SUCA2_ARATH
ID SUCA2_ARATH Reviewed; 341 AA.
AC Q8LAD2; O82661; P53586; Q9FMX5;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
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;
GN OrderedLocusNames=At5g23250; ORFNames=MKD15.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. C24; TISSUE=Flower bud;
RA Yu D.-Y., Quigley F., Mache R.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-116.
RC STRAIN=cv. C24; TISSUE=Flower bud;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-37.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
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: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222,
CC ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8LAD2-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_03222}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA48891.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA79188.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X69138; CAA48891.1; ALT_FRAME; mRNA.
DR EMBL; AB007648; BAB11180.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93141.1; -; Genomic_DNA.
DR EMBL; AY092994; AAM12993.1; -; mRNA.
DR EMBL; AY114607; AAM47926.1; -; mRNA.
DR EMBL; AY087899; AAM65450.1; -; mRNA.
DR EMBL; Z18444; CAA79188.1; ALT_FRAME; mRNA.
DR PIR; S30579; S30579.
DR RefSeq; NP_197716.1; NM_122231.4. [Q8LAD2-1]
DR AlphaFoldDB; Q8LAD2; -.
DR SMR; Q8LAD2; -.
DR BioGRID; 17664; 18.
DR STRING; 3702.AT5G23250.1; -.
DR iPTMnet; Q8LAD2; -.
DR PaxDb; Q8LAD2; -.
DR PRIDE; Q8LAD2; -.
DR ProteomicsDB; 245231; -. [Q8LAD2-1]
DR EnsemblPlants; AT5G23250.1; AT5G23250.1; AT5G23250. [Q8LAD2-1]
DR GeneID; 832389; -.
DR Gramene; AT5G23250.1; AT5G23250.1; AT5G23250. [Q8LAD2-1]
DR KEGG; ath:AT5G23250; -.
DR Araport; AT5G23250; -.
DR TAIR; locus:2166756; AT5G23250.
DR eggNOG; KOG1255; Eukaryota.
DR InParanoid; Q8LAD2; -.
DR OMA; GEGMKHT; -.
DR OrthoDB; 1247548at2759; -.
DR PhylomeDB; Q8LAD2; -.
DR BioCyc; ARA:AT5G23250-MON; -.
DR UniPathway; UPA00223; UER00999.
DR PRO; PR:Q8LAD2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LAD2; baseline and differential.
DR Genevisible; Q8LAD2; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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 Alternative splicing; Ligase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 38..341
FT /note="Succinate--CoA ligase [ADP-forming] subunit alpha-2,
FT mitochondrial"
FT /id="PRO_0000033336"
FT ACT_SITE 293
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 61..64
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 87
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 140..142
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 204
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT CONFLICT 22
FT /note="S -> T (in Ref. 1; CAA48891 and 6; CAA79188)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="A -> R (in Ref. 1; CAA48891)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="I -> T (in Ref. 4; AAM65450)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="I -> L (in Ref. 1; CAA48891)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 35317 MW; 5BFA16519C429FE7 CRC64;
MSRQVTRLLG SLRHSGGGCS GSSKVCSLTS LVQSRSFGTT PPPPAAVFVD KNTRVICQGI
TGKNGTFHTE QAIEYGTKMV AGVTPKKGGT EHLGLPVFNT VAEAKAETKA NASVIYVPAP
FAAAAIMEGL AAELDLIVCI TEGIPQHDMV RVKAALNSQS KTRLIGPNCP GIIKPGECKI
GIMPGYIHKP GKIGIVSRSG TLTYEAVFQT TAVGLGQSTC VGIGGDPFNG TNFVDCLEKF
FVDPQTEGIV LIGEIGGTAE EDAAALIKEN GTDKPVVAFI AGLTAPPGRR MGHAGAIVSG
GKGTAQDKIK SLRDAGVKVV ESPAKIGAAM FELFQERGLL K
