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Database: UniProt
Entry: A0A0M3TU54_9GAMM
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ID   A0A0M3TU54_9GAMM        Unreviewed;       390 AA.
AC   A0A0M3TU54;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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   ECO:0000313|EMBL:ALE52641.1};
GN   ORFNames=SP60_05120 {ECO:0000313|EMBL:ALE52641.1};
OS   Candidatus Thioglobus autotrophicus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX   NCBI_TaxID=1705394 {ECO:0000313|EMBL:ALE52641.1, ECO:0000313|Proteomes:UP000058020};
RN   [1] {ECO:0000313|EMBL:ALE52641.1, ECO:0000313|Proteomes:UP000058020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF1 {ECO:0000313|EMBL:ALE52641.1,
RC   ECO:0000313|Proteomes:UP000058020};
RX   PubMed=26494660;
RA   Shah V., Morris R.M.;
RT   "Genome Sequence of 'Candidatus Thioglobus autotrophica' Strain EF1, a
RT   Chemoautotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL   Genome Announc. 3:e01156-15(2015).
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   -!- 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:0000256|HAMAP-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}.
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DR   EMBL; CP010552; ALE52641.1; -; Genomic_DNA.
DR   RefSeq; WP_053951604.1; NZ_CP010552.1.
DR   AlphaFoldDB; A0A0M3TU54; -.
DR   STRING; 1705394.SP60_05120; -.
DR   KEGG; tho:SP60_05120; -.
DR   PATRIC; fig|1705394.5.peg.1026; -.
DR   OrthoDB; 9802602at2; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000058020; 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; 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   NCBIfam; TIGR01016; sucCoAbeta; 1.
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   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00558, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
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}; Reference proteome {ECO:0000313|Proteomes:UP000058020};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW   Rule:MF_00558}.
FT   DOMAIN          9..227
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT   BINDING         53..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT   BINDING         102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT   BINDING         107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT   BINDING         199
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT   BINDING         321..323
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
SQ   SEQUENCE   390 AA;  41854 MW;  07FAA83DBF51D894 CRC64;
     MHIHEYQAKG LFRQYNIQTP KAVLISAVDE ASKACGELGG DIWVVKAQVH AGGRGKGGGV
     ILCRSVKAVE AACEKLLGSN LITPQTDDKG LPINQLLIEG GQNIERELYL GLLVDRQTQK
     ITILASTEGG MDIEKVASET PEKIIKFGVD PLGALSTNDC ASIASQLNLN NTLTDQFITT
     LMGLYQIFIE KDVSLIEINP LITTAENTLL ALDGKIDFDD NALYRHEDIV TMRDKSQEDE
     KENEASEYQL NYISLDGTIG CMVNGAGLAM ATMDLIEHHG GSPANFLDVG GGTTADRVAK
     AFELIQTEAN VQGILVNIFG GIVRCDLIAE GILQAIEKVG LNLPIVVRLE GTNATAGLKL
     LDESTADIHT EADLTQAAIK IVELSKGVLQ
//
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