EzCatDB: M00035

DB codeM00035
RLCP classification3.113.310400.385
CATH domainDomain 13.40.50.720
Domain 23.40.50.261Catalytic domain
Domain 33.30.470.20Catalytic domain
Domain 43.30.1490.20Catalytic domain
Domain 53.40.50.261
E.C.6.2.1.4

CATH domainRelated DB codes (homologues)
3.30.1490.20T00082,M00037,T00107,T00108
3.30.470.20T00082,D00298,M00037,M00051,T00107,T00108
3.40.50.720S00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,T00109

Enzyme Name
Swiss-protKEGG

O19069P53590
Protein nameSuccinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrialSuccinyl-CoA ligase [GDP-forming] subunit beta, mitochondrialsuccinate---CoA ligase (GDP-forming)
succinyl-CoA synthetase (GDP-forming)
succinyl coenzyme A synthetase (guanosine diphosphate-forming)
succinate thiokinase
succinic thiokinase
succinyl coenzyme A synthetase
succinate-phosphorylating enzyme
P-enzyme
SCS
G-STK
succinyl coenzyme A synthetase (GDP-forming)
succinyl CoA synthetase
succinyl coenzyme A synthetase
SynonymsEC 6.2.1.4
Succinyl-CoA synthetase subunit alpha
SCS-alpha
EC 6.2.1.4
GTP-specific succinyl-CoA synthetase subunit beta
Succinyl-CoA synthetase beta-G chain
SCS-betaG

KEGG pathways
MAP codePathways
MAP00020Citrate cycle (TCA cycle)
MAP00640Propanoate metabolism

Swiss-prot:Accession NumberO19069P53590
Entry nameSUCA_PIGSUCB2_PIG
ActivityGTP + succinate + CoA = GDP + phosphate + succinyl-CoA.GTP + succinate + CoA = GDP + phosphate + succinyl-CoA.
SubunitHeterodimer of an alpha and a beta subunit.Heterodimer of an alpha and a beta subunit.
Subcellular locationMitochondrion (By similarity).Mitochondrion.
Cofactor



SubstratesProductsintermediates
KEGG-idC00044C00042C00010C00035C00009C00091
CompoundGTPSuccinateCoAGDPOrthophosphateSuccinyl-CoA
Typeamide group,amine group,nucleotidecarboxyl groupamine group,carbohydrate,nucleotide,peptide/protein,sulfhydryl groupamide group,amine group,nucleotidephosphate group/phosphate ionamine group,carbohydrate,carboxyl group,nucleotide,peptide/protein,sulfide group
1eucA01UnboundUnboundUnboundUnboundUnboundUnbound
1eudA01UnboundUnboundUnboundUnboundUnboundUnbound
1eucA02UnboundUnboundUnboundUnboundBound:PO4Unbound
1eudA02UnboundUnboundUnboundUnboundUnboundUnbound1st-intermediate-bound:NEP
1eucB01UnboundUnboundUnboundUnboundUnboundUnbound
1eudB01UnboundUnboundUnboundUnboundUnboundUnbound
1eucB02UnboundUnboundUnboundUnboundUnboundUnbound
1eudB02UnboundUnboundUnboundUnboundUnboundUnbound
1eucB03UnboundUnboundUnboundUnboundUnboundUnbound
1eudB03UnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [4] & [5]
pdbCatalytic residuesCofactor-binding residuesModified residuesMain-chain involved in catalysis
1eucA01



1eudA01



1eucA02THR 164;GLU 217;HIS 259

                       
GLY 163;THR 164
1eudA02THR 164;GLU 217;       

NEP 259(phospholylated)
GLY 163;THR 164
1eucB01
ASN 206;ASP 220(magnesium binding)


1eudB01
ASN 206;ASP 220(magnesium binding)


1eucB02ARG 54


GLY 55
1eudB02ARG 54


GLY 55
1eucB03


GLY 272;ALA 273;GLY 274
1eudB03


GLY 272;ALA 273;GLY 274


references
[1]
PubMed ID3535876
JournalBiochemistry
Year1986
Volume25
Pages5420-5
AuthorsWolodko WT, Kay CM, Bridger WA
TitleActive enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-CoA synthetases of porcine heart and Escherichia coli.
[2]
PubMed ID8060491
JournalJ Protein Chem
Year1994
Volume13
Pages177-85
AuthorsUm HD, Klein C
TitleRegulatory role of GDP in the phosphoenzyme formation of guanine nucleotide: specific forms of succinyl coenzyme A synthetase.
[3]
PubMed ID9261120
JournalJ Biol Chem
Year1997
Volume272
Pages21151-9
AuthorsRyan DG, Lin T, Brownie E, Bridger WA, Wolodko WT
TitleMutually exclusive splicing generates two distinct isoforms of pig heart succinyl-CoA synthetase.
[4]
PubMed ID9765291
JournalJ Biol Chem
Year1998
Volume273
Pages27580-6
AuthorsJohnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO
TitleGenetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes.
[5]
CommentsX-ray crystallography
PubMed ID10873456
JournalJ Mol Biol
Year2000
Volume299
Pages1325-39
AuthorsFraser ME, James MN, Bridger WA, Wolodko WT
TitlePhosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase.
Related PDB1euc,1eud

comments
This enzyme catalyzes two transfer reactions, phosphoryl transfer and acyl transfer, according to the literature [5].
The first phosphoryl transfer proceeds as follows:
(1) The interaction of the sidechain of Glu217 (A chain) with that of His259 (A chain) maintains the protonation/charged state of His259 properly, so that His259 can act as a nucleophile.
(2) His259 makes a nucleophilic attack on the gamma-phosphate of the nucleotide (GTP) substrate, resulting in the transient formation of phosphohistidine intermediate. At this reaction, mainchain amide atoms (of Gly163, Thr164 (A chain), Gly55 & residues 272-274 (B chain)) and sidechains of Arg54 (B chain) and Thr164 (A chain) at active site stabilize the transferred phosphate group, whilst magnesium ion may stabilize the leaving alpha- and beta-phosphae of the nucleotide substrate.
(3) The carboxyl oxygen of the second substrate, succinate, may be in-line for a nucleophilic attack on the phoshorylated histidine, releasing the phosphorylated succinate intermediate. Thr164 (A chain) may assist the attacking oxygen atom, by interacting with it.
The second acyl transfer is supposed to be from the phosphorylated intermediate to the sulfur atom of the third substrate, CoA. However, the detailed mechanism has not been elucidated yet.

createdupdated
2004-09-222009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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