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Conserved domains on  [gi|16128702|ref|NP_415255|]
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dihydrolipoyltranssuccinylase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

dihydrolipoyllysine-residue succinyltransferase( domain architecture ID 11481525)

dihydrolipoyllysine-residue succinyltransferase is the E2 component of 2-oxoglutarate dehydrogenase complex, which catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2)

EC:  2.3.1.61
Gene Ontology:  GO:0004149|GO:0006099|GO:0045252
PubMed:  10739245

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
2-405 0e+00

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


:

Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 750.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    2 SSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:PRK05704   1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   82 SAGK--ETSAKSEEKASTPAQRQQASLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESA 159
Cdd:PRK05704  81 AAGAaaAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  160 PAAAAPAAQPALAA-RSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFY 238
Cdd:PRK05704 161 PAAAAPAAAPAPLGaRPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  239 VKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTG 318
Cdd:PRK05704 241 VKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  319 GNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDP 398
Cdd:PRK05704 321 GTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDP 400


                 ....*..
gi 16128702  399 TRLLLDV 405
Cdd:PRK05704 401 ERLLLDL 407
 
Name Accession Description Interval E-value
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
2-405 0e+00

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 750.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    2 SSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:PRK05704   1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   82 SAGK--ETSAKSEEKASTPAQRQQASLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESA 159
Cdd:PRK05704  81 AAGAaaAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  160 PAAAAPAAQPALAA-RSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFY 238
Cdd:PRK05704 161 PAAAAPAAAPAPLGaRPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  239 VKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTG 318
Cdd:PRK05704 241 VKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  319 GNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDP 398
Cdd:PRK05704 321 GTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDP 400


                 ....*..
gi 16128702  399 TRLLLDV 405
Cdd:PRK05704 401 ERLLLDL 407
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 4-405 0e+00

2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]


Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 690.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702     4 VDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSA 83
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    84 GKETSAKS-EEKASTPAQRQQASLEEQNN-DALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESAPA 161
Cdd:TIGR01347  81 TAAPPAKSgEEKEETPAASAAAAPTAAANrPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   162 AAAPAAQPALAaRSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKA 241
Cdd:TIGR01347 161 AAAAAAPAAAT-RPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   242 VVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNF 321
Cdd:TIGR01347 240 VVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTF 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   322 TITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRL 401
Cdd:TIGR01347 320 TITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRL 399


                  ....
gi 16128702   402 LLDV 405
Cdd:TIGR01347 400 LLDL 403
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 192-402 4.39e-100

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 296.38  E-value: 4.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   192 LLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGiRLGFMSFYVKAVVEALKRYPEVNASIDGDD--VVYHNYFDV 269
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   270 SMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMH 349
Cdd:pfam00198  80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 16128702   350 AIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLL 402
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 2-77 5.05e-26

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: 99.76  E-value: 5.05e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128702   2 SSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:COG0508   1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 4-77 1.57e-24

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: 95.55  E-value: 1.57e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128702   4 VDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:cd06849   1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
 
Name Accession Description Interval E-value
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
2-405 0e+00

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 750.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    2 SSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:PRK05704   1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   82 SAGK--ETSAKSEEKASTPAQRQQASLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESA 159
Cdd:PRK05704  81 AAGAaaAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  160 PAAAAPAAQPALAA-RSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFY 238
Cdd:PRK05704 161 PAAAAPAAAPAPLGaRPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  239 VKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTG 318
Cdd:PRK05704 241 VKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  319 GNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDP 398
Cdd:PRK05704 321 GTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDP 400


                 ....*..
gi 16128702  399 TRLLLDV 405
Cdd:PRK05704 401 ERLLLDL 407
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 4-405 0e+00

2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]


Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 690.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702     4 VDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSA 83
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    84 GKETSAKS-EEKASTPAQRQQASLEEQNN-DALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESAPA 161
Cdd:TIGR01347  81 TAAPPAKSgEEKEETPAASAAAAPTAAANrPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   162 AAAPAAQPALAaRSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKA 241
Cdd:TIGR01347 161 AAAAAAPAAAT-RPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   242 VVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNF 321
Cdd:TIGR01347 240 VVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTF 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   322 TITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRL 401
Cdd:TIGR01347 320 TITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRL 399


                  ....
gi 16128702   402 LLDV 405
Cdd:TIGR01347 400 LLDL 403
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 6-405 1.41e-159

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 455.30  E-value: 1.41e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    6 ILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLregnsagK 85
Cdd:PTZ00144  47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEI-------D 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   86 ETSAKSEEKASTPAQRQQASLEEQNNDALSPAirrllaehnldASAIKgtgvggrltrEDVEKHLAKAPAKESAPAAAAP 165
Cdd:PTZ00144 120 TGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPT-----------PEPPA----------ASKPTPPAAAKPPEPAPAAKPP 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  166 AAQPALAARSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAVVEA 245
Cdd:PTZ00144 179 PTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIA 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  246 LKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITN 325
Cdd:PTZ00144 259 LKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISN 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  326 GGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLLDV 405
Cdd:PTZ00144 339 GGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 4-404 1.55e-137

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 399.17  E-value: 1.55e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    4 VDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSA 83
Cdd:PRK11856   3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   84 GKETSAKSEEKASTPAQRQQASLEEQNNDAL--------------SPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKH 149
Cdd:PRK11856  83 EAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAaaapaapaaaaakaSPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  150 LAKAPAKESAPAAAAPAAQPALAARSEkRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYgeafeKRHG 229
Cdd:PRK11856 163 AAAAAPAAAAAAAAAAAPPAAAAEGEE-RVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQL-----KAIG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  230 IRLGFMSFYVKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDG 309
Cdd:PRK11856 237 VKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREG 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  310 KLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLV 389
Cdd:PRK11856 317 KLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLK 396

                        410
                 ....*....|....*
gi 16128702  390 TIKELLEDPTRLLLD 404
Cdd:PRK11856 397 ALKELLENPALLLLE 411
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 3-405 2.86e-118

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 352.14  E-value: 2.86e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    3 SVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNS 82
Cdd:PLN02226  91 TVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   83 AGKETsAKSEEKASTPAQRQQASLEeqnnDALSPAIrrllaEHNLDASAIKGTGVGGRLTREDVEKHLAKAPakesapaa 162
Cdd:PLN02226 171 AASQV-TPSQKIPETTDPKPSPPAE----DKQKPKV-----ESAPVAEKPKAPSSPPPPKQSAKEPQLPPKE-------- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  163 aapaaqpalaarSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAV 242
Cdd:PLN02226 233 ------------RERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAA 300

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  243 VEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFT 322
Cdd:PLN02226 301 VSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFT 380

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  323 ITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLL 402
Cdd:PLN02226 381 VSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLL 460


                 ...
gi 16128702  403 LDV 405
Cdd:PLN02226 461 LDI 463
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 2-403 7.42e-109

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 330.63  E-value: 7.42e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    2 SSVDILVPDLPEsVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:PRK11855 118 GVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAA 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   82 SAGKETSAKSEEK---------------ASTPAQRQQASLEEQNNDAL-SPAIRRLLAEHNLDASAIKGTGVGGRLTRED 145
Cdd:PRK11855 197 AAPAAAAAPAAAApaaaaaaapapapaaAAAPAAAAPAAAAAPGKAPHaSPAVRRLARELGVDLSQVKGTGKKGRITKED 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  146 VEKHL--AKAPAKESAPAAAAPAAQPALAARSEK----------RVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPI 213
Cdd:PRK11855 277 VQAFVkgAMSAAAAAAAAAAAAGGGGLGLLPWPKvdfskfgeieTKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDL 356

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  214 MDLRKQYGEAFEKrHGIRLGFMSFYVKAVVEALKRYPEVNASID--GDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLG 291
Cdd:PRK11855 357 EALRKQLKKEAEK-AGVKLTMLPFFIKAVVAALKEFPVFNASLDedGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKS 435

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  292 MADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLA 371
Cdd:PRK11855 436 LLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLS 515

                        410       420       430
                 ....*....|....*....|....*....|..
gi 16128702  372 LSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 403
Cdd:PRK11855 516 LSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 192-402 4.39e-100

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 296.38  E-value: 4.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   192 LLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGiRLGFMSFYVKAVVEALKRYPEVNASIDGDD--VVYHNYFDV 269
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   270 SMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMH 349
Cdd:pfam00198  80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 16128702   350 AIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLL 402
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 2-403 1.95e-93

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 293.45  E-value: 1.95e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    2 SSVDILVPDLpeSVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:PRK11854 205 GVKDVNVPDI--GGDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEG 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   82 SAG------------KETSAKSEEKASTPAQRQQASLEEQNNDAL---SPAIRRLLAEHNLDASAIKGTGVGGRLTREDV 146
Cdd:PRK11854 283 AAPaaapakqeaaapAPAAAKAEAPAAAPAAKAEGKSEFAENDAYvhaTPLVRRLAREFGVNLAKVKGTGRKGRILKEDV 362

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  147 EKHLAKAPAKESAPAAAAPAAQPALAARSEKRV-----------PMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMD 215
Cdd:PRK11854 363 QAYVKDAVKRAEAAPAAAAAGGGGPGLLPWPKVdfskfgeieevELGRIQKISGANLHRNWVMIPHVTQFDKADITELEA 442

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  216 LRK-QYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASI--DGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGM 292
Cdd:PRK11854 443 FRKqQNAEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGI 522

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  293 ADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPmaVNGQVEILP--MMYL 370
Cdd:PRK11854 523 IELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEP--VWNGKEFAPrlMLPL 600

                        410       420       430
                 ....*....|....*....|....*....|...
gi 16128702  371 ALSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 403
Cdd:PRK11854 601 SLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 2-397 5.27e-92

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: 288.06  E-value: 5.27e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702     2 SSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:TIGR02927 125 EATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDAN 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    82 SAGKETS--------------------------------AKSEEKASTPAQRQQASlEEQNNDALSPAIRRLLAEHNLDA 129
Cdd:TIGR02927 205 AAPAEPAeeeapapseagsepapdpaaraphaapdppapAPAPAKTAAPAAAAPVS-SGDSGPYVTPLVRKLAKDKGVDL 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   130 SAIKGTGVGGRLTREDVEKHLAKAPAKESAPAAAAPAAQPALAARSEKRV------------PMTRLRKRVAERLLEAKN 197
Cdd:TIGR02927 284 STVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAAAAKPAepdtaklrgttqKMNRIRQITADKTIESLQ 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   198 STAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASI--DGDDVVYHNYFDVSMAVST 275
Cdd:TIGR02927 364 TSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVDT 443

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   276 PRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRP 355
Cdd:TIGR02927 444 PRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRP 523

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 16128702   356 MAV-----NGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLED 397
Cdd:TIGR02927 524 RVIkdedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 6-403 2.10e-85

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: 266.66  E-value: 2.10e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702     6 ILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTT-----------------V 68
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKdvpvnkpiavlveekedV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    69 TSRQILGRLREGNSAGKETSAK--------------SEEKASTPAQRQQASLEEQNND-ALSPAIRRLLAEHNLDASAIK 133
Cdd:TIGR01349  82 ADAFKNYKLESSASPAPKPSEIaptappsapkpspaPQKQSPEPSSPAPLSDKESGDRiFASPLAKKLAKEKGIDLSAVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   134 GTGVGGRLTREDVEKHLAKAPAKESAPAAAAPAAQPALAARSE----KRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVN 209
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAAAPVStgsyEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   210 MKPIMDLRKQYGEAFEKRhgIRLGFMSFYVKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDT 289
Cdd:TIGR01349 242 VDKLLALRKELNAMASEV--YKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADA 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   290 LGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQ---VEILP 366
Cdd:TIGR01349 320 KGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVAS 399

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 16128702   367 MMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 403
Cdd:TIGR01349 400 IMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 5-403 2.44e-71

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: 233.61  E-value: 2.44e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702     5 DILVPDLpESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLR--EGNS 82
Cdd:TIGR01348 118 EVTVPDI-GDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSvaGSTP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    83 AGKETSAKSEEKASTPAQRQQA-------------------SLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTR 143
Cdd:TIGR01348 197 ATAPAPASAQPAAQSPAATQPEpaaapaaakaqapapqqagTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILR 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   144 EDVEKHLAKAPAKESAPAAAAPAAQPALAARSE---------KRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIM 214
Cdd:TIGR01348 277 EDVQRFVKEPSVRAQAAAASAAGGAPGALPWPNvdfskfgevEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEME 356

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   215 DLRKQYGEAFEKRhGIRLGFMSFYVKAVVEALKRYPEVNASID--GDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGM 292
Cdd:TIGR01348 357 AFRKQQNAAVEKE-GVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGI 435

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   293 ADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLAL 372
Cdd:TIGR01348 436 TELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSL 515

                         410       420       430
                  ....*....|....*....|....*....|.
gi 16128702   373 SYDHRLIDGRESVGFLVTIKELLEDPTRLLL 403
Cdd:TIGR01348 516 SYDHRVIDGADAARFTTYICESLADIRRLLL 546
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 5-403 1.15e-64

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 215.87  E-value: 1.15e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    5 DILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGT-----------TVTSRQI 73
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAkeikvgeviaiTVEEEED 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   74 LGRLREGNSAGKETSAKSEEKASTPA-----QRQQASLEEQNNDAL------------SPAIRRLLAEHNLDASAIKGTG 136
Cdd:PLN02744 194 IGKFKDYKPSSSAAPAAPKAKPSPPPpkeeeVEKPASSPEPKASKPsappssgdrifaSPLARKLAEDNNVPLSSIKGTG 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  137 VGGRLTREDVEKHLAKAPAKESAPAAAAPAAQPAlaarSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDL 216
Cdd:PLN02744 274 PDGRIVKADIEDYLASGGKGATAPPSTDSKAPAL----DYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMAL 349

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  217 RKQYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASIDGDDV-VYHNyFDVSMAVSTPRGLVTPVLRDVDTLGMADI 295
Cdd:PLN02744 350 RSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIrQYHN-VNINVAVQTENGLYVPVVKDADKKGLSTI 428

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  296 EKKIKELAVKGRDGKLTVEDLTGGNFTITN-GGVFGSLMSTPIINPPQSAILGMHAIKDR--PMAVNGQVEILPMMYLAL 372
Cdd:PLN02744 429 AEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMSVTL 508

                        410       420       430
                 ....*....|....*....|....*....|.
gi 16128702  373 SYDHRLIDGRESVGFLVTIKELLEDPTRLLL 403
Cdd:PLN02744 509 SCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 115-401 4.10e-56

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 186.92  E-value: 4.10e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  115 SPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHL----------AKAPAKESAPAAAAPAAQPALAARSEKRVPMTRL 184
Cdd:PRK11857   5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIkslksaptpaEAASVSSAQQAAKTAAPAAAPPKLEGKREKVAPI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  185 RKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASID--GDDVV 262
Cdd:PRK11857  85 RKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDeaTSELV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  263 YHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQ 342
Cdd:PRK11857 165 YPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPE 244

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16128702  343 SAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRL 401
Cdd:PRK11857 245 LAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 104-403 1.08e-54

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 184.34  E-value: 1.08e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  104 ASLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESAPAAAAPAAQPALAARSEK-----R 178
Cdd:PRK14843  41 ETYKDTNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDNVTPygeieR 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  179 VPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASI-- 256
Cdd:PRK14843 121 IPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLte 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  257 DGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTP 336
Cdd:PRK14843 201 DGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGP 280

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128702  337 IINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 403
Cdd:PRK14843 281 IINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 6-403 1.21e-48

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 170.29  E-value: 1.21e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    6 ILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSAGK 85
Cdd:PLN02528   1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   86 ETSAKSEEKASTPAQRQQASLEEQNNDA---LSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHL-----------A 151
Cdd:PLN02528  81 RSDSLLLPTDSSNIVSLAESDERGSNLSgvlSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAaqkgvvkdsssA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  152 KAPAKESAPAAAAPAAQPALAARSEKRVPMtrlrkRVAERLLeAKNSTAMLTT-----FNEVNMKPIMDLRKQYGEAfEK 226
Cdd:PLN02528 161 EEATIAEQEEFSTSVSTPTEQSYEDKTIPL-----RGFQRAM-VKTMTAAAKVphfhyVEEINVDALVELKASFQEN-NT 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  227 RHGIRLGFMSFYVKAVVEALKRYPEVNASIDGD--DVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAV 304
Cdd:PLN02528 234 DPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQH 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702  305 KGRDGKLTVEDLTGGNFTITN----GGVFGSlmstPIINPPQSAILGMHAIKDRPMAVN-GQVEILPMMYLALSYDHRLI 379
Cdd:PLN02528 314 LAAENKLNPEDITGGTITLSNigaiGGKFGS----PVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIGADHRVL 389

                        410       420
                 ....*....|....*....|....
gi 16128702  380 DGRESVGFLVTIKELLEDPTRLLL 403
Cdd:PLN02528 390 DGATVARFCNEWKSYVEKPELLML 413
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 2-77 5.05e-26

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: 99.76  E-value: 5.05e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128702   2 SSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:COG0508   1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 4-77 1.57e-24

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: 95.55  E-value: 1.57e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128702   4 VDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:cd06849   1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 5-77 4.07e-24

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: 94.82  E-value: 4.07e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128702   5 DILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:cd06663   1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 241-395 1.34e-21

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 97.27  E-value: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   241 AVVEALKRYPEVNASIDGDD----VVYHNYFDVSMAVSTP-----RGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKL 311
Cdd:PRK12270  179 ALVQALKAFPNMNRHYAEVDgkptLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702   312 TVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIkDRPMAVNGQVE-------ILPMMYLALSYDHRLIDGRES 384
Cdd:PRK12270  259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGASEerlaelgISKVMTLTSTYDHRIIQGAES 337

                         170
                  ....*....|.
gi 16128702   385 VGFLVTIKELL 395
Cdd:PRK12270  338 GEFLRTIHQLL 348
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 6-113 2.19e-14

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 73.82  E-value: 2.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    6 ILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSAGK 85
Cdd:PRK14875   5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSDA 84

                         90       100
                 ....*....|....*....|....*...
gi 16128702   86 ETSAkseekASTPAQRQQASLEEQNNDA 113
Cdd:PRK14875  85 EIDA-----FIAPFARRFAPEGIDEEDA 107
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 3-118 1.56e-12

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 68.79  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    3 SVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGT------TVTSRqILGr 76
Cdd:PRK11892   2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTegvkvnTPIAV-LLE- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 16128702   77 lrEGNSAGKETSAKSEEKASTPAQRQQASLEEQNNDALSPAI 118
Cdd:PRK11892  80 --EGESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAA 119
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 4-77 3.44e-12

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: 61.46  E-value: 3.44e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128702     4 VDILVPDLPESVAdATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:pfam00364   1 TEIKSPMIGESVR-EGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 3-107 2.24e-10

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 62.33  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128702    3 SVDILVPDLpeSVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNS 82
Cdd:PRK11854   2 AIEIKVPDI--GADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADG 79

                         90       100
                 ....*....|....*....|....*
gi 16128702   83 AGKETSAKSEEKASTPAQRQQASLE 107
Cdd:PRK11854  80 AADAAPAQAEEKKEAAPAAAPAAAA 104
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 115-147 6.37e-10

e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.


Pssm-ID: 460710 [Multi-domain]  Cd Length: 36  Bit Score: 53.84  E-value: 6.37e-10
                          10        20        30
                  ....*....|....*....|....*....|...
gi 16128702   115 SPAIRRLLAEHNLDASAIKGTGVGGRLTREDVE 147
Cdd:pfam02817   4 SPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 19-77 1.37e-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: 45.48  E-value: 1.37e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16128702  19 TVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:cd06850   9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 26-74 6.93e-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: 36.80  E-value: 6.93e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 16128702  26 KPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQIL 74
Cdd:COG0511  84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPL 132
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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