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Conserved domains on  [gi|1847896875|ref|XP_034686362|]
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lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial [Vitis riparia]

Protein Classification

lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex( domain architecture ID 11476929)

lipoamide acyltransferase component (E2) of branched-chain alpha-keto acid dehydrogenase complex that catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2)

CATH:  3.30.559.10
EC:  2.3.1.168
Gene Ontology:  GO:0043754|GO:0016407|GO:0031625|GO:0031405|GO:0009083

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 96-518 0e+00

2-oxoisovalerate dehydrogenase E2 component


:

Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 762.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  96 IPLAQTGEGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKMVVEESQG- 174
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 175 ---SNLTSNAPDDMKSMGaevcdssiqSSDLRNSNTGGVLATPAVRNLAKQYGVDINHILGTGQDGRVLKEDVLTHAVQK 251
Cdd:PLN02528   81 rsdSLLLPTDSSNIVSLA---------ESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 252 GLCKEPSSLSVNSVEhfQGEEKYSHTLAADGWQYEDKTVPIRGFQRAMIKSMTLAAKIPHFHYVEEINCDALVKLKASFQ 331
Cdd:PLN02528  152 GVVKDSSSAEEATIA--EQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 332 EENRDPEVKHTFLPFMIKTLSMALSKYPLLNSCFNEELQEITVKGSHNIGIAMATPHGLVVPNIKRVQSLSILEITKELA 411
Cdd:PLN02528  230 ENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELS 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 412 QLQQLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIAIGRLQKVPQFVDDENMYPASIMTVNIGADHRVL 491
Cdd:PLN02528  310 RLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVL 389

                         410       420
                  ....*....|....*....|....*..
gi 1847896875 492 DGATVARFCNEWKLYIEKPEQLMLHMK 518
Cdd:PLN02528  390 DGATVARFCNEWKSYVEKPELLMLHMR 416
 
Name Accession Description Interval E-value
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 96-518 0e+00

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 762.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  96 IPLAQTGEGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKMVVEESQG- 174
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 175 ---SNLTSNAPDDMKSMGaevcdssiqSSDLRNSNTGGVLATPAVRNLAKQYGVDINHILGTGQDGRVLKEDVLTHAVQK 251
Cdd:PLN02528   81 rsdSLLLPTDSSNIVSLA---------ESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 252 GLCKEPSSLSVNSVEhfQGEEKYSHTLAADGWQYEDKTVPIRGFQRAMIKSMTLAAKIPHFHYVEEINCDALVKLKASFQ 331
Cdd:PLN02528  152 GVVKDSSSAEEATIA--EQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 332 EENRDPEVKHTFLPFMIKTLSMALSKYPLLNSCFNEELQEITVKGSHNIGIAMATPHGLVVPNIKRVQSLSILEITKELA 411
Cdd:PLN02528  230 ENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELS 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 412 QLQQLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIAIGRLQKVPQFVDDENMYPASIMTVNIGADHRVL 491
Cdd:PLN02528  310 RLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVL 389

                         410       420
                  ....*....|....*....|....*..
gi 1847896875 492 DGATVARFCNEWKLYIEKPEQLMLHMK 518
Cdd:PLN02528  390 DGATVARFCNEWKSYVEKPELLMLHMR 416
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 303-514 2.31e-84

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: 259.78  E-value: 2.31e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 303 MTLAA-KIPHFHYVEEINCDALVKLKASFQEENRDPEVKHTFLPFMIKTLSMALSKYPLLNSCFNEELQEITVKGSHNIG 381
Cdd:pfam00198   1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 382 IAMATPHGLVVPNIKRVQSLSILEITKELAQLQQLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIAIGR 461
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1847896875 462 LQKVPQFVDDEnMYPASIMTVNIGADHRVLDGATVARFCNEWKLYIEKPEQLM 514
Cdd:pfam00198 161 IRKRPVVVDGE-IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 87-499 4.57e-61

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: 209.73  E-value: 4.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  87 DLPASGIVSIPLAQTGeGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLK 166
Cdd:TIGR01348 110 AGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILT 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 167 MVVEES-------------QGSNLTSNAPDDMKSMGAEVCDSSI-QSSDLRNSNTGGvLATPAVRNLAKQYGVDINHILG 232
Cdd:TIGR01348 189 LSVAGStpatapapasaqpAAQSPAATQPEPAAAPAAAKAQAPApQQAGTQNPAKVD-HAAPAVRRLAREFGVDLSAVKG 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 233 TGQDGRVLKEDVLTHAvqkglcKEPSslsvnsvehfqGEEKYSHTLAADG------WQYED-------KTVPIRGFQRAM 299
Cdd:TIGR01348 268 TGIKGRILREDVQRFV------KEPS-----------VRAQAAAASAAGGapgalpWPNVDfskfgevEEVDMSRIRKIS 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 300 IKSMTLA-AKIPHFHYVEEINCDALVKLKASFQEENRDPEVKHTFLPFMIKTLSMALSKYPLLNSCFNEELQEITVKGSH 378
Cdd:TIGR01348 331 GANLTRNwTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYV 410

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 379 NIGIAMATPHGLVVPNIKRVQSLSILEITKELAQLQQLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIA 458
Cdd:TIGR01348 411 NIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILG 490

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1847896875 459 IGRLQKVPQFvDDENMYPASIMTVNIGADHRVLDGATVARF 499
Cdd:TIGR01348 491 VSKSGMEPVW-NGKEFEPRLMLPLSLSYDHRVIDGADAARF 530
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 94-167 5.07e-25

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: 98.25  E-value: 5.07e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1847896875  94 VSIPLAQTGEGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKM 167
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 93-168 1.16e-22

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 91.67  E-value: 1.16e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1847896875  93 IVSIPLAQTGEGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKMV 168
Cdd:COG0508     2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
 
Name Accession Description Interval E-value
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 96-518 0e+00

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 762.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  96 IPLAQTGEGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKMVVEESQG- 174
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 175 ---SNLTSNAPDDMKSMGaevcdssiqSSDLRNSNTGGVLATPAVRNLAKQYGVDINHILGTGQDGRVLKEDVLTHAVQK 251
Cdd:PLN02528   81 rsdSLLLPTDSSNIVSLA---------ESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 252 GLCKEPSSLSVNSVEhfQGEEKYSHTLAADGWQYEDKTVPIRGFQRAMIKSMTLAAKIPHFHYVEEINCDALVKLKASFQ 331
Cdd:PLN02528  152 GVVKDSSSAEEATIA--EQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 332 EENRDPEVKHTFLPFMIKTLSMALSKYPLLNSCFNEELQEITVKGSHNIGIAMATPHGLVVPNIKRVQSLSILEITKELA 411
Cdd:PLN02528  230 ENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELS 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 412 QLQQLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIAIGRLQKVPQFVDDENMYPASIMTVNIGADHRVL 491
Cdd:PLN02528  310 RLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVL 389

                         410       420
                  ....*....|....*....|....*..
gi 1847896875 492 DGATVARFCNEWKLYIEKPEQLMLHMK 518
Cdd:PLN02528  390 DGATVARFCNEWKSYVEKPELLMLHMR 416
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 102-516 1.24e-120

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 360.26  E-value: 1.24e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 102 GEGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKMVVEESQG------S 175
Cdd:PRK11856   11 GEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAEaaaaaeA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 176 NLTSNAPDDMKSMGAEVCDSSIQSSDLRNSNTGGVLATPAVRNLAKQYGVDINHILGTGQDGRVLKEDVLTHAVQKGLCK 255
Cdd:PRK11856   91 APEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 256 EPSSLSVNSVEHFQGEEkyshtlaadgwqyeDKTVPIRGFQRAMIKSMTLA-AKIPHFHYVEEINCDALVKLKASFQEEn 334
Cdd:PRK11856  171 AAAAAAAAAPPAAAAEG--------------EERVPLSGMRKAIAKRMVESkREIPHFTLTDEVDVTALLALRKQLKAI- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 335 rdpEVKHTFLPFMIKTLSMALSKYPLLNSCFNEElqEITVKGSHNIGIAMATPHGLVVPNIKRVQSLSILEITKELAQLQ 414
Cdd:PRK11856  236 ---GVKLTVTDFLIKAVALALKKFPELNASWDDD--AIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLA 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 415 QLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIAIGRLQKVPQFVDDEnMYPASIMTVNIGADHRVLDGA 494
Cdd:PRK11856  311 EKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE-IVVRKVMPLSLSFDHRVIDGA 389

                         410       420
                  ....*....|....*....|..
gi 1847896875 495 TVARFCNEWKLYIEKPEQLMLH 516
Cdd:PRK11856  390 DAARFLKALKELLENPALLLLE 411
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 89-515 2.48e-114

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 348.74  E-value: 2.48e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  89 PASGIVSIPLAQTGEgIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKMV 168
Cdd:PRK11855  115 AGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 169 VEESQGSNL-----------TSNAPDDMKSMGAEVCDSSIQSSDLRNsntGGVLATPAVRNLAKQYGVDINHILGTGQDG 237
Cdd:PRK11855  194 VAAAAPAAAaapaaaapaaaAAAAPAPAPAAAAAPAAAAPAAAAAPG---KAPHASPAVRRLARELGVDLSQVKGTGKKG 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 238 RVLKEDVLTHAvqKGLCKEPSSLSVNSVEHFQGEEKYSHTLAADGWQY-EDKTVPIRGFQRAMIKSMTLA-AKIPHFHYV 315
Cdd:PRK11855  271 RITKEDVQAFV--KGAMSAAAAAAAAAAAAGGGGLGLLPWPKVDFSKFgEIETKPLSRIKKISAANLHRSwVTIPHVTQF 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 316 EEINCDALVKLKASFQEENRDPEVKHTFLPFMIKTLSMALSKYPLLNSCFNEELQEITVKGSHNIGIAMATPHGLVVPNI 395
Cdd:PRK11855  349 DEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVI 428

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 396 KRVQSLSILEITKELAQLQQLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIAIGRLQKVPqFVDDENMY 475
Cdd:PRK11855  429 KDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-VWDGKEFV 507

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1847896875 476 PASIMTVNIGADHRVLDGATVARFCNEWKLYIEKPEQLML 515
Cdd:PRK11855  508 PRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 303-514 2.31e-84

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: 259.78  E-value: 2.31e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 303 MTLAA-KIPHFHYVEEINCDALVKLKASFQEENRDPEVKHTFLPFMIKTLSMALSKYPLLNSCFNEELQEITVKGSHNIG 381
Cdd:pfam00198   1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 382 IAMATPHGLVVPNIKRVQSLSILEITKELAQLQQLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIAIGR 461
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1847896875 462 LQKVPQFVDDEnMYPASIMTVNIGADHRVLDGATVARFCNEWKLYIEKPEQLM 514
Cdd:pfam00198 161 IRKRPVVVDGE-IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 104-499 3.68e-66

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 225.27  E-value: 3.68e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 104 GIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKMVVE---------ESQG 174
Cdd:PRK11854  215 GGDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEgaapaaapaKQEA 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 175 SNLTSNAPDDMKSMGAEVCDSSIQSSDLRNSNTggVLATPAVRNLAKQYGVDINHILGTGQDGRVLKEDVLTHAvqKGLC 254
Cdd:PRK11854  295 AAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAY--VHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYV--KDAV 370

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 255 KEPSSLSVNSVEHFQGeekyshtLAADGW-------QYEDKTVPIRGFQRamIKSMTLA---AKIPH---FHYVEEINCD 321
Cdd:PRK11854  371 KRAEAAPAAAAAGGGG-------PGLLPWpkvdfskFGEIEEVELGRIQK--ISGANLHrnwVMIPHvtqFDKADITELE 441

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 322 ALVKLKASFqEENRDPEVKHTFLPFMIKTLSMALSKYPLLNSCFNEELQEITVKGSHNIGIAMATPHGLVVPNIKRVQSL 401
Cdd:PRK11854  442 AFRKQQNAE-AEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKK 520

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 402 SILEITKELAQLQQLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIAIGRLQKVPqfVDD-ENMYPASIM 480
Cdd:PRK11854  521 GIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEP--VWNgKEFAPRLML 598

                         410
                  ....*....|....*....
gi 1847896875 481 TVNIGADHRVLDGATVARF 499
Cdd:PRK11854  599 PLSLSYDHRVIDGADGARF 617
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 87-499 4.57e-61

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: 209.73  E-value: 4.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  87 DLPASGIVSIPLAQTGeGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLK 166
Cdd:TIGR01348 110 AGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILT 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 167 MVVEES-------------QGSNLTSNAPDDMKSMGAEVCDSSI-QSSDLRNSNTGGvLATPAVRNLAKQYGVDINHILG 232
Cdd:TIGR01348 189 LSVAGStpatapapasaqpAAQSPAATQPEPAAAPAAAKAQAPApQQAGTQNPAKVD-HAAPAVRRLAREFGVDLSAVKG 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 233 TGQDGRVLKEDVLTHAvqkglcKEPSslsvnsvehfqGEEKYSHTLAADG------WQYED-------KTVPIRGFQRAM 299
Cdd:TIGR01348 268 TGIKGRILREDVQRFV------KEPS-----------VRAQAAAASAAGGapgalpWPNVDfskfgevEEVDMSRIRKIS 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 300 IKSMTLA-AKIPHFHYVEEINCDALVKLKASFQEENRDPEVKHTFLPFMIKTLSMALSKYPLLNSCFNEELQEITVKGSH 378
Cdd:TIGR01348 331 GANLTRNwTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYV 410

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 379 NIGIAMATPHGLVVPNIKRVQSLSILEITKELAQLQQLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIA 458
Cdd:TIGR01348 411 NIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILG 490

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1847896875 459 IGRLQKVPQFvDDENMYPASIMTVNIGADHRVLDGATVARF 499
Cdd:TIGR01348 491 VSKSGMEPVW-NGKEFEPRLMLPLSLSYDHRVIDGADAARF 530
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 210-513 2.17e-59

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 198.48  E-value: 2.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 210 VLATPAVRNLAKQYGVDINHILGTGQDGRVLKEDVLthAVQKGLCKEPSSLSVNSVEHFQGEEKYSHTLAADGW--QYED 287
Cdd:PRK11857    2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVE--NFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKleGKRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 288 KTVPIRgfqRAMIKSMTLA-AKIPHFHYVEEINCDALVKLKASFQEENRDPE-VKHTFLPFMIKTLSMALSKYPLLNSCF 365
Cdd:PRK11857   80 KVAPIR---KAIARAMTNSwSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEgVKLTFLPFIAKAILIALKEFPIFAAKY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 366 NEELQEITVKGSHNIGIAMATPHGLVVPNIKRVQSLSILEITKELAQLQQLALANNLCPEDISGGTITLSNIGAIGGKFG 445
Cdd:PRK11857  157 DEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYG 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1847896875 446 SPLLNPPEVSIIAIGRLQKVPqFVDDENMYPASIMTVNIGADHRVLDGATVARFCNEWKLYIEKPEQL 513
Cdd:PRK11857  237 VPVINYPELAIAGVGAIIDKA-IVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 110-515 5.83e-59

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: 201.18  E-value: 5.83e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 110 LLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPG-DIVKVGeTLLKMVVEES-------QGSNLTSNA 181
Cdd:TIGR01349  16 LAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVN-KPIAVLVEEKedvadafKNYKLESSA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 182 PDDMKSM----GAEVCDSSIQSSDLRNSNT-------------GGVLATPAVRNLAKQYGVDINHILGTGQDGRVLKEDV 244
Cdd:TIGR01349  95 SPAPKPSeiapTAPPSAPKPSPAPQKQSPEpsspaplsdkesgDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDI 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 245 LTHAVQKglcKEPSSLSVNSVehfqGEEKYSHTLAADGWQYEDktVPIRGFqRAMIKSMTLAAK--IPHFHYVEEINCDA 322
Cdd:TIGR01349 175 ESFVPQS---PASANQQAAAT----TPATYPAAAPVSTGSYED--VPLSNI-RKIIAKRLLESKqtIPHYYVSIECNVDK 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 323 LVKLKASFQEENRDpEVKHTFLPFMIKTLSMALSKYPLLNSCFNEElqeiTVKGSHN--IGIAMATPHGLVVPNIKRVQS 400
Cdd:TIGR01349 245 LLALRKELNAMASE-VYKLSVNDFIIKASALALREVPEANSSWTDN----FIRRYKNvdISVAVATPDGLITPIVRNADA 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 401 LSILEITKELAQLQQLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIAIGRLQKVPqFVDDENMYP---A 477
Cdd:TIGR01349 320 KGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVA-VVDNDEEKGfavA 398

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1847896875 478 SIMTVNIGADHRVLDGATVARFCNEWKLYIEKPEQLML 515
Cdd:TIGR01349 399 SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 94-515 3.96e-51

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: 179.54  E-value: 3.96e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  94 VSIPLAQTGEGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKMVVEESQ 173
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 174 GSNLTSNAPDDMKSMGAEVCDSSIQSSDLRNSntggvlATPAVRNLAKQYGVDINHILGTGQDGRVLKEDVLTHAVQKGL 253
Cdd:TIGR01347  81 TAAPPAKSGEEKEETPAASAAAAPTAAANRPS------LSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPAS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 254 CKEPSSlsvnsvehfqgeekysHTLAADGWQYE--DKTVPI-RGFQRA---MIKSMTLAAKIPHFHyveEINCDALVKLK 327
Cdd:TIGR01347 155 AQPPAA----------------AAAAAAPAAATrpEERVKMtRLRQRIaerLKEAQNSTAMLTTFN---EVDMSAVMELR 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 328 ASFQEE-NRDPEVKHTFLPFMIKTLSMALSKYPLLNSCFNEelQEITVKGSHNIGIAMATPHGLVVPNIKRVQSLSILEI 406
Cdd:TIGR01347 216 KRYKEEfEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDG--DDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADI 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 407 TKELAQLQQLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIAIGRLQKVPQFVDDeNMYPASIMTVNIGA 486
Cdd:TIGR01347 294 EKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNG-QIEIRPMMYLALSY 372

                         410       420
                  ....*....|....*....|....*....
gi 1847896875 487 DHRVLDGATVARFCNEWKLYIEKPEQLML 515
Cdd:TIGR01347 373 DHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 50-515 6.80e-51

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 181.98  E-value: 6.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  50 IVSRYAMASFS--MVNDKLMDLNIPYSIKRSCFSSHAllDLPASGIVSIP-LAQTgegIAECELLKWFVKEGDQVEEFQP 126
Cdd:PLN02744   71 NISRTARKNGSpmTGSGLFKSLSSSQMQSARGFSSSS--DLPPHQEIGMPsLSPT---MTEGNIARWLKKEGDKVSPGEV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 127 LCEVQSDKATIEITSRYKGTVSQIIYVPG--DIvKVGETLLKMVVEESQGSNL------TSNAPDDMKSMGA------EV 192
Cdd:PLN02744  146 LCEVETDKATVEMECMEEGYLAKIVKGDGakEI-KVGEVIAITVEEEEDIGKFkdykpsSSAAPAAPKAKPSppppkeEE 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 193 CDSSIQSSDLRNSNT-------GGVLATPAVRNLAKQYGVDINHILGTGQDGRVLKEDVLTHAVQKGLckepsslsvnsv 265
Cdd:PLN02744  225 VEKPASSPEPKASKPsappssgDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGK------------ 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 266 ehfQGEEKYSHTLAADGWQYEDktvpIRGFQ-RAMIKSMTLAAK--IPHFHYVEEINCDALVKLKA---SFQEENRDPEV 339
Cdd:PLN02744  293 ---GATAPPSTDSKAPALDYTD----IPNTQiRKVTASRLLQSKqtIPHYYLTVDTRVDKLMALRSqlnSLQEASGGKKI 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 340 khTFLPFMIKTLSMALSKYPLLNSCFNEELqeitVKGSHNIGIAMA--TPHGLVVPNIKRVQSLSILEITKELAQLQQLA 417
Cdd:PLN02744  366 --SVNDLVIKAAALALRKVPQCNSSWTDDY----IRQYHNVNINVAvqTENGLYVPVVKDADKKGLSTIAEEVKQLAQKA 439

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 418 LANNLCPEDISGGTITLSNigaIGGKFG----SPLLNPPEVSIIAIGRLQK--VPQFVDDENMYpASIMTVNIGADHRVL 491
Cdd:PLN02744  440 RENSLKPEDYEGGTFTVSN---LGGPFGikqfCAIINPPQSAILAVGSAEKrvIPGSGPDQYNF-ASFMSVTLSCDHRVI 515

                         490       500
                  ....*....|....*....|....
gi 1847896875 492 DGATVARFCNEWKLYIEKPEQLML 515
Cdd:PLN02744  516 DGAIGAEWLKAFKGYIENPESMLL 539
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
102-515 4.02e-44

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 160.77  E-value: 4.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 102 GEGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKMVVEESQGSNLTSNA 181
Cdd:PRK05704   11 PESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAGAAAAAAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 182 PDDMKsmgAEVCDSSIQSSdlrNSNTGGVLATPAVRNLAKQYGVDINHILGTGQDGRVLKEDVLTHAVQKGLCKEPSSLS 261
Cdd:PRK05704   91 AAAAA---AAAPAQAQAAA---AAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 262 VNSVehfqgeekyshTLAADGWQYEdKTVP---IRgfQRA---MIKSMTLAAKIPHFHyveEINCDALVKLKASFQEE-N 334
Cdd:PRK05704  165 APAA-----------APAPLGARPE-ERVPmtrLR--KTIaerLLEAQNTTAMLTTFN---EVDMTPVMDLRKQYKDAfE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 335 RDPEVKHTFLPFMIKTLSMALSKYPLLNScfneELQ--EITVKGSHNIGIAMATPHGLVVPNIKRVQSLSILEITKELAQ 412
Cdd:PRK05704  228 KKHGVKLGFMSFFVKAVVEALKRYPEVNA----SIDgdDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAE 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 413 LQQLALANNLCPEDISGGTITLSNigaiGGKFGS----PLLNPPEVSIIAIGRLQKVPQFVDDE-----NMYPAsimtvn 483
Cdd:PRK05704  304 LAKKARDGKLSIEELTGGTFTITN----GGVFGSlmstPIINPPQSAILGMHKIKERPVAVNGQivirpMMYLA------ 373

                         410       420       430
                  ....*....|....*....|....*....|..
gi 1847896875 484 IGADHRVLDGATVARFCNEWKLYIEKPEQLML 515
Cdd:PRK05704  374 LSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 48-515 4.15e-41

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 152.91  E-value: 4.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  48 QPIVSRYAMaSFSMVNDKLMDLNIPYSIKRSCFSshalldlpasgIVSIPLAQTGEGIAECELLKWFVKEGDQVEEFQPL 127
Cdd:PTZ00144   11 KPLLSSVKG-MFRRFSLRKLQPACSAHFSKSYFS-----------IKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 128 CEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKMVveesqgsnlTSNAPDDMKSMGAEVcdssiqssdlrnsnt 207
Cdd:PTZ00144   79 CIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEID---------TGGAPPAAAPAAAAA--------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 208 ggvlATPAVRNLAKQygvdinhilgtgQDGRVLKEDVLTHavqkglcKEPSSLSVNSVEHFQGEEKYSHTLAADGwqYED 287
Cdd:PTZ00144  135 ----AKAEKTTPEKP------------KAAAPTPEPPAAS-------KPTPPAAAKPPEPAPAAKPPPTPVARAD--PRE 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 288 KTVPI-----RGFQRaMIKSMTLAAKIPHFHyveEINCDALVKLKASFQEE--NRDPeVKHTFLPFMIKTLSMALSKYPL 360
Cdd:PTZ00144  190 TRVPMsrmrqRIAER-LKASQNTCAMLTTFN---ECDMSALMELRKEYKDDfqKKHG-VKLGFMSAFVKASTIALKKMPI 264

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 361 LNSCFNEElqEITVKGSHNIGIAMATPHGLVVPNIKRVQSLSILEITKELAQLQQLALANNLCPEDISGGTITLSNIGAI 440
Cdd:PTZ00144  265 VNAYIDGD--EIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVF 342

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847896875 441 GGKFGSPLLNPPEVSIIAIGRLQKVPQFVDDEnMYPASIMTVNIGADHRVLDGATVARFCNEWKLYIEKPEQLML 515
Cdd:PTZ00144  343 GSLMGTPIINPPQSAILGMHAIKKRPVVVGNE-IVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 94-167 5.07e-25

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: 98.25  E-value: 5.07e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1847896875  94 VSIPLAQTGEGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKM 167
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 93-168 1.16e-22

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 91.67  E-value: 1.16e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1847896875  93 IVSIPLAQTGEGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKMV 168
Cdd:COG0508     2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 212-515 1.68e-22

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 98.82  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 212 ATPAVRNLAKQYGVDINHILGTGQDGRVLKEDVLTHAVQKGLCKEPSSLSV---NSV--EHFQG---------------- 270
Cdd:PRK14843    8 ATPAARKLADDLGINLYDVSGSGANGRVHKEDVETYKDTNVVRISPLAKRIaleHNIawQEIQGtghrgkimkkdvlall 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 271 -EEKYSHTLAADGW-----QYEDKT--------VPIRGFQRAMIKSMT---LAAkiPHFHYVEEINCDALVKLKASFQEE 333
Cdd:PRK14843   88 pENIENDSIKSPAQiekveEVPDNVtpygeierIPMTPMRKVIAQRMVesyLTA--PTFTLNYEVDMTEMLALRKKVLEP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 334 NRDPEVKHTFLPFMIK-TLSMALSKYPLLNSCFNEELQEITVKGSHNIGIAMATPHGLVVPNIKRVQSLSILEITKELAQ 412
Cdd:PRK14843  166 IMEATGKKTTVTDLLSlAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKD 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 413 LQQLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIAIGRLQKVPQFVDDEnMYPASIMTVNIGADHRVLD 492
Cdd:PRK14843  246 VIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGE-IVIRPIMSLGLTIDHRVVD 324

                         330       340
                  ....*....|....*....|...
gi 1847896875 493 GATVARFCNEWKLYIEKPEQLML 515
Cdd:PRK14843  325 GMAGAKFMKDLKELIETPISMLI 347
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 93-515 5.05e-21

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 95.98  E-value: 5.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  93 IVSIPLAQTGEGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKMVVEES 172
Cdd:PLN02226   91 TVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 173 QGSNLTSNapddmksmgaevcDSSIQSSDLRNSNTGGVLATPAVRNlakqygvdinhilgtgqdgrvlkedvlTHAVQKG 252
Cdd:PLN02226  171 AASQVTPS-------------QKIPETTDPKPSPPAEDKQKPKVES---------------------------APVAEKP 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 253 LCKEPSSLSVNSVEHFQGEEKYshtlaadgwqyEDKTVPIRGFQRAMIK----SMTLAAKIPHFHYVEEINcdaLVKLKA 328
Cdd:PLN02226  211 KAPSSPPPPKQSAKEPQLPPKE-----------RERRVPMTRLRKRVATrlkdSQNTFALLTTFNEVDMTN---LMKLRS 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 329 SFQEENRDPE-VKHTFLPFMIKTLSMALSKYPLLNSCFNEElqEITVKGSHNIGIAMATPHGLVVPNIKRVQSLSILEIT 407
Cdd:PLN02226  277 QYKDAFYEKHgVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIE 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 408 KELAQLQQLALANNLCPEDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIAIGRLQKVPQFVDDeNMYPASIMTVNIGAD 487
Cdd:PLN02226  355 KTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGG-SVVPRPMMYVALTYD 433

                         410       420
                  ....*....|....*....|....*...
gi 1847896875 488 HRVLDGATVARFCNEWKLYIEKPEQLML 515
Cdd:PLN02226  434 HRLIDGREAVYFLRRVKDVVEDPQRLLL 461
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 96-167 2.19e-15

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: 70.71  E-value: 2.19e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847896875  96 IPLAQTGEGIAECELlKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKM 167
Cdd:pfam00364   3 IKSPMIGESVREGVV-EWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 210-245 5.14e-14

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: 65.79  E-value: 5.14e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1847896875 210 VLATPAVRNLAKQYGVDINHILGTGQDGRVLKEDVL 245
Cdd:pfam02817   1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 104-175 6.14e-10

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 61.56  E-value: 6.14e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847896875 104 GIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLlkMVVEESQGS 175
Cdd:PRK11854   11 GADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALI--MIFESADGA 80
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 110-167 3.87e-09

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: 52.80  E-value: 3.87e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1847896875 110 LLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKM 167
Cdd:cd06850    10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 277-499 8.57e-08

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 55.28  E-value: 8.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  277 TLAADGWQYEDKTVPIRGFQRAMIKSMTLAAKIPHFHYVEEINCDALVKLKA---SFQEENRDPEVKHTFLP--FMIKtl 351
Cdd:PRK12270   105 AAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVPTATSVRAVPAKLLIDNRIvinNHLKRTRGGKVSFTHLIgyALVQ-- 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  352 smALSKYPLLNSCFNEEL-QEITVKGSH-NIGIA--MATPHG---LVVPNIKRVQSLSILEITKELAQLQQLALANNLCP 424
Cdd:PRK12270   183 --ALKAFPNMNRHYAEVDgKPTLVTPAHvNLGLAidLPKKDGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTA 260

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  425 EDISGGTITLSNIGAIGGKFGSPLLNPPEVSIIAIGRLQkvpqfvddenmYPAS----------------IMTVNIGADH 488
Cdd:PRK12270   261 DDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAME-----------YPAEfqgaseerlaelgiskVMTLTSTYDH 329

                          250
                   ....*....|.
gi 1847896875  489 RVLDGATVARF 499
Cdd:PRK12270   330 RIIQGAESGEF 340
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 114-170 1.70e-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: 50.28  E-value: 1.70e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1847896875 114 FVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLlkMVVE 170
Cdd:COG0511    82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPL--FVIE 136
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 102-244 2.30e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 53.02  E-value: 2.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875 102 GEGIAECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLlkMVVEEsqgsnltsna 181
Cdd:PRK14875   11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL--AVVAD---------- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1847896875 182 pddmksmgAEVCDSSIQssdlrnsntggVLATPAVRNLAkQYGVDINHILGTGQDGRVLKEDV 244
Cdd:PRK14875   79 --------AEVSDAEID-----------AFIAPFARRFA-PEGIDEEDAGPAPRKARIGGRTV 121
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 112-166 1.54e-06

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: 45.90  E-value: 1.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1847896875 112 KWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLK 166
Cdd:cd06663    18 KWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVK 72
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 110-170 6.26e-06

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 48.69  E-value: 6.26e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1847896875 110 LLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLlkMVVE 170
Cdd:PRK09282  533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVL--MEIE 591
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 110-165 1.18e-05

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 44.80  E-value: 1.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1847896875 110 LLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLL 165
Cdd:PRK06549   72 ILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 112-167 1.55e-05

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 42.85  E-value: 1.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1847896875 112 KWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLLKM 167
Cdd:PRK08225   14 KIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEI 69
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 107-171 7.94e-05

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 45.29  E-value: 7.94e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1847896875 107 ECELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPG-DIVKVGeTLLKMVVEE 171
Cdd:PRK11892   16 EGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVN-TPIAVLLEE 80
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 89-167 9.79e-04

putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 39.85  E-value: 9.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896875  89 PASGIVSIPL-AQTGEGIAEC----ELLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGET 163
Cdd:PRK05641   69 PVAPAAPAPApASAGENVVTApmpgKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQP 148


                  ....
gi 1847896875 164 LLKM 167
Cdd:PRK05641  149 LIEL 152
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
94-165 1.38e-03

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 41.45  E-value: 1.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847896875  94 VSIPLAQTgegiaeceLLKWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGTVSQIIYVPGDIVKVGETLL 165
Cdd:PRK14040  527 VTAPLAGN--------IFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 110-167 1.72e-03

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: 41.22  E-value: 1.72e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847896875  110 LLKWFVKEGDQVEEFQPLcevqsdkATIE-------ITSRYKGTVSQIIYVPGDIVKVGETLLKM 167
Cdd:COG1038   1087 VVKVLVKEGDEVKKGDPL-------LTIEamkmettITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
 
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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