|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-463 |
1.94e-154 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 444.62 E-value: 1.94e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 1 MTQVFRLPDLGEGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITVAAla 80
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 81 daeayrTEERAGSTPPERQSAEPgssssperplvgygaseaprrarrrraaagdvAVASSPVPEPVSQSAIKVVSPPAPE 160
Cdd:PRK11856 79 ------EGEAEAAAAAEAAPEAP--------------------------------APEPAPAAAAAAAAAPAAAAAPAAP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 161 PVSQSaikVISPLVRKLVTEARIDLASITATGDGGVIRRADVEAAISSRASGSVPDSAAPTDTgwitygalPATVAPADE 240
Cdd:PRK11856 121 AAAAA---KASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAAAAAAAP--------PAAAAEGEE 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 241 RIPLTGIRKAIAEKLSTSRREIPDATTWVDVDATELLATKDALKAarQDDAIGILALLARITVAGLRAFPELNSSVEGDE 320
Cdd:PRK11856 190 RVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKA--IGVKLTVTDFLIKAVALALKKFPELNASWDDDA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 321 IVKHGSINLGFAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVFGVDGSTPIINH 400
Cdd:PRK11856 268 IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINP 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1707083200 401 PEAAMLGIGRIIDKPWAHEAQVALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLLA 463
Cdd:PRK11856 348 PEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
5-462 |
1.01e-101 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 314.45 E-value: 1.01e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 5 FRLPDLGEgLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITVAALADAEA 84
Cdd:PRK11855 122 VKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 85 yrteeragsTPPERQSAEPgssssperplvgygaseaprrarrrraaagdvAVASSPVPEPVSQSAIKVVSPPAPEPVSQ 164
Cdd:PRK11855 201 ---------AAAAPAAAAP--------------------------------AAAAAAAPAPAPAAAAAPAAAAPAAAAAP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 165 SAIKVISPLVRKLVTEARIDLASITATGDGGVIRRADVEAAISSRASGSVPDSAAPTDTGWITYGALPATVAPAD----- 239
Cdd:PRK11855 240 GKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAAAAAGGGGLGLLPWPKVDFSkfgei 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 240 ERIPLTGIRKAIAEKLSTSRREIPDATTWVDVDATELLATKDALKAARQDDAIGI--LALLARITVAGLRAFPELNSSV- 316
Cdd:PRK11855 320 ETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLtmLPFFIKAVVAALKEFPVFNASLd 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 317 -EGDEIVKHGSINLGFAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVFGVDGST 395
Cdd:PRK11855 400 eDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFT 479
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707083200 396 PIINHPEAAMLGIGRIIDKP-WAHEaQVALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 462
Cdd:PRK11855 480 PIINAPEVAILGVGKSQMKPvWDGK-EFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
255-462 |
1.20e-80 |
|
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: 248.61 E-value: 1.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 255 LSTSRREIPDATTWVDVDATELLATKDALKAARQDDA--IGILALLARITVAGLRAFPELNSSVEGD--EIVKHGSINLG 330
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtkLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 331 FAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGIGR 410
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1707083200 411 IIDKPWAHEAQVALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 462
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
8-465 |
1.11e-77 |
|
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: 247.72 E-value: 1.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 8 PDLGEGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITVaaladaeayrt 87
Cdd:TIGR01347 6 PELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 88 eeRAGSTPPERQSAEPGSSSSPerplvgygaseaprrarrrraaagdvavasspvpepvsqsaiKVVSPPAPEPVSQSAI 167
Cdd:TIGR01347 75 --EEGNDATAAPPAKSGEEKEE------------------------------------------TPAASAAAAPTAAANR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 168 KVISPLVRKLVTEARIDLASITATGDGGVIRRADVEAAISSRASGSVPDSAAPTdtgwitygALPATVAPADERIPLTGI 247
Cdd:TIGR01347 111 PSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAAA--------AAPAAATRPEERVKMTRL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 248 RKAIAEKLSTSRREIPDATTWVDVDATELLATKDALKAA---RQDDAIGILALLARITVAGLRAFPELNSSVEGDEIVKH 324
Cdd:TIGR01347 183 RQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEfekKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYK 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 325 GSINLGFAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAA 404
Cdd:TIGR01347 263 DYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSA 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1707083200 405 MLGIGRIIDKPWAHEAQVALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLLAGL 465
Cdd:TIGR01347 343 ILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-462 |
1.91e-75 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 242.05 E-value: 1.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 1 MTQVfRLPDLGEGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITVAAla 80
Cdd:PRK05704 2 MVEI-KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 81 daeayrteeragstpperqsaepgssssperplvgygaseaprrarrrraaaGDVAVASSPVPEPVSQSAIKVVSPPAPE 160
Cdd:PRK05704 79 ----------------------------------------------------GAAAGAAAAAAAAAAAAAAAPAQAQAAA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 161 PVSQSAIkVISPLVRKLVTEARIDLASITATGDGGVIRRADVEAAISSRASGSVPDSAAPTdtgwitygalPATVAPAD- 239
Cdd:PRK05704 107 AAEQSND-ALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAAP----------AAAPAPLGa 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 240 ---ERIPLTGIRKAIAEKLSTSRREIPDATTWVDVDATELLAtkdaLKAARQDD-------AIGILALLARITVAGLRAF 309
Cdd:PRK05704 176 rpeERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMD----LRKQYKDAfekkhgvKLGFMSFFVKAVVEALKRY 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 310 PELNSSVEGDEIVKHGSINLGFAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVF 389
Cdd:PRK05704 252 PEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVF 331
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1707083200 390 GVDGSTPIINHPEAAMLGIGRIIDKPWAHEAQVALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 462
Cdd:PRK05704 332 GSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLL 404
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
8-456 |
1.95e-67 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 227.19 E-value: 1.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 8 PDLGegLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITVaaladaeayrt 87
Cdd:PRK11854 212 PDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRF----------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 88 eERAGSTPperqSAEPgssssperplvgygaseaprrarrrraaagdvAVASSPVPEPVSQSAIKVVSPPAPEPVSQSAI 167
Cdd:PRK11854 279 -EVEGAAP----AAAP--------------------------------AKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEF 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 168 KV------ISPLVRKLVTEARIDLASITATGDGGVIRRADVEAAISSrASGSVPDSAAPTDTGWITYGALP-ATVAPAD- 239
Cdd:PRK11854 322 AEndayvhATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKD-AVKRAEAAPAAAAAGGGGPGLLPwPKVDFSKf 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 240 ---ERIPLTGIRKAIAEKLSTSRREIPDATTWVDVDATELLATKDALKAARQDDAIGI----LALLARITVAGLRAFPEL 312
Cdd:PRK11854 401 geiEEVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNAEAEKRKLGVkitpLVFIMKAVAAALEQMPRF 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 313 NSSV--EGDEIVKHGSINLGFAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVFG 390
Cdd:PRK11854 481 NSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLG 560
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707083200 391 VDGSTPIINHPEAAMLGIGRIIDKPWAHEAQVALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVE 456
Cdd:PRK11854 561 TTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
4-465 |
1.68e-64 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 213.78 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 4 VFRLPDLGEGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITVAaladae 83
Cdd:PTZ00144 46 VIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEID------ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 84 ayrTEERAGSTPPERQSAEPGSSSSPERPlvgygaseaprrarrrraaagdvaVASSPVPEPVSQSaiKVVSPPAPEPVS 163
Cdd:PTZ00144 120 ---TGGAPPAAAPAAAAAAKAEKTTPEKP------------------------KAAAPTPEPPAAS--KPTPPAAAKPPE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 164 QSAikvisplvrklvtearidlasitatgdggvirradveaaissrasgSVPDSAAPTdtgwitygalpATVAPADERIP 243
Cdd:PTZ00144 171 PAP----------------------------------------------AAKPPPTPV-----------ARADPRETRVP 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 244 LTGIRKAIAEKLSTSRREIPDATTWVDVDATELLATKDALKAARQDD---AIGILALLARITVAGLRAFPELNSSVEGDE 320
Cdd:PTZ00144 194 MSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKhgvKLGFMSAFVKASTIALKKMPIVNAYIDGDE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 321 IVKHGSINLGFAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVFGVDGSTPIINH 400
Cdd:PTZ00144 274 IVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINP 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707083200 401 PEAAMLGIGRIIDKPWAHEAQVALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLLAGL 465
Cdd:PTZ00144 354 PQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-462 |
1.83e-61 |
|
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: 209.35 E-value: 1.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 3 QVFRLPDLGeGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITVaalada 82
Cdd:TIGR01348 117 QEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTL------ 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 83 eayRTEERAGSTPPERQSAEPGSSSSperplvgygASEAPrrarrrraaagdvAVASSPVPEPvSQSAIKVVSPPapepV 162
Cdd:TIGR01348 190 ---SVAGSTPATAPAPASAQPAAQSP---------AATQP-------------EPAAAPAAAK-AQAPAPQQAGT----Q 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 163 SQSAIKVISPLVRKLVTEARIDLASITATGDGGVIRRADVEAAISSrASGSVPDSAAPTDTGWItyGALPATVAPAD--- 239
Cdd:TIGR01348 240 NPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKE-PSVRAQAAAASAAGGAP--GALPWPNVDFSkfg 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 240 --ERIPLTGIRKAIAEKLSTSRREIPDATTWVDVDATELLATKDALKAA--RQDDAIGILALLARITVAGLRAFPELNSS 315
Cdd:TIGR01348 317 evEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAveKEGVKLTVLHILMKAVAAALKKFPKFNAS 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 316 VE--GDEIVKHGSINLGFAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVFGVDG 393
Cdd:TIGR01348 397 LDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTA 476
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707083200 394 STPIINHPEAAMLGIGRIIDKPWAHEAQVALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 462
Cdd:TIGR01348 477 FTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
6-457 |
1.96e-61 |
|
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: 209.87 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 6 RLPDLGEGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLitvAALADAEAY 85
Cdd:TIGR02927 130 KMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVL---AIIGDANAA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 86 RTEERAGSTPPErqsAEPGSSSSPERplvgygASEAPrrarrrraaagdvavASSPVPEPVSQSAIKVVSPPAPEPVSQS 165
Cdd:TIGR02927 207 PAEPAEEEAPAP---SEAGSEPAPDP------AARAP---------------HAAPDPPAPAPAPAKTAAPAAAAPVSSG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 166 A-IKVISPLVRKLVTEARIDLASITATGDGGVIRRADVEAAISSRASGSVPDSAAPTDTGWITYGALPATVAPADERI-- 242
Cdd:TIGR02927 263 DsGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAAAAKPAEPDTAKLrg 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 243 ---PLTGIRKAIAEKLSTSRREIPDATTWVDVDATELLATKDALKA---ARQDDAIGILALLARITVAGLRAFPELNSSV 316
Cdd:TIGR02927 343 ttqKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNdflEKNGVNLTFLPFFVQAVTEALKAHPNVNASY 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 317 --EGDEIVKHGSINLGFAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVFGVDGS 394
Cdd:TIGR02927 423 naETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFD 502
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707083200 395 TPIINHPEAAMLGIGRIIDKPWAHEAQ-----VALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVEQ 457
Cdd:TIGR02927 503 TPILNPPQAAILGTGAIVKRPRVIKDEdggesIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
5-462 |
6.70e-48 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 169.90 E-value: 6.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 5 FRLPDLGEGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITVAaladaea 84
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIM------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 85 yrTEEragstpperqsaepgssssperplvgygaseaprrarrrraaaGDVAVASSPVPEPVSQSAIKVVSPPAPEPVSQ 164
Cdd:PLN02528 74 --VED-------------------------------------------SQHLRSDSLLLPTDSSNIVSLAESDERGSNLS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 165 SAIKviSPLVRKLVTEARIDLASITATGDGGVIRRADV------EAAISSRASGSVPDSAAPTDTGwiTYGALPATVAPA 238
Cdd:PLN02528 109 GVLS--TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVlkyaaqKGVVKDSSSAEEATIAEQEEFS--TSVSTPTEQSYE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 239 DERIPLTGIRKAIAeKLSTSRREIPDATTWVDVDATELLATKDALKAARQDDAIGI--LALLARITVAGLRAFPELNSSV 316
Cdd:PLN02528 185 DKTIPLRGFQRAMV-KTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPTVKHtfLPFLIKSLSMALSKYPLLNSCF 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 317 EGD--EIVKHGSINLGFAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVFGVDGS 394
Cdd:PLN02528 264 NEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFG 343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707083200 395 TPIINHPEAAMLGIGRIIDKP-WAHEAQVALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 462
Cdd:PLN02528 344 SPVLNLPEVAIIALGRIQKVPrFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLM 412
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
7-462 |
1.23e-47 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 171.96 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 7 LPDLGEGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAG-VVTTLHTTPGQELAVGAPL-ITVAALADAEA 84
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGyLAKIVKGDGAKEIKVGEVIaITVEEEEDIGK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 85 YRTEERAGSTPPerqsAEPGSSSSPERPLVgygaseaprrarrrraaagDVAVASSPVPEPvsqsaiKVVSPPAPepvSQ 164
Cdd:PLN02744 197 FKDYKPSSSAAP----AAPKAKPSPPPPKE-------------------EEVEKPASSPEP------KASKPSAP---PS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 165 SAIKVI-SPLVRKLVTEARIDLASITATGDGGVIRRADVEAAISSRASGSVPDSAAPTDTGWITYgalpatvapadERIP 243
Cdd:PLN02744 245 SGDRIFaSPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPALDY-----------TDIP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 244 LTGIRKAIAEKLSTSRREIPDATTWVDVDATELLATK---DALKAARQDDAIGILALLARITVAGLRAFPELNSSVEGDE 320
Cdd:PLN02744 314 NTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRsqlNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDY 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 321 IVKHGSINLGFAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNY-GVFGVDGSTPIIN 399
Cdd:PLN02744 394 IRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIIN 473
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1707083200 400 HPEAAMLGIG----RIIdkPWAHEAQVALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 462
Cdd:PLN02744 474 PPQSAILAVGsaekRVI--PGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESML 538
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
170-462 |
6.05e-46 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 162.77 E-value: 6.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 170 ISPLVRKLVTEARIDLASITATGDGGVIRRADVEAAISSRASGSVPDSAAPTDTGWItygaLPATVAPAD--ERIPLTGI 247
Cdd:PRK14843 51 ISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEE----VPDNVTPYGeiERIPMTPM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 248 RKAIAEKLSTSRREIPDATTWVDVDATELLATKDALK---AARQDDAIGILALLARITVAGLRAFPELNSSV--EGDEIV 322
Cdd:PRK14843 127 RKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLepiMEATGKKTTVTDLLSLAVVKTLMKHPYINASLteDGKTII 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 323 KHGSINLGFAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVFGVDGSTPIINHPE 402
Cdd:PRK14843 207 THNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPN 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 403 AAMLGIGRIIDKPWAHEAQVALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 462
Cdd:PRK14843 287 SAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISML 346
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
170-461 |
4.73e-44 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 156.88 E-value: 4.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 170 ISPLVRKLVTEARIDLASITATGDGGVIRRADVEAAISSRASGSVPDSAAPTDTGWITYG-ALPATVAPADE--RIPLTG 246
Cdd:PRK11857 4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKtAAPAAAPPKLEgkREKVAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 247 IRKAIAEKLSTSRREIPDATTWVDVDATELLATKDALKAARQDDA---IGILALLARITVAGLRAFPELNSSVE--GDEI 321
Cdd:PRK11857 84 IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEgvkLTFLPFIAKAILIALKEFPIFAAKYDeaTSEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 322 VKHGSINLGFAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVFGVDGSTPIINHP 401
Cdd:PRK11857 164 VYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYP 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 402 EAAMLGIGRIIDKPWAHEAQVALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVL 461
Cdd:PRK11857 244 ELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
7-462 |
1.03e-41 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 154.53 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 7 LPDLGEGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITVAALADAEAYR 86
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 87 TEERAGSTPPERQSAEPGSSSSPERplvgygaseaprrarrrraaagdvaVASSPVPEpvsqsaiKVVSPPAPEPVSQSA 166
Cdd:PLN02226 176 TPSQKIPETTDPKPSPPAEDKQKPK-------------------------VESAPVAE-------KPKAPSSPPPPKQSA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 167 IKVISPlvrklvtearidlasitatgdggvirradveaaissrasgsvpdsaaPTDTgwitygalpatvapaDERIPLTG 246
Cdd:PLN02226 224 KEPQLP-----------------------------------------------PKER---------------ERRVPMTR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 247 IRKAIAEKLSTSRREIPDATTWVDVDATELLATKDALKAA---RQDDAIGILALLARITVAGLRAFPELNSSVEGDEIVK 323
Cdd:PLN02226 242 LRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAfyeKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 324 HGSINLGFAAQSPRGLVVPVVHGAHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVFGVDGSTPIINHPEA 403
Cdd:PLN02226 322 RDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQS 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1707083200 404 AMLGIGRIIDKPWAHEAQVALRKVTQLSFTFDHRVCDGGTAGGFLRYVADCVEQPAVLL 462
Cdd:PLN02226 402 AILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLL 460
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-77 |
1.03e-27 |
|
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: 105.15 E-value: 1.03e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1707083200 1 MTQVFRLPDLGEGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITVA 77
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-76 |
7.53e-24 |
|
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: 94.39 E-value: 7.53e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707083200 3 QVFRLPDLGEGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITV 76
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
200-451 |
4.31e-21 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 96.88 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 200 ADVEAAISSRASGSVPDSAAPTDTGWITYGALPATVAPADERIPLTGIRKAIAEKLSTSRrEIPDATTWVDVDATELLAT 279
Cdd:PRK12270 76 AAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASL-EVPTATSVRAVPAKLLIDN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 280 K----DALKAARqDDAIGILALLARITVAGLRAFPELNSS---VEGD-EIVKHGSINLGFAAQSP-----RGLVVPVVHG 346
Cdd:PRK12270 155 RivinNHLKRTR-GGKVSFTHLIGYALVQALKAFPNMNRHyaeVDGKpTLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 347 AHAMTTAQLAGALRTLTEAAREGTITPAQLTGGTFTLNNYGVFGVDGSTPIINHPEAAMLGIGRiIDKPWAHE------- 419
Cdd:PRK12270 234 AETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGA-MEYPAEFQgaseerl 312
|
250 260 270
....*....|....*....|....*....|..
gi 1707083200 420 AQVALRKVTQLSFTFDHRVCDGGTAGGFLRYV 451
Cdd:PRK12270 313 AELGISKVMTLTSTYDHRIIQGAESGEFLRTI 344
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
7-112 |
1.53e-13 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 71.90 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 7 LPDLGEGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLitvAALADAEAYR 86
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL---AVVADAEVSD 83
|
90 100
....*....|....*....|....*.
gi 1707083200 87 TEERAGSTPPERQSAEPGSSSSPERP 112
Cdd:PRK14875 84 AEIDAFIAPFARRFAPEGIDEEDAGP 109
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-76 |
8.28e-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: 63.39 E-value: 8.28e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1707083200 4 VFRLPDLGEGLTEAtVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITV 76
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
18-76 |
6.73e-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: 52.03 E-value: 6.73e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1707083200 18 TVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITV 76
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
170-203 |
3.04e-07 |
|
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: 46.53 E-value: 3.04e-07
10 20 30
....*....|....*....|....*....|....
gi 1707083200 170 ISPLVRKLVTEARIDLASITATGDGGVIRRADVE 203
Cdd:pfam02817 3 ASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
6-74 |
3.56e-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: 47.44 E-value: 3.56e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707083200 6 RLPDLGEGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLI 74
Cdd:cd06663 3 LIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLV 71
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
18-77 |
6.94e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 42.49 E-value: 6.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 18 TVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITVA 77
Cdd:PRK06549 71 TILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITIG 130
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
24-76 |
2.63e-04 |
|
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: 41.03 E-value: 2.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1707083200 24 VAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITV 76
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
25-57 |
9.61e-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: 38.95 E-value: 9.61e-04
10 20 30
....*....|....*....|....*....|...
gi 1707083200 25 AEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVT 57
Cdd:COG0509 46 EVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVV 78
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
26-57 |
1.19e-03 |
|
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: 38.28 E-value: 1.19e-03
10 20 30
....*....|....*....|....*....|..
gi 1707083200 26 EGDTVTIDQEVVTVETAKAAVEVPCPYAGVVT 57
Cdd:cd06848 39 VGTEVKKGDPFGSVESVKAASDLYSPVSGEVV 70
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
23-77 |
1.77e-03 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 40.68 E-value: 1.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1707083200 23 HVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITVA 77
Cdd:PRK14040 539 IVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-144 |
2.07e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 40.29 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707083200 1 MTQVfRLPDLGEGLTEATVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQE-LAVGAPLITVaaL 79
Cdd:PRK11892 2 AIEI-LMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTPIAVL--L 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707083200 80 ADAEAyrTEERAGSTPPERQSAEPGSSSSPErplvgygASEAPRRARRRRAAAGDVAVASSP-VPE 144
Cdd:PRK11892 79 EEGES--ASDAGAAPAAAAEAAAAAPAAAAA-------AAAKKAAPAPAAPAAPAAEVAADPdIPA 135
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
18-76 |
2.27e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 40.60 E-value: 2.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1707083200 18 TVLEWHVAEGDTVTIDQEVVTVETAKAAVEVPCPYAGVVTTLHTTPGQELAVGAPLITV 76
Cdd:PRK09282 532 TVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| |
