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Database: UniProt
Entry: Q87A98
LinkDB: Q87A98
Original site: Q87A98 
ID   SUCC_XYLFT              Reviewed;         387 AA.
AC   Q87A98;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   05-DEC-2018, entry version 106.
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=PD_1930;
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=183190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Temecula1 / ATCC 700964;
RX   PubMed=12533478; DOI=10.1128/JB.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B.,
RA   Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H.,
RA   Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R.,
RA   Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M.,
RA   Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J.,
RA   Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E.,
RA   Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M.,
RA   Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V.,
RA   da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T.,
RA   Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D.,
RA   de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G.,
RA   Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C.,
RA   Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's
RT   disease and citrus variegated chlorosis strains of Xylella
RT   fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(2003).
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; AE009442; AAO29760.1; -; Genomic_DNA.
DR   RefSeq; WP_004090371.1; NC_004556.1.
DR   ProteinModelPortal; Q87A98; -.
DR   SMR; Q87A98; -.
DR   EnsemblBacteria; AAO29760; AAO29760; PD_1930.
DR   GeneID; 33198101; -.
DR   KEGG; xft:PD_1930; -.
DR   KO; K01903; -.
DR   OMA; LCMDAKF; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000002516; 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;
KW   ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Tricarboxylic acid cycle.
FT   CHAIN         1    387       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta.
FT                                /FTId=PRO_0000102879.
FT   DOMAIN        9    244       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   NP_BIND      53     55       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   REGION      321    323       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   METAL       199    199       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   METAL       213    213       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   BINDING      46     46       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     102    102       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     107    107       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     264    264       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ   SEQUENCE   387 AA;  41018 MW;  C119CFCC1536370F CRC64;
     MNFHEYQAKQ LFAEYGIPVP AGRIASSADE AVTAAKSLGN GPWMVKAQIH AGGRGKAGGV
     KFCKTTDEVK QAAATMLGTK MATYQSAGVA LPVNLVLVTE AGEITKELYL SVLVDRGTRS
     ITYIASSEGG VDIEHVAAET PEKIQTLNVD FVEGLQPYQG RDIGFHLGLE AKQVNQLSKI
     MISLYQLFND KDLSLIELNP LAILSNGDLY ALDGKINSDD NATFRHKELA AMRDKTQEDE
     TEVLASENDL NYVTMDGNIG CMVNGAGLAM ATMDVIKLNG GEPANFLDVG GGATKERVTT
     AFKLILSSNK VKAIFVNIFG GIVRCDMIAE GIIAAVKEVG VKVPVIVRLE GTNVDAGKQL
     LATSGLAIIP ADDINDGAKK AVAAVTV
//
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