|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
2-426 |
1.04e-158 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 454.25 E-value: 1.04e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 2 EIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIDTGEKRD 81
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 82 DIDSETEANHSyEKQSSSYKNDLSQSKINENTNDSSLQPKNNGRFSPVVFKLASENNIDLTQVVGTGFSGRVTKKDIEKV 161
Cdd:PRK11856 84 AAAAAEAAPEA-PAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 162 INNPEmienttsnstsnqsqnnqSSQKTLQSQSQSESDVTYNQGSTIPVKGVRKAIAQNMVTSVTEIPHGWMMIEADATN 241
Cdd:PRK11856 163 AAAAA------------------PAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 242 LVKTRNHHKNTfkqneGYNLTFFAFFLKAVADALKAHPLLNSTWQGDEIIIHKDINISIAVADKDKLYVPVIKHADEKSI 321
Cdd:PRK11856 225 LLALRKQLKAI-----GVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 322 KGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVESVVKKPVVIDDMIAIRSMVNLCI 401
Cdd:PRK11856 300 FELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSL 379
|
410 420
....*....|....*....|....*
gi 515409136 402 SIDHRILDGLQTGQFMNHIKKRIEQ 426
Cdd:PRK11856 380 SFDHRVIDGADAARFLKALKELLEN 404
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
2-430 |
3.72e-99 |
|
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).
Pssm-ID: 200219 [Multi-domain] Cd Length: 579 Bit Score: 307.71 E-value: 3.72e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 2 EIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIDTGEKRD 81
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 82 DIDSETEANHSYEKQSS-----------SYKNDLSQSKINENTND-SSLQPKNNGR----FSPVVFKLASENNIDLTQVV 145
Cdd:TIGR02927 208 AEPAEEEAPAPSEAGSEpapdpaaraphAAPDPPAPAPAPAKTAApAAAAPVSSGDsgpyVTPLVRKLAKDKGVDLSTVK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 146 GTGFSGRVTKKDIEKVINNPEmientTSNSTSNQSQNNQSSQKTLQSQSQSESDVTYNQGSTIPVKGVRKAIAQNMVTSV 225
Cdd:TIGR02927 288 GTGVGGRIRKQDVLAAAKAAE-----EARAAAAAPAAAAAPAAPAAAAKPAEPDTAKLRGTTQKMNRIRQITADKTIESL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 226 TEIPHGWMMIEADATNLVKTRNHHKNTFKQNEGYNLTFFAFFLKAVADALKAHPLLNSTWQGD--EIIIHKDINISIAVA 303
Cdd:TIGR02927 363 QTSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAEtkEVTYHDVEHVGIAVD 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 304 DKDKLYVPVIKHADEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVESVVKK 383
Cdd:TIGR02927 443 TPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKR 522
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 515409136 384 PVVIDD-----MIAIRSMVNLCISIDHRILDGLQTGQFMNHIKKRIEQYSIE 430
Cdd:TIGR02927 523 PRVIKDedggeSIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDFE 574
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
221-426 |
2.70e-92 |
|
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: 277.50 E-value: 2.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 221 MVTSVTEIPHGWMMIEADATNLVKTRNHHKNTFKQnEGYNLTFFAFFLKAVADALKAHPLLNSTWQGD--EIIIHKDINI 298
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAAD-EETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 299 SIAVADKDKLYVPVIKHADEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVE 378
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515409136 379 SVVKKPVVIDDMIAIRSMVNLCISIDHRILDGLQTGQFMNHIKKRIEQ 426
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLEN 207
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
2-74 |
9.74e-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: 110.16 E-value: 9.74e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515409136 2 EIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKI 74
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1-74 |
1.46e-28 |
|
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: 107.11 E-value: 1.46e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515409136 1 MEIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKI 74
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
2-426 |
1.04e-158 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 454.25 E-value: 1.04e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 2 EIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIDTGEKRD 81
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 82 DIDSETEANHSyEKQSSSYKNDLSQSKINENTNDSSLQPKNNGRFSPVVFKLASENNIDLTQVVGTGFSGRVTKKDIEKV 161
Cdd:PRK11856 84 AAAAAEAAPEA-PAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 162 INNPEmienttsnstsnqsqnnqSSQKTLQSQSQSESDVTYNQGSTIPVKGVRKAIAQNMVTSVTEIPHGWMMIEADATN 241
Cdd:PRK11856 163 AAAAA------------------PAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 242 LVKTRNHHKNTfkqneGYNLTFFAFFLKAVADALKAHPLLNSTWQGDEIIIHKDINISIAVADKDKLYVPVIKHADEKSI 321
Cdd:PRK11856 225 LLALRKQLKAI-----GVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 322 KGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVESVVKKPVVIDDMIAIRSMVNLCI 401
Cdd:PRK11856 300 FELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSL 379
|
410 420
....*....|....*....|....*
gi 515409136 402 SIDHRILDGLQTGQFMNHIKKRIEQ 426
Cdd:PRK11856 380 SFDHRVIDGADAARFLKALKELLEN 404
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-426 |
1.05e-108 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 331.40 E-value: 1.05e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 2 EIKMPKLGEsVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIDTGEKrD 81
Cdd:PRK11855 121 EVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA-A 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 82 DIDSETEANHSYEKQSSSYKNDLSQSKINENTNDSSLQPKNNGRF--SPVVFKLASENNIDLTQVVGTGFSGRVTKKDIE 159
Cdd:PRK11855 199 PAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPhaSPAVRRLARELGVDLSQVKGTGKKGRITKEDVQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 160 KvinnpeMIENTTSNSTSNQSQNNQSSQKTLQSQSQSESDVT-YNQGSTIPVKGVRKAIAQNMVTSVTEIPHGWMMIEAD 238
Cdd:PRK11855 279 A------FVKGAMSAAAAAAAAAAAAGGGGLGLLPWPKVDFSkFGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEAD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 239 ATNLVKTRNHHKNTFKqNEGYNLTFFAFFLKAVADALKAHPLLNST--WQGDEIIIHKDINISIAVADKDKLYVPVIKHA 316
Cdd:PRK11855 353 ITDLEALRKQLKKEAE-KAGVKLTMLPFFIKAVVAALKEFPVFNASldEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDV 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 317 DEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVESVVKKPVVIDDMIAIRSM 396
Cdd:PRK11855 432 DKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLM 511
|
410 420 430
....*....|....*....|....*....|
gi 515409136 397 VNLCISIDHRILDGLQTGQFMNHIKKRIEQ 426
Cdd:PRK11855 512 LPLSLSYDHRVIDGATAARFTNYLKQLLAD 541
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
2-426 |
3.88e-101 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 307.15 E-value: 3.88e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 2 EIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIDTGEKRD 81
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 82 DIDSETEAnhsyEKQSSSYKNDLSQSKINENTNDSSlqpknngrfSPVVFKLASENNIDLTQVVGTGFSGRVTKKDIEKV 161
Cdd:PRK05704 84 AAAAAAAA----AAAAAAAPAQAQAAAAAEQSNDAL---------SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 162 INNPEmienttsnSTSNQSQNNQSSQKTLQSQSQSESDVtynqgstiPVKGVRKAIA------QN---MVTSVTEIphgw 232
Cdd:PRK05704 151 LAAAA--------AAPAAPAAAAPAAAPAPLGARPEERV--------PMTRLRKTIAerlleaQNttaMLTTFNEV---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 233 mmieaDATNLVKTRNHHKNTFKQNEGYNLTFFAFFLKAVADALKAHPLLNSTWQGDEIIIHKDINISIAVADKDKLYVPV 312
Cdd:PRK05704 211 -----DMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 313 IKHADEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVESVVKKPVVIDDMIA 392
Cdd:PRK05704 286 LRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIV 365
|
410 420 430
....*....|....*....|....*....|....
gi 515409136 393 IRSMVNLCISIDHRILDGLQTGQFMNHIKKRIEQ 426
Cdd:PRK05704 366 IRPMMYLALSYDHRIIDGKEAVGFLVTIKELLED 399
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
2-430 |
3.72e-99 |
|
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).
Pssm-ID: 200219 [Multi-domain] Cd Length: 579 Bit Score: 307.71 E-value: 3.72e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 2 EIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIDTGEKRD 81
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 82 DIDSETEANHSYEKQSS-----------SYKNDLSQSKINENTND-SSLQPKNNGR----FSPVVFKLASENNIDLTQVV 145
Cdd:TIGR02927 208 AEPAEEEAPAPSEAGSEpapdpaaraphAAPDPPAPAPAPAKTAApAAAAPVSSGDsgpyVTPLVRKLAKDKGVDLSTVK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 146 GTGFSGRVTKKDIEKVINNPEmientTSNSTSNQSQNNQSSQKTLQSQSQSESDVTYNQGSTIPVKGVRKAIAQNMVTSV 225
Cdd:TIGR02927 288 GTGVGGRIRKQDVLAAAKAAE-----EARAAAAAPAAAAAPAAPAAAAKPAEPDTAKLRGTTQKMNRIRQITADKTIESL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 226 TEIPHGWMMIEADATNLVKTRNHHKNTFKQNEGYNLTFFAFFLKAVADALKAHPLLNSTWQGD--EIIIHKDINISIAVA 303
Cdd:TIGR02927 363 QTSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAEtkEVTYHDVEHVGIAVD 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 304 DKDKLYVPVIKHADEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVESVVKK 383
Cdd:TIGR02927 443 TPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKR 522
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 515409136 384 PVVIDD-----MIAIRSMVNLCISIDHRILDGLQTGQFMNHIKKRIEQYSIE 430
Cdd:TIGR02927 523 PRVIKDedggeSIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDFE 574
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
221-426 |
2.70e-92 |
|
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: 277.50 E-value: 2.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 221 MVTSVTEIPHGWMMIEADATNLVKTRNHHKNTFKQnEGYNLTFFAFFLKAVADALKAHPLLNSTWQGD--EIIIHKDINI 298
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAAD-EETKLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 299 SIAVADKDKLYVPVIKHADEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVE 378
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515409136 379 SVVKKPVVIDDMIAIRSMVNLCISIDHRILDGLQTGQFMNHIKKRIEQ 426
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLEN 207
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
2-425 |
1.30e-89 |
|
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: 277.38 E-value: 1.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 2 EIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIdtgEKRD 81
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL---EEGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 82 DIDSETEANHSYEKQSSsyKNDLSQSKINENTNDSSLqpknngrfSPVVFKLASENNIDLTQVVGTGFSGRVTKKDIEKV 161
Cdd:TIGR01347 79 DATAAPPAKSGEEKEET--PAASAAAAPTAAANRPSL--------SPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 162 INNPemienttsnsTSNQSQNNQSSQKTLQSQSQSESDVTYNQgstipvkgVRKAIA------QN---MVTSVTEIphgw 232
Cdd:TIGR01347 149 TEAP----------ASAQPPAAAAAAAAPAAATRPEERVKMTR--------LRQRIAerlkeaQNstaMLTTFNEV---- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 233 mmieaDATNLVKTRNHHKNTFKQNEGYNLTFFAFFLKAVADALKAHPLLNSTWQGDEIIIHKDINISIAVADKDKLYVPV 312
Cdd:TIGR01347 207 -----DMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 313 IKHADEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVESVVKKPVVIDDMIA 392
Cdd:TIGR01347 282 VRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIE 361
|
410 420 430
....*....|....*....|....*....|...
gi 515409136 393 IRSMVNLCISIDHRILDGLQTGQFMNHIKKRIE 425
Cdd:TIGR01347 362 IRPMMYLALSYDHRLIDGKEAVTFLVTIKELLE 394
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-425 |
1.62e-86 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 276.50 E-value: 1.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 2 EIKMPKLGesVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIDTG---- 77
Cdd:PRK11854 208 DVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEgaap 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 78 ----EKRDDIDSETEANHSYEKQSSSYKNDLSQSKINENtndsslqpKNNGRFSPVVFKLASENNIDLTQVVGTGFSGRV 153
Cdd:PRK11854 286 aaapAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAEN--------DAYVHATPLVRRLAREFGVNLAKVKGTGRKGRI 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 154 TKKDIEKVINNP-EMIENTTSNSTSNQSQNNQSSQKTLQSQSQSESDVTynqgstiPVKGVRKAIAQNMVTSVTEIPHGW 232
Cdd:PRK11854 358 LKEDVQAYVKDAvKRAEAAPAAAAAGGGGPGLLPWPKVDFSKFGEIEEV-------ELGRIQKISGANLHRNWVMIPHVT 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 233 MMIEADATNLVKTRNH-HKNTFKQNEGYNLTFFAFFLKAVADALKAHPLLNSTW--QGDEIIIHKDINISIAVADKDKLY 309
Cdd:PRK11854 431 QFDKADITELEAFRKQqNAEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 310 VPVIKHADEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVESVVKKPVVIDD 389
Cdd:PRK11854 511 VPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGK 590
|
410 420 430
....*....|....*....|....*....|....*.
gi 515409136 390 MIAIRSMVNLCISIDHRILDGLQTGQFMNHIKKRIE 425
Cdd:PRK11854 591 EFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
3-425 |
3.34e-78 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 248.44 E-value: 3.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 3 IKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIDTGEKRDD 82
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 83 IDSETEANHSYEKQSSSYKNDLSQSKinENTNDSSLQPKNNGRFspvvfklasennidltqvvgtgfsgrvtkkdiEKVI 162
Cdd:PTZ00144 127 AAPAAAAAAKAEKTTPEKPKAAAPTP--EPPAASKPTPPAAAKP--------------------------------PEPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 163 NNPEMIenttsnstsnqsqnnqssQKTLQSQSQSESDVtynqgstiPVKGVRKAIA------QN---MVTSVTEIphgwm 233
Cdd:PTZ00144 173 PAAKPP------------------PTPVARADPRETRV--------PMSRMRQRIAerlkasQNtcaMLTTFNEC----- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 234 mieaDATNLVKTRNHHKNTFKQNEGYNLTFFAFFLKAVADALKAHPLLNSTWQGDEIIIHKDINISIAVADKDKLYVPVI 313
Cdd:PTZ00144 222 ----DMSALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 314 KHADEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVESVVKKPVVIDDMIAI 393
Cdd:PTZ00144 298 RNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVI 377
|
410 420 430
....*....|....*....|....*....|..
gi 515409136 394 RSMVNLCISIDHRILDGLQTGQFMNHIKKRIE 425
Cdd:PTZ00144 378 RPIMYLALTYDHRLIDGRDAVTFLKKIKDLIE 409
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-425 |
1.08e-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: 240.08 E-value: 1.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 2 EIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEG-ETVSVDAVICKidTGEKR 80
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAV--LVEEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 81 DDI----------DSETEANHSYEKQSSSYKND-LSQSKINENTNDSSL-QPKN----NGRF--SPVVFKLASENNIDLT 142
Cdd:TIGR01349 79 EDVadafknykleSSASPAPKPSEIAPTAPPSApKPSPAPQKQSPEPSSpAPLSdkesGDRIfaSPLAKKLAKEKGIDLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 143 QVVGTGFSGRVTKKDIEKVInnpemienttsnsTSNQSQNNQSSQKTLQSQSQSESDVTYNQGSTIPVKGVRKAIAQNMV 222
Cdd:TIGR01349 159 AVAGSGPNGRIVKKDIESFV-------------PQSPASANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 223 TSVTEIPHGWMMIEADATNLVKTRnhhKNTFKQNEG-YNLTFFAFFLKAVADALKAHPLLNSTWQGDEIIIHKDINISIA 301
Cdd:TIGR01349 226 ESKQTIPHYYVSIECNVDKLLALR---KELNAMASEvYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 302 VADKDKLYVPVIKHADEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVESVV 381
Cdd:TIGR01349 303 VATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVE 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 515409136 382 KKPVVIDD---MIAIRSMVNLCISIDHRILDGLQTGQFMNHIKKRIE 425
Cdd:TIGR01349 383 DVAVVDNDeekGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLE 429
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
14-426 |
6.28e-65 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 214.20 E-value: 6.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 14 EGIIE----QWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIDTGEKRDDI-DSETE 88
Cdd:PLN02528 8 EGIAEcellRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRsDSLLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 89 ANHSYEKQSSSYKNDlsqskinENTNDSSLQPknngrfSPVVFKLASENNIDLTQVVGTGFSGRVTKKDIEKVINNPEMI 168
Cdd:PLN02528 88 PTDSSNIVSLAESDE-------RGSNLSGVLS------TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 169 ENTTSNSTSNQSQNnqssqkTLQSQSQSESDVTYNQGSTIPVKGVRKAIAQNMvTSVTEIPHGWMMIEADATNLVKTRNH 248
Cdd:PLN02528 155 KDSSSAEEATIAEQ------EEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTM-TAAAKVPHFHYVEEINVDALVELKAS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 249 HKNTfKQNEGYNLTFFAFFLKAVADALKAHPLLNSTWQGD--EIIIHKDINISIAVADKDKLYVPVIKHADEKSIKGIAR 326
Cdd:PLN02528 228 FQEN-NTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 327 EINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVESVVKKPVVIDD--MIAIRSMvNLCISID 404
Cdd:PLN02528 307 ELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDgnVYPASIM-TVTIGAD 385
|
410 420
....*....|....*....|..
gi 515409136 405 HRILDGLQTGQFMNHIKKRIEQ 426
Cdd:PLN02528 386 HRVLDGATVARFCNEWKSYVEK 407
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
1-425 |
5.85e-63 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 212.02 E-value: 5.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 1 MEIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEG-ETVSVDAVICKidTGEK 79
Cdd:PLN02744 113 QEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIAI--TVEE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 80 RDDIDS--ETEANHSYEKQSSSYKNDLSQSKINENTNDSSL----------QPKNNGRF--SPVVFKLASENNIDLTQVV 145
Cdd:PLN02744 191 EEDIGKfkDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSpepkaskpsaPPSSGDRIfaSPLARKLAEDNNVPLSSIK 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 146 GTGFSGRVTKKDIEKVInnpemienttsnstsnqsqnnQSSQKTLQSQSQSESDVTYNQGSTIPVKGVRKAIAQNMVTSV 225
Cdd:PLN02744 271 GTGPDGRIVKADIEDYL---------------------ASGGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSK 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 226 TEIPHGWMMIEADATNLVKTRNhHKNTFKQNE-GYNLTFFAFFLKAVADALKAHPLLNSTWQGDEIIIHKDINISIAVAD 304
Cdd:PLN02744 330 QTIPHYYLTVDTRVDKLMALRS-QLNSLQEASgGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQT 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 305 KDKLYVPVIKHADEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGS-FGSVSSMGIINHPQAAILQVESVVKK 383
Cdd:PLN02744 409 ENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAEKR 488
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 515409136 384 --PVVIDDMIAIRSMVNLCISIDHRILDGLQTGQFMNHIKKRIE 425
Cdd:PLN02744 489 viPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIE 532
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-420 |
1.54e-62 |
|
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: 211.27 E-value: 1.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 2 EIKMPKLGeSVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIDTGEKrd 81
Cdd:TIGR01348 118 EVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGS-- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 82 dIDSETEANHSYEKQSSSYKNDL-----------SQSKI--NENT-NDSSLQPKnngrfSPVVFKLASENNIDLTQVVGT 147
Cdd:TIGR01348 195 -TPATAPAPASAQPAAQSPAATQpepaaapaaakAQAPApqQAGTqNPAKVDHA-----APAVRRLAREFGVDLSAVKGT 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 148 GFSGRVTKKDIEKVINNPemienttsnstsnqsqnnqssqkTLQSQSQSES------------DVTYNQGSTI---PVKG 212
Cdd:TIGR01348 269 GIKGRILREDVQRFVKEP-----------------------SVRAQAAAASaaggapgalpwpNVDFSKFGEVeevDMSR 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 213 VRKAIAQNMVTSVTEIPHGWMMIEADATNLVKTRNHhKNTFKQNEGYNLTFFAFFLKAVADALKAHPLLNSTWQ--GDEI 290
Cdd:TIGR01348 326 IRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQ-QNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 291 IIHKDINISIAVADKDKLYVPVIKHADEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHP 370
Cdd:TIGR01348 405 ILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAP 484
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 515409136 371 QAAILQVESVVKKPVVIDDMIAIRSMVNLCISIDHRILDGLQTGQFMNHI 420
Cdd:TIGR01348 485 EVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYI 534
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
1-425 |
1.10e-52 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 183.03 E-value: 1.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 1 MEIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIDTgekr 80
Cdd:PLN02226 92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISK---- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 81 ddidSETEANHSYEKQsssykndlsqsKINENTnDSSLQPKNNGRFSPVVFklasennidltqvvgtgfSGRVTKKdiEK 160
Cdd:PLN02226 168 ----SEDAASQVTPSQ-----------KIPETT-DPKPSPPAEDKQKPKVE------------------SAPVAEK--PK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 161 VINNPEMienttsnstsnqsqnnqssqktlQSQSQSESDVT-YNQGSTIPVKGVRKAIAQNMVTSVTEIPHGWMMIEADA 239
Cdd:PLN02226 212 APSSPPP-----------------------PKQSAKEPQLPpKERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDM 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 240 TNLVKTRNHHKNTFKQNEGYNLTFFAFFLKAVADALKAHPLLNSTWQGDEIIIHKDINISIAVADKDKLYVPVIKHADEK 319
Cdd:PLN02226 269 TNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKM 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 320 SIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSMGIINHPQAAILQVESVVKKPVVIDDMIAIRSMVNL 399
Cdd:PLN02226 349 NFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYV 428
|
410 420
....*....|....*....|....*.
gi 515409136 400 CISIDHRILDGLQTGQFMNHIKKRIE 425
Cdd:PLN02226 429 ALTYDHRLIDGREAVYFLRRVKDVVE 454
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
127-426 |
1.38e-51 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 175.75 E-value: 1.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 127 SPVVFKLASENNIDLTQVVGTGFSGRVTKKDIEKVINNPEMIENTTSNSTSNQSQNNQSSQKTLQSQSQSEsdvtynqGS 206
Cdd:PRK11857 5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLE-------GK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 207 TIPVKGVRKAIAQNMVTSVTEIPHGWMMIEADATNLVKTRNHHKNTFKQNEGYNLTFFAFFLKAVADALKAHPLLNSTW- 285
Cdd:PRK11857 78 REKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 286 -QGDEIIIHKDINISIAVADKDKLYVPVIKHADEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGSVSSM 364
Cdd:PRK11857 158 eATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515409136 365 GIINHPQAAILQVESVVKKPVVIDDMIAIRSMVNLCISIDHRILDGLQTGQFMNHIKKRIEQ 426
Cdd:PRK11857 238 PVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEK 299
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
125-425 |
1.98e-49 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 171.24 E-value: 1.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 125 RFSPVVFKLASENNIDLTQVVGTGFSGRVTKKDIEKVInnPEMIENTTSNSTSNQSqnnqssqktlQSQSQSESDVTYNQ 204
Cdd:PRK14843 50 RISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL--PENIENDSIKSPAQIE----------KVEEVPDNVTPYGE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 205 GSTIPVKGVRKAIAQNMVTSVTEIPHGWMMIEADATNLVKTRNHHKNTFKQNEGYNLTFFAFFLKAVADALKAHPLLNS- 283
Cdd:PRK14843 118 IERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINAs 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 284 -TWQGDEIIIHKDINISIAVADKDKLYVPVIKHADEKSIKGIAREINDLATKARNGQLTQADMEGGTFTVNNTGSFGsVS 362
Cdd:PRK14843 198 lTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFG-VQ 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515409136 363 SMG-IINHPQAAILQVESVVKKPVVIDDMIAIRSMVNLCISIDHRILDGLQTGQFMNHIKKRIE 425
Cdd:PRK14843 277 SFGpIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIE 340
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
2-74 |
9.74e-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: 110.16 E-value: 9.74e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515409136 2 EIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKI 74
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1-74 |
1.46e-28 |
|
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: 107.11 E-value: 1.46e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515409136 1 MEIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKI 74
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
2-74 |
3.59e-19 |
|
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: 81.11 E-value: 3.59e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515409136 2 EIKMPKLGESVHEGIIEqWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKI 74
Cdd:pfam00364 2 EIKSPMIGESVREGVVE-WLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
2-84 |
2.51e-17 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 83.07 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 2 EIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIDTGEKRD 81
Cdd:PRK14875 4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSD 83
|
....
gi 515409136 82 -DID 84
Cdd:PRK14875 84 aEID 87
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
207-427 |
8.72e-17 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 83.02 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 207 TIPVKGVRKAIAQNMV--------TSVTEIPhgwmmieadATNLVKTRNHHKNTFKQNEGYNLTFFAFFLKAVADALKAH 278
Cdd:PRK12270 117 VTPLRGAAAAVAKNMDaslevptaTSVRAVP---------AKLLIDNRIVINNHLKRTRGGKVSFTHLIGYALVQALKAF 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 279 PLLNSTWqgDEI------IIHKDINISIA--VADKD---KLYVPVIKHADEKSIKGIAREINDLATKARNGQLTQADMEG 347
Cdd:PRK12270 188 PNMNRHY--AEVdgkptlVTPAHVNLGLAidLPKKDgsrQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 348 GTFTVNNTGSFGSVSSMGIINHPQAAILQVESvvkkpvvID----------DMIA---IRSMVNLCISIDHRILDGLQTG 414
Cdd:PRK12270 266 TTISLTNPGGIGTVHSVPRLMKGQGAIIGVGA-------MEypaefqgaseERLAelgISKVMTLTSTYDHRIIQGAESG 338
|
250
....*....|...
gi 515409136 415 QFMnhikKRIEQY 427
Cdd:PRK12270 339 EFL----RTIHQL 347
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-75 |
9.09e-17 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 82.74 E-value: 9.09e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515409136 2 EIKMPKLGesVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKID 75
Cdd:PRK11854 4 EIKVPDIG--ADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
2-74 |
9.01e-12 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 60.53 E-value: 9.01e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515409136 2 EIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKI 74
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
127-159 |
3.88e-10 |
|
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: 54.61 E-value: 3.88e-10
10 20 30
....*....|....*....|....*....|...
gi 515409136 127 SPVVFKLASENNIDLTQVVGTGFSGRVTKKDIE 159
Cdd:pfam02817 4 SPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
2-99 |
1.16e-08 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 56.85 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 2 EIKMPKLGESVHEGIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEG-ETVSVDAVICKI-DTGEK 79
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLlEEGES 83
|
90 100
....*....|....*....|
gi 515409136 80 RDDIDSETEANHSYEKQSSS 99
Cdd:PRK11892 84 ASDAGAAPAAAAEAAAAAPA 103
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
15-74 |
2.95e-08 |
|
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: 50.11 E-value: 2.95e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 15 GIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKI 74
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
15-74 |
3.02e-05 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 46.37 E-value: 3.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409136 15 GIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKI 74
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
21-75 |
7.77e-05 |
|
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: 42.19 E-value: 7.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 515409136 21 LVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKID 75
Cdd:COG0511 82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
22-76 |
5.93e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 35.76 E-value: 5.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 515409136 22 VAVGDEVGeyepLCEVItdKVTAEVPSTVSGKVTELIVNEGETVSVDAVICKIDT 76
Cdd:PRK07051 32 VAAGDVVG----LIEVM--KQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
15-65 |
7.73e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 36.33 E-value: 7.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 515409136 15 GIIEQWLVAVGDEVGEYEPLCEVITDKVTAEVPSTVSGKVTELIVNEGETV 65
Cdd:PRK06549 70 GTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVV 120
|
|
| |
