SUCA_BLAHN
ID SUCA_BLAHN Reviewed; 318 AA.
AC B3FHT4; B3FHN9;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha {ECO:0000305|PubMed:18452512};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:18452512};
DE AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000303|PubMed:18452512};
DE Short=SCS-alpha {ECO:0000255|HAMAP-Rule:MF_03222};
DE Flags: Precursor;
GN Name=SCSa;
OS Blastocystis sp. subtype 1 (strain ATCC 50177 / NandII).
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=478820;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 50177 / NandII;
RX PubMed=18452512; DOI=10.1111/j.1365-2958.2008.06228.x;
RA Hamblin K., Standley D.M., Rogers M.B., Stechmann A., Roger A.J.,
RA Maytum R., van der Giezen M.;
RT "Localization and nucleotide specificity of Blastocystis succinyl-CoA
RT synthetase.";
RL Mol. Microbiol. 68:1395-1405(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50177 / NandII;
RA Gentekaki E., Curtis B., Stairs C., Eme L., Herman E., Klimes V.,
RA Arias M.C., Elias M., Hilliou F., Klute M., Malik S.-B., Pightling A.,
RA Rachubinski R., Salas D., Schlacht A., Suga H., Archibald J., Ball S.G.,
RA Clark G., Dacks J., Van Der Giezen M., Tsaousis A., Roger A.;
RT "Nuclear genome of Blastocystis sp. subtype 1 NandII.";
RL Submitted (MAY-2016) 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 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 ECO:0000269|PubMed:18452512}.
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, ECO:0000269|PubMed:18452512};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 133 min(-1) with ATP as substrate.
CC {ECO:0000269|PubMed:18452512};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03222, ECO:0000305|PubMed:18452512}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC {ECO:0000255|HAMAP-Rule:MF_03222}.
CC -!- SUBCELLULAR LOCATION: Hydrogenosome {ECO:0000269|PubMed:18452512}.
CC Note=Found in the matrix of the mitochondrion-like organelles (MLO) of
CC Blastocystis. {ECO:0000269|PubMed:18452512}.
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; EU076378; ABY62723.1; -; mRNA.
DR EMBL; EU090061; ABW76150.1; -; Genomic_DNA.
DR EMBL; LXWW01000228; OAO14631.1; -; Genomic_DNA.
DR AlphaFoldDB; B3FHT4; -.
DR SMR; B3FHT4; -.
DR STRING; 478820.B3FHT4; -.
DR OrthoDB; 1247548at2759; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000078348; Unassembled WGS sequence.
DR GO; GO:0042566; C:hydrogenosome; 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 Hydrogenosome; Ligase; Nucleotide-binding; Reference proteome;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..18
FT /note="Hydrogenosome"
FT /evidence="ECO:0000255"
FT CHAIN 19..318
FT /note="Succinate--CoA ligase [ADP-forming] subunit alpha"
FT /id="PRO_0000438594"
FT ACT_SITE 271
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 38..41
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 64
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 117..119
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 181
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
SQ SEQUENCE 318 AA; 33380 MW; 9BAC52317C9237E1 CRC64;
MLSRVSQVSR VGFSLARASS TARVWVDKNT RVIGQGITGK NGTFHTQQAI EYGTKMVGGV
NPKKAGTTHL GLPIFASVEE AKKATNADAT VIYVPPSGAA GAILEAVAAE IPLIVCITEG
IPQHDMLRVK DIMKSQNKSR LIGPNCPGII KPEECKIGIM PGYIHKKGKI GIVSRSGTLT
YEAVHQTTMY GLGQSTVVGI GGDPFNGTNF IDCLERFTND PQTEGIVMIG EIGGTAEEDA
AEWLKQYGNP NKPVVSFIAG RTAPPGRRMG HAGAIISGGK GTAKAKMEAL TSAGVKVVET
PAMIGEAMFN MMKAAGKA
