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Conserved domains on  [gi|446492073|ref|WP_000569927|]
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MULTISPECIES: 2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase [Bacillus]

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;
1-417 0e+00

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


:

Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 655.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   1 MIEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGA 80
Cdd:PRK05704   2 MVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  81 PVAvSTPAPVAEQPKQETTEAPKAAAPNAEQTATLqglpntnrpiaSPAARKMARELGIDLNDVRSTDPLGRVRPHDVQA 160
Cdd:PRK05704  82 AGA-AAAAAAAAAAAAAAPAQAQAAAAAEQSNDAL-----------SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 161 HAAAPKEAPAAPKSPAPVAKT--EFEKPVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMSAIMELRKERKDAFEKK 238
Cdd:PRK05704 150 ALAAAAAAPAAPAAAAPAAAPapLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKK 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 239 HDVRLGFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKAR 318
Cdd:PRK05704 230 HGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKAR 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 319 DNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIDNErMENRPMMYIALSYDHRIVDGKEAVS 398
Cdd:PRK05704 310 DGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQ-IVIRPMMYLALSYDHRIIDGKEAVG 388

                        410
                 ....*....|....*....
gi 446492073 399 FLVAVKDMLEDPKSLLLEG 417
Cdd:PRK05704 389 FLVTIKELLEDPERLLLDL 407
 
Name Accession Description Interval E-value
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
1-417 0e+00

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 655.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   1 MIEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGA 80
Cdd:PRK05704   2 MVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  81 PVAvSTPAPVAEQPKQETTEAPKAAAPNAEQTATLqglpntnrpiaSPAARKMARELGIDLNDVRSTDPLGRVRPHDVQA 160
Cdd:PRK05704  82 AGA-AAAAAAAAAAAAAAPAQAQAAAAAEQSNDAL-----------SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 161 HAAAPKEAPAAPKSPAPVAKT--EFEKPVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMSAIMELRKERKDAFEKK 238
Cdd:PRK05704 150 ALAAAAAAPAAPAAAAPAAAPapLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKK 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 239 HDVRLGFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKAR 318
Cdd:PRK05704 230 HGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKAR 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 319 DNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIDNErMENRPMMYIALSYDHRIVDGKEAVS 398
Cdd:PRK05704 310 DGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQ-IVIRPMMYLALSYDHRIIDGKEAVG 388

                        410
                 ....*....|....*....
gi 446492073 399 FLVAVKDMLEDPKSLLLEG 417
Cdd:PRK05704 389 FLVTIKELLEDPERLLLDL 407
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 2-416 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: 568.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073    2 IEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILdANGAP 81
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL-EEGND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   82 VAVSTPAPvAEQPKQETTEAPKAAAPNAEQtatlqglpntNRPIASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQAH 161
Cdd:TIGR01347  80 ATAAPPAK-SGEEKEETPAASAAAAPTAAA----------NRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  162 AAAPKEAPAAPKSPAPVAKTEFEKPVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMSAIMELRKERKDAFEKKHDV 241
Cdd:TIGR01347 149 TEAPASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGV 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  242 RLGFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDNK 321
Cdd:TIGR01347 229 KLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGK 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  322 LSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIdNERMENRPMMYIALSYDHRIVDGKEAVSFLV 401
Cdd:TIGR01347 309 LTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAV-NGQIEIRPMMYLALSYDHRLIDGKEAVTFLV 387

                         410
                  ....*....|....*
gi 446492073  402 AVKDMLEDPKSLLLE 416
Cdd:TIGR01347 388 TIKELLEDPRRLLLD 402
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 203-414 3.23e-92

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


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 276.73  E-value: 3.23e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  203 LVEVQQTSAMLTTFNEVDMSAIMELRKERKDAFEKKHDvRLGFMSFFTKAVVAALKQFPLLNAEIQGD--ELIIKKFYDI 280
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  281 GIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMH 360
Cdd:pfam00198  80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446492073  361 KIQVRPVAIDNErMENRPMMYIALSYDHRIVDGKEAVSFLVAVKDMLEDPKSLL 414
Cdd:pfam00198 160 RIRKRPVVVDGE-IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 1-75 1.64e-27

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: 103.99  E-value: 1.64e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446492073   1 MIEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:COG0508    2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 2-75 2.01e-27

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: 103.64  E-value: 2.01e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446492073   2 IEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:cd06849    1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
 
Name Accession Description Interval E-value
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
1-417 0e+00

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 655.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   1 MIEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGA 80
Cdd:PRK05704   2 MVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  81 PVAvSTPAPVAEQPKQETTEAPKAAAPNAEQTATLqglpntnrpiaSPAARKMARELGIDLNDVRSTDPLGRVRPHDVQA 160
Cdd:PRK05704  82 AGA-AAAAAAAAAAAAAAPAQAQAAAAAEQSNDAL-----------SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 161 HAAAPKEAPAAPKSPAPVAKT--EFEKPVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMSAIMELRKERKDAFEKK 238
Cdd:PRK05704 150 ALAAAAAAPAAPAAAAPAAAPapLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKK 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 239 HDVRLGFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKAR 318
Cdd:PRK05704 230 HGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKAR 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 319 DNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIDNErMENRPMMYIALSYDHRIVDGKEAVS 398
Cdd:PRK05704 310 DGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQ-IVIRPMMYLALSYDHRIIDGKEAVG 388

                        410
                 ....*....|....*....
gi 446492073 399 FLVAVKDMLEDPKSLLLEG 417
Cdd:PRK05704 389 FLVTIKELLEDPERLLLDL 407
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 2-416 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: 568.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073    2 IEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILdANGAP 81
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL-EEGND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   82 VAVSTPAPvAEQPKQETTEAPKAAAPNAEQtatlqglpntNRPIASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQAH 161
Cdd:TIGR01347  80 ATAAPPAK-SGEEKEETPAASAAAAPTAAA----------NRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  162 AAAPKEAPAAPKSPAPVAKTEFEKPVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMSAIMELRKERKDAFEKKHDV 241
Cdd:TIGR01347 149 TEAPASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGV 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  242 RLGFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDNK 321
Cdd:TIGR01347 229 KLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGK 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  322 LSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIdNERMENRPMMYIALSYDHRIVDGKEAVSFLV 401
Cdd:TIGR01347 309 LTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAV-NGQIEIRPMMYLALSYDHRLIDGKEAVTFLV 387

                         410
                  ....*....|....*
gi 446492073  402 AVKDMLEDPKSLLLE 416
Cdd:TIGR01347 388 TIKELLEDPRRLLLD 402
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 4-416 8.76e-156

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 446.44  E-value: 8.76e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   4 IKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGAPVA 83
Cdd:PTZ00144  47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPA 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  84 VSTPAPVAEQPKQETTEAPKAAAPNAEQtatlqglPNTNRPIASPAARKMArelgidlndvrsTDPLGRVRPHDVQAHAa 163
Cdd:PTZ00144 127 AAPAAAAAAKAEKTTPEKPKAAAPTPEP-------PAASKPTPPAAAKPPE------------PAPAAKPPPTPVARAD- 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 164 apkeapaapkspapvaktefeKPVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMSAIMELRKERKDAFEKKHDVRL 243
Cdd:PTZ00144 187 ---------------------PRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 244 GFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDNKLS 323
Cdd:PTZ00144 246 GFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLT 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 324 LKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIDNErMENRPMMYIALSYDHRIVDGKEAVSFLVAV 403
Cdd:PTZ00144 326 LEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNE-IVIRPIMYLALTYDHRLIDGRDAVTFLKKI 404

                        410
                 ....*....|...
gi 446492073 404 KDMLEDPKSLLLE 416
Cdd:PTZ00144 405 KDLIEDPARMLLD 417
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 1-416 1.19e-150

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 433.06  E-value: 1.19e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   1 MIEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGA 80
Cdd:PRK11856   2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  81 PVAVSTPAPVAEQPKQETTEAPKAAAPNAEQTATLQGLPNTNRPIASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQA 160
Cdd:PRK11856  82 AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 161 HAAAPKEAPAAPKSPAPVAKTEFEKPVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMSAIMELRKErkdafEKKHD 240
Cdd:PRK11856 162 AAAAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQ-----LKAIG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 241 VRLGFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDN 320
Cdd:PRK11856 237 VKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREG 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 321 KLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIDNErMENRPMMYIALSYDHRIVDGKEAVSFL 400
Cdd:PRK11856 317 KLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE-IVVRKVMPLSLSFDHRVIDGADAARFL 395

                        410
                 ....*....|....*.
gi 446492073 401 VAVKDMLEDPKSLLLE 416
Cdd:PRK11856 396 KALKELLENPALLLLE 411
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 2-415 1.52e-126

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 376.47  E-value: 1.52e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   2 IEIKVPELAEsITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILD-ANGA 80
Cdd:PRK11855 120 VEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEvAAAA 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  81 PVAVSTPAPVAEQPKQETTEAP-KAAAPNAEQTATLQGLPNTNRPIASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQ 159
Cdd:PRK11855 199 PAAAAAPAAAAPAAAAAAAPAPaPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQ 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 160 AHAAAPKEAPAAPKSPAPVA-----------KTEFEK--PVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMSAIME 226
Cdd:PRK11855 279 AFVKGAMSAAAAAAAAAAAAgggglgllpwpKVDFSKfgEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEA 358

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 227 LRKERKDAFEKKhDVRLGFMSFFTKAVVAALKQFPLLNAEI--QGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFA 304
Cdd:PRK11855 359 LRKQLKKEAEKA-GVKLTMLPFFIKAVVAALKEFPVFNASLdeDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLL 437

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 305 EIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAiDNERMENRPMMYIAL 384
Cdd:PRK11855 438 EIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVW-DGKEFVPRLMLPLSL 516

                        410       420       430
                 ....*....|....*....|....*....|.
gi 446492073 385 SYDHRIVDGKEAVSFLVAVKDMLEDPKSLLL 415
Cdd:PRK11855 517 SYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 3-415 4.57e-112

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 341.98  E-value: 4.57e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   3 EIKVPELAesITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL-DANGAP 81
Cdd:PRK11854 208 DVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFeVEGAAP 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  82 VAVSTPAPVAEQPKQETTEAPKAAAPNAEQTATLQGLPNTNRPIASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQAH 161
Cdd:PRK11854 286 AAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAY 365

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 162 AAAPKEAPAAPKSPAPVA----------KTEFEK--PVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMSAIMELRK 229
Cdd:PRK11854 366 VKDAVKRAEAAPAAAAAGgggpgllpwpKVDFSKfgEIEEVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRK 445

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 230 ERKD-AFEKKHDVRLGFMSFFTKAVVAALKQFPLLNAEI--QGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEI 306
Cdd:PRK11854 446 QQNAeAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIEL 525

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 307 ESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAiDNERMENRPMMYIALSY 386
Cdd:PRK11854 526 SRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVW-NGKEFAPRLMLPLSLSY 604

                        410       420
                 ....*....|....*....|....*....
gi 446492073 387 DHRIVDGKEAVSFLVAVKDMLEDPKSLLL 415
Cdd:PRK11854 605 DHRVIDGADGARFITIINDRLSDIRRLVL 633
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 2-416 2.04e-104

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 317.08  E-value: 2.04e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   2 IEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGAp 81
Cdd:PLN02226  92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED- 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  82 vAVSTPAPVAEQPKqetTEAPKAAAP-NAEQTATLQGLPNTNRPIAS---PAARKMARElgidlndvrstdplGRVRPHD 157
Cdd:PLN02226 171 -AASQVTPSQKIPE---TTDPKPSPPaEDKQKPKVESAPVAEKPKAPsspPPPKQSAKE--------------PQLPPKE 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 158 VQahaaapkeapaapkspapvaktefekpvERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMSAIMELRKERKDAFEK 237
Cdd:PLN02226 233 RE----------------------------RRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYE 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 238 KHDVRLGFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKA 317
Cdd:PLN02226 285 KHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKA 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 318 RDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIDNERMEnRPMMYIALSYDHRIVDGKEAV 397
Cdd:PLN02226 365 NEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVP-RPMMYVALTYDHRLIDGREAV 443

                        410
                 ....*....|....*....
gi 446492073 398 SFLVAVKDMLEDPKSLLLE 416
Cdd:PLN02226 444 YFLRRVKDVVEDPQRLLLD 462
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 3-409 8.42e-98

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: 303.47  E-value: 8.42e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073    3 EIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL-DANGAP 81
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgDANAAP 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   82 VAVSTP-------APVAEQP----------KQETTEAPKAAAPnAEQTATLQGLPNTNRPIASPAARKMARELGIDLNDV 144
Cdd:TIGR02927 208 AEPAEEeapapseAGSEPAPdpaaraphaaPDPPAPAPAPAKT-AAPAAAAPVSSGDSGPYVTPLVRKLAKDKGVDLSTV 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  145 RSTDPLGRVRPHDV----QAHAAAPKEAPAAPKSPAPVAKTEFEKPVE---------RVKMSRRRQTIAKRLVEVQQTSA 211
Cdd:TIGR02927 287 KGTGVGGRIRKQDVlaaaKAAEEARAAAAAPAAAAAPAAPAAAAKPAEpdtaklrgtTQKMNRIRQITADKTIESLQTSA 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  212 MLTTFNEVDMSAIMELRKERKDAFEKKHDVRLGFMSFFTKAVVAALKQFPLLNAEIQGD--ELIIKKFYDIGIAVAAPDG 289
Cdd:TIGR02927 367 QLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAEtkEVTYHDVEHVGIAVDTPRG 446

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  290 LVVPVVRDANQLNFAEIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAI 369
Cdd:TIGR02927 447 LLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVI 526

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 446492073  370 ----DNERMENRPMMYIALSYDHRIVDGKEAVSFLVAVKDMLED 409
Cdd:TIGR02927 527 kdedGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 203-414 3.23e-92

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


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 276.73  E-value: 3.23e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  203 LVEVQQTSAMLTTFNEVDMSAIMELRKERKDAFEKKHDvRLGFMSFFTKAVVAALKQFPLLNAEIQGD--ELIIKKFYDI 280
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  281 GIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMH 360
Cdd:pfam00198  80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446492073  361 KIQVRPVAIDNErMENRPMMYIALSYDHRIVDGKEAVSFLVAVKDMLEDPKSLL 414
Cdd:pfam00198 160 RIRKRPVVVDGE-IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 2-415 9.13e-92

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: 287.16  E-value: 9.13e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073    2 IEIKVPELAeSITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGA- 80
Cdd:TIGR01348 117 QEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSt 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   81 PVAVSTPA---PVAEQPKQETTEAPKAAAPNAEQTATLQGLPNTNR---PIASPAARKMARELGIDLNDVRSTDPLGRVR 154
Cdd:TIGR01348 196 PATAPAPAsaqPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQNPakvDHAAPAVRRLAREFGVDLSAVKGTGIKGRIL 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  155 PHDVQAHAAAPKEAPAAPKSPAPVA--------KTEFEK--PVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMSAI 224
Cdd:TIGR01348 276 REDVQRFVKEPSVRAQAAAASAAGGapgalpwpNVDFSKfgEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEM 355

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  225 MELRKERKDAFEKKhDVRLGFMSFFTKAVVAALKQFPLLNAEIQ--GDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLN 302
Cdd:TIGR01348 356 EAFRKQQNAAVEKE-GVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKG 434

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  303 FAEIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAiDNERMENRPMMYI 382
Cdd:TIGR01348 435 ITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVW-NGKEFEPRLMLPL 513

                         410       420       430
                  ....*....|....*....|....*....|...
gi 446492073  383 ALSYDHRIVDGKEAVSFLVAVKDMLEDPKSLLL 415
Cdd:TIGR01348 514 SLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 11-415 1.47e-64

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 212.66  E-value: 1.47e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  11 ESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGAPVAVstpaPV 90
Cdd:PLN02528   8 EGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLR----SD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  91 AEQPKQETTEAPKAAAPNAEQTATLQGLpntnrpiASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQAHAAAPKEAPA 170
Cdd:PLN02528  84 SLLLPTDSSNIVSLAESDERGSNLSGVL-------STPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVVKD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 171 APKSPAPVAKTEFEKPVE---RVKMSRRRQTIAKR-----LVEVQQTSAMLTTF---NEVDMSAIMELRKERKDAfEKKH 239
Cdd:PLN02528 157 SSSAEEATIAEQEEFSTSvstPTEQSYEDKTIPLRgfqraMVKTMTAAAKVPHFhyvEEINVDALVELKASFQEN-NTDP 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 240 DVRLGFMSFFTKAVVAALKQFPLLNAEIQGD--ELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKA 317
Cdd:PLN02528 236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 318 RDNKLSLKELQGGTFTITN----GGVFGSlmstPILNSPQVGILGMHKIQVRPVAIDNERMENRPMMYIALSYDHRIVDG 393
Cdd:PLN02528 316 AENKLNPEDITGGTITLSNigaiGGKFGS----PVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDG 391

                        410       420
                 ....*....|....*....|..
gi 446492073 394 KEAVSFLVAVKDMLEDPKSLLL 415
Cdd:PLN02528 392 ATVARFCNEWKSYVEKPELLML 413
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 3-415 5.08e-58

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 198.54  E-value: 5.08e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   3 EIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLL-GEPGDTVEVGATIAI------- 74
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVkGDGAKEIKVGEVIAItveeeed 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  75 -----------LDANGAPVAVSTPAPVAEQPKQETTEAPKAAAPNAEQTATlqglpNTNRPIASPAARKMARELGIDLND 143
Cdd:PLN02744 194 igkfkdykpssSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPS-----SGDRIFASPLARKLAEDNNVPLSS 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 144 VRSTDPLGRVRPHDVQAHAAAPKEAPAAPKSPAPVAKTefekpVERVKM--SRRRQTIAKRLVEVQQT--SAMLTTFNEV 219
Cdd:PLN02744 269 IKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPA-----LDYTDIpnTQIRKVTASRLLQSKQTipHYYLTVDTRV 343

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 220 DmsAIMELRKERKDAFEKKHDVRLGFMSFFTKAVVAALKQFPLLNAEIQGDelIIKKFYDIGIAVA--APDGLVVPVVRD 297
Cdd:PLN02744 344 D--KLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDD--YIRQYHNVNINVAvqTENGLYVPVVKD 419

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 298 ANQLNFAEIESEIRELGKKARDNKLSLKELQGGTFTITN-GGVFGSLMSTPILNSPQVGILGMHKIQVRPV-AIDNERME 375
Cdd:PLN02744 420 ADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRVIpGSGPDQYN 499

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 446492073 376 NRPMMYIALSYDHRIVDGKEAVSFLVAVKDMLEDPKSLLL 415
Cdd:PLN02744 500 FASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 125-413 1.46e-53

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 180.37  E-value: 1.46e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 125 IASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQAHAAAPKEAPAAPKSPAPVAKTEFEK---PV--------ERVKMS 193
Cdd:PRK11857   3 LATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKtaaPAaappklegKREKVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 194 RRRQTIAKRLVEVQQTSAMLTTFNEVDMSAIMELRKERKDAFEKKHDVRLGFMSFFTKAVVAALKQFPLLNAEI--QGDE 271
Cdd:PRK11857  83 PIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYdeATSE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 272 LIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNS 351
Cdd:PRK11857 163 LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINY 242

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446492073 352 PQVGILGMHKIQVRPVAIDNERMENRpMMYIALSYDHRIVDGKEAVSFLVAVKDMLEDPKSL 413
Cdd:PRK11857 243 PELAIAGVGAIIDKAIVKNGQIVAGK-VMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 127-415 1.52e-42

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 152.75  E-value: 1.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 127 SPAARKMARELGIDLNDVRSTDPLGRVRPHDV-------QAHAAAPKEAPAAPKSPAPVAKTEFEKpVERVKMSRRRQTI 199
Cdd:PRK14843  52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVlallpenIENDSIKSPAQIEKVEEVPDNVTPYGE-IERIPMTPMRKVI 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 200 AKRLVEVQQTSAMLTTFNEVDMSAIMELRKERKDAFEKKHDVRLGFMSFFTKAVVAALKQFPLLNAEI--QGDELIIKKF 277
Cdd:PRK14843 131 AQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLteDGKTIITHNY 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073 278 YDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGIL 357
Cdd:PRK14843 211 VNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAIL 290

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446492073 358 GMHKIQVRPVAIDNErMENRPMMYIALSYDHRIVDGKEAVSFLVAVKDMLEDPKSLLL 415
Cdd:PRK14843 291 GVSSTIEKPVVVNGE-IVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 1-75 1.64e-27

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: 103.99  E-value: 1.64e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446492073   1 MIEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:COG0508    2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 2-75 2.01e-27

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: 103.64  E-value: 2.01e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446492073   2 IEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:cd06849    1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 1-114 3.94e-18

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 86.12  E-value: 3.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   1 MIEIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPG-DTVEVGATIAILDANG 79
Cdd:PRK11892   2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLEEG 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446492073  80 --APVAVSTPAPVAEQPKQETTEAPKAAAPNAEQTAT 114
Cdd:PRK11892  82 esASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPA 118
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 3-117 4.11e-18

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 85.38  E-value: 4.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073   3 EIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGAP- 81
Cdd:PRK14875   4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSd 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446492073  82 ---VAVSTP--APVAEQPKQETTEAPkaaapnAEQTATLQG 117
Cdd:PRK14875  84 aeiDAFIAPfaRRFAPEGIDEEDAGP------APRKARIGG 118
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 3-75 2.50e-17

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: 76.10  E-value: 2.50e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446492073    3 EIKVPELAESITEGtISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:pfam00364   2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 252-400 2.56e-17

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 84.56  E-value: 2.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  252 AVVAALKQFPLLN---AEIQGDELIIK-KFYDIGIA--VAAPDG---LVVPVVRDANQLNFAEIESEIRELGKKARDNKL 322
Cdd:PRK12270  179 ALVQALKAFPNMNrhyAEVDGKPTLVTpAHVNLGLAidLPKKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  323 SLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHkiqvrpvAID--------NERMENR----PMMYIALSYDHRI 390
Cdd:PRK12270  259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVG-------AMEypaefqgaSEERLAElgisKVMTLTSTYDHRI 331

                         170
                  ....*....|
gi 446492073  391 VDGKEAVSFL 400
Cdd:PRK12270  332 IQGAESGEFL 341
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 124-159 4.79e-12

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


Pssm-ID: 460710 [Multi-domain]  Cd Length: 36  Bit Score: 60.01  E-value: 4.79e-12
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 446492073  124 PIASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQ 159
Cdd:pfam02817   1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 3-69 5.84e-11

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: 58.22  E-value: 5.84e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446492073   3 EIKVPELAESITEGTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVG 69
Cdd:cd06663    1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGD 67
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 16-75 2.18e-10

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: 56.27  E-value: 2.18e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:cd06850    8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 22-76 3.62e-07

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: 49.12  E-value: 3.62e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446492073  22 LINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILD 76
Cdd:COG0511   82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 16-75 5.64e-07

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 51.77  E-value: 5.64e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
PRK05889 PRK05889
biotin/lipoyl-binding carrier protein;
17-76 1.35e-05

biotin/lipoyl-binding carrier protein;


Pssm-ID: 180306 [Multi-domain]  Cd Length: 71  Bit Score: 42.87  E-value: 1.35e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  17 TISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILD 76
Cdd:PRK05889  12 SVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVIS 71
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
16-75 2.21e-05

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 46.46  E-value: 2.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492073  16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAIL 75
Cdd:PRK14040 533 GNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 16-76 2.63e-05

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 42.08  E-value: 2.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446492073  16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILD 76
Cdd:PRK08225  10 GNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 16-69 1.80e-04

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 43.91  E-value: 1.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446492073   16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVG 69
Cdd:COG1038  1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAG 1138
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 23-87 1.83e-03

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 39.82  E-value: 1.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446492073  23 INVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEpgdtvevgatiaildaNGAPVAVSTP 87
Cdd:PLN02983 220 VKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAE----------------DGKPVSVDTP 268
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 16-69 6.43e-03

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 36.71  E-value: 6.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446492073  16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVG 69
Cdd:PRK06549  70 GTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPG 123
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 16-72 8.84e-03

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 38.16  E-value: 8.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446492073  16 GTISQWLINVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATI 72
Cdd:PRK14042 534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVL 590
 
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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