|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-502 |
1.89e-163 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 468.89 E-value: 1.89e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 1 MKEVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALIDETGG 80
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 81 GASSSAPSAmqaiqdTAESPATADAQLPPQAQEEreqiggsiveashlpkadddssslfkafasdeqvkvqglggrtPAP 160
Cdd:PRK11856 82 AEAAAAAEA------APEAPAPEPAPAAAAAAAA-------------------------------------------APA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 161 QGAAQPVRNDGRVLAVPAARQLARELGLDLNRIQGSGPNGRIRVSDVLAQTQGQTASSTAAssmpasapapqpastaqaa 240
Cdd:PRK11856 113 AAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAA------------------- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 241 aqpapasskaaqgglpvAPVQYRTPKGYEHLEDRVPLRGMRRAISNQMVASHLYTVRTLTVDEVNLTRLVEFRNRVKDEA 320
Cdd:PRK11856 174 -----------------AAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIG 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 321 kaadVKLSYLPFIFKAVAVALRKYPSLNTSFDEatQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAREVVDLA 400
Cdd:PRK11856 237 ----VKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLA 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 401 GRAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRPIVdEDDNIVVAHMMYLSLSFDHRLVDGA 480
Cdd:PRK11856 311 EKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVV-VDGEIVVRKVMPLSLSFDHRVIDGA 389
|
490 500
....*....|....*....|..
gi 226319387 481 EAARFCKEVIRLLENPDRLMLE 502
Cdd:PRK11856 390 DAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
288-500 |
4.88e-100 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 299.84 E-value: 4.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 288 MVASHLYTVRTLTVDEVNLTRLVEFRNRVKDEAKAADVKLSYLPFIFKAVAVALRKYPSLNTSFDEATQEIVQKRYYNMG 367
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 368 MAVATDAGLTVPVLKDVGRKSVFELAREVVDLAGRAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHS 447
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 226319387 448 IVKRPIVdEDDNIVVAHMMYLSLSFDHRLVDGAEAARFCKEVIRLLENPDRLM 500
Cdd:pfam00198 161 IRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
3-502 |
1.16e-99 |
|
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: 305.89 E-value: 1.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 3 EVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALIDEtggGA 82
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEE---GN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 83 SSSAPSAMQAIQDTAESPATadaqlppqaqeereqiggsiveashlpkadddssslfkafasdeqvkvqglggrTPAPQG 162
Cdd:TIGR01347 79 DATAAPPAKSGEEKEETPAA------------------------------------------------------SAAAAP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 163 AAQPVRNDgrvlAVPAARQLARELGLDLNRIQGSGPNGRIRVSDVLAQTQgqtasstaassmpasapapqpastaqaaaq 242
Cdd:TIGR01347 105 TAAANRPS----LSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTE------------------------------ 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 243 papassKAAQGGLPVAPVQYRTPKGYEHLEDRVPLRGMRRAISNQMVASHLYTVRTLTVDEVNLTRLVEFRNRVKDE-AK 321
Cdd:TIGR01347 151 ------APASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEfEK 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 322 AADVKLSYLPFIFKAVAVALRKYPSLNTSFDEatQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAREVVDLAG 401
Cdd:TIGR01347 225 KHGVKLGFMSFFVKAVVAALKRFPEVNAEIDG--DDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGK 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 402 RAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRPIVdEDDNIVVAHMMYLSLSFDHRLVDGAE 481
Cdd:TIGR01347 303 KARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVA-VNGQIEIRPMMYLALSYDHRLIDGKE 381
|
490 500
....*....|....*....|.
gi 226319387 482 AARFCKEVIRLLENPDRLMLE 502
Cdd:TIGR01347 382 AVTFLVTIKELLEDPRRLLLD 402
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-75 |
1.03e-30 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 113.62 E-value: 1.03e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226319387 1 MKEVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALI 75
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
2-75 |
7.82e-29 |
|
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: 108.65 E-value: 7.82e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226319387 2 KEVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALI 75
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-502 |
1.89e-163 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 468.89 E-value: 1.89e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 1 MKEVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALIDETGG 80
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 81 GASSSAPSAmqaiqdTAESPATADAQLPPQAQEEreqiggsiveashlpkadddssslfkafasdeqvkvqglggrtPAP 160
Cdd:PRK11856 82 AEAAAAAEA------APEAPAPEPAPAAAAAAAA-------------------------------------------APA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 161 QGAAQPVRNDGRVLAVPAARQLARELGLDLNRIQGSGPNGRIRVSDVLAQTQGQTASSTAAssmpasapapqpastaqaa 240
Cdd:PRK11856 113 AAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAA------------------- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 241 aqpapasskaaqgglpvAPVQYRTPKGYEHLEDRVPLRGMRRAISNQMVASHLYTVRTLTVDEVNLTRLVEFRNRVKDEA 320
Cdd:PRK11856 174 -----------------AAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIG 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 321 kaadVKLSYLPFIFKAVAVALRKYPSLNTSFDEatQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAREVVDLA 400
Cdd:PRK11856 237 ----VKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLA 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 401 GRAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRPIVdEDDNIVVAHMMYLSLSFDHRLVDGA 480
Cdd:PRK11856 311 EKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVV-VDGEIVVRKVMPLSLSFDHRVIDGA 389
|
490 500
....*....|....*....|..
gi 226319387 481 EAARFCKEVIRLLENPDRLMLE 502
Cdd:PRK11856 390 DAARFLKALKELLENPALLLLE 411
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1-501 |
9.70e-145 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 426.16 E-value: 9.70e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 1 MKEVLLPELAEsVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALIDETGG 80
Cdd:PRK11855 2 AIEFKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 81 GASSSAPSAMQAIQDTAESPATADAQLPPQAQeerEQIGGSIVEAsHLP------------------------------- 129
Cdd:PRK11855 81 AAAAAAPAAAAAPAAAAAAAPAPAAAAPAAAA---AAAGGGVVEV-KVPdigeiteveviewlvkvgdtveedqslitve 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 130 --KAD------------------DDSSS----LFK---AFASDEQVKVQ----------------GLGGRTPAPQGAAQP 166
Cdd:PRK11855 157 tdKATmeipspvagvvkeikvkvGDKVSvgslLVVievAAAAPAAAAAPaaaapaaaaaaapapaPAAAAAPAAAAPAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 167 VRNDGRVLAVPAARQLARELGLDLNRIQGSGPNGRIRVSDVLAQTQG--QTASSTAASSmpasapapqpastaqaaaqpa 244
Cdd:PRK11855 237 AAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGamSAAAAAAAAA--------------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 245 pasSKAAQGGLPVAPVQYRTPKGYEHLEdRVPLRGMRRAISNQMVAShLYTVRTLTV-DEVNLTRLVEFRNRVKDEAKAA 323
Cdd:PRK11855 296 ---AAAGGGGLGLLPWPKVDFSKFGEIE-TKPLSRIKKISAANLHRS-WVTIPHVTQfDEADITDLEALRKQLKKEAEKA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 324 DVKLSYLPFIFKAVAVALRKYPSLNTSFDEATQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAREVVDLAGRA 403
Cdd:PRK11855 371 GVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 404 QAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRPiVDEDDNIVVAHMMYLSLSFDHRLVDGAEAA 483
Cdd:PRK11855 451 RDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-VWDGKEFVPRLMLPLSLSYDHRVIDGATAA 529
|
570
....*....|....*...
gi 226319387 484 RFCKEVIRLLENPDRLML 501
Cdd:PRK11855 530 RFTNYLKQLLADPRRMLL 547
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-502 |
1.26e-108 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 328.72 E-value: 1.26e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 1 MKEVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALIDETGG 80
Cdd:PRK05704 2 MVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 81 GASSSAPSAmqaiqdTAESPATADAqlppqaqeereqiggsiveashlpkadddssslfkafasdeqvkvqglggrtPAP 160
Cdd:PRK05704 82 AGAAAAAAA------AAAAAAAAPA----------------------------------------------------QAQ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 161 QGAAQPVRNDGrvlAVPAARQLARELGLDLNRIQGSGPNGRIRVSDVLAQTQGQTASSTAAssmpasapapqpastaqaa 240
Cdd:PRK05704 104 AAAAAEQSNDA---LSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAP------------------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 241 aqpapasskaaqgglPVAPVQYRTPKGYEHLEDRVPLRGMRRAISNQMVASHLYTVRTLTVDEVNLTRLVEFRNRVKDE- 319
Cdd:PRK05704 162 ---------------AAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAf 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 320 AKAADVKLSYLPFIFKAVAVALRKYPSLNTSFDeaTQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAREVVDL 399
Cdd:PRK05704 227 EKKHGVKLGFMSFFVKAVVEALKRYPEVNASID--GDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAEL 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 400 AGRAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRPIVdEDDNIVVAHMMYLSLSFDHRLVDG 479
Cdd:PRK05704 305 AKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVA-VNGQIVIRPMMYLALSYDHRIIDG 383
|
490 500
....*....|....*....|...
gi 226319387 480 AEAARFCKEVIRLLENPDRLMLE 502
Cdd:PRK05704 384 KEAVGFLVTIKELLEDPERLLLD 406
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-501 |
2.70e-103 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 322.34 E-value: 2.70e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 2 KEVLLPELAesVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALIdETGGG 81
Cdd:PRK11854 106 KDVHVPDIG--SDEVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVF-EVAGE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 82 ASSSAPSAMQAIQDTAESPATADAQ---LPPQAQEERE------QIGGSIVEASHL-----PKADDDSSSLFK------A 141
Cdd:PRK11854 183 APAAAPAAAEAAAPAAAPAAAAGVKdvnVPDIGGDEVEvtevmvKVGDKVEAEQSLitvegDKASMEVPAPFAgtvkeiK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 142 FASDEQVKVQGLGGR----------TPAPQGAAQP------------------------VRNDGRVLAVPAARQLARELG 187
Cdd:PRK11854 263 VNVGDKVKTGSLIMRfevegaapaaAPAKQEAAAPapaaakaeapaaapaakaegksefAENDAYVHATPLVRRLAREFG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 188 LDLNRIQGSGPNGRIRVSDVL-----AQTQGQTASSTAAssmpasapapqpastaqaaaqpapasskAAQGGLPVAPVQY 262
Cdd:PRK11854 343 VNLAKVKGTGRKGRILKEDVQayvkdAVKRAEAAPAAAA----------------------------AGGGGPGLLPWPK 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 263 RTPKGYEHLEDrVPLRGMRRaISNQMVASHLYTVRTLT-VDEVNLTRLVEFRNRVKDEA--KAADVKLSYLPFIFKAVAV 339
Cdd:PRK11854 395 VDFSKFGEIEE-VELGRIQK-ISGANLHRNWVMIPHVTqFDKADITELEAFRKQQNAEAekRKLGVKITPLVFIMKAVAA 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 340 ALRKYPSLNTSFDEATQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAREVVDLAGRAQAGKLQPDELAGSTFS 419
Cdd:PRK11854 473 ALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFT 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 420 ITNIGSIGALFSFPIINVPDAAILGVHSIVKRPiVDEDDNIVVAHMMYLSLSFDHRLVDGAEAARFCKEVIRLLENPDRL 499
Cdd:PRK11854 553 ISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEP-VWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRL 631
|
..
gi 226319387 500 ML 501
Cdd:PRK11854 632 VL 633
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
288-500 |
4.88e-100 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 299.84 E-value: 4.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 288 MVASHLYTVRTLTVDEVNLTRLVEFRNRVKDEAKAADVKLSYLPFIFKAVAVALRKYPSLNTSFDEATQEIVQKRYYNMG 367
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 368 MAVATDAGLTVPVLKDVGRKSVFELAREVVDLAGRAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHS 447
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 226319387 448 IVKRPIVdEDDNIVVAHMMYLSLSFDHRLVDGAEAARFCKEVIRLLENPDRLM 500
Cdd:pfam00198 161 IRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
3-502 |
1.16e-99 |
|
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: 305.89 E-value: 1.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 3 EVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALIDEtggGA 82
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEE---GN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 83 SSSAPSAMQAIQDTAESPATadaqlppqaqeereqiggsiveashlpkadddssslfkafasdeqvkvqglggrTPAPQG 162
Cdd:TIGR01347 79 DATAAPPAKSGEEKEETPAA------------------------------------------------------SAAAAP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 163 AAQPVRNDgrvlAVPAARQLARELGLDLNRIQGSGPNGRIRVSDVLAQTQgqtasstaassmpasapapqpastaqaaaq 242
Cdd:TIGR01347 105 TAAANRPS----LSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTE------------------------------ 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 243 papassKAAQGGLPVAPVQYRTPKGYEHLEDRVPLRGMRRAISNQMVASHLYTVRTLTVDEVNLTRLVEFRNRVKDE-AK 321
Cdd:TIGR01347 151 ------APASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEfEK 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 322 AADVKLSYLPFIFKAVAVALRKYPSLNTSFDEatQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAREVVDLAG 401
Cdd:TIGR01347 225 KHGVKLGFMSFFVKAVVAALKRFPEVNAEIDG--DDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGK 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 402 RAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRPIVdEDDNIVVAHMMYLSLSFDHRLVDGAE 481
Cdd:TIGR01347 303 KARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVA-VNGQIEIRPMMYLALSYDHRLIDGKE 381
|
490 500
....*....|....*....|.
gi 226319387 482 AARFCKEVIRLLENPDRLMLE 502
Cdd:TIGR01347 382 AVTFLVTIKELLEDPRRLLLD 402
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
3-497 |
3.85e-97 |
|
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: 305.01 E-value: 3.85e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 3 EVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALIDETGGGA 82
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 83 SSSAPSAMQAIQDTAESPATADAQLPPQAQEEREqiggsiveashlPKADDDSsslfkafasdeqvkvqglggRTPAPQG 162
Cdd:TIGR02927 208 AEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPP------------APAPAPA--------------------KTAAPAA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 163 AAQPVRNDGRVLAVPAARQLARELGLDLNRIQGSGPNGRIRVSDVLAQTQGQTASSTAASSmpasapapqpastaqaaAQ 242
Cdd:TIGR02927 256 AAPVSSGDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAA-----------------PA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 243 PAPASSKAAQGGLPVAPvqyrtpkgyehleDRVPLRG-------MRRAISNQMVASHLYTVRTLTVDEVNLTRLVEFRNR 315
Cdd:TIGR02927 319 AAAAPAAPAAAAKPAEP-------------DTAKLRGttqkmnrIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRAR 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 316 VKDEAKAAD-VKLSYLPFIFKAVAVALRKYPSLNTSFDEATQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAR 394
Cdd:TIGR02927 386 AKNDFLEKNgVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAK 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 395 EVVDLAGRAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRP--IVDED--DNIVVAHMMYLSL 470
Cdd:TIGR02927 466 AINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPrvIKDEDggESIAIRSVCYLPL 545
|
490 500
....*....|....*....|....*..
gi 226319387 471 SFDHRLVDGAEAARFCKEVIRLLENPD 497
Cdd:TIGR02927 546 TYDHRLVDGADAGRFLTTIKKRLEEGD 572
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
4-501 |
1.38e-92 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 288.16 E-value: 1.38e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 4 VLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALIDETGGGAS 83
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 84 SsapsamqaiqdtaespatadaqlppqaqeereqiggsiveasHLPKADDDSSSLFKAFASDEQvkvqglGGRTPapqga 163
Cdd:PLN02528 81 R------------------------------------------SDSLLLPTDSSNIVSLAESDE------RGSNL----- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 164 aqpvrndGRVLAVPAARQLARELGLDLNRIQGSGPNGRIRVSDVL---AQTQGQTASSTAASSmpasapapqpastaqaa 240
Cdd:PLN02528 108 -------SGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLkyaAQKGVVKDSSSAEEA----------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 241 aqpapassKAAQGGLPVAPVQYRTPKGYEhlEDRVPLRGMRRAISNQMVAS----HLYTVrtltvDEVNLTRLVEFRNRV 316
Cdd:PLN02528 164 --------TIAEQEEFSTSVSTPTEQSYE--DKTIPLRGFQRAMVKTMTAAakvpHFHYV-----EEINVDALVELKASF 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 317 KDEAKAADVKLSYLPFIFKAVAVALRKYPSLNTSFDEATQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAREV 396
Cdd:PLN02528 229 QENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKEL 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 397 VDLAGRAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRPIVDEDDNIVVAHMMYLSLSFDHRL 476
Cdd:PLN02528 309 SRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRV 388
|
490 500
....*....|....*....|....*
gi 226319387 477 VDGAEAARFCKEVIRLLENPDRLML 501
Cdd:PLN02528 389 LDGATVARFCNEWKSYVEKPELLML 413
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-501 |
4.30e-84 |
|
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: 270.21 E-value: 4.30e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 2 KEVLLPELAeSVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALIDETGgg 81
Cdd:TIGR01348 117 QEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAG-- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 82 asssapsamqAIQDTAESPATADAQLPPQAQEEREQiggsiVEASHLPKADddssslfkafasdeqvkvqglggrTPAPQ 161
Cdd:TIGR01348 194 ----------STPATAPAPASAQPAAQSPAATQPEP-----AAAPAAAKAQ------------------------APAPQ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 162 GAaqPVRNDGRVL-AVPAARQLARELGLDLNRIQGSGPNGRIRVSDV--LAQTQGQTASSTAASsmpasapapqpastaq 238
Cdd:TIGR01348 235 QA--GTQNPAKVDhAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVqrFVKEPSVRAQAAAAS---------------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 239 aaaqpapasskAAQGGLPVAPVQYRTPKGYEHLEdRVPLRGMRRAISNQMVASHLYTVRTLTVDEVNLTRLVEFRNRVKD 318
Cdd:TIGR01348 297 -----------AAGGAPGALPWPNVDFSKFGEVE-EVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNA 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 319 EAKAADVKLSYLPFIFKAVAVALRKYPSLNTSFDEATQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAREVVD 398
Cdd:TIGR01348 365 AVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSD 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 399 LAGRAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRPIVDEDDnIVVAHMMYLSLSFDHRLVD 478
Cdd:TIGR01348 445 LAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKE-FEPRLMLPLSLSYDHRVID 523
|
490 500
....*....|....*....|...
gi 226319387 479 GAEAARFCKEVIRLLENPDRLML 501
Cdd:TIGR01348 524 GADAARFTTYICESLADIRRLLL 546
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
2-502 |
3.31e-80 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 256.15 E-value: 3.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 2 KEVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALIDeTGGG 81
Cdd:PTZ00144 45 KVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEID-TGGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 82 ASSSAPSAMQAIQDTAESPATADAQLPPQAQEEREqiggsiveashlpkadddssslfkafasdeqvkvqglggrTPAPQ 161
Cdd:PTZ00144 124 PPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAAS----------------------------------------KPTPP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 162 GAAQPVrndgrvlavpaarqlarelgldlnriqgsgpngrirvsdvlaqtqgqTASSTAASSMpasapapqpastaqaaa 241
Cdd:PTZ00144 164 AAAKPP-----------------------------------------------EPAPAAKPPP----------------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 242 qpapasskaaqgglpvAPVQYRTPKgyehlEDRVPLRGMRRAISNQMVASHLYTVRTLTVDEVNLTRLVEFRNRVKDE-A 320
Cdd:PTZ00144 180 ----------------TPVARADPR-----ETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDfQ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 321 KAADVKLSYLPFIFKAVAVALRKYPSLNTSFDEatQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAREVVDLA 400
Cdd:PTZ00144 239 KKHGVKLGFMSAFVKASTIALKKMPIVNAYIDG--DEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 401 GRAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRPIVdEDDNIVVAHMMYLSLSFDHRLVDGA 480
Cdd:PTZ00144 317 EKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVV-VGNEIVIRPIMYLALTYDHRLIDGR 395
|
490 500
....*....|....*....|..
gi 226319387 481 EAARFCKEVIRLLENPDRLMLE 502
Cdd:PTZ00144 396 DAVTFLKKIKDLIEDPARMLLD 417
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
172-499 |
1.76e-75 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 240.08 E-value: 1.76e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 172 RVLAVPAARQLARELGLDLNRIQGSGPNGRIRVSDVLAQTQGQTASSTAASSmpasapapqpastaqaaaQPAPASSKAA 251
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEA------------------ASVSSAQQAA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 252 QGGLPVAPVQYRTPKgyehledRVPLRGMRRAISNQMVASHLYTVRTLTVDEVNLTRLVEFRNRVKDEA-KAADVKLSYL 330
Cdd:PRK11857 63 KTAAPAAAPPKLEGK-------REKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVlKTEGVKLTFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 331 PFIFKAVAVALRKYPSLNTSFDEATQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAREVVDLAGRAQAGKLQP 410
Cdd:PRK11857 136 PFIAKAILIALKEFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 411 DELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRPIVdEDDNIVVAHMMYLSLSFDHRLVDGAEAARFCKEVI 490
Cdd:PRK11857 216 DEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVK 294
|
....*....
gi 226319387 491 RLLENPDRL 499
Cdd:PRK11857 295 ELLEKPEIL 303
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-501 |
1.04e-74 |
|
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: 242.39 E-value: 1.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 3 EVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEG-DVVAVHAAIALIDETGGg 81
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEEKE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 82 assSAPSAMQAIQ-DTAESPATADAQLPPQAQEEREQiggsiveashlpkadddssslfKAFASDEQVKvqglggrTPAP 160
Cdd:TIGR01349 80 ---DVADAFKNYKlESSASPAPKPSEIAPTAPPSAPK----------------------PSPAPQKQSP-------EPSS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 161 QGAAQPVRNDGRVLAVPAARQLARELGLDLNRIQGSGPNGRIRVSDVLAQTQGQTASSTAASsmpasapapqpastaqaa 240
Cdd:TIGR01349 128 PAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFVPQSPASANQQA------------------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 241 aqpapasskAAQGGLPVAPVQYRTPKGYEHledrVPLRGMRRAISNQMVAS-----HLYtvrtLTVDeVNLTRLVEFRnr 315
Cdd:TIGR01349 190 ---------AATTPATYPAAAPVSTGSYED----VPLSNIRKIIAKRLLESkqtipHYY----VSIE-CNVDKLLALR-- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 316 vKDEAKAAD--VKLSYLPFIFKAVAVALRKYPSLNTSFDEatQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELA 393
Cdd:TIGR01349 250 -KELNAMASevYKLSVNDFIIKASALALREVPEANSSWTD--NFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTIS 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 394 REVVDLAGRAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRPIV--DEDDNIVVAHMMYLSLS 471
Cdd:TIGR01349 327 NEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVdnDEEKGFAVASIMSVTLS 406
|
490 500 510
....*....|....*....|....*....|
gi 226319387 472 FDHRLVDGAEAARFCKEVIRLLENPDRLML 501
Cdd:TIGR01349 407 CDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
170-501 |
3.26e-54 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 185.88 E-value: 3.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 170 DGRVLAVPAARQLARELGLDLNRIQGSGPNGRIRVSDVLA-QTQGQTASSTAASSMPASAPAPQPASTAQAAAQPAPASS 248
Cdd:PRK14843 3 DDKLRATPAARKLADDLGINLYDVSGSGANGRVHKEDVETyKDTNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 249 KAAQGGLPVAPVQYRTPKGYEHLE------------DRVPLRGMRRAISNQMVASHLyTVRTLTVD-EVNLTRLVEFRNR 315
Cdd:PRK14843 83 VLALLPENIENDSIKSPAQIEKVEevpdnvtpygeiERIPMTPMRKVIAQRMVESYL-TAPTFTLNyEVDMTEMLALRKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 316 VKDE-AKAADVKLSYLPFIFKAVAVALRKYPSLNTSFDEATQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAR 394
Cdd:PRK14843 162 VLEPiMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 395 EVVDLAGRAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRPIVdEDDNIVVAHMMYLSLSFDH 474
Cdd:PRK14843 242 AFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVV-VNGEIVIRPIMSLGLTIDH 320
|
330 340
....*....|....*....|....*..
gi 226319387 475 RLVDGAEAARFCKEVIRLLENPDRLML 501
Cdd:PRK14843 321 RVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
2-501 |
8.79e-52 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 184.29 E-value: 8.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 2 KEVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEG-DVVAVHAAIALIDETGG 80
Cdd:PLN02744 113 QEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIAITVEEEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 81 GASS---SAPSAmqaiqdTAESPATADAQLPPQAQEEREQiggsivEASHLPKAdddssslfkafasdeqvkvqglggRT 157
Cdd:PLN02744 193 DIGKfkdYKPSS------SAAPAAPKAKPSPPPPKEEEVE------KPASSPEP------------------------KA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 158 PAPQGAAQPvrnDGRVLAVPAARQLARELGLDLNRIQGSGPNGRIRVSDVLAqtqgqtasstaassmpasapapqpasta 237
Cdd:PLN02744 237 SKPSAPPSS---GDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIED---------------------------- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 238 qaaaqpapASSKAAQGGLPVAPVQYRTPkGYEHLEdrVPLRGMRRAISNQMVAS-----HLYtvrtLTVDeVNLTRLVEF 312
Cdd:PLN02744 286 --------YLASGGKGATAPPSTDSKAP-ALDYTD--IPNTQIRKVTASRLLQSkqtipHYY----LTVD-TRVDKLMAL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 313 R---NRVKDEAKAAdvKLSYLPFIFKAVAVALRKYPSLNTSFdeaTQE-IVQKRYYNMGMAVATDAGLTVPVLKDVGRKS 388
Cdd:PLN02744 350 RsqlNSLQEASGGK--KISVNDLVIKAAALALRKVPQCNSSW---TDDyIRQYHNVNINVAVQTENGLYVPVVKDADKKG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 389 VFELAREVVDLAGRAQAGKLQPDELAGSTFSITNIGSIGALFSF-PIINVPDAAILGVHSIVKRPIVDE-DDNIVVAHMM 466
Cdd:PLN02744 425 LSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQFcAIINPPQSAILAVGSAEKRVIPGSgPDQYNFASFM 504
|
490 500 510
....*....|....*....|....*....|....*
gi 226319387 467 YLSLSFDHRLVDGAEAARFCKEVIRLLENPDRLML 501
Cdd:PLN02744 505 SVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
3-502 |
3.75e-50 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 178.03 E-value: 3.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 3 EVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALIDETGGGA 82
Cdd:PLN02226 93 EAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 83 SSSAPSamqaiQDTAESPATADAqlPPQAQEEREQIGGSIVeaSHLPKAdddssslfkafasdeqvkvqglggrtPAPQg 162
Cdd:PLN02226 173 SQVTPS-----QKIPETTDPKPS--PPAEDKQKPKVESAPV--AEKPKA--------------------------PSSP- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 163 aaqpvrndgrvlavPAARQLARElgldlnriqgsgpngrirvsdvlaqtqgqtasstaassmpasapapqpastaqaaaq 242
Cdd:PLN02226 217 --------------PPPKQSAKE--------------------------------------------------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 243 papasskaaqgglPVAPVQYRtpkgyehlEDRVPLRGMRRAISNQMVASHLYTVRTLTVDEVNLTRLVEFRNRVKDE-AK 321
Cdd:PLN02226 226 -------------PQLPPKER--------ERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAfYE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 322 AADVKLSYLPFIFKAVAVALRKYPSLNTSFDeaTQEIVQKRYYNMGMAVATDAGLTVPVLKDVGRKSVFELAREVVDLAG 401
Cdd:PLN02226 285 KHGVKLGLMSGFIKAAVSALQHQPVVNAVID--GDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 402 RAQAGKLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIVKRPIVdEDDNIVVAHMMYLSLSFDHRLVDGAE 481
Cdd:PLN02226 363 KANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV-VGGSVVPRPMMYVALTYDHRLIDGRE 441
|
490 500
....*....|....*....|.
gi 226319387 482 AARFCKEVIRLLENPDRLMLE 502
Cdd:PLN02226 442 AVYFLRRVKDVVEDPQRLLLD 462
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-75 |
1.03e-30 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 113.62 E-value: 1.03e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226319387 1 MKEVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALI 75
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
2-75 |
7.82e-29 |
|
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: 108.65 E-value: 7.82e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226319387 2 KEVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALI 75
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
256-497 |
3.29e-18 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 88.41 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 256 PVAPVQYRTPKGYEHLEDRVPLRGMRRAISNQMVAShlYTVRTLT-VDEVNLTRLVEFRNRVKDE-AKAADVKLSYLPFI 333
Cdd:PRK12270 99 PPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDAS--LEVPTATsVRAVPAKLLIDNRIVINNHlKRTRGGKVSFTHLI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 334 FKAVAVALRKYPSLNTSFDEA--TQEIVQKRYYNMGMA--VATDAG---LTVPVLKDVGRKSVFELAREVVDLAGRAQAG 406
Cdd:PRK12270 177 GYALVQALKAFPNMNRHYAEVdgKPTLVTPAHVNLGLAidLPKKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRARDG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 407 KLQPDELAGSTFSITNIGSIGALFSFPIINVPDAAILGVHSIV---------KRPIVDeddnIVVAHMMYLSLSFDHRLV 477
Cdd:PRK12270 257 KLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEypaefqgasEERLAE----LGISKVMTLTSTYDHRII 332
|
250 260
....*....|....*....|
gi 226319387 478 DGAEAARFCKEVIRLLENPD 497
Cdd:PRK12270 333 QGAESGEFLRTIHQLLLGED 352
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
2-145 |
2.38e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 80.76 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 2 KEVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALIDEtGGG 81
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVAD-AEV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226319387 82 ASSSAPSAMQAIQDTAESPATADAQLPPqaQEEREQIGGSIVEASHLPKADDDSSSLFKAFASD 145
Cdd:PRK14875 82 SDAEIDAFIAPFARRFAPEGIDEEDAGP--APRKARIGGRTVRYLRLGEGDGTPVVLIHGFGGD 143
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
2-75 |
1.45e-15 |
|
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: 71.48 E-value: 1.45e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226319387 2 KEVLLPELAESVVEGeILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALI 75
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
173-208 |
3.77e-13 |
|
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: 63.47 E-value: 3.77e-13
10 20 30
....*....|....*....|....*....|....*.
gi 226319387 173 VLAVPAARQLARELGLDLNRIQGSGPNGRIRVSDVL 208
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
3-111 |
6.43e-12 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 67.64 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226319387 3 EVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEG-DVVAVHAAIALIDETGGG 81
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEEGES 83
|
90 100 110
....*....|....*....|....*....|
gi 226319387 82 ASSSAPSAMQAIQDTAESPATADAQLPPQA 111
Cdd:PRK11892 84 ASDAGAAPAAAAEAAAAAPAAAAAAAAKKA 113
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
3-66 |
1.36e-07 |
|
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: 48.59 E-value: 1.36e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226319387 3 EVLLPELAESVVEGEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVV 66
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKV 64
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
16-75 |
4.21e-07 |
|
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: 47.03 E-value: 4.21e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226319387 16 GEILKWLVQEGDTIALEQPLC--EVMtdKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALI 75
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAvlEAM--KMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
7-66 |
2.37e-04 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 41.77 E-value: 2.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226319387 7 PELAESVVE----GEILKWLVQEGDTIALEQPLCEVMTDKVTVELPSPVAGVLRQRLANEGDVV 66
Cdd:PRK05641 80 ASAGENVVTapmpGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTV 143
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
16-75 |
3.80e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 39.83 E-value: 3.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226319387 16 GEILKWLVQEGDTIALEQPLC--EVMtdKVTVELPSPVAGVLRQRLANEGDVVAVHAAIALI 75
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLvlEAM--KMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| |
