ID A0A3E1EUK7_9FLAO Unreviewed; 403 AA. AC A0A3E1EUK7; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 13-FEB-2019, entry version 2. 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; Bacteroidetes; 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 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:0000256|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:0000256|HAMAP- CC Rule:MF_00558}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00558}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00558}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC succinate from succinyl-CoA (ligase route): step 1/1. CC {ECO:0000256|HAMAP-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 CC subunit family. {ECO:0000256|HAMAP-Rule:MF_00558, CC ECO:0000256|SAAS:SAAS00551500}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00558}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 UniPathway; UPA00223; UER00999. DR Proteomes; UP000257127; Unassembled WGS sequence. DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.40.50.261; -; 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; 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; PS01217; SUCCINYL_COA_LIG_3; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00558}; KW Complete proteome {ECO:0000313|Proteomes:UP000257127}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00558, KW ECO:0000256|SAAS:SAAS00043448, ECO:0000313|EMBL:RFC53237.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00558, KW ECO:0000256|SAAS:SAAS01086150}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00558, KW ECO:0000256|SAAS:SAAS01086152}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00558, KW ECO:0000256|SAAS:SAAS00043434}; KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00558, KW ECO:0000256|SAAS:SAAS01085245}. FT DOMAIN 2 217 ATP-grasp_2. {ECO:0000259|Pfam:PF08442}. FT DOMAIN 278 388 Ligase_CoA. {ECO:0000259|Pfam:PF00549}. FT NP_BIND 57 59 ATP. {ECO:0000256|HAMAP-Rule:MF_00558}. FT REGION 337 339 Substrate binding; shared with subunit FT alpha. {ECO:0000256|HAMAP-Rule:MF_00558}. FT METAL 215 215 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00558}. FT METAL 229 229 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00558}. FT BINDING 50 50 ATP. {ECO:0000256|HAMAP-Rule:MF_00558}. FT BINDING 113 113 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00558}. FT BINDING 123 123 ATP. {ECO:0000256|HAMAP-Rule:MF_00558}. FT BINDING 280 280 Substrate; shared with subunit alpha. FT {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 //