|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1-515 |
0e+00 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 728.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 1 MSQDFILPDIGEgIVECEVVEWLISEGDTVTEDQPICDVMTDKALVQIPAVHNGVITKLYYQKGEIAKVHEPLFAMDVAG 80
Cdd:PRK11855 1 MAIEFKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 81 AIENNSPAQSTSEA---NHEQSENIEMA-------AGTALEDFILPDIGEgIVECEIVDWLVAEGDEIKEDQAVCDVMTD 150
Cdd:PRK11855 80 AAAAAAAPAAAAAPaaaAAAAPAPAAAApaaaaaaAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 151 KALVQIPAKHTGTVTKLYHQKGEIAKVHAPLFQMQVA------------SAQVIDIQKKVVDAQQNAPAKQVPEALPAVA 218
Cdd:PRK11855 159 KATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAaaapaaaaapaaAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 219 NAGKAVASPAVRRLAREHNLDISQVSGSGKNGRVYKEDIQRFLNGENSNQVSTPALSQSQP-----------VETSS--N 285
Cdd:PRK11855 239 PGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAAAAAGggglgllpwpkVDFSKfgE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 286 TRVEPIRGMQAAMAKQMMDSVSTIPHFTLSDEIDLTDLINLRKDLKEQYAKQGVKLTMMPFFIKALSLALKEFPVINSQV 365
Cdd:PRK11855 319 IETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 366 NADCTELTYFDDHNIGMAVDSKLGLLVPNIKSCQTKNMVEIANEVSRLTDQAREGRVSPQDLKGGTISISNIGAIGGTTA 445
Cdd:PRK11855 399 DEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAF 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 446 TPIINKPEVAIVALGKLQHLPrFNANGEVESRAIMQISWSGDHRIIDGATMARFNNLWKHYLETPSAMLM 515
Cdd:PRK11855 479 TPIINAPEVAILGVGKSQMKP-VWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
112-515 |
9.75e-150 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 434.60 E-value: 9.75e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 112 DFILPDIGEGIVECEIVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKGEIAKVHAPLFQMQV----- 186
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEegeae 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 187 -----ASAQVIDIQKKVVDAQQNAPAKQVPEALPAVANAGKAVASPAVRRLAREHNLDISQVSGSGKNGRVYKEDIQRFL 261
Cdd:PRK11856 84 aaaaaEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 262 NGENSNQVSTPALSQSQPVETSSNTRVEPIRGMQAAMAKQMMDSVSTIPHFTLSDEIDLTDLINLRKDLKEqyakQGVKL 341
Cdd:PRK11856 164 AAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKA----IGVKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 342 TMMPFFIKALSLALKEFPVINSQVNADctELTYFDDHNIGMAVDSKLGLLVPNIKSCQTKNMVEIANEVSRLTDQAREGR 421
Cdd:PRK11856 240 TVTDFLIKAVALALKKFPELNASWDDD--AIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 422 VSPQDLKGGTISISNIGAIGGTTATPIINKPEVAIVALGKLQHLPRFNaNGEVESRAIMQISWSGDHRIIDGATMARFNN 501
Cdd:PRK11856 318 LKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVV-DGEIVVRKVMPLSLSFDHRVIDGADAARFLK 396
|
410
....*....|....
gi 728052414 502 LWKHYLETPSAMLM 515
Cdd:PRK11856 397 ALKELLENPALLLL 410
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
113-517 |
3.51e-139 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 407.95 E-value: 3.51e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 113 FILPDIGEGIVECEIVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKGEIAKVHAPLFQMQVASAQVI 192
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 193 DIQKKVvdaQQNAPAKQVPEALPAV--ANAGKAVASPAVRRLAREHNLDISQVSGSGKNGRVYKEDIQRFL--------- 261
Cdd:PLN02528 81 RSDSLL---LPTDSSNIVSLAESDErgSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAaqkgvvkds 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 262 -NGENSN--QVSTPALSQSQPVETSSNTRVEPIRGMQAAMAKQMMDSVStIPHFTLSDEIDLTDLINLRKDLKEQYAKQG 338
Cdd:PLN02528 158 sSAEEATiaEQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAK-VPHFHYVEEINVDALVELKASFQENNTDPT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 339 VKLTMMPFFIKALSLALKEFPVINSQVNADCTELTYFDDHNIGMAVDSKLGLLVPNIKSCQTKNMVEIANEVSRLTDQAR 418
Cdd:PLN02528 237 VKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 419 EGRVSPQDLKGGTISISNIGAIGGTTATPIINKPEVAIVALGKLQHLPRFNANGEVESRAIMQISWSGDHRIIDGATMAR 498
Cdd:PLN02528 317 ENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVAR 396
|
410
....*....|....*....
gi 728052414 499 FNNLWKHYLETPSAMLMAM 517
Cdd:PLN02528 397 FCNEWKSYVEKPELLMLHM 415
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-515 |
9.07e-104 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 324.26 E-value: 9.07e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 2 SQDFILPDIGEGivECEVVEWLISEGDTVTEDQPICDVMTDKALVQIPAVHNGVITKLYYQKGEIAKVHEPLFAMDVAGA 81
Cdd:PRK11854 105 AKDVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 82 IENNSPAQSTSEANHEQSeniemAAGTALEDFILPDIGEGivECEIVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHT 161
Cdd:PRK11854 183 APAAAPAAAEAAAPAAAP-----AAAAGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 162 GTVTKLYHQKGEIAKVHAPLFQMQV---ASAQVIDIQKKVVDAQQNAPAKQvPEALPAVANAGKAV---------ASPAV 229
Cdd:PRK11854 256 GTVKEIKVNVGDKVKTGSLIMRFEVegaAPAAAPAKQEAAAPAPAAAKAEA-PAAAPAAKAEGKSEfaendayvhATPLV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 230 RRLAREHNLDISQVSGSGKNGRVYKEDIQRFLNGENSNQVSTPA------------------LSQSQPVETSSNTRVEPI 291
Cdd:PRK11854 335 RRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAaaaaggggpgllpwpkvdFSKFGEIEEVELGRIQKI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 292 RGMQAAMAKQMmdsvstIPHFTLSDEIDLTDLINLRKDLKEQYAKQ--GVKLTMMPFFIKALSLALKEFPVINSQVNADC 369
Cdd:PRK11854 415 SGANLHRNWVM------IPHVTQFDKADITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDG 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 370 TELTYFDDHNIGMAVDSKLGLLVPNIKSCQTKNMVEIANEVSRLTDQAREGRVSPQDLKGGTISISNIGAIGGTTATPII 449
Cdd:PRK11854 489 QRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIV 568
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 728052414 450 NKPEVAIVALGKLQHLPRFNANgEVESRAIMQISWSGDHRIIDGATMARFNNLWKHYLETPSAMLM 515
Cdd:PRK11854 569 NAPEVAILGVSKSAMEPVWNGK-EFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
7-515 |
1.03e-103 |
|
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: 321.44 E-value: 1.03e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 7 LPDIGEGiVECEVVEWLISEGDTVTEDQPICDVMTDKALVQIPAVHNGVITKLYYQKGEIAKVHEPLFAMDVAGAIENNS 86
Cdd:TIGR01348 5 VPDIGDN-EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGAQAQA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 87 ----------PAQSTSEANHEQSENIEmAAGTALEDFILPDIGeGIVECEIVDWLVAEGDEIKEDQAVCDVMTDKALVQI 156
Cdd:TIGR01348 84 eakkeaapapTAGAPAPAAQAQAAPAA-GQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 157 PAKHTGTVTKLYHQKGEIAKVHAPLFQMQVA-SAQVIDIQKKVVDAQQNAPAKQVPE--ALPAVANAGKAV--------- 224
Cdd:TIGR01348 162 PAPASGVVKSVKVKVGDSVPTGDLILTLSVAgSTPATAPAPASAQPAAQSPAATQPEpaAAPAAAKAQAPApqqagtqnp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 225 -----ASPAVRRLAREHNLDISQVSGSGKNGRVYKEDIQRFLNgENSNQVSTPALSQSQPV-----------ETSSNTRV 288
Cdd:TIGR01348 242 akvdhAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVK-EPSVRAQAAAASAAGGApgalpwpnvdfSKFGEVEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 289 EPIRGMQAAMAKQMMDSVSTIPHFTLSDEIDLTDLINLRKDLKEQYAKQGVKLTMMPFFIKALSLALKEFPVINSQVNAD 368
Cdd:TIGR01348 321 VDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 369 CTELTYFDDHNIGMAVDSKLGLLVPNIKSCQTKNMVEIANEVSRLTDQAREGRVSPQDLKGGTISISNIGAIGGTTATPI 448
Cdd:TIGR01348 401 GEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPI 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 728052414 449 INKPEVAIVALGKLQHLPRFNANgEVESRAIMQISWSGDHRIIDGATMARFNNLWKHYLETPSAMLM 515
Cdd:TIGR01348 481 VNAPEVAILGVSKSGMEPVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
302-514 |
2.83e-100 |
|
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: 300.61 E-value: 2.83e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 302 MMDSVSTIPHFTLSDEIDLTDLINLRKDLKEQYAKQGVKLTMMPFFIKALSLALKEFPVINSQVNADCTELTYFDDHNIG 381
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 382 MAVDSKLGLLVPNIKSCQTKNMVEIANEVSRLTDQAREGRVSPQDLKGGTISISNIGAIGGTTATPIINKPEVAIVALGK 461
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 728052414 462 LQHLPRFnANGEVESRAIMQISWSGDHRIIDGATMARFNNLWKHYLETPSAML 514
Cdd:pfam00198 161 IRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
1-509 |
3.03e-87 |
|
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: 279.59 E-value: 3.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 1 MSQDFILPDIGEGIVECEVVEWLISEGDTVTEDQPICDVMTDKALVQIPAVHNGVITKLYYQK-------GEIAKVHEPL 73
Cdd:TIGR02927 1 MAESVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEddtvevgGVLAIIGEPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 74 FAMDVAGAIENNSPAQSTSEANHEQSENIEMA---------AGTALEDFILPDIGEGIVECEIVDWLVAEGDEIKEDQAV 144
Cdd:TIGR02927 81 EAGSEPAPAAPEPEAAPEPEAPAPAPTPAAEApapaapqagGSGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 145 CDVMTDKALVQIPAKHTGTVTKLYHQKGEIAKVHAPLFQMQVASAQVIDIQKKVVDAQQNAPAKQVPE------------ 212
Cdd:TIGR02927 161 LEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAPAEPAEEEAPAPSEAGSEPAPDpaaraphaapdp 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 213 ---------------ALPAVANAGKAVASPAVRRLAREHNLDISQVSGSGKNGRVYKEDIQRFLNGEN----SNQVSTPA 273
Cdd:TIGR02927 241 papapapaktaapaaAAPVSSGDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEearaAAAAPAAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 274 LSQSQPVETSSNTRVE--PIRGMQAAM-------AKQMMDSVSTIPHFTLSDEIDLTDLINLRKDLKEQY-AKQGVKLTM 343
Cdd:TIGR02927 321 AAPAAPAAAAKPAEPDtaKLRGTTQKMnrirqitADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFlEKNGVNLTF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 344 MPFFIKALSLALKEFPVINSQVNADCTELTYFDDHNIGMAVDSKLGLLVPNIKSCQTKNMVEIANEVSRLTDQAREGRVS 423
Cdd:TIGR02927 401 LPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 424 PQDLKGGTISISNIGAIGGTTATPIINKPEVAIVALGKLQHLPRF----NANGEVESRAIMQISWSGDHRIIDGATMARF 499
Cdd:TIGR02927 481 PDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVikdeDGGESIAIRSVCYLPLTYDHRLVDGADAGRF 560
|
570
....*....|
gi 728052414 500 NNLWKHYLET 509
Cdd:TIGR02927 561 LTTIKKRLEE 570
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
116-515 |
3.29e-87 |
|
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: 274.30 E-value: 3.29e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 116 PDIGEGIVECEIVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKGEIAKVHAPLFQMQVASAQVIDIQ 195
Cdd:TIGR01347 6 PELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATAAPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 196 KKVVDAQQNAPAKQVPEALPAVANagKAVASPAVRRLAREHNLDISQVSGSGKNGRVYKEDIQRFLNGENSNQVSTPALS 275
Cdd:TIGR01347 86 AKSGEEKEETPAASAAAAPTAAAN--RPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 276 QSQPV-ETSSNTRVEPIRgMQAAMAKQMMDSVSTIPHFTLSDEIDLTDLINLRKDLKEQYAKQ-GVKLTMMPFFIKALSL 353
Cdd:TIGR01347 164 AAAPAaATRPEERVKMTR-LRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKhGVKLGFMSFFVKAVVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 354 ALKEFPVINSQVnaDCTELTYFDDHNIGMAVDSKLGLLVPNIKSCQTKNMVEIANEVSRLTDQAREGRVSPQDLKGGTIS 433
Cdd:TIGR01347 243 ALKRFPEVNAEI--DGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 434 ISNIGAIGGTTATPIINKPEVAIVALGKLQHLPrFNANGEVESRAIMQISWSGDHRIIDGATMARFNNLWKHYLETPSAM 513
Cdd:TIGR01347 321 ITNGGVFGSLMSTPIINPPQSAILGMHGIKERP-VAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRL 399
|
..
gi 728052414 514 LM 515
Cdd:TIGR01347 400 LL 401
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
116-493 |
1.09e-76 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 247.05 E-value: 1.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 116 PDIGEGIVECEIVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKGEIakvhaplfqmqVASAQVIDI- 194
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDT-----------VTVGQVLGRi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 195 --------QKKVVDAQQNAPAKQVPEALPAVANAGKAVASPAVRRLAREHNLDISQVSGSGKNGRVYKEDIQRFLNGENS 266
Cdd:PRK05704 77 degaaagaAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 267 NQVSTPALSQSQPVETSSNTRVEPIRgM---QAAMAKQMMDSVSTIPHFTLSDEIDLTDLINLRKDLKEQYAKQ-GVKLT 342
Cdd:PRK05704 157 APAAPAAAAPAAAPAPLGARPEERVP-MtrlRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKhGVKLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 343 MMPFFIKALSLALKEFPVINSQVnaDCTELTYFDDHNIGMAVDSKLGLLVPNIKSCQTKNMVEIANEVSRLTDQAREGRV 422
Cdd:PRK05704 236 FMSFFVKAVVEALKRYPEVNASI--DGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKL 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 728052414 423 SPQDLKGGTISISNIGAIGGTTATPIINKPEVAIVALGKLQHLPrFNANGEVESRAIMQISWSGDHRIIDG 493
Cdd:PRK05704 314 SIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERP-VAVNGQIVIRPMMYLALSYDHRIIDG 383
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
222-510 |
1.33e-75 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 240.85 E-value: 1.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 222 KAVASPAVRRLAREHNLDISQVSGSGKNGRVYKEDIQRFLNGENSNQVSTPALSQSQPVETSSNT-----------RVEP 290
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAapaaappklegKREK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 291 IRGMQAAMAKQMMDSVSTIPHFTLSDEIDLTDLINLRKDLKEQYAK-QGVKLTMMPFFIKALSLALKEFPVINSQVNADC 369
Cdd:PRK11857 81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKtEGVKLTFLPFIAKAILIALKEFPIFAAKYDEAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 370 TELTYFDDHNIGMAVDSKLGLLVPNIKSCQTKNMVEIANEVSRLTDQAREGRVSPQDLKGGTISISNIGAIGGTTATPII 449
Cdd:PRK11857 161 SELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 728052414 450 NKPEVAIVALGKLQHLPRFnANGEVESRAIMQISWSGDHRIIDGATMARFNNLWKHYLETP 510
Cdd:PRK11857 241 NYPELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
127-515 |
9.89e-71 |
|
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: 232.38 E-value: 9.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 127 IVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKG-EIAKVHAPL-------------FQMQVASAQVI 192
Cdd:TIGR01349 16 LAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIavlveekedvadaFKNYKLESSAS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 193 DIQKKVVDAQQN---------APAKQVPE-ALPA----VANAGKAVASPAVRRLAREHNLDISQVSGSGKNGRVYKEDIQ 258
Cdd:TIGR01349 96 PAPKPSEIAPTAppsapkpspAPQKQSPEpSSPAplsdKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 259 RFL------NGENSNQVSTPALSQSQPVETSSNTRVePIRGMQAAMAKQMMDSVSTIPHFTLSDEIDLTDLINLRKDLKE 332
Cdd:TIGR01349 176 SFVpqspasANQQAAATTPATYPAAAPVSTGSYEDV-PLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 333 QyAKQGVKLTMMPFFIKALSLALKEFPVINSQVNADCteLTYFDDHNIGMAVDSKLGLLVPNIKSCQTKNMVEIANEVSR 412
Cdd:TIGR01349 255 M-ASEVYKLSVNDFIIKASALALREVPEANSSWTDNF--IRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 413 LTDQAREGRVSPQDLKGGTISISNIGAIGGTTATPIINKPEVAIVALG--KLQHLPRFNANGEVESRAIMQISWSGDHRI 490
Cdd:TIGR01349 332 LAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGavEDVAVVDNDEEKGFAVASIMSVTLSCDHRV 411
|
410 420
....*....|....*....|....*
gi 728052414 491 IDGATMARFNNLWKHYLETPSAMLM 515
Cdd:TIGR01349 412 IDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
115-515 |
4.80e-62 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 208.77 E-value: 4.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 115 LPDIGEGIVECEIVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKGEIAKVHAPLFQMQVASAQVIDI 194
Cdd:PTZ00144 49 VPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 195 QKKVVDAQQNAPAKQVPEALPAVA---NAGKAVASPAVRRLArehnldisqvsgsgkngrvykediqrflngensnQVST 271
Cdd:PTZ00144 129 PAAAAAAKAEKTTPEKPKAAAPTPeppAASKPTPPAAAKPPE----------------------------------PAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 272 PALSQSQPVETSSNTRVEPIRGMQAAMAKQMMDSVSTIPHFTLSDEIDLTDLINLRKDLKEQYAKQ-GVKLTMMPFFIKA 350
Cdd:PTZ00144 175 AKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKhGVKLGFMSAFVKA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 351 LSLALKEFPVINSQVNADctELTYFDDHNIGMAVDSKLGLLVPNIKSCQTKNMVEIANEVSRLTDQAREGRVSPQDLKGG 430
Cdd:PTZ00144 255 STIALKKMPIVNAYIDGD--EIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 431 TISISNIGAIGGTTATPIINKPEVAIVALGKLQHLPrFNANGEVESRAIMQISWSGDHRIIDGATMARFNNLWKHYLETP 510
Cdd:PTZ00144 333 TFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRP-VVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDP 411
|
....*
gi 728052414 511 SAMLM 515
Cdd:PTZ00144 412 ARMLL 416
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
115-515 |
4.75e-55 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 193.53 E-value: 4.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 115 LPDIGEGIVECEIVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKGeiAKvhaplfQMQVASAQVI-- 192
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDG--AK------EIKVGEVIAItv 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 193 ----DIQK--------------------------KVVDAQQNAPAKQVPEALPAVANAGKAVASPAVRRLAREHNLDISQ 242
Cdd:PLN02744 189 eeeeDIGKfkdykpsssaapaapkakpsppppkeEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSS 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 243 VSGSGKNGRVYKEDIQRFLNGENSNQVSTPALSQSQPVETSSNTRVEPIRGMqaaMAKQMMDSVSTIPHFTLSDEIDLTD 322
Cdd:PLN02744 269 IKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPALDYTDIPNTQIRKV---TASRLLQSKQTIPHYYLTVDTRVDK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 323 LINLRKDLKE-QYAKQGVKLTMMPFFIKALSLALKEFPVINSQVNADCteLTYFDDHNIGMAVDSKLGLLVPNIKSCQTK 401
Cdd:PLN02744 346 LMALRSQLNSlQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDY--IRQYHNVNINVAVQTENGLYVPVVKDADKK 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 402 NMVEIANEVSRLTDQAREGRVSPQDLKGGTISISNIGA-IGGTTATPIINKPEVAIVALGKLQH--LPRfNANGEVESRA 478
Cdd:PLN02744 424 GLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAEKrvIPG-SGPDQYNFAS 502
|
410 420 430
....*....|....*....|....*....|....*..
gi 728052414 479 IMQISWSGDHRIIDGATMARFNNLWKHYLETPSAMLM 515
Cdd:PLN02744 503 FMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
226-515 |
5.02e-44 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 158.92 E-value: 5.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 226 SPAVRRLAREHNLDISQVSGSGKNGRVYKEDIQRFL--NGENSNQVSTPALSQSQPVETSSNTRVE----PIRGMQAAMA 299
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLpeNIENDSIKSPAQIEKVEEVPDNVTPYGEieriPMTPMRKVIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 300 KQMMDSVSTIPHFTLSDEIDLTDLINLRKDLKEQYAKQ-GVKLTMMPFFIKALSLALKEFPVINSQVNADCTELTYFDDH 378
Cdd:PRK14843 132 QRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEAtGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 379 NIGMAVDSKLGLLVPNIKSCQTKNMVEIANEVSRLTDQAREGRVSPQDLKGGTISISNIGAIGGTTATPIINKPEVAIVA 458
Cdd:PRK14843 212 NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILG 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 728052414 459 LGKLQHLPRFnANGEVESRAIMQISWSGDHRIIDGATMARFNNLWKHYLETPSAMLM 515
Cdd:PRK14843 292 VSSTIEKPVV-VNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
114-515 |
1.21e-41 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 155.30 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 114 ILPDIGEGIVECEIVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKGEIAKvhaplfqmqvASAQVID 193
Cdd:PLN02226 95 VVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVE----------PGTKVAI 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 194 IQKKVVDAQQNAPAKQVPEAL-PAVANAGKAVASPAVrrlarehnlDISQVSGSGKNgrvykediqrflngenSNQVSTP 272
Cdd:PLN02226 165 ISKSEDAASQVTPSQKIPETTdPKPSPPAEDKQKPKV---------ESAPVAEKPKA----------------PSSPPPP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 273 ALSQSQP-VETSSNTRVEPIRGMQAAMAKQMMDSVSTIPHFTLSDEIDLTDLINLRKDLKEQ-YAKQGVKLTMMPFFIKA 350
Cdd:PLN02226 220 KQSAKEPqLPPKERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAfYEKHGVKLGLMSGFIKA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 351 LSLALKEFPVINSQVNADctELTYFDDHNIGMAVDSKLGLLVPNIKSCQTKNMVEIANEVSRLTDQAREGRVSPQDLKGG 430
Cdd:PLN02226 300 AVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 431 TISISNIGAIGGTTATPIINKPEVAIVALGKLQHLPRFnANGEVESRAIMQISWSGDHRIIDGATMARFNNLWKHYLETP 510
Cdd:PLN02226 378 SFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV-VGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDP 456
|
....*
gi 728052414 511 SAMLM 515
Cdd:PLN02226 457 QRLLL 461
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-73 |
1.85e-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: 102.07 E-value: 1.85e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 728052414 1 MSQDFILPDIGEGIVECEVVEWLISEGDTVTEDQPICDVMTDKALVQIPAVHNGVITKLYYQKGEIAKVHEPL 73
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVI 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
111-181 |
4.97e-24 |
|
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: 95.52 E-value: 4.97e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 728052414 111 EDFILPDIGEGIVECEIVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKGEIAKVHAPL 181
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVI 73
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-74 |
1.37e-23 |
|
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: 94.01 E-value: 1.37e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 728052414 3 QDFILPDIGEGIVECEVVEWLISEGDTVTEDQPICDVMTDKALVQIPAVHNGVITKLYYQKGEIAKVHEPLF 74
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIA 72
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
112-182 |
3.74e-23 |
|
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: 92.85 E-value: 3.74e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 728052414 112 DFILPDIGEGIVECEIVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKGEIAKVHAPLF 182
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIA 72
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
272-499 |
1.26e-15 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 80.32 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 272 PALSQSQPVETSSNTRVEPIRGMQAAMAKQMMDSVStIPHFTLSDEIDLTDLINLRKDLKEQYAKQG---VKLTMMPFFi 348
Cdd:PRK12270 101 AAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLE-VPTATSVRAVPAKLLIDNRIVINNHLKRTRggkVSFTHLIGY- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 349 kALSLALKEFPVIN---SQVNADCTELTyfDDH-NIGMAVD--SKLG---LLVPNIKSCQTKNMVEIANEVSRLTDQARE 419
Cdd:PRK12270 179 -ALVQALKAFPNMNrhyAEVDGKPTLVT--PAHvNLGLAIDlpKKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRARD 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 420 GRVSPQDLKGGTISISNIGAIGGTTATPIINKPEVAIVALGKLQHLPRFNANGEvESRA------IMQISWSGDHRIIDG 493
Cdd:PRK12270 256 GKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFQGASE-ERLAelgiskVMTLTSTYDHRIIQG 334
|
....*.
gi 728052414 494 ATMARF 499
Cdd:PRK12270 335 AESGEF 340
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
225-258 |
6.56e-15 |
|
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: 68.48 E-value: 6.56e-15
10 20 30
....*....|....*....|....*....|....
gi 728052414 225 ASPAVRRLAREHNLDISQVSGSGKNGRVYKEDIQ 258
Cdd:pfam02817 3 ASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-76 |
3.89e-14 |
|
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: 67.24 E-value: 3.89e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 728052414 4 DFILPDIGEGIVEcEVVEWLISEGDTVTEDQPICDVMTDKALVQIPAVHNGVITKLYYQKGEIAKVHEPLFAM 76
Cdd:pfam00364 2 EIKSPMIGESVRE-GVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
111-182 |
2.26e-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: 65.31 E-value: 2.26e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 728052414 111 EDFILPDIGEGIVEcEIVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKGEIAKVHAPLF 182
Cdd:pfam00364 1 TEIKSPMIGESVRE-GVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLA 71
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
114-261 |
8.98e-09 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 57.26 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 114 ILPDIGEGIVECEIVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKGEIAKVHAPLfqmqvasaQVID 193
Cdd:PRK14875 6 TMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL--------AVVA 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 728052414 194 iqkkvvdaqqnapAKQVPEAlpavanAGKAVASPAVRRLAREHNlDISQVSGSGKNGRVYKEDIqRFL 261
Cdd:PRK14875 78 -------------DAEVSDA------EIDAFIAPFARRFAPEGI-DEEDAGPAPRKARIGGRTV-RYL 124
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
6-73 |
3.03e-06 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 49.56 E-value: 3.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 728052414 6 ILPDIGEGIVECEVVEWLISEGDTVTEDQPICDVMTDKALVQIPAVHNGVITKLYYQKGEIAKVHEPL 73
Cdd:PRK14875 6 TMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
7-74 |
1.23e-05 |
|
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: 43.20 E-value: 1.23e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 728052414 7 LPDIGEGIVECEVVEWLISEGDTVTEDQPICDVMTDKALVQIPAVHNGVITKLYYQKGEIAKVHEPLF 74
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLV 71
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
115-182 |
1.35e-05 |
|
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: 43.20 E-value: 1.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 728052414 115 LPDIGEGIVECEIVDWLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKGEIAKVHAPLF 182
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLV 71
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
130-229 |
4.10e-05 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 46.06 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 130 WLVAEGDEIKEDQAVCDVMTDKALVQIPAKHTGTVTKLYHQKG-EIAKVHAP---LFQMQVASAQVIDIQKKVVDAQQNA 205
Cdd:PRK11892 22 WLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPiavLLEEGESASDAGAAPAAAAEAAAAA 101
|
90 100
....*....|....*....|....
gi 728052414 206 PAKQVPEALPAVANAGKAVASPAV 229
Cdd:PRK11892 102 PAAAAAAAAKKAAPAPAAPAAPAA 125
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
127-184 |
6.58e-05 |
|
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: 40.86 E-value: 6.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 127 IVDWLVAEGDEIKEDQAVC--DVMtdKALVQIPAKHTGTVTKLYHQKGEIAKVHAPLFQM 184
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAvlEAM--KMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
19-74 |
2.71e-04 |
|
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: 39.32 E-value: 2.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 728052414 19 VVEWLISEGDTVTEDQPIC--DVMtdKALVQIPAVHNGVITKLYYQKGEIAKVHEPLF 74
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAvlEAM--KMENEVTAPVAGVVKEILVKEGDQVEAGQLLV 65
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
22-109 |
2.31e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 40.29 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 728052414 22 WLISEGDTVTEDQPICDVMTDKALVQIPAVHNGVITKLYYQKG-EIAKVHEPLFAMDVAGAIENNSPAQSTSEANHEQSE 100
Cdd:PRK11892 22 WLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEEGESASDAGAAPAAAAEAAAAA 101
|
....*....
gi 728052414 101 NIEMAAGTA 109
Cdd:PRK11892 102 PAAAAAAAA 110
|
|
| |
