(data stored in ACNUC7421 zone)

SWISSPROT: Q5LXC4_RUEPO

ID   Q5LXC4_RUEPO            Unreviewed;       397 AA.
AC   Q5LXC4;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 109.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000256|HAMAP-Rule:MF_00558};
DE            EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_00558};
DE   AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000256|HAMAP-Rule:MF_00558};
DE            Short=SCS-beta {ECO:0000256|HAMAP-Rule:MF_00558};
GN   Name=sucC {ECO:0000256|HAMAP-Rule:MF_00558};
GN   OrderedLocusNames=SPO0347 {ECO:0000313|EMBL:AAV93665.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93665.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93665.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93665.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid
CC       cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC       synthesis of either ATP or GTP and thus represents the only step
CC       of 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:0000256|HAMAP-
CC       Rule:MF_00558, ECO:0000256|SAAS:SAAS01084253}.
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:0000256|HAMAP-
CC         Rule:MF_00558};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00558};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00558};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00558, ECO:0000256|SAAS:SAAS01084252}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00558, ECO:0000256|SAAS:SAAS01084240}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family. {ECO:0000256|HAMAP-Rule:MF_00558,
CC       ECO:0000256|SAAS:SAAS00551500}.
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DR   EMBL; CP000031; AAV93665.1; -; Genomic_DNA.
DR   RefSeq; WP_011046108.1; NC_003911.12.
DR   STRING; 246200.SPO0347; -.
DR   EnsemblBacteria; AAV93665; AAV93665; SPO0347.
DR   KEGG; sil:SPO0347; -.
DR   eggNOG; ENOG4105CMV; Bacteria.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   KO; K01903; -.
DR   OMA; LGGITRC; -.
DR   OrthoDB; 316012at2; -.
DR   BioCyc; RPOM246200:G1G48-354-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000001023; Chromosome.
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   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; 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;
DR   PRODOM; Q5LXC4.
DR   SWISS-2DPAGE; Q5LXC4.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00558, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00558,
KW   ECO:0000256|SAAS:SAAS00043448, ECO:0000313|EMBL:AAV93665.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00558,
KW   ECO:0000256|SAAS:SAAS01086150};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00558,
KW   ECO:0000256|SAAS:SAAS01086152};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00558,
KW   ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS00436163};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00558,
KW   ECO:0000256|SAAS:SAAS01085245}.
FT   DOMAIN        9     55       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   NP_BIND      53     55       ATP. {ECO:0000256|HAMAP-Rule:MF_00558}.
FT   REGION      331    333       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000256|HAMAP-Rule:MF_00558}.
FT   METAL       209    209       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00558}.
FT   METAL       223    223       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00558}.
FT   BINDING      46     46       ATP. {ECO:0000256|HAMAP-Rule:MF_00558}.
FT   BINDING     109    109       ATP. {ECO:0000256|HAMAP-Rule:MF_00558}.
FT   BINDING     112    112       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00558}.
FT   BINDING     117    117       ATP. {ECO:0000256|HAMAP-Rule:MF_00558}.
FT   BINDING     274    274       Substrate; shared with subunit alpha.
FT                                {ECO:0000256|HAMAP-Rule:MF_00558}.
SQ   SEQUENCE   397 AA;  42409 MW;  24ED5F5EDAFA4C89 CRC64;
     MNIHEYQAKA LLRSYGAPVS DGRVVLRAED AKTAAGELDG PLWVVKAQIH AGGRGKGKFK
     EADAGEKGGV RLTKSVEEAA EEAKKMLGRT LVTHQTGPVG KQVNRIYIEA GSGIERELYL
     ALLVDRQTSR ISFVCSTEGG MDIEEVAAST PEKILSFSVD PVTGYQPYHG RRIAFSLGLE
     GPQVKQCVAL MGLLYKAFVE KDMEMLEINP LIVAEGGSLK VLDAKVGFDG NAIYRHSDIA
     ELRDTTEEDP KELEASKYDL NYIALDGEIG CMVNGAGLAM ATMDIIKLYG AEPANFLDVG
     GGATKEKVTE AFKIITSDPN VKGILVNIFG GIMRCDVIAE GVVAAVKEVG LQVPLVVRLE
     GTNVEKGKEI INTSGLNVIA ADNLSDGAEK IVKAVKG
//

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