|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
43-468 |
2.11e-131 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 386.07 E-value: 2.11e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 43 IREIFMPALSSTMTEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALLAESEE 122
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 123 DVALAVAQAQALSSGQAQQAPPPSDADAPPPPSPPPAAAApapvaaGTKGVATPQAKKLAKQHRVDLAKVTGTGQFGRIT 202
Cdd:PRK11856 82 AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPA------AAAAKASPAVRKLARELGVDLSTVKGSGPGGRIT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 203 PADVEAAAGIQPKPKVAPPtaaapvaapsvrAVPQASVLPPVPGATVVPFTAMQAAVSKNMVES-LSVPAFRVGYPILTD 281
Cdd:PRK11856 156 KEDVEAAAAAAAPAAAAAA------------AAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESkREIPHFTLTDEVDVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 282 KLDELYEKVKP--KGVTMTVLLAKAAAMALAQYPVVNASCRDGAsFTYNSSINIAVAVAIDGGLITPVLEQADKLDIYLL 359
Cdd:PRK11856 224 ALLALRKQLKAigVKLTVTDFLIKAVALALKKFPELNASWDDDA-IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 360 SQKWKELVKKARAKQLQPNEYNSGTFTLSNLGMFGVDRFDAILPPGQGAIMAVGASKPTVTAdKDGFFSVKNKMLVNVTA 439
Cdd:PRK11856 303 AREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVV-VDGEIVVRKVMPLSLSF 381
|
410 420
....*....|....*....|....*....
gi 960478043 440 DHRIVYGADLAAFLQTFAKIIEDPESLTL 468
Cdd:PRK11856 382 DHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
45-468 |
1.47e-79 |
|
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: 253.95 E-value: 1.47e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 45 EIFMPALSSTMTEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAG-ESAPVGAPIALLAESEED 123
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 124 VALAVAQAQALSSGQ-----------AQQAPPPSDADAPPPPSPPPAAAAPAPVAAGTKGVATPQAKKLAKQHRVDLAKV 192
Cdd:TIGR01349 81 VADAFKNYKLESSASpapkpseiaptAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 193 TGTGQFGRITPADVEAAAGIQPKPKVAPPTAAAPvaapsvravPQASVLPPVPGA--TVVPFTAMQAAVSKNMVES-LSV 269
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPASANQQAAATTP---------ATYPAAAPVSTGsyEDVPLSNIRKIIAKRLLESkQTI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 270 PAFRVGYPILTDKLDELYE---KVKPKGVTMTV--LLAKAAAMALAQYPVVNASCRDGAsFTYNSSINIAVAVAIDGGLI 344
Cdd:TIGR01349 232 PHYYVSIECNVDKLLALRKelnAMASEVYKLSVndFIIKASALALREVPEANSSWTDNF-IRRYKNVDISVAVATPDGLI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 345 TPVLEQADKLDIYLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNLGMFGVDRFDAILPPGQGAIMAVGAS--KPTVTAD 422
Cdd:TIGR01349 311 TPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVedVAVVDND 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 960478043 423 KDGFFSVKNKMLVNVTADHRIVYGADLAAFLQTFAKIIEDPESLTL 468
Cdd:TIGR01349 391 EEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
44-468 |
5.32e-58 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 200.08 E-value: 5.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 44 REIFMPALSSTMTEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAG-ESAPVGAPIALLAESEE 122
Cdd:PLN02744 113 QEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIAITVEEEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 123 DVALAVAQAQALSSGQAQQAPP-------PSDADAPPPPSPPPAAAAPAPVAAGTKGVATPQAKKLAKQHRVDLAKVTGT 195
Cdd:PLN02744 193 DIGKFKDYKPSSSAAPAAPKAKpsppppkEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 196 GQFGRITPADVEAAAGIQPKPKVAPPTAAAPVAAPSVRAVPQASVLppvpgatvvPFTAMQAAVSKNMVES--LSVPAfR 273
Cdd:PLN02744 273 GPDGRIVKADIEDYLASGGKGATAPPSTDSKAPALDYTDIPNTQIR---------KVTASRLLQSKQTIPHyyLTVDT-R 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 274 VGYPI-LTDKLDELYEKVKPKGVTMTVLLAKAAAMALAQYPVVNASCRDGASFTYNsSINIAVAVAIDGGLITPVLEQAD 352
Cdd:PLN02744 343 VDKLMaLRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYH-NVNINVAVQTENGLYVPVVKDAD 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 353 KLDIYLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNL-GMFGVDRFDAILPPGQGAIMAVG-ASKPTVTADKDGFFSVK 430
Cdd:PLN02744 422 KKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGsAEKRVIPGSGPDQYNFA 501
|
410 420 430
....*....|....*....|....*....|....*...
gi 960478043 431 NKMLVNVTADHRIVYGADLAAFLQTFAKIIEDPESLTL 468
Cdd:PLN02744 502 SFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
263-466 |
6.10e-57 |
|
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: 187.37 E-value: 6.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 263 MVESL-SVPAFRVGYPILTDKLDELYEKVKPKG------VTMTVLLAKAAAMALAQYPVVNASC-RDGASFTYNSSINIA 334
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAadeetkLTFLPFLVKAVALALKKFPELNASWdGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 335 VAVAIDGGLITPVLEQADKLDIYLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNLGMFGVDRFDAILPPGQGAIMAVGA 414
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 960478043 415 SKPTVtADKDGFFSVKNKMLVNVTADHRIVYGADLAAFLQTFAKIIEDPESL 466
Cdd:pfam00198 161 IRKRP-VVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
56-468 |
2.88e-52 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 184.64 E-value: 2.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 56 TEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALLaeseEDVALAVAQAQALS 135
Cdd:PRK11855 131 TEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVI----EVAAAAPAAAAAPA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 136 SGQAQQAPPPSDADAPPPPSPPPAAAAPAPVAAGTKGVATPQAKKLAKQHRVDLAKVTGTGQFGRITPADVEAA--AGIQ 213
Cdd:PRK11855 207 AAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFvkGAMS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 214 PKPKVAPPTAAAPVAAPSVRAVPQASvLPPVPGATVVPFTAMQAAVSKNMVESLS-VP--------------AFRVgypi 278
Cdd:PRK11855 287 AAAAAAAAAAAAGGGGLGLLPWPKVD-FSKFGEIETKPLSRIKKISAANLHRSWVtIPhvtqfdeaditdleALRK---- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 279 ltdKLDELYEKvkpKGV--TMTVLLAKAAAMALAQYPVVNASC-RDGASFTYNSSINIAVAVAIDGGLITPVLEQADKLD 355
Cdd:PRK11855 362 ---QLKKEAEK---AGVklTMLPFFIKAVVAALKEFPVFNASLdEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKS 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 356 IYLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNLGMFGVDRFDAILPPGQGAIMAVGAS--KPtVTADKDgfFSVKNKM 433
Cdd:PRK11855 436 LLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSqmKP-VWDGKE--FVPRLML 512
|
410 420 430
....*....|....*....|....*....|....*
gi 960478043 434 LVNVTADHRIVYGADLAAFLQTFAKIIEDPESLTL 468
Cdd:PRK11855 513 PLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
45-468 |
3.17e-43 |
|
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: 157.20 E-value: 3.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 45 EIFMPALSSTMTEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALLAESeedv 124
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEG---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 125 alavaqaqaLSSGQAQqapppSDADAPPPPSPPPAAAAPAPVAAGTKGVATPQAKKLAKQHRVDLAKVTGTGQFGRITPA 204
Cdd:TIGR01347 78 ---------NDATAAP-----PAKSGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 205 DVEAAAGIQPKPKVAPPTAAAPVAAPSVRAVpqasvlppvpgaTVVPFTAMQAAVSKNMVESLSVPAFRVGY------PI 278
Cdd:TIGR01347 144 DIIKKTEAPASAQPPAAAAAAAAPAAATRPE------------ERVKMTRLRQRIAERLKEAQNSTAMLTTFnevdmsAV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 279 --LTDKLDELYEKVKPKGVTMTVLLAKAAAMALAQYPVVNASCrDGASFTYNSSINIAVAVAIDGGLITPVLEQADKLDI 356
Cdd:TIGR01347 212 meLRKRYKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEI-DGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSF 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 357 YLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNLGMFGVDRFDAILPPGQGAI--MAVGASKPTVTadkDGFFSVKNKML 434
Cdd:TIGR01347 291 ADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAIlgMHGIKERPVAV---NGQIEIRPMMY 367
|
410 420 430
....*....|....*....|....*....|....
gi 960478043 435 VNVTADHRIVYGADLAAFLQTFAKIIEDPESLTL 468
Cdd:TIGR01347 368 LALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
45-462 |
9.10e-41 |
|
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: 153.63 E-value: 9.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 45 EIFMPALSSTMTEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALLAES---- 120
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDAnaap 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 121 -----EEDVALAVAQAQALSSGQAQQAPPPSDADAPPPPSPPPAAAAPAPVAAGTKGVA--TPQAKKLAKQHRVDLAKVT 193
Cdd:TIGR02927 208 aepaeEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSGDSGPyvTPLVRKLAKDKGVDLSTVK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 194 GTGQFGRITPADVEAAAgiqpKPKVAPPTAAAPVAAPSVRAVPQASVLPPVPGATVVPFTAMQAA-----VSKNMVESLS 268
Cdd:TIGR02927 288 GTGVGGRIRKQDVLAAA----KAAEEARAAAAAPAAAAAPAAPAAAAKPAEPDTAKLRGTTQKMNrirqiTADKTIESLQ 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 269 VPA-FRVGYPILTDKLDELYEKVKP-----KGVTMTVLL--AKAAAMALAQYPVVNAS-CRDGASFTYNSSINIAVAVAI 339
Cdd:TIGR02927 364 TSAqLTQVHEVDMTRVAALRARAKNdflekNGVNLTFLPffVQAVTEALKAHPNVNASyNAETKEVTYHDVEHVGIAVDT 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 340 DGGLITPVLEQADKLDIYLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNLGMFGVDRFDAILPPGQGAIMAVGA--SKP 417
Cdd:TIGR02927 444 PRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAivKRP 523
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 960478043 418 TVTADKDGFFSVKNKMLVN--VTADHRIVYGADLAAFLQTFAKIIED 462
Cdd:TIGR02927 524 RVIKDEDGGESIAIRSVCYlpLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
57-468 |
2.97e-40 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 149.48 E-value: 2.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 57 EGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPiaLLAESEEDvalavaqaqalss 136
Cdd:PLN02528 12 ECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGET--LLKIMVED------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 137 GQAQQAPPPSDADAPPPPSPPPAAAAPAPVAAGTkgVATPQAKKLAKQHRVDLAKVTGTGQFGRITPADVEAAA----GI 212
Cdd:PLN02528 77 SQHLRSDSLLLPTDSSNIVSLAESDERGSNLSGV--LSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAaqkgVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 213 QPKPKVAPPTAAAPVAAPSVRAVPQASVLppvpGATVVPFTAMQAAVSKNMVESLSVPAFRVGYPILTDKLDELYEKVKP 292
Cdd:PLN02528 155 KDSSSAEEATIAEQEEFSTSVSTPTEQSY----EDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 293 ----------------KGVTMTVLlakaaamalaQYPVVNaSCRDGASF--TYNSSINIAVAVAIDGGLITPVLEQADKL 354
Cdd:PLN02528 231 nntdptvkhtflpfliKSLSMALS----------KYPLLN-SCFNEETSeiRLKGSHNIGVAMATEHGLVVPNIKNVQSL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 355 DIYLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNLGMFGVDRFDAILPPGQGAIMAVGASKPTVTADKDGFFSVKNKML 434
Cdd:PLN02528 300 SLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMT 379
|
410 420 430
....*....|....*....|....*....|....
gi 960478043 435 VNVTADHRIVYGADLAAFLQTFAKIIEDPESLTL 468
Cdd:PLN02528 380 VTIGADHRVLDGATVARFCNEWKSYVEKPELLML 413
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
41-468 |
8.34e-40 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 151.69 E-value: 8.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 41 AKIREIFMPALSSTmtEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALLaes 120
Cdd:PRK11854 204 AGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRF--- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 121 eeDVALAVAQAQALSSGQAQQAPPPSDADAPPPPSPPPAAAAPAPVAAGTKGVATPQAKKLAKQHRVDLAKVTGTGQFGR 200
Cdd:PRK11854 279 --EVEGAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGR 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 201 ITPADVEAAAGIQPKPKVAPPTAAAPVAAPsVRAVPQASVLPPVPGAT-VVPFTAMQAAVSKNMVESLsvpafrVGYPIL 279
Cdd:PRK11854 357 ILKEDVQAYVKDAVKRAEAAPAAAAAGGGG-PGLLPWPKVDFSKFGEIeEVELGRIQKISGANLHRNW------VMIPHV 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 280 T--DKLD----ELYEKVKPK-------GVTMT--VLLAKAAAMALAQYPVVNAS-CRDGASFTYNSSINIAVAVAIDGGL 343
Cdd:PRK11854 430 TqfDKADitelEAFRKQQNAeaekrklGVKITplVFIMKAVAAALEQMPRFNSSlSEDGQRLTLKKYVNIGIAVDTPNGL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 344 ITPVLEQADKLDIYLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNLGMFGVDRFDAILPPGQGAIMAVGAS--KPTVTA 421
Cdd:PRK11854 510 VVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSamEPVWNG 589
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 960478043 422 DKdgfFSVKNKMLVNVTADHRIVYGADLAAFLQTFAKIIEDPESLTL 468
Cdd:PRK11854 590 KE---FAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
175-466 |
3.06e-38 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 142.35 E-value: 3.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 175 TPQAKKLAKQHRVDLAKVTGTGQFGRITPADVEA-AAGIQPKPKVAPPTAAAPVAAPSVRAVPQASVlppvpgaTVVPFT 253
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLAlLPENIENDSIKSPAQIEKVEEVPDNVTPYGEI-------ERIPMT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 254 AMQAAVSKNMVES-LSVPAFRVGYPI-------LTDKLDELYEKVKPKGVTMTVLLAKAAAMALAQYPVVNAS-CRDGAS 324
Cdd:PRK14843 125 PMRKVIAQRMVESyLTAPTFTLNYEVdmtemlaLRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASlTEDGKT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 325 FTYNSSINIAVAVAIDGGLITPVLEQADKLDIYLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNLGMFGVDRFDAILPP 404
Cdd:PRK14843 205 IITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQ 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 960478043 405 GQGAIMAVGAS--KPTVTadkDGFFSVKNKMLVNVTADHRIVYGADLAAFLQTFAKIIEDPESL 466
Cdd:PRK14843 285 PNSAILGVSSTieKPVVV---NGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISM 345
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
45-468 |
2.39e-36 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 138.43 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 45 EIFMPALSSTMTEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALLAESEEDV 124
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 125 ALAVAQAQALSSGQAQQAPPPSDADAppppspppaaaapapvaaGTKGVATPQAKKLAKQHRVDLAKVTGTGQFGRITPA 204
Cdd:PRK05704 84 AAAAAAAAAAAAAAAPAQAQAAAAAE------------------QSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 205 DVEAAAGIQPKPKVAPPtaaapvaapsvrAVPQASVLPPVPGATV--VPFTAMQAAVSKNMVESLSVPAfrvgypILT-- 280
Cdd:PRK05704 146 DVLAALAAAAAAPAAPA------------AAAPAAAPAPLGARPEerVPMTRLRKTIAERLLEAQNTTA------MLTtf 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 281 ------------DKLDELYEK---VK-------PKGVTmtvllakaaaMALAQYPVVNASCrDGASFTYNSSINIAVAVA 338
Cdd:PRK05704 208 nevdmtpvmdlrKQYKDAFEKkhgVKlgfmsffVKAVV----------EALKRYPEVNASI-DGDDIVYHNYYDIGIAVG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 339 IDGGLITPVLEQADKLDIYLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNLGMFGVDRFDAILPPGQGAIMAVGASK-- 416
Cdd:PRK05704 277 TPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKer 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 960478043 417 PTVtadKDGFFSVKNKMLVNVTADHRIVYGADLAAFLQTFAKIIEDPESLTL 468
Cdd:PRK05704 357 PVA---VNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
68-468 |
3.61e-35 |
|
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: 137.31 E-value: 3.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 68 GDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALLAESEEDVALAVAQAQALSSGQAQQAPPPSD 147
Cdd:TIGR01348 140 GDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPATAPAPASAQPAAQSPAATQPEP 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 148 ADAPPPPSPPPAAAAPAPVAAGTK-GVATPQAKKLAKQHRVDLAKVTGTGQFGRITPADVEAAAGIQPKPKVAPptaaap 226
Cdd:TIGR01348 220 AAAPAAAKAQAPAPQQAGTQNPAKvDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAA------ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 227 vaapSVRAVPQASVLPPVPGATV--------VPFTAMQAAVSKNMVES-LSVP--------------AFRVGYPILTDKL 283
Cdd:TIGR01348 294 ----AASAAGGAPGALPWPNVDFskfgeveeVDMSRIRKISGANLTRNwTMIPhvthfdkaditemeAFRKQQNAAVEKE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 284 DelyekVKpkgVTMTVLLAKAAAMALAQYPVVNASCR-DGASFTYNSSINIAVAVAIDGGLITPVLEQADKLDIYLLSQK 362
Cdd:TIGR01348 370 G-----VK---LTVLHILMKAVAAALKKFPKFNASLDlGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 363 WKELVKKARAKQLQPNEYNSGTFTLSNLGMFGVDRFDAILPPGQGAIMavGASKPTVTADKDGF-FSVKNKMLVNVTADH 441
Cdd:TIGR01348 442 LSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAIL--GVSKSGMEPVWNGKeFEPRLMLPLSLSYDH 519
|
410 420
....*....|....*....|....*..
gi 960478043 442 RIVYGADLAAFLQTFAKIIEDPESLTL 468
Cdd:TIGR01348 520 RVIDGADAARFTTYICESLADIRRLLL 546
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
45-117 |
2.54e-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: 2.54e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 960478043 45 EIFMPALSSTMTEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALL 117
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
43-118 |
8.36e-26 |
|
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: 100.14 E-value: 8.36e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 960478043 43 IREIFMPALSSTMTEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALLA 118
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
171-466 |
5.83e-24 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 101.79 E-value: 5.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 171 KGVATPQAKKLAKQHRVDLAKVTGTGQFGRITPADVEAAAGIQPKPKVAPPTAAAPVAAPSVRAVPQASVlPPVPGATVV 250
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAA-PPKLEGKRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 251 PFTAMQAAVSKNMVESLSvpafRVGYPILTDKLD-----ELYEKVKPK-----GVTMTVLL--AKAAAMALAQYPVVNAS 318
Cdd:PRK11857 80 KVAPIRKAIARAMTNSWS----NVAYVNLVNEIDmtklwDLRKSVKDPvlkteGVKLTFLPfiAKAILIALKEFPIFAAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 319 CRDGAS-FTYNSSINIAVAVAIDGGLITPVLEQADKLDIYLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNLG----MF 393
Cdd:PRK11857 156 YDEATSeLVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGsvgsLY 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 960478043 394 GVdrfdAILPPGQGAIMAVGA--SKPTVtadKDGFFSVKNKMLVNVTADHRIVYGADLAAFLQTFAKIIEDPESL 466
Cdd:PRK11857 236 GV----PVINYPELAIAGVGAiiDKAIV---KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
46-468 |
1.15e-23 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 102.84 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 46 IFMPALSSTMTEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALLAESEEdva 125
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGA--- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 126 lavaqaqalssgqaqqapppsdadappppspppaaaapapvaagtKGVATPQAKKLAKQhrvdlakvtgtgqfGRITPAD 205
Cdd:PTZ00144 124 ---------------------------------------------PPAAAPAAAAAAKA--------------EKTTPEK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 206 VEAAAGIQPKPKVAPPTAAApvaapSVRAVPQASVLPPVPGATV--------VPFTAMQAAVSKNMVESLSVPAFRVGY- 276
Cdd:PTZ00144 145 PKAAAPTPEPPAASKPTPPA-----AAKPPEPAPAAKPPPTPVAradpretrVPMSRMRQRIAERLKASQNTCAMLTTFn 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 277 -----PI--LTDKLDELYEKVKPKGVTMTVLLAKAAAMALAQYPVVNASCrDGASFTYNSSINIAVAVAIDGGLITPVLE 349
Cdd:PTZ00144 220 ecdmsALmeLRKEYKDDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYI-DGDEIVYRNYVDISVAVATPTGLVVPVIR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 350 QADKLDIYLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNLGMFGVDRFDAILPPGQGAIMAVGA--SKPTVTADKdgfF 427
Cdd:PTZ00144 299 NCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAikKRPVVVGNE---I 375
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 960478043 428 SVKNKMLVNVTADHRIVYGADLAAFLQTFAKIIEDPESLTL 468
Cdd:PTZ00144 376 VIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
45-468 |
1.11e-21 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 97.13 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 45 EIFMPALSSTMTEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALLAESEEdv 124
Cdd:PLN02226 93 EAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED-- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 125 alavAQAQALSSGQAQQApppsdadappppspppaaaapapvaagTKGVATPQAKKLAKQhRVDLAKVTGTGQFGRITPA 204
Cdd:PLN02226 171 ----AASQVTPSQKIPET---------------------------TDPKPSPPAEDKQKP-KVESAPVAEKPKAPSSPPP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 205 DVEAAAGIQpkpkvapptaaapvaapsvravpqasvLPPVPGATVVPFTAMQAAVSKNMVESLSVPAFRVGY-------- 276
Cdd:PLN02226 219 PKQSAKEPQ---------------------------LPPKERERRVPMTRLRKRVATRLKDSQNTFALLTTFnevdmtnl 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 277 -PILTDKLDELYEKVKPKGVTMTVLLAKAAAMALAQyPVVNASCrDGASFTYNSSINIAVAVAIDGGLITPVLEQADKLD 355
Cdd:PLN02226 272 mKLRSQYKDAFYEKHGVKLGLMSGFIKAAVSALQHQ-PVVNAVI-DGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 356 IYLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNLGMFGVDRFDAILPPGQGAIMAVGA--SKPTVTAdkdGFFSVKNKM 433
Cdd:PLN02226 350 FAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSivSRPMVVG---GSVVPRPMM 426
|
410 420 430
....*....|....*....|....*....|....*
gi 960478043 434 LVNVTADHRIVYGADLAAFLQTFAKIIEDPESLTL 468
Cdd:PLN02226 427 YVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
45-123 |
1.34e-18 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 88.05 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 45 EIFMPALSSTMTEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAG-ESAPVGAPIALLAESEED 123
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEEGES 83
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
43-121 |
9.71e-18 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 84.61 E-value: 9.71e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 960478043 43 IREIFMPALSSTMTEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALLAESE 121
Cdd:PRK14875 2 ITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
45-117 |
8.25e-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: 63.39 E-value: 8.25e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 960478043 45 EIFMPALSSTMTEGkIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALL 117
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
202-455 |
2.25e-11 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 66.45 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 202 TPADVEAAAGIQPKPKVAPPTAaapvaapSVRAVPQASVLPPVP---GATVVPFTAMQAAVSKNMVESLSVP---AFR-V 274
Cdd:PRK12270 74 PPAAAAPAAPPKPAAAAAAAAA-------PAAPPAAAAAAAPAAaavEDEVTPLRGAAAAVAKNMDASLEVPtatSVRaV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 275 GYPILTDK---LDELYEKVKPKGVTMTVLLAKAAAMALAQYPVVNASCR--DGA-SFTYNSSINIAVAVAI---DGG--L 343
Cdd:PRK12270 147 PAKLLIDNrivINNHLKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAevDGKpTLVTPAHVNLGLAIDLpkkDGSrqL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 344 ITPVLEQADKLDIYLLSQKWKELVKKARAKQLQPNEYNSGTFTLSNLGMFG----VDRfdaiLPPGQGAIMAVGA----- 414
Cdd:PRK12270 227 VVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGtvhsVPR----LMKGQGAIIGVGAmeypa 302
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 960478043 415 ----SKPTVTADkdgfFSVKNKMLVNVTADHRIVYGADLAAFLQT 455
Cdd:PRK12270 303 efqgASEERLAE----LGISKVMTLTSTYDHRIIQGAESGEFLRT 343
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
45-114 |
1.52e-10 |
|
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: 57.07 E-value: 1.52e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960478043 45 EIFMPALSSTMTEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPI 114
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPL 70
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
174-207 |
2.05e-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: 55.39 E-value: 2.05e-10
10 20 30
....*....|....*....|....*....|....
gi 960478043 174 ATPQAKKLAKQHRVDLAKVTGTGQFGRITPADVE 207
Cdd:pfam02817 3 ASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
50-117 |
1.64e-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: 1.64e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 960478043 50 ALSSTMTeGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALL 117
Cdd:cd06850 1 EVTAPMP-GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
50-117 |
6.27e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 48.69 E-value: 6.27e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 960478043 50 ALSSTMTeGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALL 117
Cdd:PRK09282 524 AVTSPMP-GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
45-123 |
1.34e-05 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 47.69 E-value: 1.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 960478043 45 EIFMPALSSTmtEGKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALLaESEED 123
Cdd:PRK11854 4 EIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIF-ESADG 79
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
67-117 |
3.89e-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: 40.65 E-value: 3.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 960478043 67 EGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALL 117
Cdd:COG0511 85 VGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
58-107 |
3.97e-04 |
|
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: 43.14 E-value: 3.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 960478043 58 GKIVSWSAAEGDRVTKGDAVVVVESdkadMDVETF----YDGIVAAVLVPAGES 107
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEA----MKMETTitapRDGTVKEVLVKEGDQ 1134
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
58-106 |
9.40e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 42.05 E-value: 9.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 960478043 58 GKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGE 106
Cdd:PRK12999 1085 GSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGD 1133
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
58-118 |
1.39e-03 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 41.07 E-value: 1.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 960478043 58 GKIVSWSAAEGDRVTKGDAVVVVESDKADMDVETFYDGIVAAVLVPAGESAPVGAPIALLA 118
Cdd:PRK14040 533 GNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
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