AC   MF_00558;
DC   Protein; auto
c?   <OC:Bacteria> or <OC:Archaea>
TR   HAMAP; MF_00558; -; 1; level=0
XX
Names: Succ_CoA_beta
XX
ID   SUCC
DE   RecName: Full=Succinate--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;
XX
CC   -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC       (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
CC       either ATP or GTP and thus represents the only step of substrate-level
CC       phosphorylation in the TCA. The beta subunit provides nucleotide
CC       specificity of the enzyme and binds the substrate succinate, while the
CC       binding sites for coenzyme A and phosphate are found in the alpha
CC       subunit.
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;
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17663;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA;
CC         Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:58189;
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22122;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
end case
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC       family.
XX
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1; trigger=no
DR   PROSITE; PS50975; ATP_GRASP; 1; trigger=no
DR   Pfam; PF08442; ATP-grasp_2; 1; trigger=no
DR   Pfam; PF00549; Ligase_CoA; 1; trigger=no
DR   NCBIfam; TIGR01016; SucCoAbeta; 1; trigger=no
DR   PIRSF; PIRSF001554; SucCS_beta; 1; trigger=no
XX
KW   ATP-binding
KW   Ligase
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
KW   Nucleotide-binding
KW   Tricarboxylic acid cycle
XX
GO   GO:0005524; F:ATP binding
case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0004775; F:succinate-CoA ligase (ADP-forming) activity
GO   GO:0006099; P:tricarboxylic acid cycle
XX
FT   From: SUCC_ECOLI (P0A836)
case <Feature:PS50975>
FT   DOMAIN          9..244
FT                   /note="ATP-grasp"
end case
FT   BINDING         53..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-R-G
FT   BINDING         321..323
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit alpha"
FT   Condition: G-I-[VAMTL]
FT   BINDING         199
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: N
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: E
FT   BINDING         102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   BINDING         107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: E
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit alpha"
FT   Condition: N
XX
Size: 364-399;
Related: MF_03220!; MF_03221!;
Template: P0A836; P25126; P80886; P53590;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in ARCFU, STRCO
Plasmid: None
Comments: It is not possible to automatically make a distinction between a bona-fide
 sucC and mtkA (not shown in alignment).
XX
# Revision 1.37 2023/06/01
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