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Database: UniProt
Entry: Q869S7
LinkDB: Q869S7
Original site: Q869S7 
ID   SUCB2_DICDI             Reviewed;         420 AA.
AC   Q869S7; Q554Z0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   05-DEC-2018, entry version 110.
DE   RecName: Full=Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03221};
DE            EC=6.2.1.4 {ECO:0000255|HAMAP-Rule:MF_03221};
DE   AltName: Full=GTP-specific succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_03221};
DE            Short=G-SCS {ECO:0000255|HAMAP-Rule:MF_03221};
DE            Short=GTPSCS {ECO:0000255|HAMAP-Rule:MF_03221};
DE   AltName: Full=Succinyl-CoA synthetase beta-G chain {ECO:0000255|HAMAP-Rule:MF_03221};
DE            Short=SCS-betaG {ECO:0000255|HAMAP-Rule:MF_03221};
GN   Name=scsB; Synonyms=suclg2; ORFNames=DDB_G0274449;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
RA   Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
RA   Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
RA   Platzer M., Rosenthal A., Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: GTP-specific succinyl-CoA synthetase functions in the
CC       citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA
CC       to the synthesis of GTP and thus represents the only step of
CC       substrate-level phosphorylation in the TCA. The beta subunit
CC       provides nucleotide specificity of the enzyme and binds the
CC       substrate succinate, while the binding sites for coenzyme A and
CC       phosphate are found in the alpha subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03221}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA;
CC         Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:58189; EC=6.2.1.4; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03221};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03221};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03221};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_03221}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta
CC       subunit determines specificity for GTP. {ECO:0000255|HAMAP-
CC       Rule:MF_03221}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-
CC       Rule:MF_03221}.
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-
CC       terminal transit peptide but none has been predicted.
CC       {ECO:0000255|HAMAP-Rule:MF_03221}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family. GTP-specific subunit beta subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03221}.
DR   EMBL; AAFI02000012; EAL70117.1; -; Genomic_DNA.
DR   RefSeq; XP_644183.1; XM_639091.1.
DR   ProteinModelPortal; Q869S7; -.
DR   SMR; Q869S7; -.
DR   STRING; 44689.DDB0231358; -.
DR   PaxDb; Q869S7; -.
DR   EnsemblProtists; EAL70117; EAL70117; DDB_G0274449.
DR   GeneID; 8619612; -.
DR   KEGG; ddi:DDB_G0274449; -.
DR   dictyBase; DDB_G0274449; scsB.
DR   eggNOG; KOG1447; Eukaryota.
DR   eggNOG; COG0045; LUCA.
DR   InParanoid; Q869S7; -.
DR   KO; K01900; -.
DR   OMA; VQIEINP; -.
DR   PhylomeDB; Q869S7; -.
DR   Reactome; R-DDI-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER00999.
DR   PRO; PR:Q869S7; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   Proteomes; UP000002195; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006104; P:succinyl-CoA metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.261; -; 1.
DR   HAMAP; MF_00558; Succ_CoA_beta; 1.
DR   HAMAP; MF_03221; Succ_CoA_betaG_euk; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR034722; Succ_CoA_betaG_euk.
DR   InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR11815; PTHR11815; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001554; SucCS_beta; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; GTP-binding; Ligase; Magnesium; Metal-binding;
KW   Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    420       Succinate--CoA ligase [GDP-forming]
FT                                subunit beta, mitochondrial.
FT                                /FTId=PRO_0000328366.
FT   DOMAIN       35    263       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   NP_BIND      78     80       GTP. {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   REGION      354    356       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   METAL       232    232       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   METAL       246    246       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   BINDING      46     46       GTP. {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   BINDING     135    135       GTP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   BINDING     297    297       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   SITE         67     67       Important for substrate specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   SITE        136    136       Important for substrate specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221}.
SQ   SEQUENCE   420 AA;  45664 MW;  81245E0C90C8BC4E CRC64;
     MSLFNSANKV IGGVLKFNPS KYQVRYLNLH EYQSKSLMDK YGVNTQKWRV VTKASDAIKA
     ASELNGELVV KAQVHAGGRG KGSFIETGFK GGVHLCKTGK EAERLCDEML GKHLVTKQTT
     KEGTKVQSVM LAESVDPKRE LYFAIVMDRK YGGPVMIASP QGGVDIESVA EETPDLIFKE
     PIDIVKGIRP EQTKNLAEKL GFTGEKAKIA QQQMENLYQL FIKSDATQVE INPFAETTDG
     QVICMDAKIN FDDNASFRQK EIFEMRDTAE EDPREVEAGK FGLNYIGLDG NIGCMVNGAG
     LAMATMDIIK LKGGIPANFL DVGGSASEQA VTEAFKILTK DPRVKCLLVN IFGGIMKCDI
     IASGIVNASK QVGLKIPLVV RLEGTNVNIG KEILEKSGLN ITSASDLDDA AIKAVNCLKK
//
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