GenomeNet

Database: UniProt
Entry: Q883Z4
LinkDB: Q883Z4
Original site: Q883Z4 
ID   SUCC_PSESM              Reviewed;         388 AA.
AC   Q883Z4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JAN-2019, entry version 108.
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=PSPTO_2202; ORFNames=PSPTO2202;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F.,
RA   Madupu R., Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H.,
RA   Nelson W.C., Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q.,
RA   Khouri H.M., Fedorova N.B., Tran B., Russell D., Berry K.J.,
RA   Utterback T.R., Van Aken S.E., Feldblyum T.V., D'Ascenzo M.,
RA   Deng W.-L., Ramos A.R., Alfano J.R., Cartinhour S., Chatterjee A.K.,
RA   Delaney T.P., Lazarowitz S.G., Martin G.B., Schneider D.J., Tang X.,
RA   Bender C.L., White O., Fraser C.M., Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(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; AE016853; AAO55718.1; -; Genomic_DNA.
DR   RefSeq; NP_792023.1; NC_004578.1.
DR   RefSeq; WP_002552981.1; NC_004578.1.
DR   ProteinModelPortal; Q883Z4; -.
DR   SMR; Q883Z4; -.
DR   STRING; 223283.PSPTO_2202; -.
DR   World-2DPAGE; 0008:Q883Z4; -.
DR   PRIDE; Q883Z4; -.
DR   EnsemblBacteria; AAO55718; AAO55718; PSPTO_2202.
DR   GeneID; 1183853; -.
DR   KEGG; pst:PSPTO_2202; -.
DR   PATRIC; fig|223283.9.peg.2234; -.
DR   eggNOG; ENOG4105CMV; Bacteria.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   KO; K01903; -.
DR   OMA; LCMDAKF; -.
DR   OrthoDB; 316012at2; -.
DR   PhylomeDB; Q883Z4; -.
DR   BioCyc; PSYR223283:G1G0D-2247-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000002515; 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; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN         1    388       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta.
FT                                /FTId=PRO_1000129214.
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      99     99       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   388 AA;  41212 MW;  010075DE988AC48F CRC64;
     MNLHEYQGKQ LFAEYGLPVS KGYAVDTPEA AAEACDKIGG TEWVVKAQVH AGGRGKAGGV
     KLVRSKEDAA AFAQQWLGKR LVTYQTDANG QPVTKILVES CTDIAKELYL GAVVDRSSRR
     IVFMASTEGG VDIEKIAHDT PEKILKATID PLVGAQPFQG RDLAFQLGLE GKQVTQFAKI
     FTGLAKLFQD HDLALLEVNP LVIKADGDLH CLDAKINIDA NAMYRQPKLK GFHDPSQDDP
     REAHAAKFEL NYVALEGNIG CMVNGAGLAM GTMDIVNLHG GKPANFLDVG GGATKERVTE
     AFKIILSDTN VAAVLVNIFG GIVRCDMIAE GIIGAVKEVG VKIPVVVRLE GNNAELGAKV
     LAESGLNIIA ATSLTDAAQQ VVKAAEGK
//
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