SUCA2_SOLLC
ID SUCA2_SOLLC Reviewed; 337 AA.
AC Q6DQL1;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha-2, 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-2 {ECO:0000255|HAMAP-Rule:MF_03222};
DE Short=SCS-alpha-2 {ECO:0000255|HAMAP-Rule:MF_03222};
DE Flags: Precursor;
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=Root;
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; AY650029; AAT67464.1; -; mRNA.
DR RefSeq; NP_001234574.1; NM_001247645.2.
DR AlphaFoldDB; Q6DQL1; -.
DR SMR; Q6DQL1; -.
DR STRING; 4081.Solyc02g005350.2.1; -.
DR PaxDb; Q6DQL1; -.
DR PRIDE; Q6DQL1; -.
DR GeneID; 543943; -.
DR KEGG; sly:543943; -.
DR eggNOG; KOG1255; Eukaryota.
DR OrthoDB; 1247548at2759; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q6DQL1; 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..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT CHAIN 36..337
FT /note="Succinate--CoA ligase [ADP-forming] subunit alpha-2,
FT mitochondrial"
FT /id="PRO_0000402565"
FT ACT_SITE 290
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 58..61
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 84
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 137..139
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 201
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
SQ SEQUENCE 337 AA; 35375 MW; 5531B0703BD3DF0D CRC64;
MARQATRLIS NLSTKLNPSS PTMSASPLWH QYRYFGSPPP PPAVFVDKNT RVICQGITGK
NGTFHTEQAI EYGTKMVGGV TPKKGGTEHL GLPVFNTVAE AKVETKANAS VVYVPPPFAA
AAIMEAMEAE LDLVVCITEG IPQHDMVRVK AALKKQLRTR LIGPNCPGII KPGECKIGIM
PGYIHKPGRI GIVSRSGTLT YEAVFQTTAV GLGQSTCVGI GGDPFNGTNF VDCLERFIAD
PQTEGIVLIG EIGGTAEEDA AALIKESGTQ KPVVAFIAGL TAPPGRRMGH AGAIVSGGKG
TAQDKIKALK EAGVTVCESP AKIGVTMLDV FKQRGLA
