|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
2-423 |
2.44e-177 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 500.86 E-value: 2.44e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 2 GTHVIKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEVEG 81
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 82 AGNVKESAQPAPVKEAPVVAPKVEAVVESKPVAAPAPkaavcqgpmvARAADERPLASPAVRKHALDLGIQLRLVRGTGP 161
Cdd:PRK11856 81 EAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAP----------AAPAAAAAKASPAVRKLARELGVDLSTVKGSGP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 162 AGRVLHEDLDAYLAQGQSNASTVSSAYTQRT-----DEQQIPVIGMRRKIAQRMQDATQRAAHFSYVEEIDVTAVEELRA 236
Cdd:PRK11856 151 GGRITKEDVEAAAAAAAPAAAAAAAAAAAPPaaaaeGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 237 HLNEKhgatRGKLTLLPFLVRAMVVALRDFPQINARYDDEAqvITRLGAVHVGIATQADIGLMVPVVRHAEARSLWDSAA 316
Cdd:PRK11856 231 QLKAI----GVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 317 EISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPMVIKGQIVVRKMMNLSSSFDHR 396
Cdd:PRK11856 305 EIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHR 384
|
410 420
....*....|....*....|....*..
gi 2063487316 397 VVDGMDAALFIQAIRGLLEQPATLFVD 423
Cdd:PRK11856 385 VIDGADAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
210-421 |
2.67e-93 |
|
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: 279.81 E-value: 2.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 210 MQDATQRAAHFSYVEEIDVTAVEELRAHLNEKHGATRGKLTLLPFLVRAMVVALRDFPQINARYDDEAQVITRLGAVHVG 289
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 290 IATQADIGLMVPVVRHAEARSLWDSAAEISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNK 369
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2063487316 370 IVERPMVIKGQIVVRKMMNLSSSFDHRVVDGMDAALFIQAIRGLLEQPATLF 421
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
6-423 |
2.91e-93 |
|
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: 286.63 E-value: 2.91e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 6 IKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEvEGAGNV 85
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE-EGNDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 86 KESAQPAPVKEAPVVAPKVEAVVEskpvaapapkaavcqgpmvarAADERPLASPAVRKHALDLGIQLRLVRGTGPAGRV 165
Cdd:TIGR01347 82 AAPPAKSGEEKEETPAASAAAAPT---------------------AAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 166 LHEDLDAYL-----AQGQSNASTVSSAYTQRTDEQQIPVIGMRRKIAQRMQDATQRAAHFSYVEEIDVTAVEELRAHLNE 240
Cdd:TIGR01347 141 TKEDIIKKTeapasAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 241 ----KHGAtrgKLTLLPFLVRAMVVALRDFPQINARYDDEaQVITRlGAVHVGIATQADIGLMVPVVRHAEARSLWDSAA 316
Cdd:TIGR01347 221 efekKHGV---KLGFMSFFVKAVVAALKRFPEVNAEIDGD-DIVYK-DYYDISVAVSTDRGLVVPVVRNADRMSFADIEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 317 EISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPMVIKGQIVVRKMMNLSSSFDHR 396
Cdd:TIGR01347 296 EIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHR 375
|
410 420
....*....|....*....|....*..
gi 2063487316 397 VVDGMDAALFIQAIRGLLEQPATLFVD 423
Cdd:TIGR01347 376 LIDGKEAVTFLVTIKELLEDPRRLLLD 402
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
3-77 |
1.00e-24 |
|
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: 96.67 E-value: 1.00e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2063487316 3 THVIKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISI 77
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
6-77 |
1.91e-23 |
|
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: 92.85 E-value: 1.91e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2063487316 6 IKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISI 77
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
2-423 |
2.44e-177 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 500.86 E-value: 2.44e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 2 GTHVIKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEVEG 81
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 82 AGNVKESAQPAPVKEAPVVAPKVEAVVESKPVAAPAPkaavcqgpmvARAADERPLASPAVRKHALDLGIQLRLVRGTGP 161
Cdd:PRK11856 81 EAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAP----------AAPAAAAAKASPAVRKLARELGVDLSTVKGSGP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 162 AGRVLHEDLDAYLAQGQSNASTVSSAYTQRT-----DEQQIPVIGMRRKIAQRMQDATQRAAHFSYVEEIDVTAVEELRA 236
Cdd:PRK11856 151 GGRITKEDVEAAAAAAAPAAAAAAAAAAAPPaaaaeGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 237 HLNEKhgatRGKLTLLPFLVRAMVVALRDFPQINARYDDEAqvITRLGAVHVGIATQADIGLMVPVVRHAEARSLWDSAA 316
Cdd:PRK11856 231 QLKAI----GVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 317 EISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPMVIKGQIVVRKMMNLSSSFDHR 396
Cdd:PRK11856 305 EIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHR 384
|
410 420
....*....|....*....|....*..
gi 2063487316 397 VVDGMDAALFIQAIRGLLEQPATLFVD 423
Cdd:PRK11856 385 VIDGADAARFLKALKELLENPALLLLE 411
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-420 |
1.39e-128 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 381.86 E-value: 1.39e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 2 GTHVIKMPDIGEgIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEVEG 81
Cdd:PRK11855 118 GVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 82 AGNVKESAQPAPVKEAPVVAPKVEAVVESKPVAAPAPKAavcqgpmvARAADERPLASPAVRKHALDLGIQLRLVRGTGP 161
Cdd:PRK11855 197 AAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAA--------AAAPGKAPHASPAVRRLARELGVDLSQVKGTGK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 162 AGRVLHEDLDAYLAQGQSNASTVSSA------------------YTQRTDEQQIPVIGMRRKIAQRMQDATQRAAHFSYV 223
Cdd:PRK11855 269 KGRITKEDVQAFVKGAMSAAAAAAAAaaaagggglgllpwpkvdFSKFGEIETKPLSRIKKISAANLHRSWVTIPHVTQF 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 224 EEIDVTAVEELRAHLNEKHGATRGKLTLLPFLVRAMVVALRDFPQINARYDDEAQVITRLGAVHVGIATQADIGLMVPVV 303
Cdd:PRK11855 349 DEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 304 RHAEARSLWDSAAEISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPMVIKGQIVV 383
Cdd:PRK11855 429 KDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVP 508
|
410 420 430
....*....|....*....|....*....|....*..
gi 2063487316 384 RKMMNLSSSFDHRVVDGMDAALFIQAIRGLLEQPATL 420
Cdd:PRK11855 509 RLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRM 545
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
210-421 |
2.67e-93 |
|
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: 279.81 E-value: 2.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 210 MQDATQRAAHFSYVEEIDVTAVEELRAHLNEKHGATRGKLTLLPFLVRAMVVALRDFPQINARYDDEAQVITRLGAVHVG 289
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 290 IATQADIGLMVPVVRHAEARSLWDSAAEISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNK 369
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2063487316 370 IVERPMVIKGQIVVRKMMNLSSSFDHRVVDGMDAALFIQAIRGLLEQPATLF 421
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
6-423 |
2.91e-93 |
|
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: 286.63 E-value: 2.91e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 6 IKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEvEGAGNV 85
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE-EGNDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 86 KESAQPAPVKEAPVVAPKVEAVVEskpvaapapkaavcqgpmvarAADERPLASPAVRKHALDLGIQLRLVRGTGPAGRV 165
Cdd:TIGR01347 82 AAPPAKSGEEKEETPAASAAAAPT---------------------AAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 166 LHEDLDAYL-----AQGQSNASTVSSAYTQRTDEQQIPVIGMRRKIAQRMQDATQRAAHFSYVEEIDVTAVEELRAHLNE 240
Cdd:TIGR01347 141 TKEDIIKKTeapasAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 241 ----KHGAtrgKLTLLPFLVRAMVVALRDFPQINARYDDEaQVITRlGAVHVGIATQADIGLMVPVVRHAEARSLWDSAA 316
Cdd:TIGR01347 221 efekKHGV---KLGFMSFFVKAVVAALKRFPEVNAEIDGD-DIVYK-DYYDISVAVSTDRGLVVPVVRNADRMSFADIEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 317 EISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPMVIKGQIVVRKMMNLSSSFDHR 396
Cdd:TIGR01347 296 EIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHR 375
|
410 420
....*....|....*....|....*..
gi 2063487316 397 VVDGMDAALFIQAIRGLLEQPATLFVD 423
Cdd:TIGR01347 376 LIDGKEAVTFLVTIKELLEDPRRLLLD 402
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
6-423 |
2.39e-91 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 281.72 E-value: 2.39e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 6 IKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEVEGAGNV 85
Cdd:PRK05704 5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 86 KESAQPAPVKEAPVVAPKVEAvveskpvaapapkaavcqgpmvARAADERPLASPAVRKHALDLGIQLRLVRGTGPAGRV 165
Cdd:PRK05704 85 AAAAAAAAAAAAAAPAQAQAA----------------------AAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 166 LHEDLDAYLAQGQSNASTVSSAYTQRTD-------EQQIPVIGMRRKIAQRMQDATQRAAHFSYVEEIDVTAVEELRAHL 238
Cdd:PRK05704 143 TKEDVLAALAAAAAAPAAPAAAAPAAAPaplgarpEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 239 NE----KHGAtrgKLTLLPFLVRAMVVALRDFPQINARYDDEaQVITRlGAVHVGIATQADIGLMVPVVRHAEARSLWDS 314
Cdd:PRK05704 223 KDafekKHGV---KLGFMSFFVKAVVEALKRYPEVNASIDGD-DIVYH-NYYDIGIAVGTPRGLVVPVLRDADQLSFAEI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 315 AAEISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPMVIKGQIVVRKMMNLSSSFD 394
Cdd:PRK05704 298 EKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYD 377
|
410 420
....*....|....*....|....*....
gi 2063487316 395 HRVVDGMDAALFIQAIRGLLEQPATLFVD 423
Cdd:PRK05704 378 HRIIDGKEAVGFLVTIKELLEDPERLLLD 406
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
10-420 |
7.95e-88 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 273.13 E-value: 7.95e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 10 DIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEVEGAGNVKESA 89
Cdd:PLN02528 5 QTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRSDS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 90 qpapvKEAPVVAPKVEAVVESKpvaapapkaavcqgpmvARAADERP-LASPAVRKHALDLGIQLRLVRGTGPAGRVLHE 168
Cdd:PLN02528 85 -----LLLPTDSSNIVSLAESD-----------------ERGSNLSGvLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 169 DLDAYLAQ-----------------GQSNASTVSSAYTQRTDEQQIPVIGMRRKIAQRMQDATQrAAHFSYVEEIDVTAV 231
Cdd:PLN02528 143 DVLKYAAQkgvvkdsssaeeatiaeQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAK-VPHFHYVEEINVDAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 232 EELRAHLNEKHGATRGKLTLLPFLVRAMVVALRDFPQINARYDDEAQVITRLGAVHVGIATQADIGLMVPVVRHAEARSL 311
Cdd:PLN02528 222 VELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 312 WDSAAEISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERP-MVIKGQIVVRKMMNLS 390
Cdd:PLN02528 302 LEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPrFVDDGNVYPASIMTVT 381
|
410 420 430
....*....|....*....|....*....|
gi 2063487316 391 SSFDHRVVDGMDAALFIQAIRGLLEQPATL 420
Cdd:PLN02528 382 IGADHRVLDGATVARFCNEWKSYVEKPELL 411
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
6-415 |
3.51e-81 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 261.86 E-value: 3.51e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 6 IKMPDIGEGiaEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEVEGAGNV 85
Cdd:PRK11854 209 VNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 86 KESA---QPAPVKEAPVVAPKVEAVVESKPVAAPAPkaavcqgpmvarAADERPLASPAVRKHALDLGIQLRLVRGTGPA 162
Cdd:PRK11854 287 AAPAkqeAAAPAPAAAKAEAPAAAPAAKAEGKSEFA------------ENDAYVHATPLVRRLAREFGVNLAKVKGTGRK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 163 GRVLHEDLDAY----LAQGQSNA---------------STVSSAYTQRTDEQQIPVIgmrRKI-AQRMQDATQRAAHFSY 222
Cdd:PRK11854 355 GRILKEDVQAYvkdaVKRAEAAPaaaaaggggpgllpwPKVDFSKFGEIEEVELGRI---QKIsGANLHRNWVMIPHVTQ 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 223 VEEIDVTAVEELRAHLN-----EKHGAtrgKLTLLPFLVRAMVVALRDFPQINARYDDEAQVITRLGAVHVGIATQADIG 297
Cdd:PRK11854 432 FDKADITELEAFRKQQNaeaekRKLGV---KITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 298 LMVPVVRHAEARSLWDSAAEISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPMVI 377
Cdd:PRK11854 509 LVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWN 588
|
410 420 430
....*....|....*....|....*....|....*...
gi 2063487316 378 KGQIVVRKMMNLSSSFDHRVVDGMDAALFIQAIRGLLE 415
Cdd:PRK11854 589 GKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
5-423 |
4.34e-75 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 239.97 E-value: 4.34e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 5 VIKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEVEGAGN 84
Cdd:PTZ00144 46 VIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 85 VKESAQPAPVKEAPVVAPKVEAvveskpvaapapkaavcQGPMVARAADERPLASPAVRKHAldlgiqlrlvrgtgpagr 164
Cdd:PTZ00144 126 AAAPAAAAAAKAEKTTPEKPKA-----------------AAPTPEPPAASKPTPPAAAKPPE------------------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 165 vlhedldaylaqgQSNASTVSSAYTQRTD--EQQIPVIGMRRKIAQRMQDATQRAAHFSYVEEIDVTAVEELRAHLNE-- 240
Cdd:PTZ00144 171 -------------PAPAAKPPPTPVARADprETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDdf 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 241 --KHGAtrgKLTLLPFLVRAMVVALRDFPQINArYDDEAQVITRlGAVHVGIATQADIGLMVPVVRHAEARSLWDSAAEI 318
Cdd:PTZ00144 238 qkKHGV---KLGFMSAFVKASTIALKKMPIVNA-YIDGDEIVYR-NYVDISVAVATPTGLVVPVIRNCENKSFAEIEKEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 319 SRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPMVIKGQIVVRKMMNLSSSFDHRVV 398
Cdd:PTZ00144 313 ADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLI 392
|
410 420
....*....|....*....|....*
gi 2063487316 399 DGMDAALFIQAIRGLLEQPATLFVD 423
Cdd:PTZ00144 393 DGRDAVTFLKKIKDLIEDPARMLLD 417
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
6-416 |
8.16e-75 |
|
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: 244.15 E-value: 8.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 6 IKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEVEGAGNV 85
Cdd:TIGR02927 129 VKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAPA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 86 KESAQPAPVKEAPVVAPKVEAVVESKPVAAPAPKAAVCQGPMVARAA-------DERPLASPAVRKHALDLGIQLRLVRG 158
Cdd:TIGR02927 209 EPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAaapvssgDSGPYVTPLVRKLAKDKGVDLSTVKG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 159 TGPAGRVLHEDL-----------DAYLAQGQSNASTVSSAYTQRTDEQQIPVIG-------MRRKIAQRMQDATQRAAHF 220
Cdd:TIGR02927 289 TGVGGRIRKQDVlaaakaaeearAAAAAPAAAAAPAAPAAAAKPAEPDTAKLRGttqkmnrIRQITADKTIESLQTSAQL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 221 SYVEEIDVTAVEELRAH----LNEKHGAtrgKLTLLPFLVRAMVVALRDFPQINARYDDEAQVITRLGAVHVGIATQADI 296
Cdd:TIGR02927 369 TQVHEVDMTRVAALRARakndFLEKNGV---NLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPR 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 297 GLMVPVVRHAEARSLWDSAAEISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPMV 376
Cdd:TIGR02927 446 GLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRV 525
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2063487316 377 IKGQ-----IVVRKMMNLSSSFDHRVVDGMDAALFIQAIRGLLEQ 416
Cdd:TIGR02927 526 IKDEdggesIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
6-420 |
3.32e-74 |
|
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: 241.70 E-value: 3.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 6 IKMPDIGeGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEVEGAGNV 85
Cdd:TIGR01348 119 VTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 86 KEsAQPAPvKEAPVVAPKVEAVVESKPVAAPAPKAAVCQGPMvARAADERPLASPAVRKHALDLGIQLRLVRGTGPAGRV 165
Cdd:TIGR01348 198 TA-PAPAS-AQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAG-TQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 166 LHEDLDAYL--AQGQSNASTVSSA-------------YTQRTDEQQIPVIGMRRKIAQRMQDATQRAAHFSYVEEIDVTA 230
Cdd:TIGR01348 275 LREDVQRFVkePSVRAQAAAASAAggapgalpwpnvdFSKFGEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 231 VEELRAHLNEKHGATRGKLTLLPFLVRAMVVALRDFPQINARYDDEAQVITRLGAVHVGIATQADIGLMVPVVRHAEARS 310
Cdd:TIGR01348 355 MEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKG 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 311 LWDSAAEISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPMVIKGQIVVRKMMNLS 390
Cdd:TIGR01348 435 ITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLS 514
|
410 420 430
....*....|....*....|....*....|
gi 2063487316 391 SSFDHRVVDGMDAALFIQAIRGLLEQPATL 420
Cdd:TIGR01348 515 LSYDHRVIDGADAARFTTYICESLADIRRL 544
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
137-422 |
3.28e-65 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 211.19 E-value: 3.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 137 LASPAVRKHALDLGIQLRLVRGTGPAGRVLHEDLDAYLAQGQSN---ASTVSSAYTQRTDEQQIP-------------VI 200
Cdd:PRK11857 3 LATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAptpAEAASVSSAQQAAKTAAPaaappklegkrekVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 201 GMRRKIAQRMQDATQRAAHFSYVEEIDVTAVEELRAHLNEKHGATRG-KLTLLPFLVRAMVVALRDFPQINARYDDEAQV 279
Cdd:PRK11857 83 PIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGvKLTFLPFIAKAILIALKEFPIFAAKYDEATSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 280 ITRLGAVHVGIATQADIGLMVPVVRHAEARSLWDSAAEISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNL 359
Cdd:PRK11857 163 LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINY 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2063487316 360 PEVAIVGVNKIVERPMVIKGQIVVRKMMNLSSSFDHRVVDGMDAALFIQAIRGLLEQPATLFV 422
Cdd:PRK11857 243 PELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEILGV 305
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
6-420 |
8.32e-53 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 184.67 E-value: 8.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 6 IKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHG---KVIAlgGQPGEVMAVGSVlISIEVEGA 82
Cdd:PLN02744 115 IGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGylaKIVK--GDGAKEIKVGEV-IAITVEEE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 83 GNVKE--------SAQPAPVKEAPVVAPKVEAVVESKPVAAPAPKAAvcqgPMVARAADERPLASPAVRKHALDLGIQLR 154
Cdd:PLN02744 192 EDIGKfkdykpssSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASK----PSAPPSSGDRIFASPLARKLAEDNNVPLS 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 155 LVRGTGPAGRVLHEDLDAYLAQGQSNASTVSSAYTQRT--DEQQIPVIGMRRKIAQRMQDATQRAAHFSYVEEIDVTAVE 232
Cdd:PLN02744 268 SIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPalDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLM 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 233 ELRAHLNEKHGATRGK-LTLLPFLVRAMVVALRDFPQINARYDDEaqVITRLGAVHVGIATQADIGLMVPVVRHAEARSL 311
Cdd:PLN02744 348 ALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSWTDD--YIRQYHNVNINVAVQTENGLYVPVVKDADKKGL 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 312 WDSAAEISRLATAARNGKASRDELSGSSITLTSLGALGGIVS-TPVLNLPEVAIVGVNKIVER--PMVIKGQIVVRKMMN 388
Cdd:PLN02744 426 STIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQfCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMS 505
|
410 420 430
....*....|....*....|....*....|..
gi 2063487316 389 LSSSFDHRVVDGMDAALFIQAIRGLLEQPATL 420
Cdd:PLN02744 506 VTLSCDHRVIDGAIGAEWLKAFKGYIENPESM 537
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
139-422 |
8.02e-49 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 169.32 E-value: 8.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 139 SPAVRKHALDLGIQLRLVRGTGPAGRVLHEDLDAYLAQGQSNASTVSSAYTQRTDE-----------QQIPVIGMRRKIA 207
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEvpdnvtpygeiERIPMTPMRKVIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 208 QRMQDATQRAAHFSYVEEIDVTAVEELRAHLNEK-HGATRGKLTLLPFLVRAMVVALRDFPQINARYDDEAQVITRLGAV 286
Cdd:PRK14843 132 QRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPiMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 287 HVGIATQADIGLMVPVVRHAEARSLWDSAAEISRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVG 366
Cdd:PRK14843 212 NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILG 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2063487316 367 VNKIVERPMVIKGQIVVRKMMNLSSSFDHRVVDGMDAALFIQAIRGLLEQPATLFV 422
Cdd:PRK14843 292 VSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
8-423 |
5.82e-48 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 170.32 E-value: 5.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 8 MPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGS--VLISIEVEGAGNV 85
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTkvAIISKSEDAASQV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 86 KESaQPAPVKEAPVVAPKVEAVveskpvaapapkaavcQGPMVARA-ADERPLA--SPAVRKHaldlgiqlrlvrgtgpa 162
Cdd:PLN02226 176 TPS-QKIPETTDPKPSPPAEDK----------------QKPKVESApVAEKPKApsSPPPPKQ----------------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 163 grvlhedldaylaqgqsnaSTVSSAYTQRTDEQQIPVIGMRRKIAQRMQDATQRAAHFSYVEEIDVTAVEELRAHLN--- 239
Cdd:PLN02226 222 -------------------SAKEPQLPPKERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKdaf 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 240 -EKHGAtrgKLTLLPFLVRAMVVALRDFPQINARYDDEaQVITRlGAVHVGIATQADIGLMVPVVRHAEARSLWDSAAEI 318
Cdd:PLN02226 283 yEKHGV---KLGLMSGFIKAAVSALQHQPVVNAVIDGD-DIIYR-DYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 319 SRLATAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNKIVERPMVIKGQIVVRKMMNLSSSFDHRVV 398
Cdd:PLN02226 358 NGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLI 437
|
410 420
....*....|....*....|....*
gi 2063487316 399 DGMDAALFIQAIRGLLEQPATLFVD 423
Cdd:PLN02226 438 DGREAVYFLRRVKDVVEDPQRLLLD 462
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
3-77 |
1.00e-24 |
|
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: 96.67 E-value: 1.00e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2063487316 3 THVIKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISI 77
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
6-77 |
1.91e-23 |
|
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: 92.85 E-value: 1.91e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2063487316 6 IKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISI 77
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
181-414 |
2.31e-15 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 78.39 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 181 ASTVSSAYTQRTDEQQIPVIGMRRKIAQRMQD------ATQraahfsyVEEIDVTAVEELRAHLNEKHGATRG-KLTLLP 253
Cdd:PRK12270 102 AAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDAslevptATS-------VRAVPAKLLIDNRIVINNHLKRTRGgKVSFTH 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 254 FLVRAMVVALRDFPQINARY---DDEAQVITRlGAVHVGIA--TQADIG---LMVPVVRHAEA---RSLWDSAAEISRla 322
Cdd:PRK12270 175 LIGYALVQALKAFPNMNRHYaevDGKPTLVTP-AHVNLGLAidLPKKDGsrqLVVPAIKGAETmdfAQFWAAYEDIVR-- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 323 tAARNGKASRDELSGSSITLTSLGALGGIVSTPVLNLPEVAIVGVNKIvERPMVIKG-------QIVVRKMMNLSSSFDH 395
Cdd:PRK12270 252 -RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGaseerlaELGISKVMTLTSTYDH 329
|
250
....*....|....*....
gi 2063487316 396 RVVDGMDAALFIQAIRGLL 414
Cdd:PRK12270 330 RIIQGAESGEFLRTIHQLL 348
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-77 |
5.59e-14 |
|
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: 66.47 E-value: 5.59e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2063487316 4 HVIKMPDIGEGIAEVELSvWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISI 77
Cdd:pfam00364 1 TEIKSPMIGESVREGVVE-WLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
136-171 |
1.59e-09 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 52.69 E-value: 1.59e-09
10 20 30
....*....|....*....|....*....|....*.
gi 2063487316 136 PLASPAVRKHALDLGIQLRLVRGTGPAGRVLHEDLD 171
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
4-82 |
6.23e-08 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 54.18 E-value: 6.23e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2063487316 4 HVIKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIEVEGA 82
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEV 81
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
6-59 |
8.10e-08 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 48.98 E-value: 8.10e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2063487316 6 IKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIA 59
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKK 55
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
6-133 |
5.61e-05 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 45.29 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063487316 6 IKMPDIGEGIAEVELSVWHVKVGDMVVEDQVLADVMTDKAMVDIPS---PVHGKVIALGGQPGevMAVGSVLISIEVEGA 82
Cdd:PRK11892 5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAvdeGTLGKILVPEGTEG--VKVNTPIAVLLEEGE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2063487316 83 GNVKESAQPAPVKEAPVVAPKVEAVVESKPVAAPAPKAAVcqgPMVARAAD 133
Cdd:PRK11892 83 SASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAA---PAAEVAAD 130
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
23-77 |
2.77e-04 |
|
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: 38.94 E-value: 2.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2063487316 23 WHVKVGDMVVEDQVLA--DVMtdKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISI 77
Cdd:cd06850 13 VLVKEGDKVEAGQPLAvlEAM--KMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
25-78 |
3.82e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 42.52 E-value: 3.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2063487316 25 VKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIE 78
Cdd:PRK09282 538 VKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
26-59 |
1.22e-03 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 37.90 E-value: 1.22e-03
10 20 30
....*....|....*....|....*....|....
gi 2063487316 26 KVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIA 59
Cdd:cd06848 38 EVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVE 71
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-78 |
1.64e-03 |
|
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: 38.34 E-value: 1.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2063487316 25 VKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIALGGQPGEVMAVGSVLISIE 78
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
15-59 |
3.24e-03 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 37.41 E-value: 3.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2063487316 15 IAEVELsvwhVKVGDMVVEDQVLADVMTDKAMVDIPSPVHGKVIA 59
Cdd:COG0509 39 IVFVEL----PEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVE 79
|
|
| |
