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Database: UniProt
Entry: Q3ATR4
LinkDB: Q3ATR4
Original site: Q3ATR4 
ID   SUCC_CHLCH              Reviewed;         390 AA.
AC   Q3ATR4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   16-JAN-2019, entry version 91.
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=Cag_0338;
OS   Chlorobium chlorochromatii (strain CaD3).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=340177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CaD3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL   Submitted (AUG-2005) 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; CP000108; ABB27611.1; -; Genomic_DNA.
DR   RefSeq; WP_011361384.1; NC_007514.1.
DR   ProteinModelPortal; Q3ATR4; -.
DR   SMR; Q3ATR4; -.
DR   STRING; 340177.Cag_0338; -.
DR   EnsemblBacteria; ABB27611; ABB27611; Cag_0338.
DR   KEGG; cch:Cag_0338; -.
DR   eggNOG; ENOG4105CMV; Bacteria.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   KO; K01903; -.
DR   OMA; LCMDAKF; -.
DR   OrthoDB; 316012at2; -.
DR   BioCyc; CCHL340177:G1G4Y-361-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000002708; 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    390       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta.
FT                                /FTId=PRO_1000082060.
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   390 AA;  42015 MW;  B5334A043002AA23 CRC64;
     MNIHEYQGKD ILRKFGVTVP KGIVAYSADE AKQAAEQLFA ETGSSVVVVK AQIHAGGRGK
     AGGVKLAKSP EEAFEIARQM IGMTLITHQT GPEGKVVSRL LIEEGMGIEK EFYVGITLDR
     ATSRNVLMVS TEGGMEIETV AEETPEKLLK IQIDPLFGMQ GFQAREAAFF LGLEGEQFRN
     AVNFITALYK AYTSIDASVA EINPLVVTSE GKVIALDAKI NFDDNALYRH KEYMELRDTS
     EEDPFEVEAS KSNLNYVRLD GNVGCMVNGA GLAMGTMDII QLAGGKPANF LDVGGTASPQ
     TVEEGFKIIL SDKNVRAILV NIFGGIVRCD RVAGGIMEAA KKMDLHLPVI VRLEGTNASI
     AQQMLDESGL SLIAAKGLRD AAQKVQEALA
//
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