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Entry: A0A3B7MS66_9BACT
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ID   A0A3B7MS66_9BACT        Unreviewed;       291 AA.
AC   A0A3B7MS66;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha {ECO:0000256|HAMAP-Rule:MF_01988};
DE            EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_01988};
DE   AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01988};
DE            Short=SCS-alpha {ECO:0000256|HAMAP-Rule:MF_01988};
GN   Name=sucD {ECO:0000256|HAMAP-Rule:MF_01988};
GN   ORFNames=D3H65_18300 {ECO:0000313|EMBL:AXY75816.1};
OS   Paraflavitalea soli.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Paraflavitalea.
OX   NCBI_TaxID=2315862 {ECO:0000313|EMBL:AXY75816.1, ECO:0000313|Proteomes:UP000263900};
RN   [1] {ECO:0000313|EMBL:AXY75816.1, ECO:0000313|Proteomes:UP000263900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5GH32-13 {ECO:0000313|EMBL:AXY75816.1,
RC   ECO:0000313|Proteomes:UP000263900};
RA   Weon H.-Y., Heo J., Kwon S.-W.;
RT   "Genome sequencing of strain 6GH32-13.";
RL   Submitted (SEP-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 alpha subunit of the enzyme binds the
CC       substrates coenzyme A and phosphate, while succinate binding and
CC       nucleotide specificity is provided by the beta subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_01988, ECO:0000256|RuleBase:RU000699}.
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_01988, ECO:0000256|RuleBase:RU000699};
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_01988};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01988, ECO:0000256|RuleBase:RU000699}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_01988, ECO:0000256|RuleBase:RU000699}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC       family. {ECO:0000256|HAMAP-Rule:MF_01988,
CC       ECO:0000256|RuleBase:RU000677}.
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DR   EMBL; CP032157; AXY75816.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B7MS66; -.
DR   KEGG; pseg:D3H65_18300; -.
DR   OrthoDB; 9807196at2; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000263900; Chromosome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR   HAMAP; MF_01988; Succ_CoA_alpha; 1.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR   InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR005810; CoA_lig_alpha.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   NCBIfam; TIGR01019; sucCoAalpha; 1.
DR   PANTHER; PTHR11117:SF2; SUCCINATE--COA LIGASE [ADP/GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001553; SucCS_alpha; 1.
DR   PRINTS; PR01798; SCOASYNTHASE.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01988, ECO:0000256|RuleBase:RU000677};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01988}; Reference proteome {ECO:0000313|Proteomes:UP000263900};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW   Rule:MF_01988}.
FT   DOMAIN          4..100
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
FT   ACT_SITE        248
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01988,
FT                   ECO:0000256|PIRSR:PIRSR001553-1"
FT   BINDING         17..20
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
FT   BINDING         43
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
FT   BINDING         96..98
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit beta"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
SQ   SEQUENCE   291 AA;  29922 MW;  232AB07A742133FF CRC64;
     MSILVNKQSK ILVQGFTGTE GTFHATQMIE YGTNVVGGVT PNKGGTTHLD RPVFNTVAEA
     VHTTGANVSI IFVPPAFAAD AIMEAAEAGI GLVVCITEGI PVQDMVKAKL FLQSTGTRLI
     GPNCPGVITA GECKVGIMPG FVFKKGKIGI VSKSGTLTYE ASDQVAKAGL GVSTAVGIGG
     DPIIGTTTKE ALEMFMNDPE TEGIVMIGEI GGGMEAEAAR WYKEQKVKKP VVGFIAGQTA
     PPGRRMGHAG AIVGGAEDTA AAKMAIMEEC GINVVSSPAD IGATMARIIK K
//
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