NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19923748|ref|NP_001924|]
View 

dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial isoform 1 precursor [Homo sapiens]

Protein Classification

sucB family protein( domain architecture ID 11492245)

sucB family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 71-453 0e+00

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


:

Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 576.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748    71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAA 149
Cdd:TIGR01347   1 IEIKVPELAESITEGTVaEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   150 PAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPT-------------QMPPVPSPSQPPSGKPVSAVKPTVAPPLAEPGAG 216
Cdd:TIGR01347  81 TAAPPAKSGEEKEETPAASAAAAPTAAANRPSLspaarrlakehgiDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   217 --------KGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKAS 288
Cdd:TIGR01347 161 aaaaaapaAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   289 AFALQEQPVVNAVIDDTtkEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGT 368
Cdd:TIGR01347 241 VAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGT 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   369 FTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRV 448
Cdd:TIGR01347 319 FTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRR 398


                  ....*
gi 19923748   449 LLLDL 453
Cdd:TIGR01347 399 LLLDL 403
 
Name Accession Description Interval E-value
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 71-453 0e+00

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


Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 576.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748    71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAA 149
Cdd:TIGR01347   1 IEIKVPELAESITEGTVaEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   150 PAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPT-------------QMPPVPSPSQPPSGKPVSAVKPTVAPPLAEPGAG 216
Cdd:TIGR01347  81 TAAPPAKSGEEKEETPAASAAAAPTAAANRPSLspaarrlakehgiDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   217 --------KGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKAS 288
Cdd:TIGR01347 161 aaaaaapaAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   289 AFALQEQPVVNAVIDDTtkEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGT 368
Cdd:TIGR01347 241 VAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGT 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   369 FTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRV 448
Cdd:TIGR01347 319 FTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRR 398


                  ....*
gi 19923748   449 LLLDL 453
Cdd:TIGR01347 399 LLLDL 403
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 47-453 0e+00

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 526.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   47 KVVINNSVFSVRF--FRTTAVCKD-------DLVTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVP 116
Cdd:PTZ00144  12 PLLSSVKGMFRRFslRKLQPACSAhfsksyfSIKVIKVPTMGDSISEGTVvEWKKKVGDYVKEDEVICIIETDKVSVDIR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  117 SPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQmppvpspsQPPSG 196
Cdd:PTZ00144  92 APASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAAS--------KPTPP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  197 KPVSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNL 276
Cdd:PTZ00144 164 AAAKPPEPAPAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGV 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  277 KLGFMSAFVKASAFALQEQPVVNAVIDdtTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARK 356
Cdd:PTZ00144 244 KLGFMSAFVKASTIALKKMPIVNAYID--GDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARN 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  357 NELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFL 436
Cdd:PTZ00144 322 NKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFL 401

                        410
                 ....*....|....*..
gi 19923748  437 RKIKAAVEDPRVLLLDL 453
Cdd:PTZ00144 402 KKIKDLIEDPARMLLDL 418
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 238-450 7.38e-96

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: 287.13  E-value: 7.38e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   238 LKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNlKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDI 317
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   318 SVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMH 397
Cdd:pfam00198  80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 19923748   398 GIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLL 450
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 71-143 6.34e-24

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 94.39  E-value: 6.34e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923748  71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:cd06849   1 TEIKMPDLGESMTEGTIvEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 71-143 8.78e-23

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


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 91.67  E-value: 8.78e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923748  71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:COG0508   3 IEIKMPDLGESMTEGTIvEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
 
Name Accession Description Interval E-value
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 71-453 0e+00

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


Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 576.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748    71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAA 149
Cdd:TIGR01347   1 IEIKVPELAESITEGTVaEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   150 PAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPT-------------QMPPVPSPSQPPSGKPVSAVKPTVAPPLAEPGAG 216
Cdd:TIGR01347  81 TAAPPAKSGEEKEETPAASAAAAPTAAANRPSLspaarrlakehgiDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   217 --------KGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKAS 288
Cdd:TIGR01347 161 aaaaaapaAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   289 AFALQEQPVVNAVIDDTtkEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGT 368
Cdd:TIGR01347 241 VAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGT 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   369 FTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRV 448
Cdd:TIGR01347 319 FTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRR 398


                  ....*
gi 19923748   449 LLLDL 453
Cdd:TIGR01347 399 LLLDL 403
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 47-453 0e+00

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 526.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   47 KVVINNSVFSVRF--FRTTAVCKD-------DLVTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVP 116
Cdd:PTZ00144  12 PLLSSVKGMFRRFslRKLQPACSAhfsksyfSIKVIKVPTMGDSISEGTVvEWKKKVGDYVKEDEVICIIETDKVSVDIR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  117 SPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQmppvpspsQPPSG 196
Cdd:PTZ00144  92 APASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAAS--------KPTPP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  197 KPVSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNL 276
Cdd:PTZ00144 164 AAAKPPEPAPAAKPPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGV 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  277 KLGFMSAFVKASAFALQEQPVVNAVIDdtTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARK 356
Cdd:PTZ00144 244 KLGFMSAFVKASTIALKKMPIVNAYID--GDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARN 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  357 NELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFL 436
Cdd:PTZ00144 322 NKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFL 401

                        410
                 ....*....|....*..
gi 19923748  437 RKIKAAVEDPRVLLLDL 453
Cdd:PTZ00144 402 KKIKDLIEDPARMLLDL 418
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
73-453 5.89e-171

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 485.88  E-value: 5.89e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   73 VKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRkTGAAPA 151
Cdd:PRK05704   5 IKVPTLPESVTEATIaTWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRID-EGAAAG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  152 KAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPP--------------------SGKPVSAVKPTVAPPLA 211
Cdd:PRK05704  84 AAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENgldasavkgtgkggrvtkedVLAALAAAAAAPAAPAA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  212 EPGAGK----GLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKA 287
Cdd:PRK05704 164 AAPAAApaplGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVKA 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  288 SAFALQEQPVVNAVIDDTtkEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGG 367
Cdd:PRK05704 244 VVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGG 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  368 TFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPR 447
Cdd:PRK05704 322 TFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPE 401


                 ....*.
gi 19923748  448 VLLLDL 453
Cdd:PRK05704 402 RLLLDL 407
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 29-453 3.78e-127

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 376.40  E-value: 3.78e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   29 RSLPGVSLCqgpgypnSRKVVINNSVFSvRFFRTTAVCKDDLVTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIE 107
Cdd:PLN02226  58 LALPGNSGI-------SRSASLVSSTLQ-RWVRPFSSESGDTVEAVVPHMGESITDGTLaTFLKKPGERVQADEAIAQIE 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  108 TDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPV 187
Cdd:PLN02226 130 TDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQVTPSQKIPETTDPKPSPPAEDKQKPKVESAPVAEK 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  188 PSPSQPPSGKPVSAVKPTVAPPlaepgagkglRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHK 267
Cdd:PLN02226 210 PKAPSSPPPPKQSAKEPQLPPK----------ERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYK 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  268 EAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDttKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTI 347
Cdd:PLN02226 280 DAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDG--DDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTI 357

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  348 TELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLI 427
Cdd:PLN02226 358 NGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLI 437

                        410       420
                 ....*....|....*....|....*.
gi 19923748  428 DGREAVTFLRKIKAAVEDPRVLLLDL 453
Cdd:PLN02226 438 DGREAVYFLRRVKDVVEDPQRLLLDI 463
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 71-452 1.44e-105

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 319.43  E-value: 1.44e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   71 VTVKTPAFAESVTEGD-VRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAA 149
Cdd:PRK11856   3 FEFKMPDLGEGMTEGEiVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  150 PAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQP---------------------------------PSG 196
Cdd:PRK11856  83 EAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKaspavrklarelgvdlstvkgsgpggritkedvEAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  197 KPVSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARhkeafLKKHNL 276
Cdd:PRK11856 163 AAAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQ-----LKAIGV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  277 KLGFMSAFVKASAFALQEQPVVNAVIDDTTkeVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARK 356
Cdd:PRK11856 238 KLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKARE 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  357 NELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFL 436
Cdd:PRK11856 316 GKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFL 395

                        410
                 ....*....|....*.
gi 19923748  437 RKIKAAVEDPRVLLLD 452
Cdd:PRK11856 396 KALKELLENPALLLLE 411
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 238-450 7.38e-96

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: 287.13  E-value: 7.38e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   238 LKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNlKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDI 317
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   318 SVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMH 397
Cdd:pfam00198  80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 19923748   398 GIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLL 450
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 71-451 1.31e-87

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 277.47  E-value: 1.31e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   71 VTVKTPAFAEsVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAA 149
Cdd:PRK11855 120 VEVKVPDIGE-ITEVEViEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAA 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  150 PAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPP----------------------------------- 194
Cdd:PRK11855 199 PAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPhaspavrrlarelgvdlsqvkgtgkkgritkedvq 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  195 --SGKPVSAVKPTVAPPLAEPGAGKGL----------RSEHREK-MNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQE 261
Cdd:PRK11855 279 afVKGAMSAAAAAAAAAAAAGGGGLGLlpwpkvdfskFGEIETKpLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEA 358

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  262 MRARHKEAFlKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFA 341
Cdd:PRK11855 359 LRKQLKKEA-EKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLL 437

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  342 DIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALT 421
Cdd:PRK11855 438 EIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLS 517

                        410       420       430
                 ....*....|....*....|....*....|
gi 19923748  422 YDHRLIDGREAVTFLRKIKAAVEDPRVLLL 451
Cdd:PRK11855 518 YDHRVIDGATAARFTNYLKQLLADPRRMLL 547
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 73-445 1.04e-76

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: 249.93  E-value: 1.04e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748    73 VKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPA 151
Cdd:TIGR02927 129 VKMPELGESVTEGTVtSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAPA 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   152 KAKPAEAPA---------AAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPPSGKPVSAVKPTV---------------- 206
Cdd:TIGR02927 209 EPAEEEAPApseagsepaPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSGDSGPYVTPLVrklakdkgvdlstvkg 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   207 ----------------------------APPLAEPGAGKG-----------LRSEhREKMNRMRQRIAQRLKEAQNTCAM 247
Cdd:TIGR02927 289 tgvggrirkqdvlaaakaaeearaaaaaPAAAAAPAAPAAaakpaepdtakLRGT-TQKMNRIRQITADKTIESLQTSAQ 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   248 LTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGL 327
Cdd:TIGR02927 368 LTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGL 447

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   328 VVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAI- 406
Cdd:TIGR02927 448 LVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIk 527

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 19923748   407 ----GGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVED 445
Cdd:TIGR02927 528 dedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 82-451 8.73e-66

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 222.19  E-value: 8.73e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   82 VTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPA 160
Cdd:PRK11854 216 GDEVEVtEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAAAPAKQEAA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  161 AAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPPSGKPV-----------------------------SAVKPTVAPPLA 211
Cdd:PRK11854 296 APAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLVrrlarefgvnlakvkgtgrkgrilkedvqAYVKDAVKRAEA 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  212 EP------GAGKGL---------RSEHRE--KMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMR-ARHKEAFLKK 273
Cdd:PRK11854 376 APaaaaagGGGPGLlpwpkvdfsKFGEIEevELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRkQQNAEAEKRK 455

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  274 HNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEK 353
Cdd:PRK11854 456 LGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKK 535

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  354 ARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAV 433
Cdd:PRK11854 536 ARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGA 615

                        410
                 ....*....|....*...
gi 19923748  434 TFLRKIKAAVEDPRVLLL 451
Cdd:PRK11854 616 RFITIINDRLSDIRRLVL 633
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 199-449 1.57e-55

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 186.54  E-value: 1.57e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  199 VSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKL 278
Cdd:PRK11857  53 ASVSSAQQAAKTAAPAAAPPKLEGKREKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  279 GFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNE 358
Cdd:PRK11857 133 TFLPFIAKAILIALKEFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERK 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  359 LAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRK 438
Cdd:PRK11857 213 IKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASR 292

                        250
                 ....*....|.
gi 19923748  439 IKAAVEDPRVL 449
Cdd:PRK11857 293 VKELLEKPEIL 303
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 73-451 1.03e-53

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: 185.77  E-value: 1.03e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748    73 VKTPAFAESVTEGD-VRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGK-VEGGTPL---------- 140
Cdd:TIGR01349   2 ITMPALSPTMTTGNlAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKdVPVNKPIavlveekedv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   141 ------FTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPS-----------QPPSGKPVSAV- 202
Cdd:TIGR01349  82 adafknYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDrifasplakklAKEKGIDLSAVa 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   203 -------------------KPTVAP-------PLAEPGAGKGLRSEHRE-KMNRMRQRIAQRLKEAQNTCAMLTTFNEID 255
Cdd:TIGR01349 162 gsgpngrivkkdiesfvpqSPASANqqaaattPATYPAAAPVSTGSYEDvPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   256 MSNIQEMRARHKEAFLKKHnlKLGFMSAFVKASAFALQEQPVVNAVIDDTTkeVVYRDYIDISVAVATPRGLVVPVIRNV 335
Cdd:TIGR01349 242 VDKLLALRKELNAMASEVY--KLSVNDFIIKASALALREVPEANSSWTDNF--IRRYKNVDISVAVATPDGLITPIVRNA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   336 EAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGK---VEV 412
Cdd:TIGR01349 318 DAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAV 397

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 19923748   413 RPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLL 451
Cdd:TIGR01349 398 ASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 93-451 2.98e-53

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: 187.00  E-value: 2.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748    93 VGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAA 172
Cdd:TIGR01348 139 VGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPATAPAPASAQPAAQSPAATQPE 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   173 VPPPAAPIPTQMPPVPSPSQPPSGKP-----------------VSAVK-------------------PTVAPPLAEPGAG 216
Cdd:TIGR01348 219 PAAAPAAAKAQAPAPQQAGTQNPAKVdhaapavrrlarefgvdLSAVKgtgikgrilredvqrfvkePSVRAQAAAASAA 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   217 KGLRSE--------------HREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAfLKKHNLKLGFMS 282
Cdd:TIGR01348 299 GGAPGAlpwpnvdfskfgevEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAA-VEKEGVKLTVLH 377

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   283 AFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIE 362
Cdd:TIGR01348 378 ILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPD 457

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   363 DMDGGTFTISN-GGVFGSLFgTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKA 441
Cdd:TIGR01348 458 EMQGACFTISSlGGIGGTAF-TPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICE 536

                         410
                  ....*....|
gi 19923748   442 AVEDPRVLLL 451
Cdd:TIGR01348 537 SLADIRRLLL 546
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 227-451 1.11e-40

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 148.51  E-value: 1.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  227 MNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTT 306
Cdd:PRK14843 123 MTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDG 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  307 KEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFG-SLFGtPI 385
Cdd:PRK14843 203 KTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGvQSFG-PI 281

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923748  386 INPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLL 451
Cdd:PRK14843 282 INQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 253-453 1.11e-37

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 142.17  E-value: 1.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  253 EIDMSNIQEMRARHKEAfLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVI 332
Cdd:PLN02528 215 EINVDALVELKASFQEN-NTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNI 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  333 RNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRP-VAIGGKVE 411
Cdd:PLN02528 294 KNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPrFVDDGNVY 373

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 19923748  412 VRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL 453
Cdd:PLN02528 374 PASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHM 415
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 76-451 2.80e-33

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 131.90  E-value: 2.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   76 PAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGK-VEGGTPLFTLRKTGAAPAKA 153
Cdd:PLN02744 118 PSLSPTMTEGNIaRWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKeIKVGEVIAITVEEEEDIGKF 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  154 KPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPPSGKPVSAVKPTVAPPLAEPGAG---------KGLRSEHR 224
Cdd:PLN02744 198 KDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEdnnvplssiKGTGPDGR 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  225 EKMNRMRQRIAQRLKEAQ---NTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNL------------------------- 276
Cdd:PLN02744 278 IVKADIEDYLASGGKGATappSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIphyyltvdtrvdklmalrsqlnslq 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  277 ------KLGFMSAFVKASAFALQEQPVVNAvidDTTKEVVyRDY--IDISVAVATPRGLVVPVIRNVEAMNFADIERTIT 348
Cdd:PLN02744 358 easggkKISVNDLVIKAAALALRKVPQCNS---SWTDDYI-RQYhnVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVK 433

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748  349 ELGEKARKNELAIEDMDGGTFTISN-GGVFGSLFGTPIINPPQSAILGMhGIFDRPVAIG---GKVEVRPMMYVALTYDH 424
Cdd:PLN02744 434 QLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAV-GSAEKRVIPGsgpDQYNFASFMSVTLSCDH 512

                        410       420
                 ....*....|....*....|....*..
gi 19923748  425 RLIDGREAVTFLRKIKAAVEDPRVLLL 451
Cdd:PLN02744 513 RVIDGAIGAEWLKAFKGYIENPESMLL 539
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 71-143 6.34e-24

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 94.39  E-value: 6.34e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923748  71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:cd06849   1 TEIKMPDLGESMTEGTIvEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 71-143 7.59e-23

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: 91.51  E-value: 7.59e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19923748    71 VTVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:pfam00364   1 TEIKSPMIGESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 71-143 8.78e-23

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


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 91.67  E-value: 8.78e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923748  71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:COG0508   3 IEIKMPDLGESMTEGTIvEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 283-439 2.47e-17

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 84.94  E-value: 2.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   283 AFVKAsafaLQEQPVVNAVID--DTTKEVVYRDYIDISVAVATP-----RGLVVPVIRNVEAMNFADIERTITELGEKAR 355
Cdd:PRK12270  179 ALVQA----LKAFPNMNRHYAevDGKPTLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRAR 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   356 KNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMhGIFDRPVAIGGKVE-------VRPMMYVALTYDHRLID 428
Cdd:PRK12270  255 DGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGV-GAMEYPAEFQGASEerlaelgISKVMTLTSTYDHRIIQ 333

                         170
                  ....*....|.
gi 19923748   429 GREAVTFLRKI 439
Cdd:PRK12270  334 GAESGEFLRTI 344
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 72-141 2.04e-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: 2.04e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19923748  72 TVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLF 141
Cdd:cd06663   1 TILIPDLAQHLGDGTVvKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLV 71
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 71-140 2.27e-14

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: 75.05  E-value: 2.27e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19923748    71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPL 140
Cdd:TIGR02927   3 ESVKMPALGESVTEGTVtSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVL 73
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 82-143 1.45e-10

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 63.48  E-value: 1.45e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19923748   82 VTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:PRK11854  12 ADEVEVtEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIF 74
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 87-143 1.58e-10

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 56.66  E-value: 1.58e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19923748  87 VRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:cd06850  11 VKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 93-144 6.66e-10

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: 56.83  E-value: 6.66e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 19923748  93 VGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLR 144
Cdd:COG0511  85 VGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 72-140 8.77e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 56.88  E-value: 8.77e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923748   72 TVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPL 140
Cdd:PRK14875   4 PITMPKWGLSMTEGKVaGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 73-143 4.78e-07

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 51.84  E-value: 4.78e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19923748   73 VKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGK-VEGGTPLFTL 143
Cdd:PRK11892   5 ILMPALSPTMEEGTLaKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTPIAVL 77
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
91-143 9.99e-06

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 43.46  E-value: 9.99e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19923748   91 KAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:PRK07051  26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 93-145 1.27e-04

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 44.45  E-value: 1.27e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19923748   93 VGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRK 145
Cdd:PRK09282 540 EGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
GCS_H cd06848
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ...
 91-125 1.76e-03

Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.


Pssm-ID: 133457 [Multi-domain]  Cd Length: 96  Bit Score: 37.51  E-value: 1.76e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 19923748  91 KAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEA 125
Cdd:cd06848  37 PEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVE 71
 
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