|
Name |
Accession |
Description |
Interval |
E-value |
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
71-453 |
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: 576.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAA 149
Cdd:TIGR01347 1 IEIKVPELAESITEGTVaEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 150 PAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPT-------------QMPPVPSPSQPPSGKPVSAVKPTVAPPLAEPGAG 216
Cdd:TIGR01347 81 TAAPPAKSGEEKEETPAASAAAAPTAAANRPSLspaarrlakehgiDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 217 --------KGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKAS 288
Cdd:TIGR01347 161 aaaaaapaAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 289 AFALQEQPVVNAVIDDTtkEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGT 368
Cdd:TIGR01347 241 VAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 369 FTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRV 448
Cdd:TIGR01347 319 FTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRR 398
|
....*
gi 12804939 449 LLLDL 453
Cdd:TIGR01347 399 LLLDL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
47-453 |
0e+00 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 526.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 47 KVVINNSVFSVRF--FRTTAVCKD-------DLVTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVP 116
Cdd:PTZ00144 12 PLLSSVKGMFRRFslRKLQPACSAhfsksyfSIKVIKVPTMGDSISEGTVvEWKKKVGDYVKEDEVICIIETDKVSVDIR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 117 SPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQmppvpspsQPPSG 196
Cdd:PTZ00144 92 APASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAAS--------KPTPP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 197 KPVSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNL 276
Cdd:PTZ00144 164 AAAKPPEPAPAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 277 KLGFMSAFVKASAFALQEQPVVNAVIDdtTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARK 356
Cdd:PTZ00144 244 KLGFMSAFVKASTIALKKMPIVNAYID--GDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 357 NELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFL 436
Cdd:PTZ00144 322 NKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFL 401
|
410
....*....|....*..
gi 12804939 437 RKIKAAVEDPRVLLLDL 453
Cdd:PTZ00144 402 KKIKDLIEDPARMLLDL 418
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
73-453 |
5.89e-171 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 485.88 E-value: 5.89e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 73 VKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRkTGAAPA 151
Cdd:PRK05704 5 IKVPTLPESVTEATIaTWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRID-EGAAAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 152 KAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPP--------------------SGKPVSAVKPTVAPPLA 211
Cdd:PRK05704 84 AAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENgldasavkgtgkggrvtkedVLAALAAAAAAPAAPAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 212 EPGAGK----GLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKA 287
Cdd:PRK05704 164 AAPAAApaplGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVKA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 288 SAFALQEQPVVNAVIDDTtkEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGG 367
Cdd:PRK05704 244 VVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 368 TFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPR 447
Cdd:PRK05704 322 TFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPE 401
|
....*.
gi 12804939 448 VLLLDL 453
Cdd:PRK05704 402 RLLLDL 407
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
29-453 |
3.78e-127 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 376.40 E-value: 3.78e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 29 RSLPGVSLCqgpgypnSRKVVINNSVFSvRFFRTTAVCKDDLVTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIE 107
Cdd:PLN02226 58 LALPGNSGI-------SRSASLVSSTLQ-RWVRPFSSESGDTVEAVVPHMGESITDGTLaTFLKKPGERVQADEAIAQIE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 108 TDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPV 187
Cdd:PLN02226 130 TDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQVTPSQKIPETTDPKPSPPAEDKQKPKVESAPVAEK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 188 PSPSQPPSGKPVSAVKPTVAPPlaepgagkglRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHK 267
Cdd:PLN02226 210 PKAPSSPPPPKQSAKEPQLPPK----------ERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 268 EAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDttKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTI 347
Cdd:PLN02226 280 DAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDG--DDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 348 TELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLI 427
Cdd:PLN02226 358 NGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLI 437
|
410 420
....*....|....*....|....*.
gi 12804939 428 DGREAVTFLRKIKAAVEDPRVLLLDL 453
Cdd:PLN02226 438 DGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
71-452 |
1.44e-105 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 319.43 E-value: 1.44e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 71 VTVKTPAFAESVTEGD-VRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAA 149
Cdd:PRK11856 3 FEFKMPDLGEGMTEGEiVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 150 PAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQP---------------------------------PSG 196
Cdd:PRK11856 83 EAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKaspavrklarelgvdlstvkgsgpggritkedvEAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 197 KPVSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARhkeafLKKHNL 276
Cdd:PRK11856 163 AAAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQ-----LKAIGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 277 KLGFMSAFVKASAFALQEQPVVNAVIDDTTkeVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARK 356
Cdd:PRK11856 238 KLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKARE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 357 NELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFL 436
Cdd:PRK11856 316 GKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFL 395
|
410
....*....|....*.
gi 12804939 437 RKIKAAVEDPRVLLLD 452
Cdd:PRK11856 396 KALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
238-450 |
7.38e-96 |
|
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: 287.13 E-value: 7.38e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 238 LKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNlKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDI 317
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 318 SVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMH 397
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 12804939 398 GIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLL 450
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
71-451 |
1.31e-87 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 277.47 E-value: 1.31e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 71 VTVKTPAFAEsVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAA 149
Cdd:PRK11855 120 VEVKVPDIGE-ITEVEViEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 150 PAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPP----------------------------------- 194
Cdd:PRK11855 199 PAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPhaspavrrlarelgvdlsqvkgtgkkgritkedvq 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 195 --SGKPVSAVKPTVAPPLAEPGAGKGL----------RSEHREK-MNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQE 261
Cdd:PRK11855 279 afVKGAMSAAAAAAAAAAAAGGGGLGLlpwpkvdfskFGEIETKpLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 262 MRARHKEAFlKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFA 341
Cdd:PRK11855 359 LRKQLKKEA-EKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 342 DIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALT 421
Cdd:PRK11855 438 EIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLS 517
|
410 420 430
....*....|....*....|....*....|
gi 12804939 422 YDHRLIDGREAVTFLRKIKAAVEDPRVLLL 451
Cdd:PRK11855 518 YDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
73-445 |
1.04e-76 |
|
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: 249.93 E-value: 1.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 73 VKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPA 151
Cdd:TIGR02927 129 VKMPELGESVTEGTVtSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAPA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 152 KAKPAEAPA---------AAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPPSGKPVSAVKPTV---------------- 206
Cdd:TIGR02927 209 EPAEEEAPApseagsepaPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSGDSGPYVTPLVrklakdkgvdlstvkg 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 207 ----------------------------APPLAEPGAGKG-----------LRSEhREKMNRMRQRIAQRLKEAQNTCAM 247
Cdd:TIGR02927 289 tgvggrirkqdvlaaakaaeearaaaaaPAAAAAPAAPAAaakpaepdtakLRGT-TQKMNRIRQITADKTIESLQTSAQ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 248 LTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGL 327
Cdd:TIGR02927 368 LTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGL 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 328 VVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAI- 406
Cdd:TIGR02927 448 LVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIk 527
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 12804939 407 ----GGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVED 445
Cdd:TIGR02927 528 dedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
82-451 |
8.73e-66 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 222.19 E-value: 8.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 82 VTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPA 160
Cdd:PRK11854 216 GDEVEVtEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAAAPAKQEAA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 161 AAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPPSGKPV-----------------------------SAVKPTVAPPLA 211
Cdd:PRK11854 296 APAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVrrlarefgvnlakvkgtgrkgrilkedvqAYVKDAVKRAEA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 212 EP------GAGKGL---------RSEHRE--KMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMR-ARHKEAFLKK 273
Cdd:PRK11854 376 APaaaaagGGGPGLlpwpkvdfsKFGEIEevELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRkQQNAEAEKRK 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 274 HNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEK 353
Cdd:PRK11854 456 LGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKK 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 354 ARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAV 433
Cdd:PRK11854 536 ARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGA 615
|
410
....*....|....*...
gi 12804939 434 TFLRKIKAAVEDPRVLLL 451
Cdd:PRK11854 616 RFITIINDRLSDIRRLVL 633
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
199-449 |
1.57e-55 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 186.54 E-value: 1.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 199 VSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKL 278
Cdd:PRK11857 53 ASVSSAQQAAKTAAPAAAPPKLEGKREKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 279 GFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNE 358
Cdd:PRK11857 133 TFLPFIAKAILIALKEFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 359 LAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRK 438
Cdd:PRK11857 213 IKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASR 292
|
250
....*....|.
gi 12804939 439 IKAAVEDPRVL 449
Cdd:PRK11857 293 VKELLEKPEIL 303
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
73-451 |
1.03e-53 |
|
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: 185.77 E-value: 1.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 73 VKTPAFAESVTEGD-VRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGK-VEGGTPL---------- 140
Cdd:TIGR01349 2 ITMPALSPTMTTGNlAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKdVPVNKPIavlveekedv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 141 ------FTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPS-----------QPPSGKPVSAV- 202
Cdd:TIGR01349 82 adafknYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDrifasplakklAKEKGIDLSAVa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 203 -------------------KPTVAP-------PLAEPGAGKGLRSEHRE-KMNRMRQRIAQRLKEAQNTCAMLTTFNEID 255
Cdd:TIGR01349 162 gsgpngrivkkdiesfvpqSPASANqqaaattPATYPAAAPVSTGSYEDvPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 256 MSNIQEMRARHKEAFLKKHnlKLGFMSAFVKASAFALQEQPVVNAVIDDTTkeVVYRDYIDISVAVATPRGLVVPVIRNV 335
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVY--KLSVNDFIIKASALALREVPEANSSWTDNF--IRRYKNVDISVAVATPDGLITPIVRNA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 336 EAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGK---VEV 412
Cdd:TIGR01349 318 DAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAV 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 12804939 413 RPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLL 451
Cdd:TIGR01349 398 ASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
93-451 |
2.98e-53 |
|
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: 187.00 E-value: 2.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 93 VGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAA 172
Cdd:TIGR01348 139 VGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPATAPAPASAQPAAQSPAATQPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 173 VPPPAAPIPTQMPPVPSPSQPPSGKP-----------------VSAVK-------------------PTVAPPLAEPGAG 216
Cdd:TIGR01348 219 PAAAPAAAKAQAPAPQQAGTQNPAKVdhaapavrrlarefgvdLSAVKgtgikgrilredvqrfvkePSVRAQAAAASAA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 217 KGLRSE--------------HREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAfLKKHNLKLGFMS 282
Cdd:TIGR01348 299 GGAPGAlpwpnvdfskfgevEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAA-VEKEGVKLTVLH 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 283 AFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIE 362
Cdd:TIGR01348 378 ILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPD 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 363 DMDGGTFTISN-GGVFGSLFgTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKA 441
Cdd:TIGR01348 458 EMQGACFTISSlGGIGGTAF-TPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICE 536
|
410
....*....|
gi 12804939 442 AVEDPRVLLL 451
Cdd:TIGR01348 537 SLADIRRLLL 546
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
227-451 |
1.11e-40 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 148.51 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 227 MNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTT 306
Cdd:PRK14843 123 MTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 307 KEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFG-SLFGtPI 385
Cdd:PRK14843 203 KTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGvQSFG-PI 281
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12804939 386 INPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLL 451
Cdd:PRK14843 282 INQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
253-453 |
1.11e-37 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 142.17 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 253 EIDMSNIQEMRARHKEAfLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVI 332
Cdd:PLN02528 215 EINVDALVELKASFQEN-NTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNI 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 333 RNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRP-VAIGGKVE 411
Cdd:PLN02528 294 KNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPrFVDDGNVY 373
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 12804939 412 VRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL 453
Cdd:PLN02528 374 PASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHM 415
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
76-451 |
2.80e-33 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 131.90 E-value: 2.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 76 PAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGK-VEGGTPLFTLRKTGAAPAKA 153
Cdd:PLN02744 118 PSLSPTMTEGNIaRWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKeIKVGEVIAITVEEEEDIGKF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 154 KPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPPSGKPVSAVKPTVAPPLAEPGAG---------KGLRSEHR 224
Cdd:PLN02744 198 KDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEdnnvplssiKGTGPDGR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 225 EKMNRMRQRIAQRLKEAQ---NTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNL------------------------- 276
Cdd:PLN02744 278 IVKADIEDYLASGGKGATappSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIphyyltvdtrvdklmalrsqlnslq 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 277 ------KLGFMSAFVKASAFALQEQPVVNAvidDTTKEVVyRDY--IDISVAVATPRGLVVPVIRNVEAMNFADIERTIT 348
Cdd:PLN02744 358 easggkKISVNDLVIKAAALALRKVPQCNS---SWTDDYI-RQYhnVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 349 ELGEKARKNELAIEDMDGGTFTISN-GGVFGSLFGTPIINPPQSAILGMhGIFDRPVAIG---GKVEVRPMMYVALTYDH 424
Cdd:PLN02744 434 QLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAV-GSAEKRVIPGsgpDQYNFASFMSVTLSCDH 512
|
410 420
....*....|....*....|....*..
gi 12804939 425 RLIDGREAVTFLRKIKAAVEDPRVLLL 451
Cdd:PLN02744 513 RVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
71-143 |
6.34e-24 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 94.39 E-value: 6.34e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12804939 71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:cd06849 1 TEIKMPDLGESMTEGTIvEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
71-143 |
7.59e-23 |
|
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: 91.51 E-value: 7.59e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12804939 71 VTVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:pfam00364 1 TEIKSPMIGESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
71-143 |
8.78e-23 |
|
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: 91.67 E-value: 8.78e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12804939 71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:COG0508 3 IEIKMPDLGESMTEGTIvEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
283-439 |
2.47e-17 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 84.94 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 283 AFVKAsafaLQEQPVVNAVID--DTTKEVVYRDYIDISVAVATP-----RGLVVPVIRNVEAMNFADIERTITELGEKAR 355
Cdd:PRK12270 179 ALVQA----LKAFPNMNRHYAevDGKPTLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRAR 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 356 KNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMhGIFDRPVAIGGKVE-------VRPMMYVALTYDHRLID 428
Cdd:PRK12270 255 DGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGV-GAMEYPAEFQGASEerlaelgISKVMTLTSTYDHRIIQ 333
|
170
....*....|.
gi 12804939 429 GREAVTFLRKI 439
Cdd:PRK12270 334 GAESGEFLRTI 344
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
72-141 |
2.04e-15 |
|
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: 70.93 E-value: 2.04e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12804939 72 TVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLF 141
Cdd:cd06663 1 TILIPDLAQHLGDGTVvKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLV 71
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
71-140 |
2.27e-14 |
|
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: 75.05 E-value: 2.27e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12804939 71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPL 140
Cdd:TIGR02927 3 ESVKMPALGESVTEGTVtSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVL 73
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
82-143 |
1.45e-10 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 63.48 E-value: 1.45e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12804939 82 VTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:PRK11854 12 ADEVEVtEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIF 74
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
87-143 |
1.58e-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: 56.66 E-value: 1.58e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 12804939 87 VRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:cd06850 11 VKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
93-144 |
6.66e-10 |
|
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: 56.83 E-value: 6.66e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 12804939 93 VGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLR 144
Cdd:COG0511 85 VGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
72-140 |
8.77e-09 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 56.88 E-value: 8.77e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12804939 72 TVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPL 140
Cdd:PRK14875 4 PITMPKWGLSMTEGKVaGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
73-143 |
4.78e-07 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 51.84 E-value: 4.78e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12804939 73 VKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGK-VEGGTPLFTL 143
Cdd:PRK11892 5 ILMPALSPTMEEGTLaKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTPIAVL 77
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
91-143 |
9.99e-06 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 43.46 E-value: 9.99e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 12804939 91 KAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
93-145 |
1.27e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 44.45 E-value: 1.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 12804939 93 VGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRK 145
Cdd:PRK09282 540 EGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
91-125 |
1.76e-03 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 37.51 E-value: 1.76e-03
10 20 30
....*....|....*....|....*....|....*
gi 12804939 91 KAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEA 125
Cdd:cd06848 37 PEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVE 71
|
|
| |
