ID   SUCA1_TRIVA             Reviewed;         309 AA.
AC   P53399;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha-1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03222};
DE            EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03222};
DE   AltName: Full=Succinyl-CoA synthetase subunit alpha-1 {ECO:0000255|HAMAP-Rule:MF_03222};
DE            Short=SCS-alpha-1 {ECO:0000255|HAMAP-Rule:MF_03222};
DE   Flags: Precursor;
GN   Name=ALPHA-SCS1;
OS   Trichomonas vaginalis.
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=5722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 10-25, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 30001 / NIH-C1;
RX   PubMed=7808480; DOI=10.1016/0166-6851(94)90157-0;
RA   Lahti C.J., Bradley P.J., Johnson P.J.;
RT   "Molecular characterization of the alpha-subunit of Trichomonas vaginalis
RT   hydrogenosomal succinyl CoA synthetase.";
RL   Mol. Biochem. Parasitol. 66:309-318(1994).
CC   -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC       (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP
CC       and thus represents the only step of substrate-level phosphorylation in
CC       the TCA. The alpha subunit of the enzyme binds the substrates coenzyme
CC       A and phosphate, while succinate binding and nucleotide specificity is
CC       provided by the beta subunit. {ECO:0000255|HAMAP-Rule:MF_03222}.
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_03222};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_03222}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_03222}.
CC   -!- SUBCELLULAR LOCATION: Hydrogenosome lumen {ECO:0000269|PubMed:7808480}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_03222}.
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; L31929; AAC41558.1; -; Genomic_DNA.
DR   AlphaFoldDB; P53399; -.
DR   SMR; P53399; -.
DR   STRING; 5722.XP_001300482.1; -.
DR   VEuPathDB; TrichDB:TVAG_047890; -.
DR   eggNOG; KOG1255; Eukaryota.
DR   UniPathway; UPA00223; UER00999.
DR   GO; GO:0034492; C:hydrogenosome lumen; IEA:UniProtKB-SubCell.
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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.261; -; 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   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001553; SucCS_alpha; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   TIGRFAMs; TIGR01019; sucCoAalpha; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrogenosome; Ligase; Nucleotide-binding;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..9
FT                   /note="Hydrogenosome"
FT                   /evidence="ECO:0000269|PubMed:7808480"
FT   CHAIN           10..309
FT                   /note="Succinate--CoA ligase [ADP-forming] subunit alpha-1,
FT                   mitochondrial"
FT                   /id="PRO_0000033345"
FT   ACT_SITE        262
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         54
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         107..109
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit beta"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
SQ   SEQUENCE   309 AA;  32408 MW;  47FB103451F1E5E3 CRC64;
     MLAGDFSRNL HKPLLFIDKD TKVVIQGIGN QGQFHSRLMR QYGTKVVGAV HPKKAGTIIA
     GLPIFKNMKE VVKRTDANAS LIFVPAPGAA AACIEAAEAG MGLVVCITEH IPQHDMIKVK
     KVMKETGCQL IGPNCPGLIQ PGTHTKLGII PTNIFNNGKI GIVSRSGTLT YEAAYATTLA
     GLGQSTVVGI GGDPFAGQLH TDVVKRFAAD PQTEGIILIG EIGGTSEEDA AEWIAKTKLT
     QEKPVVASIA GATAPPGKRM GHAGAIVSGG KGTAEGKYKA LEAAGVRIAR HPGNMGKFIF
     EEMKRMGKI