|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-430 |
2.96e-158 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 452.71 E-value: 2.96e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 1 MQTYNLPDVGEGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAVAGADD 80
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 81 QPAPTAPSDPAPAAADAGGSVlvgygtGGEVKTRRRKPRHEVAVASSVGVVAKPPIRKLARDLGIDLADVTASGPAGEVT 160
Cdd:PRK11856 82 AEAAAAAEAAPEAPAPEPAPA------AAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRIT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 161 RDDVLRHAEQAKVFRNLETPQWPtererripVAPASTDDRYETIPVKGVRKATANAMVGSAYTAPHVSVWTDVDASRTME 240
Cdd:PRK11856 156 KEDVEAAAAAAAPAAAAAAAAAA--------APPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 241 FVKRLKQQPqfadVRVSPLLVFAKALLWAVQRTPEINSAWVDteqgAEIHVRNYVNLGIAAATPRGLLVPNIKDAHALSM 320
Cdd:PRK11856 228 LRKQLKAIG----VKLTVTDFLIKAVALALKKFPELNASWDD----DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 321 RELAVALQNLTQTARDGKTTPEDQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGAIRQKPWVVDGEVRPAWVTTVSG 400
Cdd:PRK11856 300 FELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSL 379
|
410 420 430
....*....|....*....|....*....|
gi 1605155346 401 SFDHRIVDGDKISRFIADIAAVLEEPALLL 430
Cdd:PRK11856 380 SFDHRVIDGADAARFLKALKELLENPALLL 409
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
5-431 |
6.29e-101 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 310.99 E-value: 6.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 5 NLPDVGEgLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAVAGADDQPAP 84
Cdd:PRK11855 123 KVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 85 TAPSDPAPAAADAGGSvlvgygtggEVKTRRRKPRHEVAVASSVGVVAK-----PPIRKLARDLGIDLADVTASGPAGEV 159
Cdd:PRK11855 202 AAAPAAAAPAAAAAAA---------PAPAPAAAAAPAAAAPAAAAAPGKaphasPAVRRLARELGVDLSQVKGTGKKGRI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 160 TRDDVLRHAEQAKVFRNLETPQWPTERERRIPVAPA-----STDDRYETIPVKGVRKATANAMVGSAYTAPHVSVWTDVD 234
Cdd:PRK11855 273 TKEDVQAFVKGAMSAAAAAAAAAAAAGGGGLGLLPWpkvdfSKFGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEAD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 235 ASRTMEFVKRLKQQPQFADVRVSPLLVFAKALLWAVQRTPEINSAwVDtEQGAEIHVRNYVNLGIAAATPRGLLVPNIKD 314
Cdd:PRK11855 353 ITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNAS-LD-EDGDELTYKKYFNIGFAVDTPNGLVVPVIKD 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 315 AHALSMRELAVALQNLTQTARDGKTTPEDQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGAIRQKPWVVDGEVRPAW 394
Cdd:PRK11855 431 VDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRL 510
|
410 420 430
....*....|....*....|....*....|....*..
gi 1605155346 395 VTTVSGSFDHRIVDGDKISRFIADIAAVLEEPALLLD 431
Cdd:PRK11855 511 MLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
217-430 |
2.76e-87 |
|
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: 264.41 E-value: 2.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 217 MVGSAYTAPHVSVWTDVDASRTMEFVKRLKQQPQFADVRVSPLLVFAKALLWAVQRTPEINSAWvdTEQGAEIHVRNYVN 296
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASW--DGEEGEIVYKKYVN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 297 LGIAAATPRGLLVPNIKDAHALSMRELAVALQNLTQTARDGKTTPEDQQGGTITITNIGVFGMDAGTPIINPGEAGIVAM 376
Cdd:pfam00198 79 IGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1605155346 377 GAIRQKPWVVDGEVRPAWVTTVSGSFDHRIVDGDKISRFIADIAAVLEEPALLL 430
Cdd:pfam00198 159 GRIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
5-431 |
3.24e-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: 245.41 E-value: 3.24e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 5 NLPDVGEGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAVAGADDQPAP 84
Cdd:TIGR01347 4 KVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 85 TAPSDPAPAAadaggsvlvgygtggEVKTRRRKPrheVAVASSVGVVAKPPIRKLARDLGIDLADVTASGPAGEVTRDDV 164
Cdd:TIGR01347 84 PPAKSGEEKE---------------ETPAASAAA---APTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 165 LRHAEQakvfRNLETPQWPTERERripvAPASTDDRYETIPVKGVRKATANAMVGSAYTAPHVSVWTDVDASRTMEFVKR 244
Cdd:TIGR01347 146 IKKTEA----PASAQPPAAAAAAA----APAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 245 LKQQPQFA-DVRVSPLLVFAKALLWAVQRTPEINsAWVDteqGAEIHVRNYVNLGIAAATPRGLLVPNIKDAHALSMREL 323
Cdd:TIGR01347 218 YKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVN-AEID---GDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 324 AVALQNLTQTARDGKTTPEDQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGAIRQKPWVVDG--EVRPawVTTVSGS 401
Cdd:TIGR01347 294 EKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGqiEIRP--MMYLALS 371
|
410 420 430
....*....|....*....|....*....|.
gi 1605155346 402 FDHRIVDGDKISRFIADIAAVLEEPA-LLLD 431
Cdd:TIGR01347 372 YDHRLIDGKEAVTFLVTIKELLEDPRrLLLD 402
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
7-431 |
1.69e-76 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 243.59 E-value: 1.69e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 7 PDVGEGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTpILAVAGADDQPAPTA 86
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQ-VLGRIDEGAAAGAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 87 PSDPAPaaadaggsvlvgygtggEVKTRRRKPRHEVAVASSVGVVAKPPIRKLARDLGIDLADVTASGPAGEVTRDDVLR 166
Cdd:PRK05704 87 AAAAAA-----------------AAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 167 HAEQAKvfrnleTPQWPTERERRIPVAPASTDDRYETIPVKGVRKATANAMVGSAYTAPHVSVWTDVDASRTMEFVKRLK 246
Cdd:PRK05704 150 ALAAAA------AAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 247 QqpQFA---DVRVSPLLVFAKALLWAVQRTPEINsAWVDteqGAEIHVRNYVNLGIAAATPRGLLVPNIKDAHALSMREL 323
Cdd:PRK05704 224 D--AFEkkhGVKLGFMSFFVKAVVEALKRYPEVN-ASID---GDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 324 AVALQNLTQTARDGKTTPEDQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGAIRQKPWVVDGEV--RPawVTTVSGS 401
Cdd:PRK05704 298 EKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIviRP--MMYLALS 375
|
410 420 430
....*....|....*....|....*....|.
gi 1605155346 402 FDHRIVDGDKISRFIADIAAVLEEPA-LLLD 431
Cdd:PRK05704 376 YDHRIIDGKEAVGFLVTIKELLEDPErLLLD 406
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
6-430 |
2.94e-73 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 235.77 E-value: 2.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 6 LPDVGEGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAVAGADDQPAPT 85
Cdd:PLN02528 3 LAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 86 APSDPAPAAADAGgsvlvgygTGGEVKTRRRKPRhevavassvGVVAKPPIRKLARDLGIDLADVTASGPAGEVTRDDVL 165
Cdd:PLN02528 83 DSLLLPTDSSNIV--------SLAESDERGSNLS---------GVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 166 RHAEQAKVFR-----NLETPQWPTERERRIPvAPASTDDRYETIPVKGVRKATANAMVGSAyTAPHVSVWTDVDASRTME 240
Cdd:PLN02528 146 KYAAQKGVVKdsssaEEATIAEQEEFSTSVS-TPTEQSYEDKTIPLRGFQRAMVKTMTAAA-KVPHFHYVEEINVDALVE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 241 FVKRLKQQPQFADVRVSPLLVFAKALLWAVQRTPEINSAWVdtEQGAEIHVRNYVNLGIAAATPRGLLVPNIKDAHALSM 320
Cdd:PLN02528 224 LKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFN--EETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 321 RELAVALQNLTQTARDGKTTPEDQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGAIRQKPWVVD-GEVRPAWVTTVS 399
Cdd:PLN02528 302 LEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVT 381
|
410 420 430
....*....|....*....|....*....|.
gi 1605155346 400 GSFDHRIVDGDKISRFIADIAAVLEEPALLL 430
Cdd:PLN02528 382 IGADHRVLDGATVARFCNEWKSYVEKPELLM 412
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
5-424 |
5.86e-71 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 235.28 E-value: 5.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 5 NLPDVGegLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPIL-------AVAG 77
Cdd:PRK11854 210 NVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMrfevegaAPAA 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 78 ADDQPAPTAPSDPAPAAADAGGSVLVGYGTGGEVKTRRRKPRhevavassvgvvAKPPIRKLARDLGIDLADVTASGPAG 157
Cdd:PRK11854 288 APAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVH------------ATPLVRRLAREFGVNLAKVKGTGRKG 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 158 EVTRDDVLRHAEQAkVFRNLETPQWPTERERRIPVAPASTDD-----RYETIPVKGVRKATANAMVGSAYTAPHVSVWTD 232
Cdd:PRK11854 356 RILKEDVQAYVKDA-VKRAEAAPAAAAAGGGGPGLLPWPKVDfskfgEIEEVELGRIQKISGANLHRNWVMIPHVTQFDK 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 233 VDASRTMEFvkrLKQQPQFA-----DVRVSPLLVFAKALLWAVQRTPEINSAWvdTEQGAEIHVRNYVNLGIAAATPRGL 307
Cdd:PRK11854 435 ADITELEAF---RKQQNAEAekrklGVKITPLVFIMKAVAAALEQMPRFNSSL--SEDGQRLTLKKYVNIGIAVDTPNGL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 308 LVPNIKDAHALSMRELAVALQNLTQTARDGKTTPEDQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGAIRQKPwVVD 387
Cdd:PRK11854 510 VVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEP-VWN 588
|
410 420 430
....*....|....*....|....*....|....*...
gi 1605155346 388 G-EVRPAWVTTVSGSFDHRIVDGDKISRFIADIAAVLE 424
Cdd:PRK11854 589 GkEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
5-430 |
8.85e-64 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273567 [Multi-domain] Cd Length: 436 Bit Score: 211.58 E-value: 8.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 5 NLPDVGEGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEG-DTVDVGTPIL-------AVA 76
Cdd:TIGR01349 3 TMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAvlveekeDVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 77 GADDQPAPTAPSDPAPAAADAGGSVLVGYGTGGEVKTRRRK----PRHEVAVASSVGVVAKPPIRKLARDLGIDLADVTA 152
Cdd:TIGR01349 83 DAFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPepssPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 153 SGPAGEVTRDDVLRHAEQAKvfRNLETPQWPTERERRIPVAPASTDDrYETIPVKGVRKATANAMVGSAYTAPHVSVWTD 232
Cdd:TIGR01349 163 SGPNGRIVKKDIESFVPQSP--ASANQQAAATTPATYPAAAPVSTGS-YEDVPLSNIRKIIAKRLLESKQTIPHYYVSIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 233 VDASRTMEFVKRL-KQQPQFADVRVSPLLVfaKALLWAVQRTPEINSAWVDTEqgaeIHVRNYVNLGIAAATPRGLLVPN 311
Cdd:TIGR01349 240 CNVDKLLALRKELnAMASEVYKLSVNDFII--KASALALREVPEANSSWTDNF----IRRYKNVDISVAVATPDGLITPI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 312 IKDAHALSMRELAVALQNLTQTARDGKTTPEDQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGAIRQKPWVVDGEVR 391
Cdd:TIGR01349 314 VRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEK 393
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1605155346 392 P---AWVTTVSGSFDHRIVDGDKISRFIADIAAVLEEPALLL 430
Cdd:TIGR01349 394 GfavASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEML 435
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
3-430 |
5.05e-62 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 206.46 E-value: 5.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 3 TYNLPDVGEGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILavagaddqp 82
Cdd:PTZ00144 46 VIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLS--------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 83 aptapsdpapaaadaggsvlvgygtggEVKTRRRKPRHEVAVASSVGVVAKPPIRKLArdlgidlADVTASGPAgevtrD 162
Cdd:PTZ00144 117 ---------------------------EIDTGGAPPAAAPAAAAAAKAEKTTPEKPKA-------AAPTPEPPA-----A 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 163 DVLRHAEQAKvfrNLETPQWPTErerriPVAPASTDDRYET-IPVKGVRKATANAMVGSAYTAPHVSVWTDVDASRTMEF 241
Cdd:PTZ00144 158 SKPTPPAAAK---PPEPAPAAKP-----PPTPVARADPRETrVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 242 VKRLKQQPQFAD-VR---VSPllvFAKALLWAVQRTPEINsAWVDteqGAEIHVRNYVNLGIAAATPRGLLVPNIKDAHA 317
Cdd:PTZ00144 230 RKEYKDDFQKKHgVKlgfMSA---FVKASTIALKKMPIVN-AYID---GDEIVYRNYVDISVAVATPTGLVVPVIRNCEN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 318 LSMRELAVALQNLTQTARDGKTTPEDQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGAIRQKPWVVDGEVRPAWVTT 397
Cdd:PTZ00144 303 KSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMY 382
|
410 420 430
....*....|....*....|....*....|...
gi 1605155346 398 VSGSFDHRIVDGDKISRFIADIAAVLEEPALLL 430
Cdd:PTZ00144 383 LALTYDHRLIDGRDAVTFLKKIKDLIEDPARML 415
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-430 |
2.24e-60 |
|
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: 205.49 E-value: 2.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 2 QTYNLPDVGeGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAVAGADD- 80
Cdd:TIGR01348 117 QEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSt 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 81 QPAPTAPSDPAPAAADAGGSVLVGYGTGGEVKTRRRKPRHEVAVASSVGVVAKPPIRKLARDLGIDLADVTASGPAGEVT 160
Cdd:TIGR01348 196 PATAPAPASAQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRIL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 161 RDDVLRHAEQAKVfrnlETPQWPTERERRIPVAPA------STDDRYETIPVKGVRKATANAMVGSAYTAPHVSVWTDVD 234
Cdd:TIGR01348 276 REDVQRFVKEPSV----RAQAAAASAAGGAPGALPwpnvdfSKFGEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKAD 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 235 ASRTMEFVKRLKQQPQFADVRVSPLLVFAKALLWAVQRTPEINSAWvdTEQGAEIHVRNYVNLGIAAATPRGLLVPNIKD 314
Cdd:TIGR01348 352 ITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASL--DLGGEQLILKKYVNIGVAVDTPNGLLVPVIKD 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 315 AHALSMRELAVALQNLTQTARDGKTTPEDQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGAIRQKPwVVDG-EVRPA 393
Cdd:TIGR01348 430 VDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEP-VWNGkEFEPR 508
|
410 420 430
....*....|....*....|....*....|....*..
gi 1605155346 394 WVTTVSGSFDHRIVDGDKISRFIADIAAVLEEPALLL 430
Cdd:TIGR01348 509 LMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
134-429 |
1.97e-46 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 162.27 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 134 PPIRKLARDLGIDLADVTASGPAGEVTRDDVLRHAEQAKvfrNLETPQWPTE-------RERRIPVAPASTDDRYETiPV 206
Cdd:PRK11857 6 PIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLK---SAPTPAEAASvssaqqaAKTAAPAAAPPKLEGKRE-KV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 207 KGVRKATANAMVGSAYTAPHVSVWTDVDASRTMEFVKRLKQQPQ-FADVRVSPLLVFAKALLWAVQRTPeINSAWVDtEQ 285
Cdd:PRK11857 82 APIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLkTEGVKLTFLPFIAKAILIALKEFP-IFAAKYD-EA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 286 GAEIHVRNYVNLGIAAATPRGLLVPNIKDAHALSMRELAVALQNLTQTARDGKTTPEDQQGGTITITNIGVFGMDAGTPI 365
Cdd:PRK11857 160 TSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1605155346 366 INPGEAGIVAMGAIRQKPWVVDGEVRPAWVTTVSGSFDHRIVDGDKISRFIADIAAVLEEPALL 429
Cdd:PRK11857 240 INYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
6-431 |
3.53e-45 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 163.00 E-value: 3.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 6 LPDVGEGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAVAGADDqpapt 85
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED----- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 86 apsdpapaaadaggsvlvgygTGGEVKTRRRKPrhevavassvgvvakppirklardlgiDLADVTASGPAGEVTRDDVl 165
Cdd:PLN02226 171 ---------------------AASQVTPSQKIP---------------------------ETTDPKPSPPAEDKQKPKV- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 166 rhaEQAKVFRNLETPQWPTERERRIPVAPASTDDRYETIPVKGVRKATANAMVGSAYTAPHVSVWTDVDASRTMEFvkRL 245
Cdd:PLN02226 202 ---ESAPVAEKPKAPSSPPPPKQSAKEPQLPPKERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKL--RS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 246 KQQPQFAD---VRVSPLLVFAKALLWAVQRTPEINsAWVDteqGAEIHVRNYVNLGIAAATPRGLLVPNIKDAHALSMRE 322
Cdd:PLN02226 277 QYKDAFYEkhgVKLGLMSGFIKAAVSALQHQPVVN-AVID---GDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 323 LAVALQNLTQTARDGKTTPEDQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGAIRQKPWVVDGEVRPAWVTTVSGSF 402
Cdd:PLN02226 353 IEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTY 432
|
410 420 430
....*....|....*....|....*....|
gi 1605155346 403 DHRIVDGDKISRFIADIAAVLEEPA-LLLD 431
Cdd:PLN02226 433 DHRLIDGREAVYFLRRVKDVVEDPQrLLLD 462
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
134-430 |
1.08e-44 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 158.92 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 134 PPIRKLARDLGIDLADVTASGPAGEVTRDDVLRHAEQAKVFRNLETPQwpteRERRIPVAPASTD--DRYETIPVKGVRK 211
Cdd:PRK14843 53 PLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPA----QIEKVEEVPDNVTpyGEIERIPMTPMRK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 212 ATANAMVGSAYTAPHVSVWTDVDASRTMEFVKRLKQ---QPQFADVRVSPLLVFA--KALLwavqRTPEINSAWvdTEQG 286
Cdd:PRK14843 129 VIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEpimEATGKKTTVTDLLSLAvvKTLM----KHPYINASL--TEDG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 287 AEIHVRNYVNLGIAAATPRGLLVPNIKDAHALSMRELAVALQNLTQTARDGKTTPEDQQGGTITITNIGVFGMDAGTPII 366
Cdd:PRK14843 203 KTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPII 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1605155346 367 NPGEAGIVAMGAIRQKPWVVDGEVRPAWVTTVSGSFDHRIVDGDKISRFIADIAAVLEEPALLL 430
Cdd:PRK14843 283 NQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISML 346
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
6-425 |
4.00e-42 |
|
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: 156.71 E-value: 4.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 6 LPDVGEGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTpILAVAG-------- 77
Cdd:TIGR02927 7 MPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGG-VLAIIGepgeagse 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 78 ----------ADDQPAPTAPSDPAPAAADAGGSVLVGYGTGGEVK----------------------------------- 112
Cdd:TIGR02927 86 papaapepeaAPEPEAPAPAPTPAAEAPAPAAPQAGGSGEATEVKmpelgesvtegtvtswlkavgdtvevdepllevst 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 113 ------------------------------------------------------------TRRRKPRHEVAVASSVGVVA 132
Cdd:TIGR02927 166 dkvdteipspvagtlleirapeddtvevgtvlaiigdanaapaepaeeeapapseagsepAPDPAARAPHAAPDPPAPAP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 133 KPP-----------------------IRKLARDLGIDLADVTASGPAGEVTRDDVLRHAEQAKVFRNLETPQWPTE---- 185
Cdd:TIGR02927 246 APAktaapaaaapvssgdsgpyvtplVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAapaa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 186 -RERRIPVAPASTDDRYETIPVKGVRKATANAMVGSAYTAPHVSVWTDVDASRTMEFVKRLKqqPQFAD---VRVSPLLV 261
Cdd:TIGR02927 326 pAAAAKPAEPDTAKLRGTTQKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAK--NDFLEkngVNLTFLPF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 262 FAKALLWAVQRTPEINSAWvdTEQGAEIHVRNYVNLGIAAATPRGLLVPNIKDAHALSMRELAVALQNLTQTARDGKTTP 341
Cdd:TIGR02927 404 FVQAVTEALKAHPNVNASY--NAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKP 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 342 EDQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGAIRQKPWVVDGE-------VRPawVTTVSGSFDHRIVDGDKISR 414
Cdd:TIGR02927 482 DELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEdggesiaIRS--VCYLPLTYDHRLVDGADAGR 559
|
570
....*....|.
gi 1605155346 415 FIADIAAVLEE 425
Cdd:TIGR02927 560 FLTTIKKRLEE 570
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
2-430 |
5.88e-41 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 152.70 E-value: 5.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 2 QTYNLPDVGEGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEG-DTVDVGTpILAVAGAD- 79
Cdd:PLN02744 113 QEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGE-VIAITVEEe 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 80 -------DQPAPTAPSDPAPAAADAGGSVLVGYGTGGEVKTRRRKPRHEVAVASSVGVVAKPPIRKLARDLGIDLADVTA 152
Cdd:PLN02744 192 edigkfkDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 153 SGPAGEVTRDDVLRHAEQAKvfrnletpqwpTERERRIPVAPASTDDRYETIPVKGVRKATANAMVGSAYTAPHVSVWTD 232
Cdd:PLN02744 272 TGPDGRIVKADIEDYLASGG-----------KGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 233 VDASRTMEFVKRL---KQQPQFADVRVSPLLVFAKALlwAVQRTPEINSAWVDTeqgaeiHVRNY--VNLGIAAATPRGL 307
Cdd:PLN02744 341 TRVDKLMALRSQLnslQEASGGKKISVNDLVIKAAAL--ALRKVPQCNSSWTDD------YIRQYhnVNINVAVQTENGL 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 308 LVPNIKDAHALSMRELAVALQNLTQTARDGKTTPEDQQGGTITITNI-GVFGMDAGTPIINPGEAGIVAMGAIRQK--PW 384
Cdd:PLN02744 413 YVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRviPG 492
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1605155346 385 VVDGEVRPAWVTTVSGSFDHRIVDGDKISRFIADIAAVLEEPALLL 430
Cdd:PLN02744 493 SGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESML 538
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-76 |
4.37e-30 |
|
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: 111.31 E-value: 4.37e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1605155346 1 MQTYNLPDVGEGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAVA 76
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
5-72 |
1.21e-27 |
|
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: 104.41 E-value: 1.21e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1605155346 5 NLPDVGEGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPI 72
Cdd:cd06849 4 KMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVI 71
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
7-73 |
1.08e-18 |
|
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: 79.95 E-value: 1.08e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1605155346 7 PDVGEGLTEAeIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPIL 73
Cdd:pfam00364 6 PMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLA 71
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
265-423 |
2.54e-17 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 84.56 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 265 ALLWAVQRTPEINSAWvDTEQGAEIHVRN-YVNLGIAAATP-----RGLLVPNIKDAHALSMRELAVALQNLTQTARDGK 338
Cdd:PRK12270 179 ALVQALKAFPNMNRHY-AEVDGKPTLVTPaHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 339 TTPEDQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGAIrqkpwvvdgEVRPAW---------------VTTVSGSFD 403
Cdd:PRK12270 258 LTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM---------EYPAEFqgaseerlaelgiskVMTLTSTYD 328
|
170 180
....*....|....*....|
gi 1605155346 404 HRIVDGDKISRFIADIAAVL 423
Cdd:PRK12270 329 HRIIQGAESGEFLRTIHQLL 348
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
6-79 |
2.82e-14 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 73.82 E-value: 2.82e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1605155346 6 LPDVGEGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAVAGAD 79
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
5-80 |
1.41e-13 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 72.73 E-value: 1.41e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1605155346 5 NLPDVGegLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAVAGADD 80
Cdd:PRK11854 6 KVPDIG--ADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADG 79
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
18-75 |
2.83e-13 |
|
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: 64.36 E-value: 2.83e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1605155346 18 IVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAV 75
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
6-72 |
6.92e-12 |
|
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: 60.53 E-value: 6.92e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1605155346 6 LPDVGEGLTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPI 72
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPL 70
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
13-79 |
1.14e-09 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 59.93 E-value: 1.14e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1605155346 13 LTEAEIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEG-DTVDVGTPIlAVAGAD 79
Cdd:PRK11892 14 MEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPI-AVLLEE 80
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
23-75 |
1.17e-09 |
|
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: 56.06 E-value: 1.17e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1605155346 23 VKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAV 75
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
134-165 |
1.50e-09 |
|
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: 53.07 E-value: 1.50e-09
10 20 30
....*....|....*....|....*....|..
gi 1605155346 134 PPIRKLARDLGIDLADVTASGPAGEVTRDDVL 165
Cdd:pfam02817 5 PAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
18-76 |
6.51e-09 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 58.02 E-value: 6.51e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1605155346 18 IVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAVA 76
Cdd:PRK14040 535 IFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
26-77 |
1.54e-07 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 48.47 E-value: 1.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1605155346 26 GDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAVAG 77
Cdd:PRK07051 29 GDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
18-77 |
2.88e-07 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 52.54 E-value: 2.88e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1605155346 18 IVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAVAG 77
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
18-69 |
4.73e-06 |
|
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: 48.92 E-value: 4.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1605155346 18 IVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVG 69
Cdd:COG1038 1087 VVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAG 1138
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
7-73 |
1.30e-05 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 44.85 E-value: 1.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1605155346 7 PDVGEGLTEA----EIVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPIL 73
Cdd:PRK05641 80 ASAGENVVTApmpgKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLI 150
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
18-69 |
1.45e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 47.44 E-value: 1.45e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1605155346 18 IVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVG 69
Cdd:PRK12999 1087 VVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAG 1138
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
23-76 |
2.78e-04 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 42.52 E-value: 2.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1605155346 23 VKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAVA 76
Cdd:PLN02983 220 VKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPLFVIE 273
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
24-57 |
3.78e-04 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 39.44 E-value: 3.78e-04
10 20 30
....*....|....*....|....*....|....
gi 1605155346 24 KPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAE 57
Cdd:cd06848 38 EVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVE 71
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
22-69 |
9.82e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 37.46 E-value: 9.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1605155346 22 HVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVG 69
Cdd:PRK08225 16 VVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEG 63
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
18-75 |
5.52e-03 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 38.93 E-value: 5.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1605155346 18 IVQWHVKPGDTVAVNDVVAEIETAKSLVELPSPYAGTVAELLVAEGDTVDVGTPILAV 75
Cdd:PRK14042 536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRV 593
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
46-73 |
6.98e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 35.08 E-value: 6.98e-03
10 20
....*....|....*....|....*...
gi 1605155346 46 ELPSPYAGTVAELLVAEGDTVDVGTPIL 73
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLA 28
|
|
| |
