ID A0A3E1EUK7_9FLAO Unreviewed; 403 AA. AC A0A3E1EUK7; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 22-FEB-2023, entry version 12. DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000256|HAMAP-Rule:MF_00558}; DE EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_00558}; DE AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000256|HAMAP-Rule:MF_00558}; DE Short=SCS-beta {ECO:0000256|HAMAP-Rule:MF_00558}; GN Name=sucC {ECO:0000256|HAMAP-Rule:MF_00558}; GN ORFNames=DXU93_14310 {ECO:0000313|EMBL:RFC53237.1}; OS Brumimicrobium aurantiacum. OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Crocinitomicaceae; Brumimicrobium. OX NCBI_TaxID=1737063 {ECO:0000313|EMBL:RFC53237.1, ECO:0000313|Proteomes:UP000257127}; RN [1] {ECO:0000313|EMBL:RFC53237.1, ECO:0000313|Proteomes:UP000257127} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N62 {ECO:0000313|EMBL:RFC53237.1, RC ECO:0000313|Proteomes:UP000257127}; RA Du Z.-J., Luo H.-R.; RT "The draft genome squence of Brumimicrobium sp. N62."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|HAMAP- CC Rule:MF_00558}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00558}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00558}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_00558}. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits. CC {ECO:0000256|HAMAP-Rule:MF_00558}. CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit CC family. {ECO:0000256|HAMAP-Rule:MF_00558}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00558}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RFC53237.1}. 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; QURB01000011; RFC53237.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3E1EUK7; -. DR EnsemblBacteria; RFC53237; RFC53237; DXU93_14310. DR OrthoDB; 9802602at2; -. DR UniPathway; UPA00223; UER00999. DR Proteomes; UP000257127; Unassembled WGS sequence. 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: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; 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:SF10; SUCCINATE--COA LIGASE [GDP-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 TIGRFAMs; TIGR01016; sucCoAbeta; 1. DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00558}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00558}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00558}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00558}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00558}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP- KW Rule:MF_00558}. FT DOMAIN 2..217 FT /note="ATP-grasp fold succinyl-CoA synthetase-type" FT /evidence="ECO:0000259|Pfam:PF08442" FT DOMAIN 278..388 FT /note="ATP-citrate lyase/succinyl-CoA ligase" FT /evidence="ECO:0000259|Pfam:PF00549" FT BINDING 50 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558" FT BINDING 57..59 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558" FT BINDING 113 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558" FT BINDING 123 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558" FT BINDING 215 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558" FT BINDING 229 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558" FT BINDING 280 FT /ligand="substrate" FT /ligand_note="ligand shared with subunit alpha" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558" FT BINDING 337..339 FT /ligand="substrate" FT /ligand_note="ligand shared with subunit alpha" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558" SQ SEQUENCE 403 AA; 43478 MW; E9C0BA25CE454E89 CRC64; MNLHEYQGKS ILKTFGVAVQ ESVVIDDVAN AVSKAKELTE KTGTEWYVVK AQIHAGGRGK GTIEETGSRG VVLAKGIDKV EEVVKGILGG HLETAQTNGV AKKVNKVMIA EDVYYPGDSE PSEIYMSVLM DRDKGRNVII YSTEGGMDIE TVAEETPELI FKEEVDPRVG LQGFQARKIA FNLGLNGKAF KEMTKFVTAL YNSYIGSDAS MFEINPVLKT SDDKVIAVDA KVTLDDTALF RHKDYAEMRD KTEEDPAEVE ADEAGLNFVK LDGNVGCMVN GAGLAMATMD IIKQSGGNPA NFLDVGGTAD AARVEKAFDI ILKDENVKAI LINIFGGIVR CDRVAQGVVD AYKNMGGIPV PIIVRLQGTN AEEAKKLIDE SGLDVHSAVL LQEASDLVKK ILA //