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1O9L

Succinate:Coenzyme-A Transferase (pig heart)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0008260molecular_functionsuccinyl-CoA:3-oxo-acid CoA-transferase activity
A0008410molecular_functionCoA-transferase activity
A0042803molecular_functionprotein homodimerization activity
A0046952biological_processketone body catabolic process
A1902224biological_processketone body metabolic process
B0005739cellular_componentmitochondrion
B0008260molecular_functionsuccinyl-CoA:3-oxo-acid CoA-transferase activity
B0008410molecular_functionCoA-transferase activity
B0042803molecular_functionprotein homodimerization activity
B0046952biological_processketone body catabolic process
B1902224biological_processketone body metabolic process
C0005739cellular_componentmitochondrion
C0008260molecular_functionsuccinyl-CoA:3-oxo-acid CoA-transferase activity
C0008410molecular_functionCoA-transferase activity
C0042803molecular_functionprotein homodimerization activity
C0046952biological_processketone body catabolic process
C1902224biological_processketone body metabolic process
D0005739cellular_componentmitochondrion
D0008260molecular_functionsuccinyl-CoA:3-oxo-acid CoA-transferase activity
D0008410molecular_functionCoA-transferase activity
D0042803molecular_functionprotein homodimerization activity
D0046952biological_processketone body catabolic process
D1902224biological_processketone body metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EMC A9003
ChainResidue
AALA433
AGLN464
ACYS465

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EMC B9004
ChainResidue
BCYS465

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EMC C9005
ChainResidue
CCYS465
CHOH2133

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EMC C9006
ChainResidue
CLEU484
CCYS504

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EMC D9000
ChainResidue
DCYS504
DASP505
DPHE506
DLEU484

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EMC D9001
ChainResidue
DVAL430
DGLY462
DLYS463
DGLN464
DCYS465

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EMC D9002
ChainResidue
DLYS455
DCYS456

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EMT A9007
ChainResidue
ATYR126
AVAL133
AGLU134
ALEU135
ASER170
APRO171
AILE172
AHOH2025

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EMT B9008
ChainResidue
BCYS465
BHOH2075
BHOH2085
BHOH2086

Functional Information from PROSITE/UniProt
site_idPS01273
Number of Residues16
DetailsCOA_TRANSF_1 Coenzyme A transferases signature 1. NGatVLVGGFglcGiP
ChainResidueDetails
AASN55-PRO70

site_idPS01274
Number of Residues9
DetailsCOA_TRANSF_2 Coenzyme A transferases signature 2. LQSENGILG
ChainResidueDetails
ALEU341-GLY349

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"5-glutamyl coenzyme A thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10034","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7915164","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P55809","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9D0K2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

251801

PDB entries from 2026-04-08

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