|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-418 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 662.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 1 MIEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGA 80
Cdd:PRK05704 2 MVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 81 PVAVSTPAPAEQPKQETAEAPKAAAPSTEQTATLqglpntnrpiaSPAARKMARELGIDLNDVRSTDPLGRVRPHDVQAH 160
Cdd:PRK05704 82 AGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDAL-----------SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 161 AAAPKEAPAAPKSPAPAPVAKTEFEKPVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMTAIMELRKERKDAFEKKH 240
Cdd:PRK05704 151 LAAAAAAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 241 DVRLGFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARD 320
Cdd:PRK05704 231 GVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 321 NKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIDNErMENRPMMYIALSYDHRIVDGKEAVSF 400
Cdd:PRK05704 311 GKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQ-IVIRPMMYLALSYDHRIIDGKEAVGF 389
|
410
....*....|....*...
gi 446492058 401 LVAVKDMLEDPKSLLLEG 418
Cdd:PRK05704 390 LVTIKELLEDPERLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
2-417 |
0e+00 |
|
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: 568.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 2 IEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILdANGAP 81
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL-EEGND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 82 VAVSTPAPAEQPKQETAEAPKAAAPSTEQtatlqglpntNRPIASPAARKMARELGIDLNDVRSTDPLGRVRPHDVqaHA 161
Cdd:TIGR01347 80 ATAAPPAKSGEEKEETPAASAAAAPTAAA----------NRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDI--IK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 162 AAPKEAPAAPKSPAPAPVAKTEFEKPVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMTAIMELRKERKDAFEKKHD 241
Cdd:TIGR01347 148 KTEAPASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 242 VRLGFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDN 321
Cdd:TIGR01347 228 VKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 322 KLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIdNERMENRPMMYIALSYDHRIVDGKEAVSFL 401
Cdd:TIGR01347 308 KLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAV-NGQIEIRPMMYLALSYDHRLIDGKEAVTFL 386
|
410
....*....|....*.
gi 446492058 402 VAVKDMLEDPKSLLLE 417
Cdd:TIGR01347 387 VTIKELLEDPRRLLLD 402
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
4-417 |
2.86e-154 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 442.58 E-value: 2.86e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 4 IKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGAPVA 83
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 84 VSTPAPAEqPKQETAEAPKAAAPSTEQTAtlqglPNTNRPIASPAARKMArelgidlndvrsTDPLGRVRPHDVQAHAaa 163
Cdd:PTZ00144 127 AAPAAAAA-AKAEKTTPEKPKAAAPTPEP-----PAASKPTPPAAAKPPE------------PAPAAKPPPTPVARAD-- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 164 pkeapaapkspapapvaktefeKPVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMTAIMELRKERKDAFEKKHDVR 243
Cdd:PTZ00144 187 ----------------------PRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 244 LGFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDNKL 323
Cdd:PTZ00144 245 LGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 324 SLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIDNErMENRPMMYIALSYDHRIVDGKEAVSFLVA 403
Cdd:PTZ00144 325 TLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNE-IVIRPIMYLALTYDHRLIDGRDAVTFLKK 403
|
410
....*....|....
gi 446492058 404 VKDMLEDPKSLLLE 417
Cdd:PTZ00144 404 IKDLIEDPARMLLD 417
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-417 |
2.17e-148 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 427.28 E-value: 2.17e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 1 MIEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGA 80
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 81 PVAVSTPAPAEQ-PKQETAEAPKAAAPSTEQTATLQGLPNTNRPIASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQA 159
Cdd:PRK11856 82 AEAAAAAEAAPEaPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 160 HAAAPKEAPAAPKSPAPAPVakTEFEKPVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMTAIMELRKErkdafEKK 239
Cdd:PRK11856 162 AAAAAAPAAAAAAAAAAAPP--AAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQ-----LKA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 240 HDVRLGFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKAR 319
Cdd:PRK11856 235 IGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 320 DNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIDNErMENRPMMYIALSYDHRIVDGKEAVS 399
Cdd:PRK11856 315 EGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE-IVVRKVMPLSLSFDHRVIDGADAAR 393
|
410
....*....|....*...
gi 446492058 400 FLVAVKDMLEDPKSLLLE 417
Cdd:PRK11856 394 FLKALKELLENPALLLLE 411
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-416 |
3.20e-128 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 380.71 E-value: 3.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 2 IEIKVPELAEsITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGAP 81
Cdd:PRK11855 120 VEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 82 VAVSTPAPAEQPKQETAEAPK---AAAPSTEQTATLQGLPNTNRPIASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQ 158
Cdd:PRK11855 199 PAAAAAPAAAAPAAAAAAAPApapAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 159 ---------AHAAAPKEAPAAPKSPAPAPVAKTEFEK--PVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMTAIME 227
Cdd:PRK11855 279 afvkgamsaAAAAAAAAAAAGGGGLGLLPWPKVDFSKfgEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 228 LRKERKDAFEKKhDVRLGFMSFFTKAVVAALKQFPLLNAEI--QGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFA 305
Cdd:PRK11855 359 LRKQLKKEAEKA-GVKLTMLPFFIKAVVAALKEFPVFNASLdeDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 306 EIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAiDNERMENRPMMYIAL 385
Cdd:PRK11855 438 EIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVW-DGKEFVPRLMLPLSL 516
|
410 420 430
....*....|....*....|....*....|.
gi 446492058 386 SYDHRIVDGKEAVSFLVAVKDMLEDPKSLLL 416
Cdd:PRK11855 517 SYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
3-416 |
8.66e-114 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 346.60 E-value: 8.66e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 3 EIKVPELAesITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL-DANGAP 81
Cdd:PRK11854 208 DVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFeVEGAAP 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 82 VAVSTPAPAEQPKQETAEAPK-AAAPSTEQTATLQGLPNTNRPIASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQAH 160
Cdd:PRK11854 286 AAAPAKQEAAAPAPAAAKAEApAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAY 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 161 AAAPKEAPAAPKSPAPAPVA--------KTEFEK--PVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMTAIMELRK 230
Cdd:PRK11854 366 VKDAVKRAEAAPAAAAAGGGgpgllpwpKVDFSKfgEIEEVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRK 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 231 ERKD-AFEKKHDVRLGFMSFFTKAVVAALKQFPLLNAEI--QGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEI 307
Cdd:PRK11854 446 QQNAeAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIEL 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 308 ESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAiDNERMENRPMMYIALSY 387
Cdd:PRK11854 526 SRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVW-NGKEFAPRLMLPLSLSY 604
|
410 420
....*....|....*....|....*....
gi 446492058 388 DHRIVDGKEAVSFLVAVKDMLEDPKSLLL 416
Cdd:PRK11854 605 DHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
2-417 |
2.02e-105 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 319.78 E-value: 2.02e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 2 IEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGAp 81
Cdd:PLN02226 92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 82 vAVSTPAPAEQPKQETAEAPKAAApSTEQTATLQGLPNTNRPIAS---PAARKMARElgidlndvrstdplGRVRPHDVQ 158
Cdd:PLN02226 171 -AASQVTPSQKIPETTDPKPSPPA-EDKQKPKVESAPVAEKPKAPsspPPPKQSAKE--------------PQLPPKERE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 159 ahaaapkeapaapkspapapvaktefekpvERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMTAIMELRKERKDAFEK 238
Cdd:PLN02226 235 ------------------------------RRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 239 KHDVRLGFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKA 318
Cdd:PLN02226 285 KHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKA 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 319 RDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIDNERMEnRPMMYIALSYDHRIVDGKEAV 398
Cdd:PLN02226 365 NEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVP-RPMMYVALTYDHRLIDGREAV 443
|
410
....*....|....*....
gi 446492058 399 SFLVAVKDMLEDPKSLLLE 417
Cdd:PLN02226 444 YFLRRVKDVVEDPQRLLLD 462
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
3-410 |
5.24e-99 |
|
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: 306.94 E-value: 5.24e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 3 EIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL------- 75
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgdanaap 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 76 ------------DANGAPVAVSTPAPAEQPKQETAEAPKAAAPStEQTATLQGLPNTNRPIASPAARKMARELGIDLNDV 143
Cdd:TIGR02927 208 aepaeeeapapsEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTA-APAAAAPVSSGDSGPYVTPLVRKLAKDKGVDLSTV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 144 RSTDPLGRVRPHDVQAHAAAPKEAPAAPKSPAPAPVAKTEF--EKPVE---------RVKMSRRRQTIAKRLVEVQQTSA 212
Cdd:TIGR02927 287 KGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAaaAKPAEpdtaklrgtTQKMNRIRQITADKTIESLQTSA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 213 MLTTFNEVDMTAIMELRKERKDAFEKKHDVRLGFMSFFTKAVVAALKQFPLLNAEIQGD--ELIIKKFYDIGIAVAAPDG 290
Cdd:TIGR02927 367 QLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAEtkEVTYHDVEHVGIAVDTPRG 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 291 LVVPVVRDANQLNFAEIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAI 370
Cdd:TIGR02927 447 LLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVI 526
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 446492058 371 ----DNERMENRPMMYIALSYDHRIVDGKEAVSFLVAVKDMLED 410
Cdd:TIGR02927 527 kdedGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-416 |
1.73e-93 |
|
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: 291.39 E-value: 1.73e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 2 IEIKVPELAeSITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGA- 80
Cdd:TIGR01348 117 QEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSt 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 81 PVAVSTPAPAEQPKQETA----EAPKAAAPSTEQTATLQGLPNTNR---PIASPAARKMARELGIDLNDVRSTDPLGRVR 153
Cdd:TIGR01348 196 PATAPAPASAQPAAQSPAatqpEPAAAPAAAKAQAPAPQQAGTQNPakvDHAAPAVRRLAREFGVDLSAVKGTGIKGRIL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 154 PHDVQAHAAAPKEAPAAPKSPAPAPVA------KTEFEK--PVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMTAI 225
Cdd:TIGR01348 276 REDVQRFVKEPSVRAQAAAASAAGGAPgalpwpNVDFSKfgEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEM 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 226 MELRKERKDAFEKKhDVRLGFMSFFTKAVVAALKQFPLLNAEIQ--GDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLN 303
Cdd:TIGR01348 356 EAFRKQQNAAVEKE-GVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKG 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 304 FAEIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAiDNERMENRPMMYI 383
Cdd:TIGR01348 435 ITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVW-NGKEFEPRLMLPL 513
|
410 420 430
....*....|....*....|....*....|...
gi 446492058 384 ALSYDHRIVDGKEAVSFLVAVKDMLEDPKSLLL 416
Cdd:TIGR01348 514 SLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
204-415 |
6.13e-93 |
|
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: 278.66 E-value: 6.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 204 LVEVQQTSAMLTTFNEVDMTAIMELRKERKDAFEKKHDvRLGFMSFFTKAVVAALKQFPLLNAEIQGD--ELIIKKFYDI 281
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 282 GIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMH 361
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446492058 362 KIQVRPVAIDNErMENRPMMYIALSYDHRIVDGKEAVSFLVAVKDMLEDPKSLL 415
Cdd:pfam00198 160 RIRKRPVVVDGE-IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
11-416 |
3.27e-65 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 214.20 E-value: 3.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 11 ESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGAT---IAILDANGAPVAVSTP 87
Cdd:PLN02528 8 EGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETllkIMVEDSQHLRSDSLLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 88 APAEQPKQETAEapkaaapSTEQTATLQGLpntnrpIASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQAHAAAPKEA 167
Cdd:PLN02528 88 PTDSSNIVSLAE-------SDERGSNLSGV------LSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 168 PAAPKSPAPAPVAKTEFEKPVE-RVKMSRRRQTIAKR-----LVEVQQTSAMLTTF---NEVDMTAIMELRKERKDAfEK 238
Cdd:PLN02528 155 KDSSSAEEATIAEQEEFSTSVStPTEQSYEDKTIPLRgfqraMVKTMTAAAKVPHFhyvEEINVDALVELKASFQEN-NT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 239 KHDVRLGFMSFFTKAVVAALKQFPLLNAEIQGD--ELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGK 316
Cdd:PLN02528 234 DPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 317 KARDNKLSLKELQGGTFTITN----GGVFGSlmstPILNSPQVGILGMHKIQVRPVAIDNERMENRPMMYIALSYDHRIV 392
Cdd:PLN02528 314 LAAENKLNPEDITGGTITLSNigaiGGKFGS----PVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVL 389
|
410 420
....*....|....*....|....
gi 446492058 393 DGKEAVSFLVAVKDMLEDPKSLLL 416
Cdd:PLN02528 390 DGATVARFCNEWKSYVEKPELLML 413
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
3-416 |
5.05e-59 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 201.24 E-value: 5.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 3 EIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLL-GEPGDTVEVGATIAIL------ 75
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVkGDGAKEIKVGEVIAITveeeed 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 76 ---------DANGAPVA-VSTPAPAEqPKQETAEAPkAAAPSTEQTATLQGLPNTNRPIASPAARKMARELGIDLNDVRS 145
Cdd:PLN02744 194 igkfkdykpSSSAAPAApKAKPSPPP-PKEEEVEKP-ASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 146 TDPLGRVRPHDVQAHAAAPKEAPAAPKSPAPAPVAKTEFEKPVERVkmsrrRQTIAKRLVEVQQT--SAMLTTFNEVDmt 223
Cdd:PLN02744 272 TGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPALDYTDIPNTQI-----RKVTASRLLQSKQTipHYYLTVDTRVD-- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 224 AIMELRKERKDAFEKKHDVRLGFMSFFTKAVVAALKQFPLLNAEIQGDelIIKKFYDIGIAVA--APDGLVVPVVRDANQ 301
Cdd:PLN02744 345 KLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDD--YIRQYHNVNINVAvqTENGLYVPVVKDADK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 302 LNFAEIESEIRELGKKARDNKLSLKELQGGTFTITN-GGVFGSLMSTPILNSPQVGILGMHKIQVRPV-AIDNERMENRP 379
Cdd:PLN02744 423 KGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRVIpGSGPDQYNFAS 502
|
410 420 430
....*....|....*....|....*....|....*..
gi 446492058 380 MMYIALSYDHRIVDGKEAVSFLVAVKDMLEDPKSLLL 416
Cdd:PLN02744 503 FMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
124-414 |
1.56e-53 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 180.37 E-value: 1.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 124 IASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQAHAAAPKEAPAAPKSPAPAPVAKTE---------FEKPVERVKMS 194
Cdd:PRK11857 3 LATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAktaapaaapPKLEGKREKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 195 RRRQTIAKRLVEVQQTSAMLTTFNEVDMTAIMELRKERKDAFEKKHDVRLGFMSFFTKAVVAALKQFPLLNAEI--QGDE 272
Cdd:PRK11857 83 PIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYdeATSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 273 LIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNS 352
Cdd:PRK11857 163 LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINY 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446492058 353 PQVGILGMHKIQVRPVAIDNERMENRpMMYIALSYDHRIVDGKEAVSFLVAVKDMLEDPKSL 414
Cdd:PRK11857 243 PELAIAGVGAIIDKAIVKNGQIVAGK-VMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
126-416 |
1.32e-42 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 152.75 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 126 SPAARKMARELGIDLNDVRSTDPLGRVRPHDV-----QAHAAAPKEAPAAPKSPAPAPVAKTEFEKpVERVKMSRRRQTI 200
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVlallpENIENDSIKSPAQIEKVEEVPDNVTPYGE-IERIPMTPMRKVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 201 AKRLVEVQQTSAMLTTFNEVDMTAIMELRKERKDAFEKKHDVRLGFMSFFTKAVVAALKQFPLLNAEI--QGDELIIKKF 278
Cdd:PRK14843 131 AQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLteDGKTIITHNY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 279 YDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGIL 358
Cdd:PRK14843 211 VNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAIL 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446492058 359 GMHKIQVRPVAIDNErMENRPMMYIALSYDHRIVDGKEAVSFLVAVKDMLEDPKSLLL 416
Cdd:PRK14843 291 GVSSTIEKPVVVNGE-IVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-75 |
1.46e-27 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 104.38 E-value: 1.46e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446492058 1 MIEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
2-75 |
1.93e-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: 103.64 E-value: 1.93e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446492058 2 IEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-109 |
5.98e-23 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 101.23 E-value: 5.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 2 IEIKVPELAesITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGAP 81
Cdd:PRK11854 3 IEIKVPDIG--ADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGA 80
|
90 100
....*....|....*....|....*...
gi 446492058 82 VAvSTPAPAEQPKQETAEAPKAAAPSTE 109
Cdd:PRK11854 81 AD-AAPAQAEEKKEAAPAAAPAAAAAKD 107
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-129 |
7.35e-19 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 88.05 E-value: 7.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 1 MIEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPG-DTVEVGATIAILDANG 79
Cdd:PRK11892 2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEEG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446492058 80 APVAVSTPAPAEQPKQETAEAPKAAAPSTEQTATLQGLPNTNRPIASPAA 129
Cdd:PRK11892 82 ESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADP 131
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
3-116 |
1.03e-18 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 86.92 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 3 EIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGAP- 81
Cdd:PRK14875 4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSd 83
|
90 100 110
....*....|....*....|....*....|....*...
gi 446492058 82 ---VAVSTPAPAEQPKQETAEApkAAAPsTEQTATLQG 116
Cdd:PRK14875 84 aeiDAFIAPFARRFAPEGIDEE--DAGP-APRKARIGG 118
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
3-75 |
2.23e-17 |
|
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: 76.10 E-value: 2.23e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446492058 3 EIKVPELAESITEGtISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
253-401 |
2.78e-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: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 253 AVVAALKQFPLLN---AEIQGDELIIK-KFYDIGIA--VAAPDG---LVVPVVRDANQLNFAEIESEIRELGKKARDNKL 323
Cdd:PRK12270 179 ALVQALKAFPNMNrhyAEVDGKPTLVTpAHVNLGLAidLPKKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 324 SLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHkiqvrpvAID--------NERMENR----PMMYIALSYDHRI 391
Cdd:PRK12270 259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVG-------AMEypaefqgaSEERLAElgisKVMTLTSTYDHRI 331
|
170
....*....|
gi 446492058 392 VDGKEAVSFL 401
Cdd:PRK12270 332 IQGAESGEFL 341
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
123-158 |
4.80e-12 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 60.01 E-value: 4.80e-12
10 20 30
....*....|....*....|....*....|....*.
gi 446492058 123 PIASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQ 158
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
3-69 |
6.21e-11 |
|
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: 57.84 E-value: 6.21e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446492058 3 EIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVG 69
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGD 67
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
16-75 |
1.94e-10 |
|
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: 56.27 E-value: 1.94e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
22-76 |
3.56e-07 |
|
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: 49.12 E-value: 3.56e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446492058 22 LINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILD 76
Cdd:COG0511 82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
16-75 |
5.66e-07 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 51.77 E-value: 5.66e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
17-76 |
1.33e-05 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 42.87 E-value: 1.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 17 TISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILD 76
Cdd:PRK05889 12 SVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVIS 71
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
16-75 |
2.25e-05 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 46.46 E-value: 2.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492058 16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:PRK14040 533 GNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
16-76 |
2.46e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 42.08 E-value: 2.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446492058 16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILD 76
Cdd:PRK08225 10 GNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
16-69 |
1.81e-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: 43.91 E-value: 1.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446492058 16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVG 69
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAG 1138
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
23-93 |
1.71e-03 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 39.82 E-value: 1.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446492058 23 INVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEpgdtvevgatiaildaNGAPVAVSTPAPAEQP 93
Cdd:PLN02983 220 VKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAE----------------DGKPVSVDTPLFVIEP 274
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
16-69 |
6.76e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 36.71 E-value: 6.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446492058 16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVG 69
Cdd:PRK06549 70 GTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPG 123
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
16-72 |
8.87e-03 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 38.16 E-value: 8.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446492058 16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATI 72
Cdd:PRK14042 534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVL 590
|
|
| |
