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Database: UniProt
Entry: P53588
LinkDB: P53588
Original site: P53588 
ID   SUCB1_CAEEL             Reviewed;         435 AA.
AC   P53588;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JAN-2019, entry version 150.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03220};
DE            EC=6.2.1.5 {ECO:0000250|UniProtKB:Q9YI37, ECO:0000255|HAMAP-Rule:MF_03220};
DE   AltName: Full=ATP-specific succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_03220};
DE            Short=A-SCS {ECO:0000255|HAMAP-Rule:MF_03220};
DE   AltName: Full=Succinyl-CoA synthetase beta-A chain {ECO:0000255|HAMAP-Rule:MF_03220};
DE            Short=SCS-betaA {ECO:0000255|HAMAP-Rule:MF_03220};
DE   Flags: Precursor;
GN   Name=suca-1 {ECO:0000312|WormBase:F47B10.1};
GN   ORFNames=F47B10.1 {ECO:0000312|WormBase:F47B10.1};
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: ATP-specific succinyl-CoA synthetase functions in the
CC       citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA
CC       to the synthesis of ATP 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_03220}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
CC         Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03220};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03220};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03220};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_03220}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta
CC       subunit determines specificity for ATP. {ECO:0000255|HAMAP-
CC       Rule:MF_03220}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-
CC       Rule:MF_03220}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family. ATP-specific subunit beta subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03220}.
DR   EMBL; Z68004; CAA91981.1; -; Genomic_DNA.
DR   PIR; T22332; T22332.
DR   RefSeq; NP_509821.1; NM_077420.3.
DR   UniGene; Cel.38657; -.
DR   ProteinModelPortal; P53588; -.
DR   SMR; P53588; -.
DR   BioGrid; 46191; 1.
DR   DIP; DIP-26345N; -.
DR   IntAct; P53588; 2.
DR   STRING; 6239.F47B10.1.1; -.
DR   EPD; P53588; -.
DR   PaxDb; P53588; -.
DR   PeptideAtlas; P53588; -.
DR   PRIDE; P53588; -.
DR   EnsemblMetazoa; F47B10.1; F47B10.1; WBGene00009812.
DR   GeneID; 181280; -.
DR   KEGG; cel:CELE_F47B10.1; -.
DR   UCSC; F47B10.1.1; c. elegans.
DR   CTD; 181280; -.
DR   WormBase; F47B10.1; CE03351; WBGene00009812; suca-1.
DR   eggNOG; KOG2799; Eukaryota.
DR   eggNOG; COG0045; LUCA.
DR   GeneTree; ENSGT00390000010170; -.
DR   HOGENOM; HOG000007059; -.
DR   InParanoid; P53588; -.
DR   KO; K01900; -.
DR   OMA; LCMDAKF; -.
DR   OrthoDB; 973871at2759; -.
DR   PhylomeDB; P53588; -.
DR   Reactome; R-CEL-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER00999.
DR   PRO; PR:P53588; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00009812; Expressed in 5 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR   GO; GO:0005524; F:ATP 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: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_03220; Succ_CoA_betaA_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; IPR034723; Succ_CoA_betaA_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   ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding;
KW   Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     20       Mitochondrion. {ECO:0000255|HAMAP-
FT                                Rule:MF_03220}.
FT   CHAIN        21    435       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta, mitochondrial.
FT                                {ECO:0000255|HAMAP-Rule:MF_03220}.
FT                                /FTId=PRO_0000033355.
FT   DOMAIN       32    259       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_03220}.
FT   NP_BIND      76     78       ATP. {ECO:0000255|HAMAP-Rule:MF_03220}.
FT   REGION      352    354       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_03220}.
FT   METAL       229    229       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03220}.
FT   METAL       243    243       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03220}.
FT   BINDING      69     69       ATP. {ECO:0000255|HAMAP-Rule:MF_03220}.
FT   BINDING     294    294       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_03220}.
FT   SITE         65     65       Important for substrate specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03220}.
FT   SITE        133    133       Important for substrate specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03220}.
SQ   SEQUENCE   435 AA;  47419 MW;  E91C4BD4CF82F7CB CRC64;
     MIGRISQPLL NTSQKFMAPA ARTLMLHEHH GMKILQNYEI KVPPFGVAQD AETAFSEAKR
     IGGKDYVVKA QVLAGGRGKG RFSSGLQGGV QIVFTPDEVK QKAGMMIGAN LITKQTDHRG
     KKCEEVMVCK RLFTRREYYF SITLDRNTNG PIVIASSQGG VNIEEVAATN PDAIVKMPID
     VNVGITKELA HEIAVKMGFS KDCEQQASEI IEKLYQMFKG SDATLVEINP MAEDVNGDVY
     CMDCKLLLDS NAEFRQAKLF DLKDKKQEDE LEIRAAAANL NYIRLDGTIG CMVNGAGLAM
     ATMDIIKLHG GEPANFLDVG GGATVEQVTE AFKIITADKD KVSAILVNIF GGIMRCDVIA
     QGIIQAAREL DLKIPIVVRL QGTKVEDAKA LIATSQLRIL PCDNLDEAAK MVVKLSNIVD
     LARATNVDVK FELSI
//
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