ID SUCC_RHOSK Reviewed; 397 AA.
AC B9KNB3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 05-DEC-2018, entry version 59.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_00558};
DE AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_00558};
GN Name=sucC {ECO:0000255|HAMAP-Rule:MF_00558};
GN OrderedLocusNames=RSKD131_2359;
OS Rhodobacter sphaeroides (strain KD131 / KCTC 12085).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=557760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD131 / KCTC 12085;
RX PubMed=19028901; DOI=10.1128/JB.01565-08;
RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S.,
RA Lee J.K.;
RT "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL J. Bacteriol. 191:1118-1119(2009).
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:0000255|HAMAP-
CC Rule:MF_00558}.
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_00558};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00558};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00558};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC succinate from succinyl-CoA (ligase route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00558}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00558}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC subunit family. {ECO:0000255|HAMAP-Rule:MF_00558}.
DR EMBL; CP001150; ACM02219.1; -; Genomic_DNA.
DR RefSeq; WP_002721255.1; NC_011963.1.
DR ProteinModelPortal; B9KNB3; -.
DR SMR; B9KNB3; -.
DR PRIDE; B9KNB3; -.
DR EnsemblBacteria; ACM02219; ACM02219; RSKD131_2359.
DR KEGG; rsk:RSKD131_2359; -.
DR HOGENOM; HOG000007059; -.
DR KO; K01903; -.
DR OMA; LCMDAKF; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000001597; Chromosome 1.
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;
KW ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Tricarboxylic acid cycle.
FT CHAIN 1 397 Succinate--CoA ligase [ADP-forming]
FT subunit beta.
FT /FTId=PRO_1000197712.
FT DOMAIN 9 254 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT NP_BIND 53 55 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT REGION 331 333 Substrate binding; shared with subunit
FT alpha. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT METAL 209 209 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT METAL 223 223 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT BINDING 46 46 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 109 109 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 112 112 ATP; via amide nitrogen.
FT {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 117 117 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 274 274 Substrate; shared with subunit alpha.
FT {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ SEQUENCE 397 AA; 42228 MW; A4D16F1C201AC264 CRC64;
MNIHEYQAKA LLRSYGAPVS DGRVVLKADE AKSAAGELGG PLWVVKAQIH AGGRGKGKFK
EPEAGEKGGV RLAKSVGEAA ELAKQMLGRT LVTHQTGPAG KQVNRIYIEE GSDIARELYL
ALLVDRGTSR ISFVVSTEGG MDIEEVAAST PEKIVSFSVD PASGLSDFHG RRVAFALGLE
GAQVKQCVQL VKNLYRAFVE KDMEMLEINP LIVMTDGNLK VLDAKVGFDN NALYRQSDVM
ALRDETEEDP KELAASKFDL NYIALDGEIG CMVNGAGLAM ATMDIIKLYG AEPANFLDVG
GGATKEKVTE AFKIITSDPN VKGILVNIFG GIMRCDIIAE GIIAAVKEVG LQVPLVVRLE
GTNVEKGKEI IANSGLNVIA GDNLSDAAQK IVKAVKG
//
