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Database: UniProt
Entry: P53589
LinkDB: P53589
Original site: P53589 
ID   SUCB2_CAEEL             Reviewed;         415 AA.
AC   P53589;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JAN-2019, entry version 143.
DE   RecName: Full=Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial {ECO:0000250|UniProtKB:Q96I99, 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};
DE   Flags: Precursor;
GN   Name=sucg-1 {ECO:0000312|WormBase:C50F7.4};
GN   ORFNames=C50F7.4 {ECO:0000312|WormBase:C50F7.4};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
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   -!- 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; FO080878; CCD67452.1; -; Genomic_DNA.
DR   PIR; T29296; T29296.
DR   RefSeq; NP_501266.1; NM_068865.4.
DR   UniGene; Cel.13261; -.
DR   ProteinModelPortal; P53589; -.
DR   SMR; P53589; -.
DR   STRING; 6239.C50F7.4; -.
DR   EPD; P53589; -.
DR   PaxDb; P53589; -.
DR   PeptideAtlas; P53589; -.
DR   PRIDE; P53589; -.
DR   EnsemblMetazoa; C50F7.4; C50F7.4; WBGene00016844.
DR   GeneID; 177555; -.
DR   KEGG; cel:CELE_C50F7.4; -.
DR   UCSC; C50F7.4; c. elegans.
DR   CTD; 177555; -.
DR   WormBase; C50F7.4; CE04242; WBGene00016844; sucg-1.
DR   eggNOG; KOG2799; Eukaryota.
DR   eggNOG; COG0045; LUCA.
DR   GeneTree; ENSGT00390000010170; -.
DR   HOGENOM; HOG000007059; -.
DR   InParanoid; P53589; -.
DR   KO; K01900; -.
DR   OMA; VQIEINP; -.
DR   OrthoDB; 973871at2759; -.
DR   PhylomeDB; P53589; -.
DR   Reactome; R-CEL-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER00999.
DR   PRO; PR:P53589; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00016844; Expressed in 5 organ(s), highest expression level in material anatomical entity.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; 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; 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   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     19       Mitochondrion. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   CHAIN        20    415       Succinate--CoA ligase [GDP-forming]
FT                                subunit beta, mitochondrial.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221}.
FT                                /FTId=PRO_0000033359.
FT   DOMAIN       28    258       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   NP_BIND      72     74       GTP. {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   REGION      349    351       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   METAL       227    227       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   METAL       241    241       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   BINDING      39     39       GTP. {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   BINDING     130    130       GTP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_03221}.
FT   BINDING     292    292       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   SITE         61     61       Important for substrate specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221}.
FT   SITE        131    131       Important for substrate specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03221}.
SQ   SEQUENCE   415 AA;  45092 MW;  A6B234E2A951E6E7 CRC64;
     MLRAAGNLSK SMMKSQRRFL NLQEFQSKEI LEKHGCSVQN FVVASNRKEA EEKWMSFGDH
     EYVVKAQILA GGRGKGKFIN GTKGIGGVFI TKEKDAALEA IDEMIGKRLV TKQTTSEGVR
     VDKVMIAEGV DIKRETYLAV LMDRESNGPV VVASPDGGMD IEAVAEKTPE RIFKTPIDIQ
     MGMTEGQSLK IAKDLQFEGK LIGVAAQEIK RLYDLFIAVD ATQVEINPLV ETADGRVFCV
     DAKMNFDDSA AYRQKEIFAY ETFEEHDPRE VDAHQFNLNY IGMDGNIACL VNGAGLAMAT
     MDLIKLHGGE PANFLDVGGA VTEDAVFNAV RIITSDPRVK CVLINIFGGI VNCATIANGV
     VSAVNKIGLN VPMVVRLEGT NVDAAKQIMK KSGLKILTAN NLDEAAAKAV SSLPK
//
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