AC MF_03221; DC Protein; auto c? or TR HAMAP; MF_03221; -; 1; level=0 XX Names: Succ_CoA_betaG_euk XX ID SUCB2 DE RecName: Full=Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial; DE EC=6.2.1.4; DE AltName: Full=GTP-specific succinyl-CoA synthetase subunit beta; DE Short=G-SCS; DE Short=GTPSCS; DE AltName: Full=Succinyl-CoA synthetase beta-G chain; DE Short=SCS-betaG; case GN Name=SUCLG2; end case XX CC -!- FUNCTION: GTP-specific succinyl-CoA synthetase functions in the citric CC acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the CC synthesis of 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=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; EC=6.2.1.4; case 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: Heterodimer of an alpha and a beta subunit. The beta subunit CC determines specificity for GTP. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit CC family. GTP-specific subunit beta subfamily. case not CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal CC transit peptide but none has been predicted. end case 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 DR General; TransitM; -; 0-1; trigger=yes XX KW GTP-binding KW Ligase case KW Magnesium KW Metal-binding end case KW Mitochondrion KW Nucleotide-binding KW Tricarboxylic acid cycle XX GO GO:0005525; F:GTP binding case 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: SUCB2_PIG (P53590) case FT DOMAIN 47..275 FT /note="ATP-grasp" end case FT BINDING 91..93 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: G-R-G FT BINDING 366..368 FT /ligand="substrate" FT /ligand_note="ligand shared with subunit alpha" FT Condition: G-I-[VM] FT BINDING 244 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: N FT BINDING 258 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: D FT BINDING 58 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: Q FT BINDING 147 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT BINDING 309 FT /ligand="substrate" FT /ligand_note="ligand shared with subunit alpha" FT Condition: N FT SITE 80 FT /note="Important for substrate specificity" FT Condition: E FT SITE 148 FT /note="Important for substrate specificity" FT Condition: [DN] XX Size: 367-542; Related: MF_00558; MF_03220; Template: P53590; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: in CANLF Plasmid: None Comments: In animals, two different isoforms of SCS exist, one specific for ATP and the other specific for GTP (PubMed:9765291). The two isoforms include the same alpha-subunit, but different beta-subunits (PubMed:9765290). This is the subfamily of GTP-specific beta subunits. XX # Revision 1.9 2023/06/01 //