SUCA1_SOLLC
ID SUCA1_SOLLC Reviewed; 332 AA.
AC Q8GTQ9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=SCOA;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Moneymaker; TISSUE=Leaf;
RX PubMed=16270230; DOI=10.1007/s11103-005-1004-1;
RA Studart-Guimaraes C., Gibon Y., Frankel N., Wood C.C., Zanor M.I.,
RA Fernie A.R., Carrari F.;
RT "Identification and characterisation of the alpha and beta subunits of
RT succinyl CoA ligase of tomato.";
RL Plant Mol. Biol. 59:781-791(2005).
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, ECO:0000269|PubMed:16270230};
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: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222,
CC ECO:0000269|PubMed:16270230}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers, leaves and
CC fruits. {ECO:0000269|PubMed:16270230}.
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; AY167586; AAN86619.1; -; mRNA.
DR AlphaFoldDB; Q8GTQ9; -.
DR SMR; Q8GTQ9; -.
DR STRING; 4081.Solyc01g007910.2.1; -.
DR PaxDb; Q8GTQ9; -.
DR PRIDE; Q8GTQ9; -.
DR eggNOG; KOG1255; Eukaryota.
DR InParanoid; Q8GTQ9; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q8GTQ9; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IDA:UniProtKB.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR GO; GO:0006105; P:succinate metabolic process; IDA:UniProtKB.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IDA:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:UniProtKB.
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 Ligase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT CHAIN 24..332
FT /note="Succinate--CoA ligase [ADP-forming] subunit alpha-1,
FT mitochondrial"
FT /id="PRO_0000402564"
FT ACT_SITE 285
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 53..56
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 79
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 132..134
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 196
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
SQ SEQUENCE 332 AA; 34684 MW; A47254516B53A6DF CRC64;
MARQATKLIA NLSKKLSSSN PHTRCSEQTV WIGAAPPAVF VDKNTRVICQ GITGKNGTFH
TEQAIEYGTK MVGGVTPKKG GTEHLGLPVF NTVEEAKAET KANASVIYVP PPFAAAAIME
GLEAELDLIV CITEGIPQHD MVRVKAALKK QSRTRLIGPN CPGIIKPGEC KIGIMPGYIH
KPGRIGIVSR SGTLTYEAVF QTTAVGLGQS TCVGIGGDPF NGTNFVDCLE KFIADPQTEG
IVLIGEIGGT AEEDAAALIK ESGTQKPVVA FIAGLTAPPG RRMGHAGAIV SGGKGTAQDK
IKALKEAGVT VCESPAKIGV SMLEVFKQRG LV
