|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
2-428 |
0e+00 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 515.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 2 GTHVIKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIEVEG 81
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 82 SGNHVDAPTKDAPKPEqvqapaapvaarPEPQKEARPAAcqaAVNHEAAPIVPRQPGDKPLASPAVRKRALDAGIELRYV 161
Cdd:PRK11856 81 EAEAAAAAEAAPEAPA------------PEPAPAAAAAA---AAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 162 HGSGPAGRILHEDLDAFMS-----KPHSAGGQAPSGYAKRTDSEQVPVIGLRRKIAQRMQDAKRRVAHFSYVEEIDVTAL 236
Cdd:PRK11856 146 KGSGPGGRITKEDVEAAAAaaapaAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 237 EALRQQLNSKhgdsRGKLTLLPFLVRALVVALRDFPQINATYDDEAqvITRHGAVHVGIATQGDNGLMVPVLRHAEAGSL 316
Cdd:PRK11856 226 LALRKQLKAI----GVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 317 WSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPVVIDGQIVVRKMMNLSS 396
Cdd:PRK11856 300 FELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSL 379
|
410 420 430
....*....|....*....|....*....|..
gi 635296002 397 SFDHRVVDGMDAALFIQAVRGLLEQPACLFVE 428
Cdd:PRK11856 380 SFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
215-426 |
2.31e-96 |
|
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: 2.31e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 215 MQDAKRRVAHFSYVEEIDVTALEALRQQLNSKHGDSRGKLTLLPFLVRALVVALRDFPQINATYDDEAQVITRHGAVHVG 294
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 295 IATQGDNGLMVPVLRHAEAGSLWSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNR 374
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 635296002 375 MVERPVVIDGQIVVRKMMNLSSSFDHRVVDGMDAALFIQAVRGLLEQPACLF 426
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
6-428 |
2.57e-88 |
|
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: 273.92 E-value: 2.57e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 6 IKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIEvegSGNH 85
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE---EGND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 86 VDAPTKDAPKPEqvqapaapvaarPEPQKEARPAACQAAvnheaapivprqPGDKPLASPAVRKRALDAGIELRYVHGSG 165
Cdd:TIGR01347 80 ATAAPPAKSGEE------------KEETPAASAAAAPTA------------AANRPSLSPAARRLAKEHGIDLSAVPGTG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 166 PAGRILHEDLDAFMSKPHSAGGQAPSGYAKRTDS-----EQVPVIGLRRKIAQRMQDAKRRVAHFSYVEEIDVTALEALR 240
Cdd:TIGR01347 136 VTGRVTKEDIIKKTEAPASAQPPAAAAAAAAPAAatrpeERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 241 QQLNS----KHGDsrgKLTLLPFLVRALVVALRDFPQINATYDDEaQVITrHGAVHVGIATQGDNGLMVPVLRHAEAGSL 316
Cdd:TIGR01347 216 KRYKEefekKHGV---KLGFMSFFVKAVVAALKRFPEVNAEIDGD-DIVY-KDYYDISVAVSTDRGLVVPVVRNADRMSF 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 317 WSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPVVIDGQIVVRKMMNLSS 396
Cdd:TIGR01347 291 ADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLAL 370
|
410 420 430
....*....|....*....|....*....|..
gi 635296002 397 SFDHRVVDGMDAALFIQAVRGLLEQPACLFVE 428
Cdd:TIGR01347 371 SYDHRLIDGKEAVTFLVTIKELLEDPRRLLLD 402
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
3-77 |
8.63e-28 |
|
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: 104.76 E-value: 8.63e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 635296002 3 THVIKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRI 77
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
6-77 |
2.95e-26 |
|
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: 100.56 E-value: 2.95e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635296002 6 IKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRI 77
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
2-428 |
0e+00 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 515.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 2 GTHVIKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIEVEG 81
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 82 SGNHVDAPTKDAPKPEqvqapaapvaarPEPQKEARPAAcqaAVNHEAAPIVPRQPGDKPLASPAVRKRALDAGIELRYV 161
Cdd:PRK11856 81 EAEAAAAAEAAPEAPA------------PEPAPAAAAAA---AAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 162 HGSGPAGRILHEDLDAFMS-----KPHSAGGQAPSGYAKRTDSEQVPVIGLRRKIAQRMQDAKRRVAHFSYVEEIDVTAL 236
Cdd:PRK11856 146 KGSGPGGRITKEDVEAAAAaaapaAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 237 EALRQQLNSKhgdsRGKLTLLPFLVRALVVALRDFPQINATYDDEAqvITRHGAVHVGIATQGDNGLMVPVLRHAEAGSL 316
Cdd:PRK11856 226 LALRKQLKAI----GVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 317 WSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPVVIDGQIVVRKMMNLSS 396
Cdd:PRK11856 300 FELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSL 379
|
410 420 430
....*....|....*....|....*....|..
gi 635296002 397 SFDHRVVDGMDAALFIQAVRGLLEQPACLFVE 428
Cdd:PRK11856 380 SFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-423 |
2.27e-132 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 391.88 E-value: 2.27e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 2 GTHVIKMPDIGEgIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIEVEG 81
Cdd:PRK11855 118 GVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 82 SGNHVDAPTKDAPKPeqvqapaapvaarPEPQKEARPAACQAAVNHEAAPIVPRQPGDKPLASPAVRKRALDAGIELRYV 161
Cdd:PRK11855 197 AAPAAAAAPAAAAPA-------------AAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 162 HGSGPAGRILHEDLDAF----MSKPHSAGGQAPSG--------------YAKRTDSEQVPVIGLRRKIAQRMQDAKRRVA 223
Cdd:PRK11855 264 KGTGKKGRITKEDVQAFvkgaMSAAAAAAAAAAAAgggglgllpwpkvdFSKFGEIETKPLSRIKKISAANLHRSWVTIP 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 224 HFSYVEEIDVTALEALRQQLNSKHGDSRGKLTLLPFLVRALVVALRDFPQINATYDDEAQVITRHGAVHVGIATQGDNGL 303
Cdd:PRK11855 344 HVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 304 MVPVLRHAEAGSLWSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPVVID 383
Cdd:PRK11855 424 VVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDG 503
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 635296002 384 GQIVVRKMMNLSSSFDHRVVDGMDAALFIQAVRGLLEQPA 423
Cdd:PRK11855 504 KEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPR 543
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
215-426 |
2.31e-96 |
|
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: 2.31e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 215 MQDAKRRVAHFSYVEEIDVTALEALRQQLNSKHGDSRGKLTLLPFLVRALVVALRDFPQINATYDDEAQVITRHGAVHVG 294
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 295 IATQGDNGLMVPVLRHAEAGSLWSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNR 374
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 635296002 375 MVERPVVIDGQIVVRKMMNLSSSFDHRVVDGMDAALFIQAVRGLLEQPACLF 426
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
6-420 |
2.39e-88 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 281.12 E-value: 2.39e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 6 IKMPDIGEGiaQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIEVEGSGNH 85
Cdd:PRK11854 209 VNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 86 VDAPTKDAPKPEqvqapaapvaarPEPQKEARPAACQAAVNHEAAPIVprQPGDKPLASPAVRKRALDAGIELRYVHGSG 165
Cdd:PRK11854 287 AAPAKQEAAAPA------------PAAAKAEAPAAAPAAKAEGKSEFA--ENDAYVHATPLVRRLAREFGVNLAKVKGTG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 166 PAGRILHEDLDAF----MSKPHSAGGQAPSG-------------YAKRTDSEQVPVIGLRRKIAQRMQDAKRRVAHFSYV 228
Cdd:PRK11854 353 RKGRILKEDVQAYvkdaVKRAEAAPAAAAAGgggpgllpwpkvdFSKFGEIEEVELGRIQKISGANLHRNWVMIPHVTQF 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 229 EEIDVTALEALRQQLNS-----KHGdsrGKLTLLPFLVRALVVALRDFPQINATYDDEAQVITRHGAVHVGIATQGDNGL 303
Cdd:PRK11854 433 DKADITELEAFRKQQNAeaekrKLG---VKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 304 MVPVLRHAEAGSLWSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPVVID 383
Cdd:PRK11854 510 VVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNG 589
|
410 420 430
....*....|....*....|....*....|....*..
gi 635296002 384 GQIVVRKMMNLSSSFDHRVVDGMDAALFIQAVRGLLE 420
Cdd:PRK11854 590 KEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
6-428 |
2.57e-88 |
|
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: 273.92 E-value: 2.57e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 6 IKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIEvegSGNH 85
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE---EGND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 86 VDAPTKDAPKPEqvqapaapvaarPEPQKEARPAACQAAvnheaapivprqPGDKPLASPAVRKRALDAGIELRYVHGSG 165
Cdd:TIGR01347 80 ATAAPPAKSGEE------------KEETPAASAAAAPTA------------AANRPSLSPAARRLAKEHGIDLSAVPGTG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 166 PAGRILHEDLDAFMSKPHSAGGQAPSGYAKRTDS-----EQVPVIGLRRKIAQRMQDAKRRVAHFSYVEEIDVTALEALR 240
Cdd:TIGR01347 136 VTGRVTKEDIIKKTEAPASAQPPAAAAAAAAPAAatrpeERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 241 QQLNS----KHGDsrgKLTLLPFLVRALVVALRDFPQINATYDDEaQVITrHGAVHVGIATQGDNGLMVPVLRHAEAGSL 316
Cdd:TIGR01347 216 KRYKEefekKHGV---KLGFMSFFVKAVVAALKRFPEVNAEIDGD-DIVY-KDYYDISVAVSTDRGLVVPVVRNADRMSF 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 317 WSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPVVIDGQIVVRKMMNLSS 396
Cdd:TIGR01347 291 ADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLAL 370
|
410 420 430
....*....|....*....|....*....|..
gi 635296002 397 SFDHRVVDGMDAALFIQAVRGLLEQPACLFVE 428
Cdd:TIGR01347 371 SYDHRLIDGKEAVTFLVTIKELLEDPRRLLLD 402
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
6-425 |
1.14e-87 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 272.48 E-value: 1.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 6 IKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIEvEGSGNH 85
Cdd:PRK05704 5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRID-EGAAAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 86 VDAPTKDAPKPeqvqapaapvaarpepqKEARPAACQAAVNHEAAPIVprqpgdkplASPAVRKRALDAGIELRYVHGSG 165
Cdd:PRK05704 84 AAAAAAAAAAA-----------------AAAAPAQAQAAAAAEQSNDA---------LSPAARKLAAENGLDASAVKGTG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 166 PAGRILHEDLDAFMSKPHSAGGQAPSGYAKRTDS-------EQVPVIGLRRKIAQRMQDAKRRVAHFSYVEEIDVTALEA 238
Cdd:PRK05704 138 KGGRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAplgarpeERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 239 LRQQLN----SKHGDsrgKLTLLPFLVRALVVALRDFPQINATYDDEAQVItrHGAVHVGIATQGDNGLMVPVLRHAEAG 314
Cdd:PRK05704 218 LRKQYKdafeKKHGV---KLGFMSFFVKAVVEALKRYPEVNASIDGDDIVY--HNYYDIGIAVGTPRGLVVPVLRDADQL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 315 SLWSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPVVIDGQIVVRKMMNL 394
Cdd:PRK05704 293 SFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYL 372
|
410 420 430
....*....|....*....|....*....|.
gi 635296002 395 SSSFDHRVVDGMDAALFIQAVRGLLEQPACL 425
Cdd:PRK05704 373 ALSYDHRIIDGKEAVGFLVTIKELLEDPERL 403
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
10-422 |
2.76e-86 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 269.28 E-value: 2.76e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 10 DIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIEVEGSGNHVDAP 89
Cdd:PLN02528 5 QTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRSDS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 90 TKdapkpeqvqapaapvaarPEPQKEARPAACQAAVNHEAAPIVprqpgdkpLASPAVRKRALDAGIELRYVHGSGPAGR 169
Cdd:PLN02528 85 LL------------------LPTDSSNIVSLAESDERGSNLSGV--------LSTPAVRHLAKQYGIDLNDILGTGKDGR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 170 ILHEDL------DAFMSKPHSA-----GGQAPSGYAKRTDSEQ------VPVIGLRRKIAQRMQDAKrRVAHFSYVEEID 232
Cdd:PLN02528 139 VLKEDVlkyaaqKGVVKDSSSAeeatiAEQEEFSTSVSTPTEQsyedktIPLRGFQRAMVKTMTAAA-KVPHFHYVEEIN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 233 VTALEALRQQLNSKHGDSRGKLTLLPFLVRALVVALRDFPQINATYDDEAQVITRHGAVHVGIATQGDNGLMVPVLRHAE 312
Cdd:PLN02528 218 VDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 313 AGSLWSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERP-VVIDGQIVVRKM 391
Cdd:PLN02528 298 SLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPrFVDDGNVYPASI 377
|
410 420 430
....*....|....*....|....*....|.
gi 635296002 392 MNLSSSFDHRVVDGMDAALFIQAVRGLLEQP 422
Cdd:PLN02528 378 MTVTIGADHRVLDGATVARFCNEWKSYVEKP 408
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
6-422 |
1.04e-85 |
|
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: 271.75 E-value: 1.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 6 IKMPDIGeGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIEVEGSGnh 85
Cdd:TIGR01348 119 VTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGST-- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 86 vdAPTKDAPKPEQVQApaapvaarPEPQKEARPAACQAAVNHEAAPIV----PRQPGDKPLASPAVRKRALDAGIELRYV 161
Cdd:TIGR01348 196 --PATAPAPASAQPAA--------QSPAATQPEPAAAPAAAKAQAPAPqqagTQNPAKVDHAAPAVRRLAREFGVDLSAV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 162 HGSGPAGRILHEDLDAFM--------SKPHSAGGQAPS-------GYAKRTDSEQVPVIGLRRKIAQRMQDAKRRVAHFS 226
Cdd:TIGR01348 266 KGTGIKGRILREDVQRFVkepsvraqAAAASAAGGAPGalpwpnvDFSKFGEVEEVDMSRIRKISGANLTRNWTMIPHVT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 227 YVEEIDVTALEALRQQLNSKHGDSRGKLTLLPFLVRALVVALRDFPQINATYDDEAQVITRHGAVHVGIATQGDNGLMVP 306
Cdd:TIGR01348 346 HFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVP 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 307 VLRHAEAGSLWSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPVVIDGQI 386
Cdd:TIGR01348 426 VIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEF 505
|
410 420 430
....*....|....*....|....*....|....*.
gi 635296002 387 VVRKMMNLSSSFDHRVVDGMDAALFIQAVRGLLEQP 422
Cdd:TIGR01348 506 EPRLMLPLSLSYDHRVIDGADAARFTTYICESLADI 541
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
6-421 |
2.57e-78 |
|
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: 253.40 E-value: 2.57e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 6 IKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIeveGSGNH 85
Cdd:TIGR02927 129 VKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAII---GDANA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 86 VDAPtKDAPKPEQVQAPAAPVAARPEPQKEARPAACQAAVNHEAAPIVPRQPGDK------PLASPAVRKRALDAGIELR 159
Cdd:TIGR02927 206 APAE-PAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVssgdsgPYVTPLVRKLAKDKGVDLS 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 160 YVHGSGPAGRILHEDLDAFMSK-----------PHSAGGQAPSGYAKRTDSEQVPVIG-------LRRKIAQRMQDAKRR 221
Cdd:TIGR02927 285 TVKGTGVGGRIRKQDVLAAAKAaeearaaaaapAAAAAPAAPAAAAKPAEPDTAKLRGttqkmnrIRQITADKTIESLQT 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 222 VAHFSYVEEIDVTALEALRQQLNSKHGDSRG-KLTLLPFLVRALVVALRDFPQINATYDDEAQVITRHGAVHVGIATQGD 300
Cdd:TIGR02927 365 SAQLTQVHEVDMTRVAALRARAKNDFLEKNGvNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTP 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 301 NGLMVPVLRHAEAGSLWSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPV 380
Cdd:TIGR02927 445 RGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPR 524
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 635296002 381 VI---DG--QIVVRKMMNLSSSFDHRVVDGMDAALFIQAVRGLLEQ 421
Cdd:TIGR02927 525 VIkdeDGgeSIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
5-428 |
3.21e-75 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 240.74 E-value: 3.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 5 VIKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIEVEGSGN 84
Cdd:PTZ00144 46 VIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 85 HVDAPTKDAPKPEQvqapaapvaarPEPQKEARPAACQAAVNHEaapivprqpgdKPLASPAVRKraldagielryvhgs 164
Cdd:PTZ00144 126 AAAPAAAAAAKAEK-----------TTPEKPKAAAPTPEPPAAS-----------KPTPPAAAKP--------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 165 gpagrilhedldafmSKPHSAGGQAPSGYAKRTDSE-QVPVIGLRRKIAQRMQDAKRRVAHFSYVEEIDVTALEALRQQL 243
Cdd:PTZ00144 169 ---------------PEPAPAAKPPPTPVARADPREtRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 244 NS----KHGdsrGKLTLLPFLVRALVVALRDFPQINAtYDDEAQVITRHgAVHVGIATQGDNGLMVPVLRHAEAGSLWSN 319
Cdd:PTZ00144 234 KDdfqkKHG---VKLGFMSAFVKASTIALKKMPIVNA-YIDGDEIVYRN-YVDISVAVATPTGLVVPVIRNCENKSFAEI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 320 AGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPVVIDGQIVVRKMMNLSSSFD 399
Cdd:PTZ00144 309 EKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYD 388
|
410 420
....*....|....*....|....*....
gi 635296002 400 HRVVDGMDAALFIQAVRGLLEQPACLFVE 428
Cdd:PTZ00144 389 HRLIDGRDAVTFLKKIKDLIEDPARMLLD 417
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
5-422 |
1.12e-69 |
|
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: 226.98 E-value: 1.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 5 VIKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSG---KVLALGGQPGevMAVGSeLIRIEVEg 81
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGylaKILVPEGTKD--VPVNK-PIAVLVE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 82 SGNHVDAPTKDAPKPEQVQAPAAPVAARP--EPQKEARPAACQAAVNHEA--APIVPRQPGDKPLASPAVRKRALDAGIE 157
Cdd:TIGR01349 77 EKEDVADAFKNYKLESSASPAPKPSEIAPtaPPSAPKPSPAPQKQSPEPSspAPLSDKESGDRIFASPLAKKLAKEKGID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 158 LRYVHGSGPAGRILHEDLDAFMSK-----PHSAGGQAPSGYAKRTDS-----EQVPVIGLRRKIAQRMQDAKRRVAHFSY 227
Cdd:TIGR01349 157 LSAVAGSGPNGRIVKKDIESFVPQspasaNQQAAATTPATYPAAAPVstgsyEDVPLSNIRKIIAKRLLESKQTIPHYYV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 228 VEEIDVTALEALRQQLNsKHGDSRGKLTLLPFLVRALVVALRDFPQINATYDDeaQVITRHGAVHVGIATQGDNGLMVPV 307
Cdd:TIGR01349 237 SIECNVDKLLALRKELN-AMASEVYKLSVNDFIIKASALALREVPEANSSWTD--NFIRRYKNVDISVAVATPDGLITPI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 308 LRHAEAGSLWSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPVVIDGQ-- 385
Cdd:TIGR01349 314 VRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEek 393
|
410 420 430
....*....|....*....|....*....|....*...
gi 635296002 386 -IVVRKMMNLSSSFDHRVVDGMDAALFIQAVRGLLEQP 422
Cdd:TIGR01349 394 gFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENP 431
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
140-427 |
1.25e-67 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 217.35 E-value: 1.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 140 KPLASPAVRKRALDAGIELRYVHGSGPAGRILHEDLDAFMSKPHSAGGQA----------------PSGYAKRTDSEQVP 203
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAeaasvssaqqaaktaaPAAAPPKLEGKREK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 204 VIGLRRKIAQRMQDAKRRVAHFSYVEEIDVTALEALRQQLNSKHGDSRG-KLTLLPFLVRALVVALRDFPQINATYDDEA 282
Cdd:PRK11857 81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGvKLTFLPFIAKAILIALKEFPIFAAKYDEAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 283 QVITRHGAVHVGIATQGDNGLMVPVLRHAEAGSLWSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVV 362
Cdd:PRK11857 161 SELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 635296002 363 NTPEVAIVGVNRMVERPVVIDGQIVVRKMMNLSSSFDHRVVDGMDAALFIQAVRGLLEQPACLFV 427
Cdd:PRK11857 241 NYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEILGV 305
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
6-422 |
1.76e-57 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 197.38 E-value: 1.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 6 IKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSG---KVLALGG----QPGEVMAvgselIRIE 78
Cdd:PLN02744 115 IGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGylaKIVKGDGakeiKVGEVIA-----ITVE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 79 VEG----------SGNHVDAPTKDAPKPeqvqapaapvaarPEPQKEARPAACQAAVNHEAAPIVPRQPGDKPLASPAVR 148
Cdd:PLN02744 190 EEEdigkfkdykpSSSAAPAAPKAKPSP-------------PPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLAR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 149 KRALDAGIELRYVHGSGPAGRILHEDLDAFMSKpHSAGGQAPSGYAKRTDS---EQVPVIGLRRKIAQRMQDAKRRVAHF 225
Cdd:PLN02744 257 KLAEDNNVPLSSIKGTGPDGRIVKADIEDYLAS-GGKGATAPPSTDSKAPAldyTDIPNTQIRKVTASRLLQSKQTIPHY 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 226 SYVEEIDVTALEALRQQLNSKHGDSRGK-LTLLPFLVRALVVALRDFPQINATYDDEaqVITRHGAVHVGIATQGDNGLM 304
Cdd:PLN02744 336 YLTVDTRVDKLMALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSWTDD--YIRQYHNVNINVAVQTENGLY 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 305 VPVLRHAEAGSLWSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVS-TPVVNTPEVAIVGVNRMVER--PVV 381
Cdd:PLN02744 414 VPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQfCAIINPPQSAILAVGSAEKRviPGS 493
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 635296002 382 IDGQIVVRKMMNLSSSFDHRVVDGMDAALFIQAVRGLLEQP 422
Cdd:PLN02744 494 GPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENP 534
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
144-427 |
5.67e-52 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 177.79 E-value: 5.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 144 SPAVRKRALDAGIELRYVHGSGPAGRILHEDLDAFMSKP-----------HSAGGQAPSGYAKRTDSEQVPVIGLRRKIA 212
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENiendsikspaqIEKVEEVPDNVTPYGEIERIPMTPMRKVIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 213 QRMQDAKRRVAHFSYVEEIDVTALEALRQQLNSKHGDSRGK-LTLLPFLVRALVVALRDFPQINATYDDEAQVITRHGAV 291
Cdd:PRK14843 132 QRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKkTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 292 HVGIATQGDNGLMVPVLRHAEAGSLWSNAGEISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVG 371
Cdd:PRK14843 212 NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILG 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 635296002 372 VNRMVERPVVIDGQIVVRKMMNLSSSFDHRVVDGMDAALFIQAVRGLLEQPACLFV 427
Cdd:PRK14843 292 VSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
8-428 |
3.58e-49 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 173.40 E-value: 3.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 8 MPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIEV-EGSGNHV 86
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKsEDAASQV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 87 ----DAPTKDAPKPEQVQAPaapvaaRPEPQKEARPAACQAAVnhEAAPIVPRQPGDKPLASPAVRKRaldagielryvh 162
Cdd:PLN02226 176 tpsqKIPETTDPKPSPPAED------KQKPKVESAPVAEKPKA--PSSPPPPKQSAKEPQLPPKERER------------ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 163 gsgpagrilhedldafmskphsaggqapsgyakrtdseQVPVIGLRRKIAQRMQDAKRRVAHFSYVEEIDVTALEALRQQ 242
Cdd:PLN02226 236 --------------------------------------RVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 243 LNSKHGDSRG-KLTLLPFLVRALVVALRDFPQINATYDDEaQVITRHgAVHVGIATQGDNGLMVPVLRHAEAGSLWSNAG 321
Cdd:PLN02226 278 YKDAFYEKHGvKLGLMSGFIKAAVSALQHQPVVNAVIDGD-DIIYRD-YVDISIAVGTSKGLVVPVIRGADKMNFAEIEK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 322 EISRLANAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMVERPVVIDGQIVVRKMMNLSSSFDHR 401
Cdd:PLN02226 356 TINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHR 435
|
410 420
....*....|....*....|....*..
gi 635296002 402 VVDGMDAALFIQAVRGLLEQPACLFVE 428
Cdd:PLN02226 436 LIDGREAVYFLRRVKDVVEDPQRLLLD 462
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
3-77 |
8.63e-28 |
|
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: 104.76 E-value: 8.63e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 635296002 3 THVIKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRI 77
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
6-77 |
2.95e-26 |
|
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: 100.56 E-value: 2.95e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635296002 6 IKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRI 77
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
89-419 |
1.36e-17 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 85.33 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 89 PTKDAPKPEQVQAPAAPVAARPEPQKEARPAACQAAVNHEAAPIVPRQPGDKPLASPAVrkraldagielryvhgsgpag 168
Cdd:PRK12270 38 PGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAP--------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 169 rilhedldafmSKPHSAGGQAPSGyAKRTDSEQVPVIGLRRKIAQRMqDAKRRVAHFSYVEEIDVTALEALRQQLNSKHG 248
Cdd:PRK12270 97 -----------AAPPAAAAAAAPA-AAAVEDEVTPLRGAAAAVAKNM-DASLEVPTATSVRAVPAKLLIDNRIVINNHLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 249 DSRG-KLTLLPFLVRALVVALRDFPQINATYD--DEAQVITRHGAVHVGIA--TQGDNG---LMVPVLRHAEA---GSLW 317
Cdd:PRK12270 164 RTRGgKVSFTHLIGYALVQALKAFPNMNRHYAevDGKPTLVTPAHVNLGLAidLPKKDGsrqLVVPAIKGAETmdfAQFW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 318 SNAGEISRlanAARKNKASRDELSGSTITLTSLGALGGIVSTPVVNTPEVAIVGVNRMvERPVVIDG-------QIVVRK 390
Cdd:PRK12270 244 AAYEDIVR---RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGaseerlaELGISK 319
|
330 340
....*....|....*....|....*....
gi 635296002 391 MMNLSSSFDHRVVDGMDAALFIQAVRGLL 419
Cdd:PRK12270 320 VMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-77 |
3.99e-16 |
|
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: 72.63 E-value: 3.99e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635296002 4 HVIKMPDIGEGIAQVElVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRI 77
Cdd:pfam00364 1 TEIKSPMIGESVREGV-VEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
141-176 |
1.38e-09 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 53.07 E-value: 1.38e-09
10 20 30
....*....|....*....|....*....|....*.
gi 635296002 141 PLASPAVRKRALDAGIELRYVHGSGPAGRILHEDLD 176
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
4-88 |
1.59e-09 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 59.19 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 4 HVIKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRI-EVEGS 82
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVaDAEVS 82
|
....*.
gi 635296002 83 GNHVDA 88
Cdd:PRK14875 83 DAEIDA 88
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
6-64 |
2.16e-07 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 47.82 E-value: 2.16e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 635296002 6 IKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLA----LGGQP 64
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKvlvkEGTKV 64
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
6-154 |
5.56e-06 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 48.38 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 6 IKMPDIGEGIAQVELVEWFVKVGDMIAEDQVVADVMTDKATVEIPS---PVSGKVLALGGQPGevMAVGSELIRIEVEG- 81
Cdd:PRK11892 5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAvdeGTLGKILVPEGTEG--VKVNTPIAVLLEEGe 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635296002 82 -SGNHVDAPTKDAPKPEQVQAPAAPVAARPEPQKEARPAACQAAVNHEaapivPRQPGDKPLASPAVRKRALDA 154
Cdd:PRK11892 83 sASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAAD-----PDIPAGTEMVTMTVREALRDA 151
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
20-77 |
9.12e-06 |
|
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: 43.17 E-value: 9.12e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 635296002 20 LVEWFVKVGDMIAEDQVVA--DVMtdKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRI 77
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAvlEAM--KMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
15-59 |
4.41e-05 |
|
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: 42.80 E-value: 4.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 635296002 15 IAQVELVEwfvkVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLA 59
Cdd:COG0509 39 IVFVELPE----VGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVE 79
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
23-59 |
7.87e-05 |
|
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: 41.37 E-value: 7.87e-05
10 20 30
....*....|....*....|....*....|....*..
gi 635296002 23 WFVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLA 59
Cdd:cd06848 35 ELPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVE 71
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
24-78 |
1.18e-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: 41.80 E-value: 1.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 635296002 24 FVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIE 78
Cdd:COG0511 82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
24-78 |
1.53e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 40.60 E-value: 1.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 635296002 24 FVKVGDMIAEDQVVADVMTDKATVEIPSPVSGKVLALGGQPGEVMAVGSELIRIE 78
Cdd:PRK09282 537 KVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| |
