ID   SUCC_ALCBS              Reviewed;         389 AA.
AC   Q0VPF7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit beta;
DE            EC=6.2.1.5;
DE   AltName: Full=Succinyl-CoA synthetase subunit beta;
DE            Short=SCS-beta;
GN   Name=sucC; OrderedLocusNames=ABO_1493;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate +
CC       succinyl-CoA.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR   EMBL; AM286690; CAL16941.1; -; Genomic_DNA.
DR   RefSeq; YP_693213.1; -.
DR   SMR; Q0VPF7; 1-385.
DR   GeneID; 4211974; -.
DR   GenomeReviews; AM286690_GR; ABO_1493.
DR   KEGG; abo:ABO_1493; -.
DR   NMPDR; fig|393595.12.peg.1500; -.
DR   HOGENOM; Q0VPF7; -.
DR   OMA; Q0VPF7; NLHCLDA.
DR   BioCyc; ABOR393595:ABO_1493-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR   HAMAP; MF_00558; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
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   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
DR   Gene3D; G3DSA:3.40.50.261; Succinyl-CoA_synth-like; 1.
DR   PANTHER; PTHR11815; CoA_lig_beta; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00549; Ligase_CoA; 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; Manganese;
KW   Metal-binding; Nucleotide-binding; Tricarboxylic acid cycle.
FT   CHAIN         1    389       Succinyl-CoA ligase [ADP-forming] subunit
FT                                beta.
FT                                /FTId=PRO_1000081994.
FT   DOMAIN        9    244       ATP-grasp.
FT   NP_BIND      35    108       ATP (By similarity).
FT   METAL       197    197       Magnesium or manganese (By similarity).
FT   METAL       199    199       Magnesium or manganese (By similarity).
SQ   SEQUENCE   389 AA;  41402 MW;  1E7F41F62F2B8AA1 CRC64;
     MNLHEYQSKQ LFADYGLPVS TGFACDTPEE VAAKAKEIGG DKWVVKAQVH AGGRGKAGGV
     KLVDTPEDAA AFAKKWLGKQ LVTFQTDEHG QPVSKILVET CTDIAKELYL SAVLDRASRR
     VVFMASTEGG VDIETVAEET PEKILKAEID PLVGAQPYQA REIAFKLGLE GKQVNQFAKI
     FVGLAKLFVD KDLALIEVNP LVITDTGDLH CLDAKINVDG SALYRHPDIK ALDDPSQEDE
     RERRAAEWDL NYVALEGNIG CMVNGAGLAM GTMDLVKLKG GAPANFLDVG GGATKERVTE
     AFKIILSDDQ VKGVLVNIFG GIVRCDLIAE GIIGAVEEVG VTVPVVVRLE GNNAELGSQK
     LAESGMNIIA AQSFDDAAEQ VVKAVGGAA
//