|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
115-505 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 700.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 115 VDIKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKVKAGAAP 194
Cdd:PRK05704 3 VEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 195 AKSDAKADAPAAKEES---------SSEGSDVLTPSVRRLIAEKGLDASKIKGSGKNGRVTKEDVDQFLKSPAPAAK--- 262
Cdd:PRK05704 83 GAAAAAAAAAAAAAAApaqaqaaaaAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAapa 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 263 --AEAAPAAPMGDRTQKRVPMTRLRKTIANRLLEAKNSTAMLTTFNEVNMKPIMDLRKQYQEVFEKRHGIRLGFMSFYVK 340
Cdd:PRK05704 163 aaAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 341 AVTEALKRFPDVNASIDGDDIVYHNYFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDMTGGN 420
Cdd:PRK05704 243 AVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 421 FTITNGGVFGSLLSTPIINLPQSSILGMHKIQDRPMAVNGKVEILPMMYLALSYDHRQIDGKESVGFLVTIKELLEDPTR 500
Cdd:PRK05704 323 FTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPER 402
|
....*
gi 639351487 501 LLLDV 505
Cdd:PRK05704 403 LLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
115-505 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 618.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 115 VDIKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKV-----K 189
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILeegndA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 190 AGAAPAKSDAKADAPAAKEESSSEGS----DVLTPSVRRLIAEKGLDASKIKGSGKNGRVTKEDVDQFLKSPAPAAKAEA 265
Cdd:TIGR01347 81 TAAPPAKSGEEKEETPAASAAAAPTAaanrPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 266 APAAPMG---DRTQKRVPMTRLRKTIANRLLEAKNSTAMLTTFNEVNMKPIMDLRKQYQEVFEKRHGIRLGFMSFYVKAV 342
Cdd:TIGR01347 161 AAAAAAPaaaTRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 343 TEALKRFPDVNASIDGDDIVYHNYFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDMTGGNFT 422
Cdd:TIGR01347 241 VAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 423 ITNGGVFGSLLSTPIINLPQSSILGMHKIQDRPMAVNGKVEILPMMYLALSYDHRQIDGKESVGFLVTIKELLEDPTRLL 502
Cdd:TIGR01347 321 ITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
|
...
gi 639351487 503 LDV 505
Cdd:TIGR01347 401 LDL 403
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
292-502 |
3.32e-95 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 287.52 E-value: 3.32e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 292 LLEAKNSTAMLTTFNEVNMKPIMDLRKQYQEVFEKRHGiRLGFMSFYVKAVTEALKRFPDVNASIDGDD--IVYHNYFDI 369
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 370 SIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDMTGGNFTITNGGVFGSLLSTPIINLPQSSILGMH 449
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 639351487 450 KIQDRPMAVNGKVEILPMMYLALSYDHRQIDGKESVGFLVTIKELLEDPTRLL 502
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-76 |
4.09e-23 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 92.82 E-value: 4.09e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639351487 1 MSTEIKVPVLPESVADASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLI 76
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
115-188 |
1.33e-22 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 91.28 E-value: 1.33e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639351487 115 VDIKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKV 188
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
115-188 |
6.65e-22 |
|
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: 89.39 E-value: 6.65e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639351487 115 VDIKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKV 188
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-76 |
6.85e-21 |
|
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: 86.30 E-value: 6.85e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639351487 3 TEIKVPVLPESVADASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLI 76
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
3-76 |
8.53e-13 |
|
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: 63.39 E-value: 8.53e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639351487 3 TEIKVPVLPESVAdASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLI 76
Cdd:pfam00364 1 TEIKSPMIGESVR-EGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1-79 |
2.44e-10 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 62.27 E-value: 2.44e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639351487 1 MSTEIKVPVLPESVADASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLIGDA 79
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADA 79
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
115-505 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 700.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 115 VDIKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKVKAGAAP 194
Cdd:PRK05704 3 VEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 195 AKSDAKADAPAAKEES---------SSEGSDVLTPSVRRLIAEKGLDASKIKGSGKNGRVTKEDVDQFLKSPAPAAK--- 262
Cdd:PRK05704 83 GAAAAAAAAAAAAAAApaqaqaaaaAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAapa 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 263 --AEAAPAAPMGDRTQKRVPMTRLRKTIANRLLEAKNSTAMLTTFNEVNMKPIMDLRKQYQEVFEKRHGIRLGFMSFYVK 340
Cdd:PRK05704 163 aaAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 341 AVTEALKRFPDVNASIDGDDIVYHNYFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDMTGGN 420
Cdd:PRK05704 243 AVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 421 FTITNGGVFGSLLSTPIINLPQSSILGMHKIQDRPMAVNGKVEILPMMYLALSYDHRQIDGKESVGFLVTIKELLEDPTR 500
Cdd:PRK05704 323 FTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPER 402
|
....*
gi 639351487 501 LLLDV 505
Cdd:PRK05704 403 LLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
115-505 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 618.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 115 VDIKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKV-----K 189
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILeegndA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 190 AGAAPAKSDAKADAPAAKEESSSEGS----DVLTPSVRRLIAEKGLDASKIKGSGKNGRVTKEDVDQFLKSPAPAAKAEA 265
Cdd:TIGR01347 81 TAAPPAKSGEEKEETPAASAAAAPTAaanrPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 266 APAAPMG---DRTQKRVPMTRLRKTIANRLLEAKNSTAMLTTFNEVNMKPIMDLRKQYQEVFEKRHGIRLGFMSFYVKAV 342
Cdd:TIGR01347 161 AAAAAAPaaaTRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 343 TEALKRFPDVNASIDGDDIVYHNYFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDMTGGNFT 422
Cdd:TIGR01347 241 VAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 423 ITNGGVFGSLLSTPIINLPQSSILGMHKIQDRPMAVNGKVEILPMMYLALSYDHRQIDGKESVGFLVTIKELLEDPTRLL 502
Cdd:TIGR01347 321 ITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
|
...
gi 639351487 503 LDV 505
Cdd:TIGR01347 401 LDL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
117-505 |
9.30e-153 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 442.20 E-value: 9.30e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 117 IKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKVKAGAAPAK 196
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 197 SDAKADAPAAKEESSSEGSDVLTPsvrrliAEKGLDASKIKGSGKNGRVTKEDVdqflkspapaaKAEAAPAAPMGDRTQ 276
Cdd:PTZ00144 127 AAPAAAAAAKAEKTTPEKPKAAAP------TPEPPAASKPTPPAAAKPPEPAPA-----------AKPPPTPVARADPRE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 277 KRVPMTRLRKTIANRLLEAKNSTAMLTTFNEVNMKPIMDLRKQYQEVFEKRHGIRLGFMSFYVKAVTEALKRFPDVNASI 356
Cdd:PTZ00144 190 TRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 357 DGDDIVYHNYFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDMTGGNFTITNGGVFGSLLSTP 436
Cdd:PTZ00144 270 DGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTP 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639351487 437 IINLPQSSILGMHKIQDRPMAVNGKVEILPMMYLALSYDHRQIDGKESVGFLVTIKELLEDPTRLLLDV 505
Cdd:PTZ00144 350 IINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1-503 |
1.36e-131 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 392.65 E-value: 1.36e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 1 MSTEIKVPVLPEsVADASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLIGDAQ 80
Cdd:PRK11855 1 MAIEFKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 81 EAS------PSKEPKEDSSASEKSEDAPAAQSAPASEGKEVDIKVPVLPEsVADATIATWHVQPGDAVTRDQNLVDIETD 154
Cdd:PRK11855 80 AAAaaaapaAAAAPAAAAAAAPAPAAAAPAAAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 155 KVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKVKAG-----------------------AAPAKSDAKADAPAAKEESS 211
Cdd:PRK11855 159 KATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAaaapaaaaapaaaapaaaaaaapAPAPAAAAAPAAAAPAAAAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 212 SEGSDVLTPSVRRLIAEKGLDASKIKGSGKNGRVTKEDVDQFLKSPAPAAKAEAAPAAPMGDRTQK-------------- 277
Cdd:PRK11855 239 PGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAAAAAGGGGLGllpwpkvdfskfge 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 278 --RVPMTRLRKTIANRLLEAKNSTAMLTTFNEVNMKPIMDLRKQYQEVFEKrHGIRLGFMSFYVKAVTEALKRFPDVNAS 355
Cdd:PRK11855 319 ieTKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAEK-AGVKLTMLPFFIKAVVAALKEFPVFNAS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 356 ID--GDDIVYHNYFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDMTGGNFTITNGGVFGSLL 433
Cdd:PRK11855 398 LDedGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTA 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639351487 434 STPIINLPQSSILGMHKIQDRPmaVNGKVEILP--MMYLALSYDHRQIDGKESVGFLVTIKELLEDPTRLLL 503
Cdd:PRK11855 478 FTPIINAPEVAILGVGKSQMKP--VWDGKEFVPrlMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
115-504 |
1.04e-128 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 380.29 E-value: 1.04e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 115 VDIKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVL-----------GEQ 183
Cdd:PRK11856 3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPvgsviavieeeGEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 184 VIGKVKAGAAPAKSDAKADAPAAKEESSSEGSDVL----------TPSVRRLIAEKGLDASKIKGSGKNGRVTKEDVDQF 253
Cdd:PRK11856 83 EAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPaapaaaaakaSPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 254 LKSPAPAAKAEAAPAAPMGDRTQ---KRVPMTRLRKTIANRLLEAKNSTAMLTTFNEVNMKPIMDLRKQYqevfeKRHGI 330
Cdd:PRK11856 163 AAAAAPAAAAAAAAAAAPPAAAAegeERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQL-----KAIGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 331 RLGFMSFYVKAVTEALKRFPDVNASIDGDDIVYHNYFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGK 410
Cdd:PRK11856 238 KLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 411 LTLDDMTGGNFTITNGGVFGSLLSTPIINLPQSSILGMHKIQDRPMAVNGKVEILPMMYLALSYDHRQIDGKESVGFLVT 490
Cdd:PRK11856 318 LKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKA 397
|
410
....*....|....
gi 639351487 491 IKELLEDPTRLLLD 504
Cdd:PRK11856 398 LKELLENPALLLLE 411
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
112-505 |
7.01e-111 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 336.73 E-value: 7.01e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 112 GKEVDIKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKVK-- 189
Cdd:PLN02226 89 GDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISks 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 190 AGAAPAKSDAKADAPAAKEESSSEGSDVLTPSVRRL-IAEKGLDASKI---KGSGKNGRVTKEDvdqflkspapaakaea 265
Cdd:PLN02226 169 EDAASQVTPSQKIPETTDPKPSPPAEDKQKPKVESApVAEKPKAPSSPpppKQSAKEPQLPPKE---------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 266 apaapmgdrTQKRVPMTRLRKTIANRLLEAKNSTAMLTTFNEVNMKPIMDLRKQYQEVFEKRHGIRLGFMSFYVKAVTEA 345
Cdd:PLN02226 233 ---------RERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAAVSA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 346 LKRFPDVNASIDGDDIVYHNYFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDMTGGNFTITN 425
Cdd:PLN02226 304 LQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSN 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 426 GGVFGSLLSTPIINLPQSSILGMHKIQDRPMAVNGKVEILPMMYLALSYDHRQIDGKESVGFLVTIKELLEDPTRLLLDV 505
Cdd:PLN02226 384 GGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
1-497 |
3.09e-104 |
|
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: 323.50 E-value: 3.09e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 1 MSTEIKVPVLPESVADASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLIGDAQ 80
Cdd:TIGR02927 1 MAESVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAIIGEPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 81 EA---------SPSKEPKEDSSASE---KSEDAPAAQSAPASEGKEVDIKVPVLPESVADATIATWHVQPGDAVTRDQNL 148
Cdd:TIGR02927 81 EAgsepapaapEPEAAPEPEAPAPAptpAAEAPAPAAPQAGGSGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 149 VDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKV-KAGAAPA-------------------------------- 195
Cdd:TIGR02927 161 LEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgDANAAPAepaeeeapapseagsepapdpaaraphaapdp 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 196 -----KSDAKADAPAAKEESSSEGSDVLTPSVRRLIAEKGLDASKIKGSGKNGRVTKEDVDQFLK--------------- 255
Cdd:TIGR02927 241 papapAPAKTAAPAAAAPVSSGDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKaaeearaaaaapaaa 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 256 ----SPAPAAKAEAAPAAPMGDRTQKrvpMTRLRKTIANRLLEAKNSTAMLTTFNEVNMKPIMDLRKQYQEVFEKRHGIR 331
Cdd:TIGR02927 321 aapaAPAAAAKPAEPDTAKLRGTTQK---MNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 332 LGFMSFYVKAVTEALKRFPDVNASI--DGDDIVYHNYFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDG 409
Cdd:TIGR02927 398 LTFLPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 410 KLTLDDMTGGNFTITNGGVFGSLLSTPIINLPQSSILGMHKIQDRPMAV-----NGKVEILPMMYLALSYDHRQIDGKES 484
Cdd:TIGR02927 478 KLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIkdedgGESIAIRSVCYLPLTYDHRLVDGADA 557
|
570
....*....|...
gi 639351487 485 VGFLVTIKELLED 497
Cdd:TIGR02927 558 GRFLTTIKKRLEE 570
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-503 |
1.75e-102 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 320.41 E-value: 1.75e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 2 STEIKVPVLpeSVADASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLIGDAqE 81
Cdd:PRK11854 105 AKDVHVPDI--GSDEVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVA-G 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 82 ASPSKEPKEDSSASEKSEDAPAaqsapaseGKEVDIKVPVLpeSVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVV 161
Cdd:PRK11854 182 EAPAAAPAAAEAAAPAAAPAAA--------AGVKDVNVPDI--GGDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 162 AQEDGVMGEIIHDEGDTVLGEQVIGKVK-AGAAPAKSDAKADAPAAKEES------------SSEGSDVL---------T 219
Cdd:PRK11854 252 APFAGTVKEIKVNVGDKVKTGSLIMRFEvEGAAPAAAPAKQEAAAPAPAAakaeapaaapaaKAEGKSEFaendayvhaT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 220 PSVRRLIAEKGLDASKIKGSGKNGRVTKEDVDQFLKSPAPAAKAEAAPAAPMGDRTQ---------------KRVPMTRL 284
Cdd:PRK11854 332 PLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAAAAAGGGGPGllpwpkvdfskfgeiEEVELGRI 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 285 RKTIANRLLEAKNSTAMLTTFNEVNMKPIMDLRK-QYQEVFEKRHGIRLGFMSFYVKAVTEALKRFPDVNASI--DGDDI 361
Cdd:PRK11854 412 QKISGANLHRNWVMIPHVTQFDKADITELEAFRKqQNAEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRL 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 362 VYHNYFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDMTGGNFTITNGGVFGSLLSTPIINLP 441
Cdd:PRK11854 492 TLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAP 571
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639351487 442 QSSILGMHKIQDRPMAvNGKvEILP--MMYLALSYDHRQIDGKESVGFLVTIKELLEDPTRLLL 503
Cdd:PRK11854 572 EVAILGVSKSAMEPVW-NGK-EFAPrlMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
292-502 |
3.32e-95 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 287.52 E-value: 3.32e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 292 LLEAKNSTAMLTTFNEVNMKPIMDLRKQYQEVFEKRHGiRLGFMSFYVKAVTEALKRFPDVNASIDGDD--IVYHNYFDI 369
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 370 SIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDMTGGNFTITNGGVFGSLLSTPIINLPQSSILGMH 449
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 639351487 450 KIQDRPMAVNGKVEILPMMYLALSYDHRQIDGKESVGFLVTIKELLEDPTRLL 502
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-503 |
7.21e-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: 269.44 E-value: 7.21e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 3 TEIKVPVLPESvADASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATV-LGDQVIGLIGDAQE 81
Cdd:TIGR01348 1 TEIKVPDIGDN-EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLpVGGVIATLEVGAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 82 ASPSKEPKEDSSA----SEKSEDAPAAQSAPASEGKEVDIKVPVLpESVADATIATWHVQPGDAVTRDQNLVDIETDKVV 157
Cdd:TIGR01348 80 QAQAEAKKEAAPAptagAPAPAAQAQAAPAAGQSSGVQEVTVPDI-GDIEKVTVIEVLVKVGDTVSADQSLITLESDKAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 158 LEVVAQEDGVMGEI---IHDE---GDTVLGEQVIGKVKAGAAPAKSDAKADAPAAKEESSSEGS---------------- 215
Cdd:TIGR01348 159 MEVPAPASGVVKSVkvkVGDSvptGDLILTLSVAGSTPATAPAPASAQPAAQSPAATQPEPAAApaaakaqapapqqagt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 216 ------DVLTPSVRRLIAEKGLDASKIKGSGKNGRVTKEDVDQFLKSPAPAAKAEAAPAAPMGDR-------------TQ 276
Cdd:TIGR01348 239 qnpakvDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGalpwpnvdfskfgEV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 277 KRVPMTRLRKTIANRLLEAKNSTAMLTTFNEVNMKPIMDLRKQYQEVFEKRhGIRLGFMSFYVKAVTEALKRFPDVNASI 356
Cdd:TIGR01348 319 EEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKE-GVKLTVLHILMKAVAAALKKFPKFNASL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 357 D--GDDIVYHNYFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDMTGGNFTITNGGVFGSLLS 434
Cdd:TIGR01348 398 DlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAF 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639351487 435 TPIINLPQSSILGMHKIQDRPMAvNGKvEILP--MMYLALSYDHRQIDGKESVGFLVTIKELLEDPTRLLL 503
Cdd:TIGR01348 478 TPIVNAPEVAILGVSKSGMEPVW-NGK-EFEPrlMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
117-503 |
3.28e-76 |
|
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: 246.24 E-value: 3.28e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 117 IKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEG-------------------- 176
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtkdvpvnkpiavlveekedv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 177 -----DTVLGEQVIG--KVKAGAAPAKSDAKADAPAAKEE-----SSSEGSDV-------LTPSVRRLIAEKGLDASKIK 237
Cdd:TIGR01349 82 adafkNYKLESSASPapKPSEIAPTAPPSAPKPSPAPQKQspepsSPAPLSDKesgdrifASPLAKKLAKEKGIDLSAVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 238 GSGKNGRVTKEDVDQFL-KSPAPAAKAEAAPAAPMGDRTQKR-------VPMTRLRKTIANRLLEAKNSTAMLTTFNEVN 309
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVpQSPASANQQAAATTPATYPAAAPVstgsyedVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 310 MKPIMDLRKQYQEVFEKRhgIRLGFMSFYVKAVTEALKRFPDVNASIDGDDIVYHNYFDISIAVSTPRGLVTPVLKDCDK 389
Cdd:TIGR01349 242 VDKLLALRKELNAMASEV--YKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 390 LSVAEIEKGIRELALKGRDGKLTLDDMTGGNFTITNGGVFGSLLSTPIINLPQSSILGMHKIQDRPMAVNGK---VEILP 466
Cdd:TIGR01349 320 KGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVAS 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 639351487 467 MMYLALSYDHRQIDGKESVGFLVTIKELLEDPTRLLL 503
Cdd:TIGR01349 400 IMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
219-501 |
2.17e-59 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 198.09 E-value: 2.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 219 TPSVRRLIAEKGLDASKIKGSGKNGRVTKEDVDQFLKSPAPAAKAEAAPAAPMGDRTQ--------------KRVPMTRL 284
Cdd:PRK11857 5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAktaapaaappklegKREKVAPI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 285 RKTIANRLLEAKNSTAMLTTFNEVNMKPIMDLRKQYQEVFEKRHGIRLGFMSFYVKAVTEALKRFPDVNASID--GDDIV 362
Cdd:PRK11857 85 RKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDeaTSELV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 363 YHNYFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDMTGGNFTITNGGVFGSLLSTPIINLPQ 442
Cdd:PRK11857 165 YPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPE 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 639351487 443 SSILGMHKIQDRPMAVNGKVEILPMMYLALSYDHRQIDGKESVGFLVTIKELLEDPTRL 501
Cdd:PRK11857 245 LAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
116-503 |
3.22e-58 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 201.62 E-value: 3.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 116 DIKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGD-----------TVLGEQV 184
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAkeikvgeviaiTVEEEED 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 185 IGKVK-----AGAAPAKSDAKADAPAAKEE-------------------SSSEGSDVLTPSVRRLIAEKGLDASKIKGSG 240
Cdd:PLN02744 194 IGKFKdykpsSSAAPAAPKAKPSPPPPKEEevekpasspepkaskpsapPSSGDRIFASPLARKLAEDNNVPLSSIKGTG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 241 KNGRVTKEDVDQFLKSPAPAAKAEAAPAAPMGDRTQKRVPMTRLRKTIANRLLEAKNSTAMLTTFNEVNMKPIMDLRKQY 320
Cdd:PLN02744 274 PDGRIVKADIEDYLASGGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 321 QEVFEKRHGIRLGFMSFYVKAVTEALKRFPDVNASIDGDDI-VYHNyFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGI 399
Cdd:PLN02744 354 NSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIrQYHN-VNINVAVQTENGLYVPVVKDADKKGLSTIAEEV 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 400 RELALKGRDGKLTLDDMTGGNFTITN-GGVFGSLLSTPIINLPQSSILGMHKIQDR--PMAVNGKVEILPMMYLALSYDH 476
Cdd:PLN02744 433 KQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMSVTLSCDH 512
|
410 420
....*....|....*....|....*..
gi 639351487 477 RQIDGKESVGFLVTIKELLEDPTRLLL 503
Cdd:PLN02744 513 RVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
124-503 |
1.87e-57 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 196.48 E-value: 1.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 124 ESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTV-LGEQVIGKVKAGAA--------- 193
Cdd:PLN02528 8 EGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVkVGETLLKIMVEDSQhlrsdslll 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 194 PAKSDAKADAPAAKEESSSEGSDVLTPSVRRLIAEKGLDASKIKGSGKNGRVTKEDV------DQFLKSPAPAAKAEAAP 267
Cdd:PLN02528 88 PTDSSNIVSLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVlkyaaqKGVVKDSSSAEEATIAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 268 AAPMGDRTQKRVPMTRLRKTIA----NRLLeAKNSTAMLTT-----FNEVNMKPIMDLRKQYQEVfEKRHGIRLGFMSFY 338
Cdd:PLN02528 168 QEEFSTSVSTPTEQSYEDKTIPlrgfQRAM-VKTMTAAAKVphfhyVEEINVDALVELKASFQEN-NTDPTVKHTFLPFL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 339 VKAVTEALKRFPDVNASIDGD--DIVYHNYFDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDM 416
Cdd:PLN02528 246 IKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 417 TGGNFTITN----GGVFGSllstPIINLPQSSILGMHKIQDRPMAVN-GKVEILPMMYLALSYDHRQIDGKESVGFLVTI 491
Cdd:PLN02528 326 TGGTITLSNigaiGGKFGS----PVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIGADHRVLDGATVARFCNEW 401
|
410
....*....|..
gi 639351487 492 KELLEDPTRLLL 503
Cdd:PLN02528 402 KSYVEKPELLML 413
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
218-503 |
4.78e-50 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 174.71 E-value: 4.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 218 LTPSVRRLIAEKGLDASKIKGSGKNGRVTKEDVDQFL----KSPAPAAKAEAAPAAPMGDRTQK-----RVPMTRLRKTI 288
Cdd:PRK14843 51 ISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLpeniENDSIKSPAQIEKVEEVPDNVTPygeieRIPMTPMRKVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 289 ANRLLEAKNSTAMLTTFNEVNMKPIMDLRKQYQEVFEKRHGIRLGFMSFYVKAVTEALKRFPDVNASI--DGDDIVYHNY 366
Cdd:PRK14843 131 AQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLteDGKTIITHNY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 367 FDISIAVSTPRGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKLTLDDMTGGNFTITNGGVFGSLLSTPIINLPQSSIL 446
Cdd:PRK14843 211 VNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAIL 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 639351487 447 GMHKIQDRPMAVNGKVEILPMMYLALSYDHRQIDGKESVGFLVTIKELLEDPTRLLL 503
Cdd:PRK14843 291 GVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-76 |
4.09e-23 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 92.82 E-value: 4.09e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639351487 1 MSTEIKVPVLPESVADASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLI 76
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
115-188 |
1.33e-22 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 91.28 E-value: 1.33e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639351487 115 VDIKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKV 188
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
115-188 |
6.65e-22 |
|
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: 89.39 E-value: 6.65e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639351487 115 VDIKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKV 188
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-76 |
6.85e-21 |
|
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: 86.30 E-value: 6.85e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639351487 3 TEIKVPVLPESVADASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLI 76
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
341-495 |
5.15e-18 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 87.64 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 341 AVTEALKRFPDVNAS---IDGDDIVY---HNYFDISIAVSTP---RGLVTPVLKDCDKLSVAEIEKGIRELALKGRDGKL 411
Cdd:PRK12270 179 ALVQALKAFPNMNRHyaeVDGKPTLVtpaHVNLGLAIDLPKKdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 412 TLDDMTGGNFTITNGGVFGSLLSTPIINLPQSSILGMHKIqDRPMAVNGKVE-------ILPMMYLALSYDHRQIDGKES 484
Cdd:PRK12270 259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGASEerlaelgISKVMTLTSTYDHRIIQGAES 337
|
170
....*....|.
gi 639351487 485 VGFLVTIKELL 495
Cdd:PRK12270 338 GEFLRTIHQLL 348
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
116-188 |
8.34e-14 |
|
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: 66.31 E-value: 8.34e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639351487 116 DIKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKV 188
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
117-250 |
2.12e-13 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 71.51 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 117 IKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKVKAGAAPak 196
Cdd:PRK14875 5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVS-- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 639351487 197 sdakadapaakeesSSEGSDVLTPSVRRLiAEKGLDASKIKGSGKNGRVTKEDV 250
Cdd:PRK14875 83 --------------DAEIDAFIAPFARRF-APEGIDEEDAGPAPRKARIGGRTV 121
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
4-76 |
7.80e-13 |
|
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: 63.61 E-value: 7.80e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639351487 4 EIKVPVLPESVADASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLI 76
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
3-76 |
8.53e-13 |
|
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: 63.39 E-value: 8.53e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639351487 3 TEIKVPVLPESVAdASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLI 76
Cdd:pfam00364 1 TEIKSPMIGESVR-EGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
219-251 |
5.49e-12 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 60.01 E-value: 5.49e-12
10 20 30
....*....|....*....|....*....|...
gi 639351487 219 TPSVRRLIAEKGLDASKIKGSGKNGRVTKEDVD 251
Cdd:pfam02817 4 SPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
115-188 |
1.76e-10 |
|
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: 56.84 E-value: 1.76e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639351487 115 VDIKVPVLPESVADAtIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKV 188
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1-79 |
2.44e-10 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 62.27 E-value: 2.44e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639351487 1 MSTEIKVPVLPESVADASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLIGDA 79
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADA 79
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-129 |
4.18e-09 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 58.78 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 1 MSTEIKVPVLPESVADASVATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEG----------ATVLGD 70
Cdd:PRK11892 1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtegvkvntpiAVLLEE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 639351487 71 qvigliGDAQEASPSKEPKEDSSASEKSEDAPAAQSAPASEGKevdiKVPVLPESVADA 129
Cdd:PRK11892 81 ------GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAP----AAPAAPAAEVAA 129
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
115-197 |
5.23e-08 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 55.31 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639351487 115 VDIKVPVLPESVADATIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEG------DTVL------GE 182
Cdd:PRK11892 3 IEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtegvkvNTPIavlleeGE 82
|
90
....*....|....*
gi 639351487 183 QVIGKVKAGAAPAKS 197
Cdd:PRK11892 83 SASDAGAAPAAAAEA 97
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
19-76 |
8.55e-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: 46.26 E-value: 8.55e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 639351487 19 VATWHVSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLI 76
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
130-188 |
6.04e-05 |
|
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: 40.86 E-value: 6.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 639351487 130 TIATWHVQPGDAVTRDQNLVDIETDKVVLEVVAQEDGVMGEIIHDEGDTVLGEQVIGKV 188
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
24-76 |
2.93e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 43.29 E-value: 2.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 639351487 24 VSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVIGLI 76
Cdd:PRK09282 538 VKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
24-73 |
3.29e-04 |
|
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: 40.65 E-value: 3.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 639351487 24 VSVGDKVSRDQNLVDIETDKVVLEVVAQNDGVITEISQEEGATVLGDQVI 73
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPL 132
|
|
| |
