NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1435033876|ref|XP_025783854|]
View 

pyruvate dehydrogenase protein X component, mitochondrial isoform X1 [Puma concolor]

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

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 58-500 8.21e-144

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: 419.97  E-value: 8.21e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  58 KILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEGED 137
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 138 -------------WKHVEIPKDVGPPSPASKPSVPcPSPEPQI---STAVEKEHIPGKLQFRLSPAARNILEKHSLDASQ 201
Cdd:TIGR01349  81 vadafknyklessASPAPKPSEIAPTAPPSAPKPS-PAPQKQSpepSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 202 GTATGPRGIFTKEDALKLVqlketgkitESRPTPAPlatpavplpPQAMATPPYTRPMIPPVSTpgqpnvvGTFTEIPAS 281
Cdd:TIGR01349 160 VAGSGPNGRIVKKDIESFV---------PQSPASAN---------QQAAATTPATYPAAAPVST-------GSYEDVPLS 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 282 NIRRVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSL---VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQL 358
Cdd:TIGR01349 215 NIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRY 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 359 PFIDISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQAC 438
Cdd:TIGR01349 295 KNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQAC 374

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1435033876 439 ILAVGRFRPVLKLTRDEEgnAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 500
Cdd:TIGR01349 375 ILAVGAVEDVAVVDNDEE--KGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 58-500 8.21e-144

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: 419.97  E-value: 8.21e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  58 KILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEGED 137
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 138 -------------WKHVEIPKDVGPPSPASKPSVPcPSPEPQI---STAVEKEHIPGKLQFRLSPAARNILEKHSLDASQ 201
Cdd:TIGR01349  81 vadafknyklessASPAPKPSEIAPTAPPSAPKPS-PAPQKQSpepSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 202 GTATGPRGIFTKEDALKLVqlketgkitESRPTPAPlatpavplpPQAMATPPYTRPMIPPVSTpgqpnvvGTFTEIPAS 281
Cdd:TIGR01349 160 VAGSGPNGRIVKKDIESFV---------PQSPASAN---------QQAAATTPATYPAAAPVST-------GSYEDVPLS 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 282 NIRRVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSL---VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQL 358
Cdd:TIGR01349 215 NIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRY 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 359 PFIDISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQAC 438
Cdd:TIGR01349 295 KNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQAC 374

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1435033876 439 ILAVGRFRPVLKLTRDEEgnAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 500
Cdd:TIGR01349 375 ILAVGAVEDVAVVDNDEE--KGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 56-500 4.12e-138

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 404.17  E-value: 4.12e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEG 135
Cdd:PRK11856    2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 136 EdwKHVEIPKDVGPPSPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTATGPRGIFTKED 215
Cdd:PRK11856   81 E--AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKED 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 216 ALKLVqlketgkiteSRPTPAPLATPAVPLPPQAMATPPYTRpmippvstpgqpnvvgtfteIPASNIRRVIAKRLTESK 295
Cdd:PRK11856  159 VEAAA----------AAAAPAAAAAAAAAAAPPAAAAEGEER--------------------VPLSGMRKAIAKRMVESK 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 296 STVPHAYATTDCDLGAVLKARQSLVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLIT 375
Cdd:PRK11856  209 REIPHFTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIV 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 376 PIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltr 453
Cdd:PRK11856  289 PVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV--- 365

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1435033876 454 deegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 500
Cdd:PRK11856  366 ----DGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 291-500 1.27e-82

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: 254.78  E-value: 1.27e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 291 LTESKSTVPHAYATTDCDLGAVLKARQSL----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDIS 364
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 365 VAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR 444
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1435033876 445 --FRPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 500
Cdd:pfam00198 161 irKRPVVV-------DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 57-131 3.46e-28

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: 106.72  E-value: 3.46e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1435033876  57 IKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLL 131
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 56-132 2.54e-25

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: 98.99  E-value: 2.54e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1435033876  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLV 132
Cdd:COG0508     2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 58-500 8.21e-144

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: 419.97  E-value: 8.21e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  58 KILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEGED 137
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 138 -------------WKHVEIPKDVGPPSPASKPSVPcPSPEPQI---STAVEKEHIPGKLQFRLSPAARNILEKHSLDASQ 201
Cdd:TIGR01349  81 vadafknyklessASPAPKPSEIAPTAPPSAPKPS-PAPQKQSpepSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 202 GTATGPRGIFTKEDALKLVqlketgkitESRPTPAPlatpavplpPQAMATPPYTRPMIPPVSTpgqpnvvGTFTEIPAS 281
Cdd:TIGR01349 160 VAGSGPNGRIVKKDIESFV---------PQSPASAN---------QQAAATTPATYPAAAPVST-------GSYEDVPLS 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 282 NIRRVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSL---VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQL 358
Cdd:TIGR01349 215 NIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRY 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 359 PFIDISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQAC 438
Cdd:TIGR01349 295 KNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQAC 374

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1435033876 439 ILAVGRFRPVLKLTRDEEgnAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 500
Cdd:TIGR01349 375 ILAVGAVEDVAVVDNDEE--KGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 56-500 4.12e-138

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 404.17  E-value: 4.12e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEG 135
Cdd:PRK11856    2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 136 EdwKHVEIPKDVGPPSPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTATGPRGIFTKED 215
Cdd:PRK11856   81 E--AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKED 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 216 ALKLVqlketgkiteSRPTPAPLATPAVPLPPQAMATPPYTRpmippvstpgqpnvvgtfteIPASNIRRVIAKRLTESK 295
Cdd:PRK11856  159 VEAAA----------AAAAPAAAAAAAAAAAPPAAAAEGEER--------------------VPLSGMRKAIAKRMVESK 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 296 STVPHAYATTDCDLGAVLKARQSLVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLIT 375
Cdd:PRK11856  209 REIPHFTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIV 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 376 PIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltr 453
Cdd:PRK11856  289 PVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV--- 365

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1435033876 454 deegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 500
Cdd:PRK11856  366 ----DGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 58-497 3.54e-113

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 344.91  E-value: 3.54e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  58 KILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEGED 137
Cdd:PLN02744  114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEED 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 138 ---WKHVEIPKDVGPPSPASKPSVPCP----------SPEPQISTAVEKEHiPGKLQFRlSPAARNILEKHSLDASQGTA 204
Cdd:PLN02744  194 igkFKDYKPSSSAAPAAPKAKPSPPPPkeeevekpasSPEPKASKPSAPPS-SGDRIFA-SPLARKLAEDNNVPLSSIKG 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 205 TGPRGIFTKEDALKLVQLKETGkitESRPTPAPLATPAVplppqamatppytrpmippvstpgqpnvvgTFTEIPASNIR 284
Cdd:PLN02744  272 TGPDGRIVKADIEDYLASGGKG---ATAPPSTDSKAPAL------------------------------DYTDIPNTQIR 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 285 RVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSL-----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLP 359
Cdd:PLN02744  319 KVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLnslqeASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYH 398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 360 FIDISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNL-GMFGIDEFTAVINPPQAC 438
Cdd:PLN02744  399 NVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSA 478

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1435033876 439 ILAVG----RFRPvlkltrdEEGNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENP 497
Cdd:PLN02744  479 ILAVGsaekRVIP-------GSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENP 534
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 291-500 1.27e-82

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: 254.78  E-value: 1.27e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 291 LTESKSTVPHAYATTDCDLGAVLKARQSL----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDIS 364
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 365 VAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR 444
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1435033876 445 --FRPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 500
Cdd:pfam00198 161 irKRPVVV-------DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 57-501 5.56e-77

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: 246.95  E-value: 5.56e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  57 IKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnirlgaligllVEEGE 136
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-----------VESGQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 137 DWKHVEIPKDVGPPSPA----SKPSVPCPSPEPQISTAVEKEHipgklqfrLSPAARNILEKHSLDASQGTATGPRGIFT 212
Cdd:TIGR01347  70 VLAILEEGNDATAAPPAksgeEKEETPAASAAAAPTAAANRPS--------LSPAARRLAKEHGIDLSAVPGTGVTGRVT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 213 KEDALKLvqlketgkiTESRPTPAPLATPAVPLPPQAmatppYTRPMippvstpgqpnvvgtfTEIPASNIRRVIAKRLT 292
Cdd:TIGR01347 142 KEDIIKK---------TEAPASAQPPAAAAAAAAPAA-----ATRPE----------------ERVKMTRLRQRIAERLK 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 293 ESKSTVphAYATT--DCDLGAVLKAR-----QSLVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISV 365
Cdd:TIGR01347 192 EAQNST--AMLTTfnEVDMSAVMELRkrykeEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISV 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 366 AVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF 445
Cdd:TIGR01347 270 AVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGI 349

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1435033876 446 --RPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRLA 501
Cdd:TIGR01347 350 keRPVAV-------NGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 70-501 7.64e-75

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 245.89  E-value: 7.64e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  70 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEGEDWKHVEIPKDVGP 149
Cdd:PRK11855  132 EVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVVIEVAAAAPAAAAAPAAAAP 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 150 PSPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKETGKIT 229
Cdd:PRK11855  211 AAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAA 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 230 ESRPTPAPLATPAVPLPPQAMATppytrpmippvstpgqpNVVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATTDCDL 309
Cdd:PRK11855  291 AAAAAAAAGGGGLGLLPWPKVDF-----------------SKFGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADI 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 310 GAVLKARQSL----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGpKQLPF---IDISVAVATDKGLITPIIKDAA 382
Cdd:PRK11855  354 TDLEALRKQLkkeaEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDG-DELTYkkyFNIGFAVDTPNGLVVPVIKDVD 432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 383 AKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVlkltrdeEGNAQ 460
Cdd:PRK11855  433 KKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSqmKPV-------WDGKE 505

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1435033876 461 LQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRLA 501
Cdd:PRK11855  506 FVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
57-500 1.12e-74

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 241.28  E-value: 1.12e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  57 IKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIRLGALIGLLVEEGE 136
Cdd:PRK05704    3 VEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 137 dwkhveipkdVGPPSPASKPSVPCPSPEPQISTAVEKEHIPGKLqfrlSPAARNILEKHSLDASQGTATGPRGIFTKEDA 216
Cdd:PRK05704   82 ----------AGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDAL----SPAARKLAAENGLDASAVKGTGKGGRVTKEDV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 217 LKLVQLKETgkitesrPTPAPLATPAVPLPPQAMATPPYTRPMippvstpgqpnvvgtfteipaSNIRRVIAKRLTESKS 296
Cdd:PRK05704  148 LAALAAAAA-------APAAPAAAAPAAAPAPLGARPEERVPM---------------------TRLRKTIAERLLEAQN 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 297 TVphAYATT--DCDLGAVLKAR-----QSLVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGP--KQlpFIDISVAV 367
Cdd:PRK05704  200 TT--AMLTTfnEVDMTPVMDLRkqykdAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIvyHN--YYDIGIAV 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 368 ATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF-- 445
Cdd:PRK05704  276 GTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIke 355

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1435033876 446 RPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 500
Cdd:PRK05704  356 RPVAV-------NGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERL 403
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 61-500 2.13e-57

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 201.38  E-value: 2.13e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  61 MPSLSPTmeEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEGEDWKH 140
Cdd:PRK11854  211 VPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMRFEVEGAAPAA 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 141 VEIPKDVGPPSPASKPSVPcPSPEPQISTAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLV 220
Cdd:PRK11854  288 APAKQEAAAPAPAAAKAEA-PAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYV 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 221 qlKETGKITESRPTPAPLATPAVPLPPqamatppytrpmIPPVStpgqPNVVGTFTEIPASNIRRVIAKRLTESKSTVPH 300
Cdd:PRK11854  367 --KDAVKRAEAAPAAAAAGGGGPGLLP------------WPKVD----FSKFGEIEEVELGRIQKISGANLHRNWVMIPH 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 301 A--YATTD-CDLGAVLKARQSLV---RDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGpKQL---PFIDISVAVATDK 371
Cdd:PRK11854  429 VtqFDKADiTELEAFRKQQNAEAekrKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDG-QRLtlkKYVNIGIAVDTPN 507

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 372 GLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR--FRPVl 449
Cdd:PRK11854  508 GLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKsaMEPV- 586

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1435033876 450 kltrdeEGNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 500
Cdd:PRK11854  587 ------WNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRL 631
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 69-500 1.16e-54

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: 192.01  E-value: 1.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  69 EEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEGEDWKHVEIPKDVG 148
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTLSVAGSTPATAPAPASAQ 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 149 PP--SPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRL---SPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVqlK 223
Cdd:TIGR01348 207 PAaqSPAATQPEPAAAPAAAKAQAPAPQQAGTQNPAKVdhaAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFV--K 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 224 ETGKITESrpTPAPLATPAvplppqamatppytrPMIPPVstpgqPNV----VGTFTEIPASNIRRVIAKRLTESKSTVP 299
Cdd:TIGR01348 285 EPSVRAQA--AAASAAGGA---------------PGALPW-----PNVdfskFGEVEEVDMSRIRKISGANLTRNWTMIP 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 300 HA--YATTD-CDLGAVLKARQSLVR-DDIKVSVNDFIIKAAAVTLKQMPDVNVSWDgEGPKQL---PFIDISVAVATDKG 372
Cdd:TIGR01348 343 HVthFDKADiTEMEAFRKQQNAAVEkEGVKLTVLHILMKAVAAALKKFPKFNASLD-LGGEQLilkKYVNIGVAVDTPNG 421

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 373 LITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR--FRPVLK 450
Cdd:TIGR01348 422 LLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKsgMEPVWN 501

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1435033876 451 LTrdeegnaQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 500
Cdd:TIGR01348 502 GK-------EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRL 544
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 59-500 1.81e-53

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 185.66  E-value: 1.81e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  59 ILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnirlgaligllVEEGEDW 138
Cdd:PTZ00144   47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDT-----------VEVGAPL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 139 khVEIPKDVGPPS-PASKPSVPCPSPEPQISTAVEKEHIPGKlqfrlspaarnilekhsldasqgtatgprgiftkedal 217
Cdd:PTZ00144  116 --SEIDTGGAPPAaAPAAAAAAKAEKTTPEKPKAAAPTPEPP-------------------------------------- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 218 klvqlketgkiTESRPTPAPLATPAvplppqamATPPYTRPMIPPVSTPGQPNvvgtfTEIPASNIRRVIAKRLTESKST 297
Cdd:PTZ00144  156 -----------AASKPTPPAAAKPP--------EPAPAAKPPPTPVARADPRE-----TRVPMSRMRQRIAERLKASQNT 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 298 vpHAYATT--DCDLGAVLKARQSL-----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATD 370
Cdd:PTZ00144  212 --CAMLTTfnECDMSALMELRKEYkddfqKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATP 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 371 KGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACIL---AVGRfRP 447
Cdd:PTZ00144  290 TGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILgmhAIKK-RP 368

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1435033876 448 VLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 500
Cdd:PTZ00144  369 VVV-------GNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARM 414
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 59-495 1.66e-50

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: 181.36  E-value: 1.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  59 ILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEgSKNIRLGALIGLLveeGEDW 138
Cdd:TIGR02927 129 VKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAII---GDAN 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 139 KHVEIPKDVGPPSPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRLSPAA------------------RNILEKHSLDAS 200
Cdd:TIGR02927 205 AAPAEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAaaapvssgdsgpyvtplvRKLAKDKGVDLS 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 201 QGTATGPRGIFTKEDALKLVQlketgKITESRPTPAPLATPAVPLPPQAMATPPytrpmippvsTPGQPNVVGTFTEipA 280
Cdd:TIGR02927 285 TVKGTGVGGRIRKQDVLAAAK-----AAEEARAAAAAPAAAAAPAAPAAAAKPA----------EPDTAKLRGTTQK--M 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 281 SNIRRVIAKRLTESKSTVPHAYATTDCDLGAVLKARQS-----LVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGp 355
Cdd:TIGR02927 348 NRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARakndfLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAET- 426

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 356 KQLPFID---ISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVI 432
Cdd:TIGR02927 427 KEVTYHDvehVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPIL 506

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1435033876 433 NPPQACILAVGRFRPVLKLTRDEEGNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLE 495
Cdd:TIGR02927 507 NPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 70-500 3.96e-45

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 163.35  E-value: 3.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  70 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLG-ALIGLLVEEGEDwkhvEIPKDVG 148
Cdd:PLN02528   12 ECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGeTLLKIMVEDSQH----LRSDSLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 149 PPSPASKPSVPCPSPEpqistavEKEHIPGKLQfrlSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKEtgki 228
Cdd:PLN02528   87 LPTDSSNIVSLAESDE-------RGSNLSGVLS---TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKG---- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 229 tesrptpaplatpAVPLPPQA-MATPPYTRPMIPPVSTP-GQPNVVGTfteIPASNIRRVIAKRLTESKStVPHAYATTD 306
Cdd:PLN02528  153 -------------VVKDSSSAeEATIAEQEEFSTSVSTPtEQSYEDKT---IPLRGFQRAMVKTMTAAAK-VPHFHYVEE 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 307 CDLGAVLKARQSL----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDISVAVATDKGLITPIIKD 380
Cdd:PLN02528  216 INVDALVELKASFqennTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEirLKGSHNIGVAMATEHGLVVPNIKN 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 381 AAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRpvlKLTR-DEEGNA 459
Cdd:PLN02528  296 VQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQ---KVPRfVDDGNV 372

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1435033876 460 QLQRhqLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 500
Cdd:PLN02528  373 YPAS--IMTVTIGADHRVLDGATVARFCNEWKSYVEKPELL 411
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 181-500 1.75e-41

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 151.60  E-value: 1.75e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 181 QFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVqlketgkitesrptPAPLATPAVPLPPQAMATppytrpmi 260
Cdd:PRK14843   48 VVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL--------------PENIENDSIKSPAQIEKV-------- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 261 ppVSTPGQPNVVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSLVrDDI------KVSVNDFIIK 334
Cdd:PRK14843  106 --EEVPDNVTPYGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVL-EPImeatgkKTTVTDLLSL 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 335 AAAVTLKQMPDVNVSWDGEGPKQLP--FIDISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQG 412
Cdd:PRK14843  183 AVVKTLMKHPYINASLTEDGKTIIThnYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQN 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 413 GSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESF 490
Cdd:PRK14843  263 STFTISNLGMFGVQSFGPIINQPNSAILGVSSTieKPVVV-------NGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDL 335

                         330
                  ....*....|
gi 1435033876 491 KANLENPIRL 500
Cdd:PRK14843  336 KELIETPISM 345
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 44-500 8.85e-41

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 152.60  E-value: 8.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  44 RWLHSTQWLRVDPIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIR 123
Cdd:PLN02226   79 RWVRPFSSESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGD-TVE 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 124 LGALIGLLVEEGEDWKHVEiPKDVGPPSPASKPSVPC-PSPEPQIstavekehipgklqfrlspaarnilekhsldasqg 202
Cdd:PLN02226  158 PGTKVAIISKSEDAASQVT-PSQKIPETTDPKPSPPAeDKQKPKV----------------------------------- 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 203 tatgprgiftkedalklvqlkETGKITESRPTPAPlatpavPLPPQAMATppytRPMIPPVSTPgqpnvvgtfTEIPASN 282
Cdd:PLN02226  202 ---------------------ESAPVAEKPKAPSS------PPPPKQSAK----EPQLPPKERE---------RRVPMTR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 283 IRRVIAKRLTESKSTVPHAYATTDCDLGAVLKARQS-----LVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQ 357
Cdd:PLN02226  242 LRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQykdafYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIY 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 358 LPFIDISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQA 437
Cdd:PLN02226  322 RDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQS 401

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1435033876 438 CILAVGRF--RPVLKltrdeeGNAQLQRhQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 500
Cdd:PLN02226  402 AILGMHSIvsRPMVV------GGSVVPR-PMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRL 459
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 56-170 4.45e-35

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 136.59  E-value: 4.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEG 135
Cdd:PRK11892    2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEG 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1435033876 136 EDWKHVEIPKDVGPPSPASKPSVPCPSPEPQISTA 170
Cdd:PRK11892   82 ESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPA 116
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 185-497 1.10e-34

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 132.22  E-value: 1.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 185 SPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVqlketgKITESRPTPAPLATpaVPLPPQAMATPPytrPMIPPVS 264
Cdd:PRK11857    5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFI------KSLKSAPTPAEAAS--VSSAQQAAKTAA---PAAAPPK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 265 TPGQPNVVGTfteipasnIRRVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSLVRD-----DIKVSVNDFIIKAAAVT 339
Cdd:PRK11857   74 LEGKREKVAP--------IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvlkteGVKLTFLPFIAKAILIA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 340 LKQMPDVNVSWDgEGPKQLPF---IDISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFS 416
Cdd:PRK11857  146 LKEFPIFAAKYD-EATSELVYpdtLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFT 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876 417 ISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANL 494
Cdd:PRK11857  225 ITNYGSVGSLYGVPVINYPELAIAGVGAIidKAIVK-------NGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELL 297


                  ...
gi 1435033876 495 ENP 497
Cdd:PRK11857  298 EKP 300
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 57-131 3.46e-28

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: 106.72  E-value: 3.46e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1435033876  57 IKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLL 131
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 56-132 2.54e-25

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: 98.99  E-value: 2.54e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1435033876  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLV 132
Cdd:COG0508     2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 58-135 5.31e-18

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 85.38  E-value: 5.31e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1435033876  58 KILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIRLGALIGLLVEEG 135
Cdd:PRK14875    4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAE 80
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 59-120 1.89e-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: 70.93  E-value: 1.89e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1435033876  59 ILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK 120
Cdd:cd06663     2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 59-120 3.75e-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: 70.32  E-value: 3.75e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1435033876  59 ILMPSLSPTMEEGnIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK 120
Cdd:pfam00364   3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT 63
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 185-443 7.68e-12

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 67.99  E-value: 7.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  185 SPAARNILEK-HSLDASQGTATGPRGIFTKEDALKLVQLKETGKITESRPTPAPLATPAVPLPPQAMATPPYTRPMIPPV 263
Cdd:PRK12270    26 DPSWREFFADyGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAA 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  264 STPGQPNVVGTFTeiPASNIRRVIAKRLTESKStVPhaYATTDCDLGAVLKARQSLVRDD-------IKVSVNDFIIKAA 336
Cdd:PRK12270   106 AAPAAAAVEDEVT--PLRGAAAAVAKNMDASLE-VP--TATSVRAVPAKLLIDNRIVINNhlkrtrgGKVSFTHLIGYAL 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  337 AVTLKQMPDVNVSWDGEGPKqlPFI----DISVAVATD-------KGLITPIIKDAAAKGIREIADSVKALSKKARDGKL 405
Cdd:PRK12270   181 VQALKAFPNMNRHYAEVDGK--PTLvtpaHVNLGLAIDlpkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1435033876  406 LPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVG 443
Cdd:PRK12270   259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVG 296
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 71-119 5.21e-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: 5.21e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1435033876  71 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGS 119
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGD 56
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 183-217 1.34e-04

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: 39.21  E-value: 1.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1435033876 183 RLSPAARNILEKHSLDASQGTATGPRGIFTKEDAL 217
Cdd:pfam02817   2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
PHA03247 PHA03247
large tegument protein UL36; Provisional
 144-269 2.71e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033876  144 PKDVGPPSPASKPSVPCPSPEP-QISTAVEKEHIPGKlQFRLSPAARnilekhsldASQGTATGPRGIFTKEDALKLVQl 222
Cdd:PHA03247  2824 PAGPLPPPTSAQPTAPPPPPGPpPPSLPLGGSVAPGG-DVRRRPPSR---------SPAAKPAAPARPPVRRLARPAVS- 2892

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1435033876  223 KETGKITESRPTPAPLATPAVPLPPQAMATPPYTRPMIPPVSTPGQP 269
Cdd:PHA03247  2893 RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 71-120 1.49e-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: 1.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1435033876   71 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK 120
Cdd:COG1038   1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ 1134
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 71-118 2.51e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 40.60  E-value: 2.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1435033876  71 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEG 118
Cdd:PRK09282  531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 79-119 8.33e-03

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


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 36.80  E-value: 8.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1435033876  79 KEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGS 119
Cdd:COG0511    84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQ 124
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH