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Database: UniProt
Entry: B3EFL3
LinkDB: B3EFL3
Original site: B3EFL3 
ID   SUCC_CHLL2              Reviewed;         392 AA.
AC   B3EFL3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   16-JAN-2019, entry version 70.
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=Clim_1943;
OS   Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 245 / NBRC 103803 / 6330;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T.,
RA   Liu Z., Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium limicola DSM 245.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001097; ACD90975.1; -; Genomic_DNA.
DR   RefSeq; WP_012466844.1; NC_010803.1.
DR   ProteinModelPortal; B3EFL3; -.
DR   SMR; B3EFL3; -.
DR   STRING; 290315.Clim_1943; -.
DR   EnsemblBacteria; ACD90975; ACD90975; Clim_1943.
DR   KEGG; cli:Clim_1943; -.
DR   eggNOG; ENOG4105CMV; Bacteria.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   KO; K01903; -.
DR   OMA; LCMDAKF; -.
DR   OrthoDB; 316012at2; -.
DR   BioCyc; CLIM290315:G1GC7-1987-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000008841; 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    392       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta.
FT                                /FTId=PRO_1000129170.
FT   DOMAIN        9    248       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   NP_BIND      57     59       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   REGION      325    327       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   METAL       203    203       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   METAL       217    217       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   BINDING      50     50       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     103    103       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     106    106       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     111    111       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     268    268       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ   SEQUENCE   392 AA;  42135 MW;  BEEB86EB2BC351A3 CRC64;
     MNIHEYQGKD ILKKFGVSVP RGIVAFSPDE AKQAAQQLFE EQGSPVVVVK AQIHAGGRGK
     AGGVKLAKSP DEAMEIARQM LGATLVTHQT GPEGKQVSRL LVEEGMNIDR EFYVGITLDR
     STSRNVLMVS TEGGMEIEKV AEETPDKLLK IQVDPLYGLQ GFQAREAAFF LGLEGEQFRN
     AVTFIIALYN AYMTIDASLA EINPLVVTKE GRVLALDAKI NFDGNALFRH KNFLELRDTN
     EEDPFEVEAS KSNLNYVRLD GNVGCMVNGA GLAMATMDMI QLAGGRPANF LDVGGGASPE
     TVEEGFKIIL SDKNVRAILV NIFGGIVRCD RVAGGIIQAA RKIGLNLPVI VRLEGTNAEI
     AQKMLDESGL NLIAANGLHD AAAKVNQALA AG
//
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