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Conserved domains on  [gi|349585158|ref|NP_001231812|]
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dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial isoform 2 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sucB super family cl36875
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 71-149 8.75e-34

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]


The actual alignment was detected with superfamily member TIGR01347:

Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 122.53  E-value: 8.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585158   71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGGK 149
Cdd:TIGR01347   1 IEIKVPELAESITEGTVaEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
 
Name Accession Description Interval E-value
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 71-149 8.75e-34

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: 122.53  E-value: 8.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585158   71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGGK 149
Cdd:TIGR01347   1 IEIKVPELAESITEGTVaEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 71-143 2.92e-26

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: 94.78  E-value: 2.92e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 349585158  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 1.07e-25

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: 93.43  E-value: 1.07e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 349585158   71 VTVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:pfam00364   1 TEIKSPMIGESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 71-143 1.84e-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: 92.82  E-value: 1.84e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 349585158  71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:COG0508    3 IEIKMPDLGESMTEGTIvEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 47-150 1.31e-23

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 95.52  E-value: 1.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585158  47 KVVINNSVFSVRF--FRTTAVCKD-------DLVTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVP 116
Cdd:PTZ00144  12 PLLSSVKGMFRRFslRKLQPACSAhfsksyfSIKVIKVPTMGDSISEGTVvEWKKKVGDYVKEDEVICIIETDKVSVDIR 91

                         90       100       110
                 ....*....|....*....|....*....|....
gi 349585158 117 SPANGVIEALLVPDGGKVEGGTPLFTLrKTGGKE 150
Cdd:PTZ00144  92 APASGVITKIFAEEGDTVEVGAPLSEI-DTGGAP 124
 
Name Accession Description Interval E-value
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 71-149 8.75e-34

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: 122.53  E-value: 8.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585158   71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGGK 149
Cdd:TIGR01347   1 IEIKVPELAESITEGTVaEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 71-143 2.92e-26

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: 94.78  E-value: 2.92e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 349585158  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 1.07e-25

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: 93.43  E-value: 1.07e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 349585158   71 VTVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:pfam00364   1 TEIKSPMIGESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 71-143 1.84e-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: 92.82  E-value: 1.84e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 349585158  71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:COG0508    3 IEIKMPDLGESMTEGTIvEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 47-150 1.31e-23

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 95.52  E-value: 1.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585158  47 KVVINNSVFSVRF--FRTTAVCKD-------DLVTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVP 116
Cdd:PTZ00144  12 PLLSSVKGMFRRFslRKLQPACSAhfsksyfSIKVIKVPTMGDSISEGTVvEWKKKVGDYVKEDEVICIIETDKVSVDIR 91

                         90       100       110
                 ....*....|....*....|....*....|....
gi 349585158 117 SPANGVIEALLVPDGGKVEGGTPLFTLrKTGGKE 150
Cdd:PTZ00144  92 APASGVITKIFAEEGDTVEVGAPLSEI-DTGGAP 124
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 71-150 2.02e-22

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 91.78  E-value: 2.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585158  71 VTVKTPAFAESVTEGD-VRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGGK 149
Cdd:PRK11856   3 FEFKMPDLGEGMTEGEiVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82


                 .
gi 349585158 150 E 150
Cdd:PRK11856  83 E 83
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
73-137 3.94e-22

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 91.05  E-value: 3.94e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 349585158  73 VKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGG 137
Cdd:PRK05704   5 IKVPTLPESVTEATIaTWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVG 70
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 73-143 4.95e-18

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 79.87  E-value: 4.95e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 349585158  73 VKTPAFAEsVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:PRK11855   5 FKVPDIGE-VVEVEViEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVI 75
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 71-143 7.07e-18

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 79.48  E-value: 7.07e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 349585158  71 VTVKTPAFAEsVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:PRK11855 120 VEVKVPDIGE-ITEVEViEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVI 192
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 72-141 4.86e-17

Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.


Pssm-ID: 133456 [Multi-domain]  Cd Length: 73  Bit Score: 71.32  E-value: 4.86e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 349585158  72 TVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLF 141
Cdd:cd06663    1 TILIPDLAQHLGDGTVvKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLV 71
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 71-140 2.34e-16

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: 75.43  E-value: 2.34e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 349585158   71 VTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPL 140
Cdd:TIGR02927   3 ESVKMPALGESVTEGTVtSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVL 73
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 73-140 7.80e-16

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: 73.89  E-value: 7.80e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 349585158   73 VKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPL 140
Cdd:TIGR02927 129 VKMPELGESVTEGTVtSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVL 197
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 29-146 3.29e-13

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 66.32  E-value: 3.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585158  29 RSLPGVSLCqgpgypnSRKVVINNSVFSvRFFRTTAVCKDDLVTVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIE 107
Cdd:PLN02226  58 LALPGNSGI-------SRSASLVSSTLQ-RWVRPFSSESGDTVEAVVPHMGESITDGTLaTFLKKPGERVQADEAIAQIE 129

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 349585158 108 TDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKT 146
Cdd:PLN02226 130 TDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKS 168
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 82-143 1.68e-12

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 64.25  E-value: 1.68e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 349585158  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 3.02e-12

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: 58.58  E-value: 3.02e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 349585158  87 VRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:cd06850   11 VKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 82-137 5.84e-12

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 62.71  E-value: 5.84e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 349585158  82 VTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGG 137
Cdd:PRK11854 216 GDEVEVtEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTG 272
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 82-138 6.06e-12

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 62.71  E-value: 6.06e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 349585158  82 VTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGT 138
Cdd:PRK11854 115 SDEVEVtEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGS 172
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 93-144 1.50e-11

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: 58.37  E-value: 1.50e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 349585158  93 VGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLR 144
Cdd:COG0511   85 VGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 73-140 6.28e-11

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: 59.42  E-value: 6.28e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585158   73 VKTPAFAESVTEGD-VRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGK-VEGGTPL 140
Cdd:TIGR01349   2 ITMPALSPTMTTGNlAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKdVPVNKPI 71
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 72-140 1.47e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 58.42  E-value: 1.47e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585158  72 TVKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPL 140
Cdd:PRK14875   4 PITMPKWGLSMTEGKVaGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 93-147 8.58e-10

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: 56.42  E-value: 8.58e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 349585158   93 VGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTG 147
Cdd:TIGR01348 139 VGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAG 193
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 76-133 6.64e-09

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 53.70  E-value: 6.64e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 349585158  76 PAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGK 133
Cdd:PLN02744 118 PSLSPTMTEGNIaRWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAK 176
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 73-143 7.27e-09

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 53.38  E-value: 7.27e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 349585158  73 VKTPAFAESVTEGDV-RWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGK-VEGGTPLFTL 143
Cdd:PRK11892   5 ILMPALSPTMEEGTLaKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTPIAVL 77
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 92-150 6.28e-08

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: 51.03  E-value: 6.28e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 349585158   92 AVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGGKE 150
Cdd:TIGR01348  22 KPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGAQ 80
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
91-143 1.18e-06

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 44.23  E-value: 1.18e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 349585158  91 KAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:PRK07051  26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 93-145 5.12e-06

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 45.22  E-value: 5.12e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 349585158  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 7.93e-04

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: 36.74  E-value: 7.93e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 349585158  91 KAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEA 125
Cdd:cd06848   37 PEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVE 71
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
93-143 8.38e-04

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 38.76  E-value: 8.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 349585158  93 VGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTL 143
Cdd:PRK14040 542 EGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 93-141 2.49e-03

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 37.13  E-value: 2.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 349585158  93 VGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLF 141
Cdd:PLN02983 222 VGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPLF 270
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 92-140 3.25e-03

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 37.01  E-value: 3.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 349585158  92 AVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPL 140
Cdd:PRK14042 542 SAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVL 590
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 92-137 3.46e-03

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 37.04  E-value: 3.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 349585158   92 AVGDTVAEDEVVCEIETDK--TSVQvpSPANGVIEALLVPDGGKVEGG 137
Cdd:PRK12999 1093 KEGDEVKAGDPLAVIEAMKmeTTIT--APVDGTVKRVLVKAGDQVEAG 1138
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 92-137 4.11e-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: 36.98  E-value: 4.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 349585158   92 AVGDTVAEDEVVCEIETDK--TSVQvpSPANGVIEALLVPDGGKVEGG 137
Cdd:COG1038  1093 KEGDEVKKGDPLLTIEAMKmeTTIT--APRDGTVKEVLVKEGDQVEAG 1138
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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