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Conserved domains on  [gi|2511703518|ref|XP_056348382|]
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pyruvate dehydrogenase protein X component, mitochondrial isoform X1 [Oenanthe melanoleuca]

Protein Classification

pyruvate dehydrogenase complex E2/E3BP family protein( domain architecture ID 1000906)

2-oxoacid dehydrogenase family protein similar to pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase-binding protein (E3BP)

CATH:  2.40.50.100
Gene Ontology:  GO:0045254

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PDHac_trf_mito super family cl36877
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 53-496 2.43e-140

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]


The actual alignment was detected with superfamily member TIGR01349:

Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 410.72  E-value: 2.43e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  53 KVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKNVRLGSLIGLLVEEGQD 132
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 133 ---WKQVEIPADAGVPSSVAPPAPAPAPAAPSVSAPPKLQHQP------------GTMQVRLSPAARSILETHGLDPSNI 197
Cdd:TIGR01349  81 vadAFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPepsspaplsdkeSGDRIFASPLAKKLAKEKGIDLSAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 198 TPTGPRGIFTKEDALKLLQEKQKgkpselkpvvspapaavPSPSQATAVTSYPRPAIPPVSTpgqpaalGTFTEIPASNI 277
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPA-----------------SANQQAAATTPATYPAAAPVST-------GSYEDVPLSNI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 278 RRVIAKRLTESKTTIPHAYAAADCVIDAVLKLRKEL---AKDDIKVSVNDFIIKATAVTLKQMPDVNVTWDGEACRRLQS 354
Cdd:TIGR01349 217 RKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKN 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 355 IDISIAVATDRGLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACIL 434
Cdd:TIGR01349 297 VDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACIL 376

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2511703518 435 AVGRArpELRIVEDEEGNEKLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLAL 496
Cdd:TIGR01349 377 AVGAV--EDVAVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 53-496 2.43e-140

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: 410.72  E-value: 2.43e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  53 KVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKNVRLGSLIGLLVEEGQD 132
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 133 ---WKQVEIPADAGVPSSVAPPAPAPAPAAPSVSAPPKLQHQP------------GTMQVRLSPAARSILETHGLDPSNI 197
Cdd:TIGR01349  81 vadAFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPepsspaplsdkeSGDRIFASPLAKKLAKEKGIDLSAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 198 TPTGPRGIFTKEDALKLLQEKQKgkpselkpvvspapaavPSPSQATAVTSYPRPAIPPVSTpgqpaalGTFTEIPASNI 277
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPA-----------------SANQQAAATTPATYPAAAPVST-------GSYEDVPLSNI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 278 RRVIAKRLTESKTTIPHAYAAADCVIDAVLKLRKEL---AKDDIKVSVNDFIIKATAVTLKQMPDVNVTWDGEACRRLQS 354
Cdd:TIGR01349 217 RKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKN 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 355 IDISIAVATDRGLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACIL 434
Cdd:TIGR01349 297 VDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACIL 376

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2511703518 435 AVGRArpELRIVEDEEGNEKLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLAL 496
Cdd:TIGR01349 377 AVGAV--EDVAVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 52-497 1.15e-134

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 395.31  E-value: 1.15e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  52 IKVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnVRLGSLIGLLVEEGQ 131
Cdd:PRK11856    3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 132 dwKQVEIPADAGVPSSVAPPAPAPAPAAPSVSAPPKLQHQPGTMQVRLSPAARSILETHGLDPSNITPTGPRGIFTKEDA 211
Cdd:PRK11856   82 --AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 212 LKLLQEkqkgkpselkpvvSPAPAAVPSPSQATAVTSYPRPAippvstpgqpaalgtfTEIPASNIRRVIAKRLTESKTT 291
Cdd:PRK11856  160 EAAAAA-------------AAPAAAAAAAAAAAPPAAAAEGE----------------ERVPLSGMRKAIAKRMVESKRE 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 292 IPHAYAAADCVIDAVLKLRKELAKDDIKVSVNDFIIKATAVTLKQMPDVNVTWDGEACRRLQSIDISIAVATDRGLITPI 371
Cdd:PRK11856  211 IPHFTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPV 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 372 IKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACILAVGRARPELRIVEDEeg 451
Cdd:PRK11856  291 IRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE-- 368

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 2511703518 452 nekLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLALN 497
Cdd:PRK11856  369 ---IVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 285-494 4.34e-79

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: 245.53  E-value: 4.34e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 285 LTESKTTIPHAYAAADCVIDAVLKLRKEL----AKDDIKVSVNDFIIKATAVTLKQMPDVNVTWDGEAC--RRLQSIDIS 358
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGeiVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 359 IAVATDRGLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACILAVGR 438
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2511703518 439 ARPELRIVEDEegnekLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRL 494
Cdd:pfam00198 161 IRKRPVVVDGE-----IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 52-126 4.00e-29

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: 109.42  E-value: 4.00e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2511703518  52 IKVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnVRLGSLIGLL 126
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 52-127 1.66e-26

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


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 102.07  E-value: 1.66e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2511703518  52 IKVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnVRLGSLIGLLV 127
Cdd:COG0508     3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 53-496 2.43e-140

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: 410.72  E-value: 2.43e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  53 KVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKNVRLGSLIGLLVEEGQD 132
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 133 ---WKQVEIPADAGVPSSVAPPAPAPAPAAPSVSAPPKLQHQP------------GTMQVRLSPAARSILETHGLDPSNI 197
Cdd:TIGR01349  81 vadAFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPepsspaplsdkeSGDRIFASPLAKKLAKEKGIDLSAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 198 TPTGPRGIFTKEDALKLLQEKQKgkpselkpvvspapaavPSPSQATAVTSYPRPAIPPVSTpgqpaalGTFTEIPASNI 277
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPA-----------------SANQQAAATTPATYPAAAPVST-------GSYEDVPLSNI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 278 RRVIAKRLTESKTTIPHAYAAADCVIDAVLKLRKEL---AKDDIKVSVNDFIIKATAVTLKQMPDVNVTWDGEACRRLQS 354
Cdd:TIGR01349 217 RKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKN 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 355 IDISIAVATDRGLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACIL 434
Cdd:TIGR01349 297 VDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACIL 376

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2511703518 435 AVGRArpELRIVEDEEGNEKLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLAL 496
Cdd:TIGR01349 377 AVGAV--EDVAVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 52-497 1.15e-134

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 395.31  E-value: 1.15e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  52 IKVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnVRLGSLIGLLVEEGQ 131
Cdd:PRK11856    3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 132 dwKQVEIPADAGVPSSVAPPAPAPAPAAPSVSAPPKLQHQPGTMQVRLSPAARSILETHGLDPSNITPTGPRGIFTKEDA 211
Cdd:PRK11856   82 --AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 212 LKLLQEkqkgkpselkpvvSPAPAAVPSPSQATAVTSYPRPAippvstpgqpaalgtfTEIPASNIRRVIAKRLTESKTT 291
Cdd:PRK11856  160 EAAAAA-------------AAPAAAAAAAAAAAPPAAAAEGE----------------ERVPLSGMRKAIAKRMVESKRE 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 292 IPHAYAAADCVIDAVLKLRKELAKDDIKVSVNDFIIKATAVTLKQMPDVNVTWDGEACRRLQSIDISIAVATDRGLITPI 371
Cdd:PRK11856  211 IPHFTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPV 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 372 IKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACILAVGRARPELRIVEDEeg 451
Cdd:PRK11856  291 IRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGE-- 368

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 2511703518 452 nekLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLALN 497
Cdd:PRK11856  369 ---IVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 50-496 2.97e-105

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 324.50  E-value: 2.97e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  50 PGIKVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKNVRLGSLIGLLVEE 129
Cdd:PLN02744  111 PHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEE 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 130 GQD---WKQVEIPADAGVPSSVAP-------PAPAPAPAAPSVSAPPKLQHQPGTM-QVRLSPAARSILETHGLDPSNIT 198
Cdd:PLN02744  191 EEDigkFKDYKPSSSAAPAAPKAKpsppppkEEEVEKPASSPEPKASKPSAPPSSGdRIFASPLARKLAEDNNVPLSSIK 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 199 PTGPRGIFTKEDALKLLQEKQKGKPSElKPVVSPAPAAvpspsqatavtsyprpaippvstpgqpaalgTFTEIPASNIR 278
Cdd:PLN02744  271 GTGPDGRIVKADIEDYLASGGKGATAP-PSTDSKAPAL-------------------------------DYTDIPNTQIR 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 279 RVIAKRLTESKTTIPHAYAAADCVIDAVLKLRKEL-----AKDDIKVSVNDFIIKATAVTLKQMPDVNVTWDGEACRRLQ 353
Cdd:PLN02744  319 KVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLnslqeASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYH 398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 354 SIDISIAVATDRGLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNL-GMFGISGFTAVINPPQAC 432
Cdd:PLN02744  399 NVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSA 478

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2511703518 433 ILAVGRArpELRIVEDeEGNEKLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLAL 496
Cdd:PLN02744  479 ILAVGSA--EKRVIPG-SGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 285-494 4.34e-79

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: 245.53  E-value: 4.34e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 285 LTESKTTIPHAYAAADCVIDAVLKLRKEL----AKDDIKVSVNDFIIKATAVTLKQMPDVNVTWDGEAC--RRLQSIDIS 358
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGeiVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 359 IAVATDRGLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACILAVGR 438
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2511703518 439 ARPELRIVEDEegnekLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRL 494
Cdd:pfam00198 161 IRKRPVVVDGE-----IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 65-496 5.46e-72

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 238.18  E-value: 5.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  65 EGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnVRLGSLIGLLVEEGQDWKQVEIPADAGV 144
Cdd:PRK11855  132 EVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVVIEVAAAAPAAAAAPAAAAP 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 145 PSSVAPPAPAPAPAAPSVSAPPKLQHQPGTMQVRLSPAARSILETHGLDPSNITPTGPRGIFTKEDALKLLQEKQKGKPS 224
Cdd:PRK11855  211 AAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAA 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 225 elkpvvsPAPAAVPSPSQATAVTSYPRPAIppvstpgqpAALGTFTEIPASNIRRVIAKRLTESKTTIPHAYAAADCVID 304
Cdd:PRK11855  291 -------AAAAAAAAGGGGLGLLPWPKVDF---------SKFGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADIT 354

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 305 AVLKLRKEL----AKDDIKVSVNDFIIKATAVTLKQMPDVN--VTWDGEACRRLQSIDISIAVATDRGLITPIIKDAAAK 378
Cdd:PRK11855  355 DLEALRKQLkkeaEKAGVKLTMLPFFIKAVVAALKEFPVFNasLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKK 434

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 379 GIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACILAVGRA--RPelrivedEEGNEKLE 456
Cdd:PRK11855  435 SLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSqmKP-------VWDGKEFV 507

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 2511703518 457 QHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLAL 496
Cdd:PRK11855  508 PRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 52-496 7.56e-72

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: 233.47  E-value: 7.56e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  52 IKVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnvrlgsligllVEEGQ 131
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-----------VESGQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 132 DWKQVEIPADAGVPSSVAPPAPAPAPAAPsvsappKLQHQPGTMQVR--LSPAARSILETHGLDPSNITPTGPRGIFTKE 209
Cdd:TIGR01347  70 VLAILEEGNDATAAPPAKSGEEKEETPAA------SAAAAPTAAANRpsLSPAARRLAKEHGIDLSAVPGTGVTGRVTKE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 210 DALKllqekqkgkpselkPVVSPAPAAVPSPSQATAvtsypRPAippvstpgqpAALGTFTEIPASNIRRVIAKRLTESK 289
Cdd:TIGR01347 144 DIIK--------------KTEAPASAQPPAAAAAAA-----APA----------AATRPEERVKMTRLRQRIAERLKEAQ 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 290 TTIPHAYAAADCVIDAVLKLRKE-----LAKDDIKVSVNDFIIKATAVTLKQMPDVNVTWDGEACRRLQSIDISIAVATD 364
Cdd:TIGR01347 195 NSTAMLTTFNEVDMSAVMELRKRykeefEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTD 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 365 RGLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACILAVG--RARPe 442
Cdd:TIGR01347 275 RGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHgiKERP- 353

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2511703518 443 lrIVEdeegNEKLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLAL 496
Cdd:TIGR01347 354 --VAV----NGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
52-497 1.75e-68

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 224.71  E-value: 1.75e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  52 IKVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSkNVRLGSLIGLLVEEGQ 131
Cdd:PRK05704    3 VEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 132 DWKQVEIPADAGVPSSVAPPAPAPApaapsvsappklqhQPGTMQVRLSPAARSILETHGLDPSNITPTGPRGIFTKEDA 211
Cdd:PRK05704   82 AGAAAAAAAAAAAAAAAPAQAQAAA--------------AAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 212 LKllqekqkgkpselkpVVSPAPAAVPSPSQATAvtsyprpaippvstPGQPAALGTFTEI--PASNIRRVIAKRLTESK 289
Cdd:PRK05704  148 LA---------------ALAAAAAAPAAPAAAAP--------------AAAPAPLGARPEErvPMTRLRKTIAERLLEAQ 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 290 ------TTIPHayaaadcvID--AVLKLRKE-----LAKDDIKVSVNDFIIKATAVTLKQMPDVNVTWDGEACRRLQSID 356
Cdd:PRK05704  199 nttamlTTFNE--------VDmtPVMDLRKQykdafEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYD 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 357 ISIAVATDRGLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACILAV 436
Cdd:PRK05704  271 IGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGM 350

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2511703518 437 G--RARPelrIVEdeegNEKLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLALN 497
Cdd:PRK05704  351 HkiKERP---VAV----NGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLLD 406
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 48-496 7.83e-55

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 194.07  E-value: 7.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  48 GTPGIK-VLMPALSPTmeEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnVRLGSLIGLL 126
Cdd:PRK11854  202 AAAGVKdVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMRF 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 127 VEEGQDWKQVEIPADAGVPSSVAPPAPAPAPAAPSVSAPpKLQHQPGTMQVRLSPAARSILETHGLDPSNITPTGPRGIF 206
Cdd:PRK11854  279 EVEGAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEG-KSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRI 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 207 TKEDALKLLqeKQKGKPSELKPVVSPAPAAVPspsqatavtsyPRPAIPPVStpgqPAALGTFTEIPASNIRRVIAKRLT 286
Cdd:PRK11854  358 LKEDVQAYV--KDAVKRAEAAPAAAAAGGGGP-----------GLLPWPKVD----FSKFGEIEEVELGRIQKISGANLH 420

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 287 ESKTTIPHAYAAADCVIDAVLKLRK------ELAKDDIKVSVNDFIIKATAVTLKQMPDVNVTW--DGEACRRLQSIDIS 358
Cdd:PRK11854  421 RNWVMIPHVTQFDKADITELEAFRKqqnaeaEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIG 500

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 359 IAVATDRGLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACILAVGR 438
Cdd:PRK11854  501 IAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSK 580

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2511703518 439 ArpelrIVEDEEGNEKLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLAL 496
Cdd:PRK11854  581 S-----AMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 52-497 2.66e-50

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 177.18  E-value: 2.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  52 IKVlmPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnvrlgsligllVEEGQ 131
Cdd:PTZ00144   47 IKV--PTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDT-----------VEVGA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 132 DWkqVEIPADAgvpssvappapapapaapsvsappklqhqpgtmqvrlSPAArSILEThgldPSNITPTGPRgiftkeda 211
Cdd:PTZ00144  114 PL--SEIDTGG-------------------------------------APPA-AAPAA----AAAAKAEKTT-------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 212 lkllQEKQKGKPSELKPVVSPAPAAVPSPSQATAvTSYPRPAIPPVSTpgqpaALGTFTEIPASNIRRVIAKRLTESKTT 291
Cdd:PTZ00144  142 ----PEKPKAAAPTPEPPAASKPTPPAAAKPPEP-APAAKPPPTPVAR-----ADPRETRVPMSRMRQRIAERLKASQNT 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 292 IPHAYAAADCVIDAVLKLRKEL-----AKDDIKVSVNDFIIKATAVTLKQMPDVNVTWDGEACRRLQSIDISIAVATDRG 366
Cdd:PTZ00144  212 CAMLTTFNECDMSALMELRKEYkddfqKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTG 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 367 LITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACILAVG--RARPELR 444
Cdd:PTZ00144  292 LVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHaiKKRPVVV 371

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2511703518 445 ivedeeGNEkLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLALN 497
Cdd:PTZ00144  372 ------GNE-IVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLD 417
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 64-496 4.42e-48

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: 174.29  E-value: 4.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  64 EEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnVRLGSLIGLLVEEGQDWKQVEIPADA- 142
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTLSVAGSTPATAPAPASAq 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 143 GVPSSVAPPAPAPAPAAPSVSAPPKLQHQPGTMQ----VRLSPAARSILETHGLDPSNITPTGPRGIFTKEDALKLLQEK 218
Cdd:TIGR01348 207 PAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQNpakvDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEP 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 219 QKGKPSelkpvvSPAPAAVPSPSQatavtsyprPAIPPVSTpgqpAALGTFTEIPASNIRRVIAKRLTESKTTIPHAYAA 298
Cdd:TIGR01348 287 SVRAQA------AAASAAGGAPGA---------LPWPNVDF----SKFGEVEEVDMSRIRKISGANLTRNWTMIPHVTHF 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 299 ADCVIDAVLKLRKELA----KDDIKVSVNDFIIKATAVTLKQMPDVNVTWD--GEACRRLQSIDISIAVATDRGLITPII 372
Cdd:TIGR01348 348 DKADITEMEAFRKQQNaaveKEGVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPVI 427

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 373 KDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACILAVGRArpelrIVEDEEGN 452
Cdd:TIGR01348 428 KDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKS-----GMEPVWNG 502

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 2511703518 453 EKLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLAL 496
Cdd:TIGR01348 503 KEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 65-496 4.43e-48

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 171.06  E-value: 4.43e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  65 EGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnVRLG-SLIGLLVEEGQdwkqveipadaG 143
Cdd:PLN02528   12 ECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGeTLLKIMVEDSQ-----------H 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 144 VPSSVAPPAPAPAPAAPSVSAPPKLQHQPGTMQvrlSPAARSILETHGLDPSNITPTGPRGIFTKEDALKLLQEKQkgkp 223
Cdd:PLN02528   80 LRSDSLLLPTDSSNIVSLAESDERGSNLSGVLS---TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKG---- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 224 selkpvvspapaAVPSPSQATAVTSyPRPAIPPVSTPGQPAALGTFTEIPASNIRRVIAKRLTESkTTIPHAYAAADCVI 303
Cdd:PLN02528  153 ------------VVKDSSSAEEATI-AEQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAA-AKVPHFHYVEEINV 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 304 DAVLKLR---KELAKDD-IKVSVNDFIIKATAVTLKQMPDVNVTWDGEA--CRRLQSIDISIAVATDRGLITPIIKDAAA 377
Cdd:PLN02528  219 DALVELKasfQENNTDPtVKHTFLPFLIKSLSMALSKYPLLNSCFNEETseIRLKGSHNIGVAMATEHGLVVPNIKNVQS 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 378 KGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACILAVGRARPELRIVEDEEgnekLEQ 457
Cdd:PLN02528  299 LSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGN----VYP 374

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2511703518 458 HQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLAL 496
Cdd:PLN02528  375 ASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLML 413
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 48-489 4.05e-46

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: 169.42  E-value: 4.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  48 GTPGIKVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEgSKNVRLGSLIGLL- 126
Cdd:TIGR02927 123 SGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAIIg 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 127 ----VEEGQDWKQVEIPADAGVPSSVAPPAPAPAPAAPSVSAPPK----------LQHQPGTMQVRLSPAARSILETHGL 192
Cdd:TIGR02927 202 danaAPAEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPApaktaapaaaAPVSSGDSGPYVTPLVRKLAKDKGV 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 193 DPSNITPTGPRGIFTKEDALKLLQEKQKGKPSELKPVVSPAPAAvpspsqATAVTSYPRPAIppvstpgqpAALGTFTEi 272
Cdd:TIGR02927 282 DLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAA------PAAAAKPAEPDT---------AKLRGTTQ- 345

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 273 PASNIRRVIAKRLTESKTTIPHAYAAADCVIDAVLKLRKE-----LAKDDIKVSVNDFIIKATAVTLKQMPDVNVTW--D 345
Cdd:TIGR02927 346 KMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARakndfLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYnaE 425

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 346 GEACRRLQSIDISIAVATDRGLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAV 425
Cdd:TIGR02927 426 TKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPI 505

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2511703518 426 INPPQACILAVGRARPELRIVEDEEGNEKLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIE 489
Cdd:TIGR02927 506 LNPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 174-494 3.75e-43

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 156.22  E-value: 3.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 174 TMQVRLSPAARSILETHGLDPSNITPTGPRGIFTKEDALKLLQEKQKGKpselkpvvspapaAVPSPSQATAVTSYPRPA 253
Cdd:PRK14843   46 TNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIEND-------------SIKSPAQIEKVEEVPDNV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 254 IPpvstpgqpaaLGTFTEIPASNIRRVIAKRLTESKTTIPHAYAAADCVIDAVLKLRKE-----LAKDDIKVSVNDFIIK 328
Cdd:PRK14843  113 TP----------YGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKvlepiMEATGKKTTVTDLLSL 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 329 ATAVTLKQMPDVN--VTWDGEACRRLQSIDISIAVATDRGLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQG 406
Cdd:PRK14843  183 AVVKTLMKHPYINasLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQN 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 407 GSFSISNLGMFGISGFTAVINPPQACILAVGRARPELRIVedeegNEKLEQHQLMTVTLSSDGRVVDDELASKFLETLKA 486
Cdd:PRK14843  263 STFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVV-----NGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKE 337


                  ....*...
gi 2511703518 487 NIENPMRL 494
Cdd:PRK14843  338 LIETPISM 345
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 52-497 1.33e-34

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 135.27  E-value: 1.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  52 IKVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnvrlgsligllVEEGQ 131
Cdd:PLN02226   92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDT-----------VEPGT 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 132 DWKQVEIPADAGVPSSVAppapapapaapsvsappklQHQPGTMQVRLSPAArsilethgldpsnitptgprgiftkeda 211
Cdd:PLN02226  161 KVAIISKSEDAASQVTPS-------------------QKIPETTDPKPSPPA---------------------------- 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 212 lkllQEKQKGKPSELKPVVSP-APAAVPSPSQatavtSYPRPAIPPVSTPgqpaalgtfTEIPASNIRRVIAKRLTESKT 290
Cdd:PLN02226  194 ----EDKQKPKVESAPVAEKPkAPSSPPPPKQ-----SAKEPQLPPKERE---------RRVPMTRLRKRVATRLKDSQN 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 291 TIPHAYAAADCVIDAVLKLRKE-----LAKDDIKVSVNDFIIKATAVTLKQMPDVNVTWDGEACRRLQSIDISIAVATDR 365
Cdd:PLN02226  256 TFALLTTFNEVDMTNLMKLRSQykdafYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSK 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 366 GLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQGGSFSISNLGMFGISGFTAVINPPQACILAVGRARPELRI 445
Cdd:PLN02226  336 GLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV 415

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2511703518 446 VedeegNEKLEQHQLMTVTLSSDGRVVDDELASKFLETLKANIENPMRLALN 497
Cdd:PLN02226  416 V-----GGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLD 462
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 52-132 7.63e-34

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 133.12  E-value: 7.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  52 IKVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKNVRLGSLIGLLVEEGQ 131
Cdd:PRK11892    3 IEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGE 82


                  .
gi 2511703518 132 D 132
Cdd:PRK11892   83 S 83
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 176-491 1.13e-31

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 123.75  E-value: 1.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 176 QVRLSPAARSILETHGLDPSNITPTGPRGIFTKEDALKLLQEkqkgkpseLKPVVSPAPAAVPSPSQATAVTSYPRPAip 255
Cdd:PRK11857    1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKS--------LKSAPTPAEAASVSSAQQAAKTAAPAAA-- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 256 pvstpgqPAALGTFTEiPASNIRRVIAKRLTESKTTIphAYAAADCVIDA--VLKLRKELAKD-----DIKVSVNDFIIK 328
Cdd:PRK11857   71 -------PPKLEGKRE-KVAPIRKAIARAMTNSWSNV--AYVNLVNEIDMtkLWDLRKSVKDPvlkteGVKLTFLPFIAK 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 329 ATAVTLKQMPDVNVTWDgEACRRL---QSIDISIAVATDRGLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEYQ 405
Cdd:PRK11857  141 AILIALKEFPIFAAKYD-EATSELvypDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMK 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518 406 GGSFSISNLGMFGISGFTAVINPPQACILAVGRARPELRIVedeegNEKLEQHQLMTVTLSSDGRVVDDELASKFLETLK 485
Cdd:PRK11857  220 GGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVK-----NGQIVAGKVMHLTVAADHRWIDGATIGRFASRVK 294


                  ....*.
gi 2511703518 486 ANIENP 491
Cdd:PRK11857  295 ELLEKP 300
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 52-126 4.00e-29

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: 109.42  E-value: 4.00e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2511703518  52 IKVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnVRLGSLIGLL 126
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 52-127 1.66e-26

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


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 102.07  E-value: 1.66e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2511703518  52 IKVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnVRLGSLIGLLV 127
Cdd:COG0508     3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 53-130 9.95e-17

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 81.53  E-value: 9.95e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2511703518  53 KVLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSkNVRLGSLIGLLVEEG 130
Cdd:PRK14875    4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAE 80
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 54-126 3.90e-16

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 73.02  E-value: 3.90e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2511703518  54 VLMPALSPTMEEGnIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnVRLGSLIGLL 126
Cdd:pfam00364   3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 54-115 1.21e-15

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: 71.70  E-value: 1.21e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2511703518  54 VLMPALSPTMEEGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSK 115
Cdd:cd06663     2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 180-484 3.54e-09

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 59.52  E-value: 3.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  180 SPAARSILETHGLDPSNITPTGPRGIFTKEDALKLLQEKQKGKPSELKPVVSPAPAAVPSPSQATAVTSYPRPAIPPVST 259
Cdd:PRK12270    26 DPSWREFFADYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAA 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  260 PGQPAALGTFTEIPASNIRRVIAKRLTESkTTIPHAYAA----ADCVIDAVLKLRKELAKD-DIKVSVNDFIIKATAVTL 334
Cdd:PRK12270   106 AAPAAAAVEDEVTPLRGAAAAVAKNMDAS-LEVPTATSVravpAKLLIDNRIVINNHLKRTrGGKVSFTHLIGYALVQAL 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  335 KQMPDVNVTW---DGEAcRRLQSIDISIAVATD-------RGLITPIIKDAAAKGIKEIAASAKALAKKARDGKLLPEEY 404
Cdd:PRK12270   185 KAFPNMNRHYaevDGKP-TLVTPAHVNLGLAIDlpkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDF 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2511703518  405 QGGSFSISNLGMFGISGFTAVINPPQACILAVG--------RARPELRIVEDeeGNEKleqhqLMTVTLSSDGRVVDDEL 476
Cdd:PRK12270   264 QGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGameypaefQGASEERLAEL--GISK-----VMTLTSTYDHRIIQGAE 336


                   ....*...
gi 2511703518  477 ASKFLETL 484
Cdd:PRK12270   337 SGEFLRTI 344
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 66-131 6.35e-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: 52.42  E-value: 6.35e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2511703518  66 GNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSKnvrlgsligllVEEGQ 131
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-----------VEAGQ 62
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 177-212 9.25e-08

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: 48.07  E-value: 9.25e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2511703518 177 VRLSPAARSILETHGLDPSNITPTGPRGIFTKEDAL 212
Cdd:pfam02817   1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 58-113 9.45e-05

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 44.83  E-value: 9.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2511703518  58 ALSPTMEeGNIVKWLKKEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEG 113
Cdd:PRK09282  524 AVTSPMP-GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 74-131 2.04e-04

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 41.42  E-value: 2.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2511703518  74 KEGDTVNVGDALCEIETDKAVVTMESSDEGVLAKILVEEGSknvrlgsliglLVEEGQ 131
Cdd:COG0511    84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQ-----------PVEYGQ 130
 
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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