKKRL 568
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
1-468 |
1.06e-53 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 188.52 E-value: 1.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPG-ETVAVGEPL-VTIDDgsddqp 78
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIaITVEE------ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 79 EEEPEFLVGHltaesgrrrrrrrGAAVSAERAPEKAPQTPtlktgPETDVEPVPEPVQPTQPRRQDPPRMDRAG-HVLAK 157
Cdd:PLN02744 191 EEDIGKFKDY-------------KPSSSAAPAAPKAKPSP-----PPPKEEEVEKPASSPEPKASKPSAPPSSGdRIFAS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 158 PPARRLAADLGIDLSTVTGTGPQGAVTRSDVKAAAEAGRQAAPEPPVVGASAGDAEFATLSvmsrrllggaptepdgHTR 237
Cdd:PLN02744 253 PLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPALDYTDIP----------------NTQ 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 238 rvpvrgVRKVTAKAMKDSLDTkaLVTAFLTCD--VTPTMDLVARLRA-DRRFKGLRVSPLTIWCKAVCLAMGRTPVVNAR 314
Cdd:PLN02744 317 ------IRKVTASRLLQSKQT--IPHYYLTVDtrVDKLMALRSQLNSlQEASGGKKISVNDLVIKAAALALRKVPQCNSS 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 315 WDDaaDQIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNV-GVFGLD 393
Cdd:PLN02744 389 WTD--DYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIK 466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488475828 394 AGTPVVNRTESAILVLGTIARRPwVVGTGDDEEVVPRWVT-TMSLgfDHRLIDGEEGSTFLHDVAEILSDPASAML 468
Cdd:PLN02744 467 QFCAIINPPQSAILAVGSAEKRV-IPGSGPDQYNFASFMSvTLSC--DHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
154-463 |
1.18e-52 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 179.60 E-value: 1.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 154 VLAKPPARRLAADLGIDLSTVTGTGPQGAVTRSDV-KAAAEAGRQAAPEPPVVGASAGDAEFATLSVMSRRLLGGaptep 232
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVeNFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEG----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 233 dghtRRVPVRGVRKVTAKAMKDSLDTKALVTAFLTCDVTPTMDLVARLRAD-RRFKGLRVSPLTIWCKAVCLAMGRTPVV 311
Cdd:PRK11857 77 ----KREKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvLKTEGVKLTFLPFIAKAILIALKEFPIF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 312 NARWDDAADQIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVFG 391
Cdd:PRK11857 153 AAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVG 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488475828 392 LDAGTPVVNRTESAILVLGTIARRPWVVgtgdDEEVVPRWVTTMSLGFDHRLIDGEEGSTFLHDVAEILSDP 463
Cdd:PRK11857 233 SLYGVPVINYPELAIAGVGAIIDKAIVK----NGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
1-468 |
1.58e-47 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 170.32 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTIDDGSDdqpee 80
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED----- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 81 epeflvghltaesgrrrrrrrgaAVSAERAPEKAPQTPtlktgpetDVEPVPEPVQPTQPRRQDPPRMDRAGHVLAKPPA 160
Cdd:PLN02226 171 -----------------------AASQVTPSQKIPETT--------DPKPSPPAEDKQKPKVESAPVAEKPKAPSSPPPP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 161 RRLAADlgidlstvtgtgpqgavtrsdvkaaaeagrqaaPEPPvvgasagdaefatlsvmsrrllggaptePDGHTRRVP 240
Cdd:PLN02226 220 KQSAKE---------------------------------PQLP----------------------------PKERERRVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 241 VRGVRKVTAKAMKDSLDTKALVTAFLTCDVTPTMDLVARLR-ADRRFKGLRVSPLTIWCKAVCLAMGRTPVVNARWDdaA 319
Cdd:PLN02226 239 MTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKdAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVID--G 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 320 DQIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVFGLDAGTPVV 399
Cdd:PLN02226 317 DDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPII 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488475828 400 NRTESAILVLGTIARRPWVVGTgddeEVVPRWVTTMSLGFDHRLIDGEEGSTFLHDVAEILSDPASAML 468
Cdd:PLN02226 397 NPPQSAILGMHSIVSRPMVVGG----SVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
158-468 |
3.09e-39 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 145.05 E-value: 3.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 158 PPARRLAADLGIDLSTVTGTGPQGAVTRSDVkaaaeagRQAAPEPPVVGASAGDAEFATLSVMSRRllggapTEPDGHTR 237
Cdd:PRK14843 53 PLAKRIALEHNIAWQEIQGTGHRGKIMKKDV-------LALLPENIENDSIKSPAQIEKVEEVPDN------VTPYGEIE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 238 RVPVRGVRKVTAKAMKDSLDTKALVTAFLTCDVTPTMDLVAR-LRADRRFKGLRVSPLTIWCKAVCLAMGRTPVVNARWD 316
Cdd:PRK14843 120 RIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 317 DAADQIVFRDQINLGIAAATPRGLMVPVVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVFGLDAGT 396
Cdd:PRK14843 200 EDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFG 279
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488475828 397 PVVNRTESAILVLGTIARRPWVVgtgdDEEVVPRWVTTMSLGFDHRLIDGEEGSTFLHDVAEILSDPASAML 468
Cdd:PRK14843 280 PIINQPNSAILGVSSTIEKPVVV----NGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-70 |
6.42e-28 |
|
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: 105.92 E-value: 6.42e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTI 70
Cdd:COG0508 7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1-70 |
2.75e-26 |
|
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: 101.33 E-value: 2.75e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTI 70
Cdd:cd06849 5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1-70 |
6.81e-19 |
|
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: 80.72 E-value: 6.81e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPGEGLTEGeVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTI 70
Cdd:pfam00364 5 SPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
200-460 |
1.02e-15 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 79.93 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 200 PEPPVVGASAGDAEFATLSVMSRRllggAPTEPDGHTRRVPVRGVRKVTAKAMKDSLdtkALVTAfltcdvTPTMDLVAR 279
Cdd:PRK12270 83 PPKPAAAAAAAAAPAAPPAAAAAA----APAAAAVEDEVTPLRGAAAAVAKNMDASL---EVPTA------TSVRAVPAK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 280 LRADRRF---------KGLRVSPLTIWCKAVCLAMGRTPVVNARWD--DAADQIVFRDQINLGIAAATP-----RGLMVP 343
Cdd:PRK12270 150 LLIDNRIvinnhlkrtRGGKVSFTHLIGYALVQALKAFPNMNRHYAevDGKPTLVTPAHVNLGLAIDLPkkdgsRQLVVP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 344 VVRNAQDMTMLELAEEITRIVAIAKEGKLQPTDYTDGTFSITNVGVFGLDAGTPVVNRTESAILVLGTIARRPWVVGTGD 423
Cdd:PRK12270 230 AIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFQGASE 309
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488475828 424 D---EEVVPRwVTTMSLGFDHRLIDGEEGSTFLHDVAEIL 460
Cdd:PRK12270 310 ErlaELGISK-VMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1-110 |
1.05e-14 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 75.37 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTIDDGsdDQPEE 80
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADA--EVSDA 84
|
90 100 110
....*....|....*....|....*....|
gi 488475828 81 EPEFLVGHLTAESGRRRRRRRGAAVSAERA 110
Cdd:PRK14875 85 EIDAFIAPFARRFAPEGIDEEDAGPAPRKA 114
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
11-70 |
9.54e-14 |
|
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: 65.90 E-value: 9.54e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 11 GEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTI 70
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
154-189 |
3.92e-12 |
|
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: 60.39 E-value: 3.92e-12
10 20 30
....*....|....*....|....*....|....*.
gi 488475828 154 VLAKPPARRLAADLGIDLSTVTGTGPQGAVTRSDVK 189
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
18-71 |
4.13e-11 |
|
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: 60.68 E-value: 4.13e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 488475828 18 VSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTID 71
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
2-70 |
1.33e-09 |
|
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: 54.37 E-value: 1.33e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488475828 2 PDPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTI 70
Cdd:cd06663 5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-145 |
9.20e-09 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 57.23 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPGEGLTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAK-LCAEPGETVAVGEPLVTIddgsddqpe 79
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKiLVPEGTEGVKVNTPIAVL--------- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488475828 80 eepeflvghltAESGRRRRRRRGAAVSAERAPEKAPQTPTLKTGPETDVEPvPEPVQPTQPRRQDP 145
Cdd:PRK11892 78 -----------LEEGESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAP-AAPAAPAAEVAADP 131
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
11-70 |
2.90e-08 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 56.00 E-value: 2.90e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 11 GEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTI 70
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
18-70 |
1.77e-05 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 47.23 E-value: 1.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488475828 18 VSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTI 70
Cdd:PRK14040 540 VTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
7-58 |
1.03e-04 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 40.98 E-value: 1.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488475828 7 GLTE------GEVVSWRV-SPGDTVKINDVLCEVETAKSIVELPSPFAGTV----AKLCAEPG 58
Cdd:cd06848 19 GITDyaqdllGDIVFVELpEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVvevnEALLDNPE 81
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
7-79 |
2.12e-04 |
|
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: 40.88 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 7 GLTE------GEVVSWRV-SPGDTVKINDVLCEVETAKSIVELPSPFAGTVaklcaepgetVAVGEPLVtiddgsdDQPE 79
Cdd:COG0509 27 GITDfaqdllGDIVFVELpEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEV----------VEVNEALE-------DDPE 89
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
18-72 |
4.55e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 38.84 E-value: 4.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 488475828 18 VSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTIDD 72
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
11-72 |
6.52e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 42.43 E-value: 6.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488475828 11 GEVVSWRVSPGDTVKINDVLCEVETAK---SIVelpSPFAGTVAKLCAEPGETVAVGEPLVTIDD 72
Cdd:PRK12999 1085 GSVVTVLVKEGDEVKAGDPLAVIEAMKmetTIT---APVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1-70 |
1.67e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 38.64 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 1 MPDPgeglTEGEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTI 70
Cdd:PRK06549 64 MPSP----MPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITI 129
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
11-70 |
1.82e-03 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 39.08 E-value: 1.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475828 11 GEVVSWRVSPGDTVKINDVLCEVETAKSIVELPSPFAGTVAKLCAEPGETVAVGEPLVTI 70
Cdd:PRK05641 93 GKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
41-70 |
4.73e-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: 39.68 E-value: 4.73e-03
10 20 30
....*....|....*....|....*....|
gi 488475828 41 ELPSPFAGTVAKLCAEPGETVAVGEPLVTI 70
Cdd:COG1038 1078 HIGAPMPGTVVKVLVKEGDEVKKGDPLLTI 1107
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
41-75 |
7.79e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 38.49 E-value: 7.79e-03
10 20 30
....*....|....*....|....*....|....*
gi 488475828 41 ELPSPFAGTVAKLCAEPGETVAVGEPLVTIDDGSD 75
Cdd:COG1566 209 TIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDD 243
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
41-70 |
8.50e-03 |
|
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: 34.70 E-value: 8.50e-03
10 20 30
....*....|....*....|....*....|
gi 488475828 41 ELPSPFAGTVAKLCAEPGETVAVGEPLVTI 70
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVL 30
|
|
| |
