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
//
