|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
2-409 |
1.26e-172 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 488.92 E-value: 1.26e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 2 EIKMPKLGESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVICHMDVEGESS 81
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 82 DNTSEEVSNDDQ----PQNDTTQVTDNSQDNKQDENAPKNNGRYSPVVFKLASENEINLSQVVGTGFEGRVTKKDIEKAI 157
Cdd:PRK11856 84 AAAAAEAAPEAPapepAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 158 KEGTAKEsshyvnAKTPPVNTPTTKGTQEPGSSIPVNGVRKQIAQNMVNSVNEIPHAWMMIEADATNLVKTRNHHKdsfk 237
Cdd:PRK11856 164 AAAAPAA------AAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLK---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 238 nKEGYNLTFFAFFVKAVAESLKAYPLLNSSWQNDEIVIHKDVNISIAVADEDKLYVPVIKNADEKSIKGIAREINDLAQK 317
Cdd:PRK11856 234 -AIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 318 ARYKKLRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQIESIVKKPVVIDDMIAIRNMVNLCLSIDHRILDGLQAG 397
Cdd:PRK11856 313 AREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAA 392
|
410
....*....|..
gi 1940089828 398 RFMNYVKTRIEQ 409
Cdd:PRK11856 393 RFLKALKELLEN 404
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-409 |
1.54e-120 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 361.06 E-value: 1.54e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 2 EIKMPKLGEsVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVICHMDVEGESS 81
Cdd:PRK11855 121 EVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 82 DNTSEEVSNDDQPQNDTTQVTDNSQ----DNKQDENAPKNNGRY--SPVVFKLASENEINLSQVVGTGFEGRVTKKDIEK 155
Cdd:PRK11855 200 AAAAAPAAAAPAAAAAAAPAPAPAAaaapAAAAPAAAAAPGKAPhaSPAVRRLARELGVDLSQVKGTGKKGRITKEDVQA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 156 AIK----------EGTAKESSHYVNAKTPPVNTPTTKGTQEPgssIPVNGVRKQIAQNMVNSVNEIPHAWMMIEADATNL 225
Cdd:PRK11855 280 FVKgamsaaaaaaAAAAAAGGGGLGLLPWPKVDFSKFGEIET---KPLSRIKKISAANLHRSWVTIPHVTQFDEADITDL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 226 VKTRNHHKDSFKnKEGYNLTFFAFFVKAVAESLKAYPLLNSSWQND--EIVIHKDVNISIAVADEDKLYVPVIKNADEKS 303
Cdd:PRK11855 357 EALRKQLKKEAE-KAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDgdELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKS 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 304 IKGIAREINDLAQKARYKKLRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQIESIVKKPVVIDDMIAIRNMVNLC 383
Cdd:PRK11855 436 LLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLS 515
|
410 420
....*....|....*....|....*.
gi 1940089828 384 LSIDHRILDGLQAGRFMNYVKTRIEQ 409
Cdd:PRK11855 516 LSYDHRVIDGATAARFTNYLKQLLAD 541
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
2-409 |
2.01e-115 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 342.97 E-value: 2.01e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 2 EIKMPKLGESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVICHMDvEGESS 81
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRID-EGAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 82 dNTSEEVSNDDQPQNDTTQVTDNSQDNKQDENAPknngrySPVVFKLASENEINLSQVVGTGFEGRVTKKDIEKAIKEGT 161
Cdd:PRK05704 83 -GAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDAL------SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 162 AKesshyvnAKTPPVNTPTTKGTQEPGSS---IPVNGVRKQIAQNMVNSVNEiphAWMMI---EADATNLVKTRNHHKDS 235
Cdd:PRK05704 156 AA-------PAAPAAAAPAAAPAPLGARPeerVPMTRLRKTIAERLLEAQNT---TAMLTtfnEVDMTPVMDLRKQYKDA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 236 FKNKEGYNLTFFAFFVKAVAESLKAYPLLNSSWQNDEIVIHKDVNISIAVADEDKLYVPVIKNADEKSIKGIAREINDLA 315
Cdd:PRK05704 226 FEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 316 QKARYKKLRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQIESIVKKPVVIDDMIAIRNMVNLCLSIDHRILDGLQ 395
Cdd:PRK05704 306 KKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKE 385
|
410
....*....|....
gi 1940089828 396 AGRFMNYVKTRIEQ 409
Cdd:PRK05704 386 AVGFLVTIKELLED 399
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
2-413 |
5.44e-106 |
|
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: 324.66 E-value: 5.44e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 2 EIKMPKLGESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVICHMDVEGESS 81
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 82 DNTSEEVS---NDDQPQNDTTQVTDNSQDNKQDENAPK-----------------NNGRY-SPVVFKLASENEINLSQVV 140
Cdd:TIGR02927 208 AEPAEEEApapSEAGSEPAPDPAARAPHAAPDPPAPAPapaktaapaaaapvssgDSGPYvTPLVRKLAKDKGVDLSTVK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 141 GTGFEGRVTKKDIEKAIK-EGTAKESSHYVNAKTPPVNTPTTKGTQEP------GSSIPVNGVRKQIAQNMVNSVNEIPH 213
Cdd:TIGR02927 288 GTGVGGRIRKQDVLAAAKaAEEARAAAAAPAAAAAPAAPAAAAKPAEPdtaklrGTTQKMNRIRQITADKTIESLQTSAQ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 214 AWMMIEADATNLVKTRNHHKDSFKNKEGYNLTFFAFFVKAVAESLKAYPLLNSSWQND--EIVIHKDVNISIAVADEDKL 291
Cdd:TIGR02927 368 LTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAEtkEVTYHDVEHVGIAVDTPRGL 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 292 YVPVIKNADEKSIKGIAREINDLAQKARYKKLRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQIESIVKKPVVID 371
Cdd:TIGR02927 448 LVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIK 527
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1940089828 372 D-----MIAIRNMVNLCLSIDHRILDGLQAGRFMNYVKTRIEQYAIE 413
Cdd:TIGR02927 528 DedggeSIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDFE 574
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
2-408 |
2.55e-105 |
|
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: 317.06 E-value: 2.55e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 2 EIKMPKLGESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVICHMDVEGESS 81
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 82 DNTSEEVSNDDQPQndttqvTDNSQDNKQDENAPKNNGrySPVVFKLASENEINLSQVVGTGFEGRVTKKDIEK-AIKEG 160
Cdd:TIGR01347 82 AAPPAKSGEEKEET------PAASAAAAPTAAANRPSL--SPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKkTEAPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 161 TAKESSHYVNAKTPPVNTPTTKgtqepgsSIPVNGVRKQIAQNMVNSVNEIPHAWMMIEADATNLVKTRNHHKDSFKNKE 240
Cdd:TIGR01347 154 SAQPPAAAAAAAAPAAATRPEE-------RVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 241 GYNLTFFAFFVKAVAESLKAYPLLNSSWQNDEIVIHKDVNISIAVADEDKLYVPVIKNADEKSIKGIAREINDLAQKARY 320
Cdd:TIGR01347 227 GVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 321 KKLRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQIESIVKKPVVIDDMIAIRNMVNLCLSIDHRILDGLQAGRFM 400
Cdd:TIGR01347 307 GKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFL 386
|
....*...
gi 1940089828 401 NYVKTRIE 408
Cdd:TIGR01347 387 VTIKELLE 394
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-408 |
4.79e-102 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 316.17 E-value: 4.79e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 2 EIKMPKLGesVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVICHMDVEG--- 78
Cdd:PRK11854 208 DVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGaap 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 79 --ESSDNTSEEVSNDDQPQNDTTQVTDNSQDNKQDENAPKNNGRYSPVVFKLASENEINLSQVVGTGFEGRVTKKDIEKA 156
Cdd:PRK11854 286 aaAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAY 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 157 IKEGTAKesshyvnAKTPPVNTPTtkGTQEPGSS---------------IPVNGVRKQIAQNMVNSVNEIPHAWMMIEAD 221
Cdd:PRK11854 366 VKDAVKR-------AEAAPAAAAA--GGGGPGLLpwpkvdfskfgeieeVELGRIQKISGANLHRNWVMIPHVTQFDKAD 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 222 ATNLVKTRNHHKD-SFKNKEGYNLTFFAFFVKAVAESLKAYPLLNSSWQND--EIVIHKDVNISIAVADEDKLYVPVIKN 298
Cdd:PRK11854 437 ITELEAFRKQQNAeAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDgqRLTLKKYVNIGIAVDTPNGLVVPVFKD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 299 ADEKSIKGIAREINDLAQKARYKKLRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQIESIVKKPVVIDDMIAIRN 378
Cdd:PRK11854 517 VNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRL 596
|
410 420 430
....*....|....*....|....*....|
gi 1940089828 379 MVNLCLSIDHRILDGLQAGRFMNYVKTRIE 408
Cdd:PRK11854 597 MLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
204-409 |
5.76e-98 |
|
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: 291.37 E-value: 5.76e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 204 MVNSVNEIPHAWMMIEADATNLVKTRNHHKDSFKnKEGYNLTFFAFFVKAVAESLKAYPLLNSSW--QNDEIVIHKDVNI 281
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAA-DEETKLTFLPFLVKAVALALKKFPELNASWdgEEGEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 282 SIAVADEDKLYVPVIKNADEKSIKGIAREINDLAQKARYKKLRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQIE 361
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1940089828 362 SIVKKPVVIDDMIAIRNMVNLCLSIDHRILDGLQAGRFMNYVKTRIEQ 409
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLEN 207
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
3-408 |
3.48e-87 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 271.17 E-value: 3.48e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 3 IKMPKLGESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVICHMDVEGESSD 82
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 83 NTSEEVSNDDQPQNDTTQvTDNSQDNKQDENAPKnngryspvvfklaseneinlsqvvgtgfegrVTKKDIEKAIKEgta 162
Cdd:PTZ00144 127 AAPAAAAAAKAEKTTPEK-PKAAAPTPEPPAASK-------------------------------PTPPAAAKPPEP--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 163 kesshyvnAKTPPVNTPTTKGTQEPGSSIPVNGVRKQIAQNMVNSVNEIPHAWMMIEADATNLVKTRNHHKDSFKNKEGY 242
Cdd:PTZ00144 172 --------APAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 243 NLTFFAFFVKAVAESLKAYPLLNSSWQNDEIVIHKDVNISIAVADEDKLYVPVIKNADEKSIKGIAREINDLAQKARYKK 322
Cdd:PTZ00144 244 KLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 323 LRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQIESIVKKPVVIDDMIAIRNMVNLCLSIDHRILDGLQAGRFMNY 402
Cdd:PTZ00144 324 LTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKK 403
|
....*.
gi 1940089828 403 VKTRIE 408
Cdd:PTZ00144 404 IKDLIE 409
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-408 |
2.82e-83 |
|
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: 261.65 E-value: 2.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 2 EIKMPKLGESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEG-ETVSVGEVICHM-----D 75
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLveekeD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 76 VEGESSDNTSEEVSNDDQPQNDTTQVTDNSQDNKQDENAPKNNGRYSPV----------VF------KLASENEINLSQV 139
Cdd:TIGR01349 81 VADAFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAplsdkesgdrIFasplakKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 140 VGTGFEGRVTKKDIEKAiKEGTAKESSHYVNAKTPPVNTPTTKGTQEPGSSIPVNGVRKQIAQNMVNSVNEIPHAWMMIE 219
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESF-VPQSPASANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 220 ADATNLVKTRNHHKDSfkNKEGYNLTFFAFFVKAVAESLKAYPLLNSSWQNDEIVIHKDVNISIAVADEDKLYVPVIKNA 299
Cdd:TIGR01349 240 CNVDKLLALRKELNAM--ASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 300 DEKSIKGIAREINDLAQKARYKKLRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQIESIVKKPVVIDD---MIAI 376
Cdd:TIGR01349 318 DAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDeekGFAV 397
|
410 420 430
....*....|....*....|....*....|..
gi 1940089828 377 RNMVNLCLSIDHRILDGLQAGRFMNYVKTRIE 408
Cdd:TIGR01349 398 ASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLE 429
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-403 |
8.37e-77 |
|
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: 248.25 E-value: 8.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 2 EIKMPKLGeSVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVIchMDVEGESS 81
Cdd:TIGR01348 118 EVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLI--LTLSVAGS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 82 DNTSEEVSNDDQPQNDTTQVTDNS---------QDNKQDENAPKNNGRY----SPVVFKLASENEINLSQVVGTGFEGRV 148
Cdd:TIGR01348 195 TPATAPAPASAQPAAQSPAATQPEpaaapaaakAQAPAPQQAGTQNPAKvdhaAPAVRRLAREFGVDLSAVKGTGIKGRI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 149 TKKDIEKAIKE--GTAKESSHYVNAKTP-----PVNTPTTKGTQEpgsSIPVNGVRKQIAQNMVNSVNEIPHAWMMIEAD 221
Cdd:TIGR01348 275 LREDVQRFVKEpsVRAQAAAASAAGGAPgalpwPNVDFSKFGEVE---EVDMSRIRKISGANLTRNWTMIPHVTHFDKAD 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 222 ATNLVKTRNHHKDSfKNKEGYNLTFFAFFVKAVAESLKAYPLLNSSWQND-EIVIHKD-VNISIAVADEDKLYVPVIKNA 299
Cdd:TIGR01348 352 ITEMEAFRKQQNAA-VEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGgEQLILKKyVNIGVAVDTPNGLLVPVIKDV 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 300 DEKSIKGIAREINDLAQKARYKKLRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQIESIVKKPVVIDDMIAIRNM 379
Cdd:TIGR01348 431 DRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLM 510
|
410 420
....*....|....*....|....
gi 1940089828 380 VNLCLSIDHRILDGLQAGRFMNYV 403
Cdd:TIGR01348 511 LPLSLSYDHRVIDGADAARFTTYI 534
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
9-409 |
2.91e-72 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 232.69 E-value: 2.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 9 GESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVICHMDVEGEssdNTSEEV 88
Cdd:PLN02528 7 GEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDS---QHLRSD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 89 SNddQPQNDTTQVTDNSQDnkqDENAPKNNGRYS-PVVFKLASENEINLSQVVGTGFEGRVTKKDIEK-AIKEGTAKESS 166
Cdd:PLN02528 84 SL--LLPTDSSNIVSLAES---DERGSNLSGVLStPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKyAAQKGVVKDSS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 167 HYVNAkTPPVNTPTTKGTQEPGSS------IPVNGVRKQIAQNMVNSVnEIPHAWMMIEADATNLVKTrnhhKDSFKNKE 240
Cdd:PLN02528 159 SAEEA-TIAEQEEFSTSVSTPTEQsyedktIPLRGFQRAMVKTMTAAA-KVPHFHYVEEINVDALVEL----KASFQENN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 241 ---GYNLTFFAFFVKAVAESLKAYPLLNSSWQND--EIVIHKDVNISIAVADEDKLYVPVIKNADEKSIKGIAREINDLA 315
Cdd:PLN02528 233 tdpTVKHTFLPFLIKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 316 QKARYKKLRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQIESIVKKPVVIDD-MIAIRNMVNLCLSIDHRILDGL 394
Cdd:PLN02528 313 HLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDgNVYPASIMTVTIGADHRVLDGA 392
|
410
....*....|....*
gi 1940089828 395 QAGRFMNYVKTRIEQ 409
Cdd:PLN02528 393 TVARFCNEWKSYVEK 407
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
1-408 |
4.09e-70 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 230.51 E-value: 4.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 1 MEIKMPKLGESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEG-ETVSVGEVICHM----- 74
Cdd:PLN02744 113 QEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIAITveeee 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 75 ------DVEGESSDNTSEEVSNDDQPQNDTTQVTDNSQDNK----QDENAPKNNGRY--SPVVFKLASENEINLSQVVGT 142
Cdd:PLN02744 193 digkfkDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEpkasKPSAPPSSGDRIfaSPLARKLAEDNNVPLSSIKGT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 143 GFEGRVTKKDIE----KAIKEGTAKESShyvnaktpPVNTPTTKGTQEPGSSIpvngvRKQIAQNMVNSVNEIPHAWMMI 218
Cdd:PLN02744 273 GPDGRIVKADIEdylaSGGKGATAPPST--------DSKAPALDYTDIPNTQI-----RKVTASRLLQSKQTIPHYYLTV 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 219 EADATNLVKTRNHHKDSFKNKEGYNLTFFAFFVKAVAESLKAYPLLNSSWQNDEIVIHKDVNISIAVADEDKLYVPVIKN 298
Cdd:PLN02744 340 DTRVDKLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKD 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 299 ADEKSIKGIAREINDLAQKARYKKLRSEDMQGGTFTVNNT-GTFGSVSSMGIINHPQAAILQIESIVKK--PVVIDDMIA 375
Cdd:PLN02744 420 ADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYN 499
|
410 420 430
....*....|....*....|....*....|...
gi 1940089828 376 IRNMVNLCLSIDHRILDGLQAGRFMNYVKTRIE 408
Cdd:PLN02744 500 FASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIE 532
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
1-408 |
2.44e-60 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 203.06 E-value: 2.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 1 MEIKMPKLGESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVICHMDvegES 80
Cdd:PLN02226 92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIIS---KS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 81 SDNTSEEVSNDDQPQNDTTQVTDNSQDNKqdenapknngryspvvfklaseneinlsqvvgtgfegrvtKKDIEKAIKEG 160
Cdd:PLN02226 169 EDAASQVTPSQKIPETTDPKPSPPAEDKQ----------------------------------------KPKVESAPVAE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 161 TAKESShyvnakTPPVNTPTTKGTQEPGSS----IPVNGVRKQIAQNMVNSVNEIPHAWMMIEADATNLVKTRNHHKDSF 236
Cdd:PLN02226 209 KPKAPS------SPPPPKQSAKEPQLPPKErerrVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 237 KNKEGYNLTFFAFFVKAVAESLKAYPLLNSSWQNDEIVIHKDVNISIAVADEDKLYVPVIKNADEKSIKGIAREINDLAQ 316
Cdd:PLN02226 283 YEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 317 KARYKKLRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQIESIVKKPVVIDDMIAIRNMVNLCLSIDHRILDGLQA 396
Cdd:PLN02226 363 KANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREA 442
|
410
....*....|..
gi 1940089828 397 GRFMNYVKTRIE 408
Cdd:PLN02226 443 VYFLRRVKDVVE 454
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
122-409 |
2.92e-60 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 198.09 E-value: 2.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 122 SPVVFKLASENEINLSQVVGTGFEGRVTKKDIEKAIKEGT-----AKESSHYVNAKTPPVNTPTTKGTQEPGSSIPVNGV 196
Cdd:PRK11857 5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKsaptpAEAASVSSAQQAAKTAAPAAAPPKLEGKREKVAPI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 197 RKQIAQNMVNSVNEIPHAWMMIEADATNLVKTRNHHKDSFKNKEGYNLTFFAFFVKAVAESLKAYPLLNSSW--QNDEIV 274
Cdd:PRK11857 85 RKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYdeATSELV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 275 IHKDVNISIAVADEDKLYVPVIKNADEKSIKGIAREINDLAQKARYKKLRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQ 354
Cdd:PRK11857 165 YPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPE 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1940089828 355 AAILQIESIVKKPVVIDDMIAIRNMVNLCLSIDHRILDGLQAGRFMNYVKTRIEQ 409
Cdd:PRK11857 245 LAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEK 299
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
104-408 |
2.39e-50 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 173.55 E-value: 2.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 104 NSQDNKQDENAPK--NNGRYSPVVFKLASENEINLSQVVGTGFEGRVTKKDIEKAIKEGTAKESSHYVNAKTPPVNTPTT 181
Cdd:PRK14843 32 NGRVHKEDVETYKdtNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 182 KGTQEPGSSIPVNGVRKQIAQNMVNSVNEIPHAWMMIEADATNLVKTRNHHKDSFKNKEGYNLTFFAFFVKAVAESLKAY 261
Cdd:PRK14843 112 VTPYGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 262 PLLNSSWQND--EIVIHKDVNISIAVADEDKLYVPVIKNADEKSIKGIAREINDLAQKARYKKLRSEDMQGGTFTVNNTG 339
Cdd:PRK14843 192 PYINASLTEDgkTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLG 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 340 TFGsVSSMG-IINHPQAAILQIESIVKKPVVIDDMIAIRNMVNLCLSIDHRILDGLQAGRFMNYVKTRIE 408
Cdd:PRK14843 272 MFG-VQSFGpIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIE 340
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
2-72 |
9.59e-32 |
|
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: 115.55 E-value: 9.59e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1940089828 2 EIKMPKLGESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVIC 72
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIA 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1-72 |
9.57e-31 |
|
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: 112.50 E-value: 9.57e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1940089828 1 MEIKMPKLGESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVIC 72
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIA 72
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
2-72 |
1.80e-20 |
|
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: 84.57 E-value: 1.80e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1940089828 2 EIKMPKLGESVHEGtIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVIC 72
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLA 71
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
2-71 |
5.66e-19 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 87.69 E-value: 5.66e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 2 EIKMPKLGESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVI 71
Cdd:PRK14875 4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
171-403 |
1.10e-16 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 82.63 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 171 AKTPPVNTPTTKGTQEPGS------SIPVNGVRKQIAQNMV--------NSVNEIPhAWMMIEADAT---NLVKTRNHhK 233
Cdd:PRK12270 92 AAAAPAAPPAAAAAAAPAAaavedeVTPLRGAAAAVAKNMDaslevptaTSVRAVP-AKLLIDNRIVinnHLKRTRGG-K 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 234 DSFKNKEGYnltffaffvkAVAESLKAYPLLNSSWqnDEI------VIHKDVNISIA--VADED---KLYVPVIKNADEK 302
Cdd:PRK12270 170 VSFTHLIGY----------ALVQALKAFPNMNRHY--AEVdgkptlVTPAHVNLGLAidLPKKDgsrQLVVPAIKGAETM 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 303 SIKGIAREINDLAQKARYKKLRSEDMQGGTFTVNNTGTFGSVSSMGIINHPQAAILQIESIV-------KKPVVIDDMiA 375
Cdd:PRK12270 238 DFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEypaefqgASEERLAEL-G 316
|
250 260
....*....|....*....|....*...
gi 1940089828 376 IRNMVNLCLSIDHRILDGLQAGRFMNYV 403
Cdd:PRK12270 317 ISKVMTLTSTYDHRIIQGAESGEFLRTI 344
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
2-95 |
5.50e-13 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 70.33 E-value: 5.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940089828 2 EIKMPKLGESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEG-ETVSVGEVICHMDVEGES 80
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEEGES 83
|
90
....*....|....*.
gi 1940089828 81 -SDNTSEEVSNDDQPQ 95
Cdd:PRK11892 84 aSDAGAAPAAAAEAAA 99
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
2-72 |
1.08e-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: 60.15 E-value: 1.08e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1940089828 2 EIKMPKLGESVHEGTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVIC 72
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLV 71
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
120-154 |
1.06e-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: 53.46 E-value: 1.06e-09
10 20 30
....*....|....*....|....*....|....*
gi 1940089828 120 RYSPVVFKLASENEINLSQVVGTGFEGRVTKKDIE 154
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
15-72 |
2.42e-09 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 53.19 E-value: 2.42e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1940089828 15 GTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVIC 72
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLV 65
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
15-71 |
9.41e-08 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 54.08 E-value: 9.41e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1940089828 15 GTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVI 71
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVL 587
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
21-71 |
1.08e-06 |
|
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: 47.58 E-value: 1.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1940089828 21 LVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGEVI 71
Cdd:COG0511 82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPL 132
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
15-71 |
1.99e-04 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 43.38 E-value: 1.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1940089828 15 GTIEQWLVSVGDTVEEYDP--ICEVItdKVTAEVPSSYTGTIKEITVNEGETVSVGEVI 71
Cdd:PRK14040 533 GNIFKVIVTEGQTVAEGDVllILEAM--KMETEIRAAQAGTVRGIAVKEGDAVAVGDTL 589
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
15-71 |
2.07e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 39.39 E-value: 2.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1940089828 15 GTIEQWLVSVGDTVEEYDPIceVITDKVTAEVP--SSYTGTIKEITVNEGETVSVGEVI 71
Cdd:PRK08225 10 GNVWKIVVKVGDTVEEGQDV--VILESMKMEIPivAEEAGTVKKINVQEGDFVNEGDVL 66
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
15-69 |
3.77e-04 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 40.18 E-value: 3.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1940089828 15 GTIEQWLVSVGDTVEEYDPICEVITDKVTAEVPSSYTGTIKEITVNEGETVSVGE 69
Cdd:PRK06549 70 GTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGD 124
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
15-71 |
2.92e-03 |
|
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: 40.06 E-value: 2.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1940089828 15 GTIEQWLVSVGDTVEEYDPIceVITD------KVTAEVpssyTGTIKEITVNEGETVSVGEVI 71
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPL--LTIEamkmetTITAPR----DGTVKEVLVKEGDQVEAGDLL 1141
|
|
| |
