SUCA3_TRIVA
ID SUCA3_TRIVA Reviewed; 309 AA.
AC P53401;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha-3, 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-3 {ECO:0000255|HAMAP-Rule:MF_03222};
DE Short=SCS-alpha-3 {ECO:0000255|HAMAP-Rule:MF_03222};
DE Flags: Precursor;
GN Name=ALPHA-SCS3;
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=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;
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}.
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DR EMBL; L31931; AAC41560.1; -; Genomic_DNA.
DR AlphaFoldDB; P53401; -.
DR SMR; P53401; -.
DR STRING; 5722.XP_001328129.1; -.
DR VEuPathDB; TrichDB:TVAG_047890; -.
DR eggNOG; KOG1255; Eukaryota.
DR OMA; TVIFIPP; -.
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:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:RHEA.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.261; -; 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-3,
FT mitochondrial"
FT /id="PRO_0000033349"
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; 32513 MW; 9D62F7FA7AFFE768 CRC64;
MLSSSFERNL HQPLLFIDKD TKVVIQGIGN QGQFHSRLMR QYGTKVVGAV HPKKAGSIIA
GLPIFKNMKE VVKRTDANAS LIFVPAPGAA AACIEAAQAG MGLVVCITEH IPQHDMIKVK
KVMKETGCQL IGPNCPGLIQ PGTHTKLGII PTNIFNNGKI GIVSRSGTLT YEAAYATTLA
GLGQSTVVGI GGDPFAGQLH TDVVKRFAAD PQTEGIILIG EIGGTSEEDA AEWIAKTKLT
QEKPVVAFIA GATAPPGKRM GHAGAIVSGG KGTAEGKYKA LEAAGVRIAR HPGNMGKFIF
EEMKRMGKI
