ID SUCC_BRUSU Reviewed; 398 AA.
AC P66868; G0K869; Q8YJE6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 05-DEC-2018, entry version 86.
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=BR1926, BS1330_I1920;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Brucellaceae; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between
RT animal and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/JB.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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; AE014291; AAN30818.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM19235.1; -; Genomic_DNA.
DR RefSeq; WP_002964994.1; NZ_KN046804.1.
DR ProteinModelPortal; P66868; -.
DR SMR; P66868; -.
DR EnsemblBacteria; AAN30818; AAN30818; BR1926.
DR EnsemblBacteria; AEM19235; AEM19235; BS1330_I1920.
DR GeneID; 29593282; -.
DR KEGG; bms:BR1926; -.
DR KEGG; bsi:BS1330_I1920; -.
DR PATRIC; fig|204722.21.peg.2977; -.
DR HOGENOM; HOG000007059; -.
DR KO; K01903; -.
DR OMA; LCMDAKF; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000007104; Chromosome I.
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 1 398 Succinate--CoA ligase [ADP-forming]
FT subunit beta.
FT /FTId=PRO_0000102821.
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 398 AA; 42527 MW; 2183A24659700A25 CRC64;
MNIHEYQAKR LLHTYGAPIA NGVAVYSVEQ AEEWAKTLPG PLYVVKSQIH AGGRGKGKFK
ELPADAKGGV RLAKSVEEVV ANAKEMLGNT LVTKQTGEAG KQVNRLYIED GADIERELYL
SILIDRSVGR PAFVVSTEGG MDIEAVAEET PEKIVTVAID PAKGVTDEDA NKLADALKLE
GGAREDGLKL FPILYKAFTE KDMSLLEINP LIVMTNGRVR VLDAKVSFDN NALFRHPDIV
ELRDLTEEDP KEIEASKYDL AYVALDGNIG CMVNGAGLAM ATMDIIKLYG AEPANFLDVG
GGASKEKVTA AFKIITADPA VEGILVNIFG GIMKCDVIAE GVIAAVKEVG LKVPLVVRLE
GTNVELGKKI INESGLNVIS ADDLDDAAQK IVAAVKGN
//
