ID SUCC_BACVZ Reviewed; 385 AA. AC A7Z4M9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 100. 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=RBAM_015920; OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42) OS (Bacillus amyloliquefaciens subsp. plantarum). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus amyloliquefaciens group. OX NCBI_TaxID=326423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42; RX PubMed=17704766; DOI=10.1038/nbt1325; RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., RA Strittmatter A., Gottschalk G., Borriss R.; RT "Comparative analysis of the complete genome sequence of the plant growth- RT promoting bacterium Bacillus amyloliquefaciens FZB42."; RL Nat. Biotechnol. 25:1007-1014(2007). 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. {ECO:0000255|HAMAP-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 PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17663; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00558}; 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; Evidence={ECO:0000255|HAMAP-Rule:MF_00558}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22122; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00558}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00558}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00558}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP- CC 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 subunit CC family. {ECO:0000255|HAMAP-Rule:MF_00558}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000560; ABS73955.1; -; Genomic_DNA. DR RefSeq; WP_003154283.1; NC_009725.2. DR AlphaFoldDB; A7Z4M9; -. DR SMR; A7Z4M9; -. DR GeneID; 66321893; -. DR KEGG; bay:RBAM_015920; -. DR HOGENOM; CLU_037430_0_2_9; -. DR UniPathway; UPA00223; UER00999. DR Proteomes; UP000001120; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProt. 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:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:RHEA. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 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; IPR017866; Succ-CoA_synthase_bsu_CS. DR InterPro; IPR005811; SUCC_ACL_C. DR InterPro; IPR005809; Succ_CoA_ligase-like_bsu. DR InterPro; IPR016102; Succinyl-CoA_synth-like. DR NCBIfam; TIGR01016; sucCoAbeta; 1. DR PANTHER; PTHR11815:SF10; SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT BETA, MITOCHONDRIAL; 1. DR PANTHER; PTHR11815; SUCCINYL-COA SYNTHETASE BETA CHAIN; 1. DR Pfam; PF08442; ATP-grasp_2; 1. DR Pfam; PF00549; Ligase_CoA; 1. DR PIRSF; PIRSF001554; SucCS_beta; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1. PE 3: Inferred from homology; KW ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Tricarboxylic acid cycle. FT CHAIN 1..385 FT /note="Succinate--CoA ligase [ADP-forming] subunit beta" FT /id="PRO_1000082004" FT DOMAIN 9..244 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558" FT BINDING 46 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558" FT BINDING 53..55 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558" FT BINDING 99 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558" FT BINDING 102 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558" FT BINDING 107 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558" FT BINDING 199 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558" FT BINDING 213 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558" FT BINDING 264 FT /ligand="substrate" FT /ligand_note="ligand shared with subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558" FT BINDING 321..323 FT /ligand="substrate" FT /ligand_note="ligand shared with subunit alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558" SQ SEQUENCE 385 AA; 41514 MW; A477F07640FF24E2 CRC64; MNIHEYQGKE VLRKYGVSVP EGKVAFTAEE AVEKAESLSS SVYVVKAQIH AGGRGKAGGV KIAKTKDEVK EYAEELLGKT LVTHQTGPDG QVIKRLLIEE GCDIKKEYYV GLVLDRATSR IVLMASEEGG TEIEEVAEKT PEKIKKAVID PAVGLQGYQA REIAFAINIP KELVGKAAKF MLGLYKAFVE KDCSIAEINP LVVTGDGNVM ALDAKLNFDS NALYRQKDIM EYRDLDEEDP KEIEASKYDL SYISLDGNIG CMVNGAGLAM STMDIIKHYG GEPANFLDVG GGATAEKVTE AFKIILSDQN VKGIFVNIFG GIMKCDVIAE GVVEATRQVG LTLPLVVRLE GTNVDLGKKI LNESGLNITS AESMADGAQK IVSLV //