SAT3_ARATH
ID SAT3_ARATH Reviewed; 391 AA.
AC Q39218; Q0V7U9; Q0WWV4; Q42532; Q43739; Q43740; Q7DLZ8; Q7DM01;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Serine acetyltransferase 3, mitochondrial;
DE Short=AtSAT-3;
DE Short=AtSERAT2;2;
DE Short=SAT-m;
DE EC=2.3.1.30;
DE Flags: Precursor;
GN Name=SAT3; Synonyms=SAT1, SATA; OrderedLocusNames=At3g13110;
GN ORFNames=MJG19.6;
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. Columbia;
RX PubMed=8639741; DOI=10.1007/bf00020814;
RA Roberts M.A., Wray J.L.;
RT "Cloning and characterization of an Arabidopsis thaliana cDNA clone
RT encoding an organellar isoform of serine acetyltransferase.";
RL Plant Mol. Biol. 30:1041-1049(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-391.
RA Ruffet M.-L., Lebrun M., Droux M., Douce R.;
RT "Gene sequence of serine acetyltransferase 1 from A. thaliana.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-391.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-391 AND 80-391, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7821427; DOI=10.1016/0014-5793(94)01392-e;
RA Bogdanova N., Bork C., Hell R.;
RT "Cysteine biosynthesis in plants: isolation and functional identification
RT of a cDNA encoding a serine acetyltransferase from Arabidopsis thaliana.";
RL FEBS Lett. 358:43-47(1995).
RN [8]
RP SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9830017; DOI=10.1074/jbc.273.49.32739;
RA Noji M., Inoue K., Kimura N., Gouda A., Saito K.;
RT "Isoform-dependent differences in feedback regulation and subcellular
RT localization of serine acetyltransferase involved in cysteine biosynthesis
RT from Arabidopsis thaliana.";
RL J. Biol. Chem. 273:32739-32745(1998).
RN [9]
RP INTERACTION WITH OASC.
RX PubMed=10940562; DOI=10.1016/s0378-1119(00)00261-4;
RA Jost R., Berkowitz O., Wirtz M., Hopkins L., Hawkesford M.J., Hell R.;
RT "Genomic and functional characterization of the oas gene family encoding O-
RT acetylserine (thiol) lyases, enzymes catalyzing the final step in cysteine
RT biosynthesis in Arabidopsis thaliana.";
RL Gene 253:237-247(2000).
RN [10]
RP TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=12650624; DOI=10.1023/a:1022349623951;
RA Howarth J.R., Dominguez-Solis J.R., Gutierrez-Alcala G., Wray J.L.,
RA Romero L.C., Gotor C.;
RT "The serine acetyltransferase gene family in Arabidopsis thaliana and the
RT regulation of its expression by cadmium.";
RL Plant Mol. Biol. 51:589-598(2003).
RN [11]
RP TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15579666; DOI=10.1104/pp.104.045377;
RA Kawashima C.G., Berkowitz O., Hell R., Noji M., Saito K.;
RT "Characterization and expression analysis of a serine acetyltransferase
RT gene family involved in a key step of the sulfur assimilation pathway in
RT Arabidopsis.";
RL Plant Physiol. 137:220-230(2005).
RN [12]
RP COMPONENT OF THE CYSTEINE SYNTHASE COMPLEX.
RX PubMed=20720017; DOI=10.1074/jbc.m110.157446;
RA Wirtz M., Birke H., Heeg C., Mueller C., Hosp F., Throm C., Koenig S.,
RA Feldman-Salit A., Rippe K., Petersen G., Wade R.C., Rybin V., Scheffzek K.,
RA Hell R.;
RT "Structure and function of the hetero-oligomeric cysteine synthase complex
RT in plants.";
RL J. Biol. Chem. 285:32810-32817(2010).
RN [13]
RP INTERACTION WITH OASC, AND COMPONENT OF THE CYSTEINE SYNTHASE COMPLEX.
RX PubMed=22730323; DOI=10.1074/jbc.m112.372656;
RA Wirtz M., Beard K.F., Lee C.P., Boltz A., Schwarzlaender M., Fuchs C.,
RA Meyer A.J., Heeg C., Sweetlove L.J., Ratcliffe R.G., Hell R.;
RT "Mitochondrial cysteine synthase complex regulates O-acetylserine
RT biosynthesis in plants.";
RL J. Biol. Chem. 287:27941-27947(2012).
RN [14]
RP INTERACTION WITH OASC.
RX PubMed=23602110; DOI=10.1016/j.plantsci.2013.02.016;
RA Wawrzynska A., Kurzyk A., Mierzwinska M., Plochocka D., Wieczorek G.,
RA Sirko A.;
RT "Direct targeting of Arabidopsis cysteine synthase complexes with synthetic
RT polypeptides to selectively deregulate cysteine synthesis.";
RL Plant Sci. 207:148-157(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-serine = CoA + O-acetyl-L-serine;
CC Xref=Rhea:RHEA:24560, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:58340; EC=2.3.1.30;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.68 mM for L-Ser (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9830017};
CC KM=0.02 mM for acetyl-CoA (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9830017};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 1/2.
CC -!- SUBUNIT: Homomultimer (By similarity). Interacts with OASC. Component
CC of the cysteine synthase complex (CSC) composed of two OAS-TL dimers
CC and one SAT hexamer. {ECO:0000250, ECO:0000269|PubMed:10940562,
CC ECO:0000269|PubMed:22730323, ECO:0000269|PubMed:23602110}.
CC -!- INTERACTION:
CC Q39218; Q43725: OASC; NbExp=6; IntAct=EBI-1633440, EBI-1633616;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9830017}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher levels in leaves and
CC siliques. Localized in vascular tissues, particularly in phloem.
CC {ECO:0000269|PubMed:12650624, ECO:0000269|PubMed:15579666,
CC ECO:0000269|PubMed:7821427}.
CC -!- INDUCTION: By light, cadmium (Cd), and slightly by sulfur deficiency.
CC {ECO:0000269|PubMed:12650624, ECO:0000269|PubMed:15579666,
CC ECO:0000269|PubMed:7821427}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB02050.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA56913.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U22964; AAB07778.1; -; mRNA.
DR EMBL; AP000375; BAB01402.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75297.1; -; Genomic_DNA.
DR EMBL; BT026471; ABH04578.1; -; mRNA.
DR EMBL; L78443; AAB02050.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK226230; BAE98394.1; -; mRNA.
DR EMBL; X80938; CAA56913.1; ALT_INIT; mRNA.
DR EMBL; X82888; CAA58061.1; -; mRNA.
DR PIR; S68469; S68469.
DR PIR; S69192; S69192.
DR RefSeq; NP_187918.1; NM_112150.4.
DR AlphaFoldDB; Q39218; -.
DR SMR; Q39218; -.
DR BioGRID; 5833; 3.
DR DIP; DIP-40499N; -.
DR IntAct; Q39218; 1.
DR STRING; 3702.AT3G13110.1; -.
DR iPTMnet; Q39218; -.
DR PaxDb; Q39218; -.
DR PRIDE; Q39218; -.
DR ProteomicsDB; 232880; -.
DR EnsemblPlants; AT3G13110.1; AT3G13110.1; AT3G13110.
DR GeneID; 820499; -.
DR Gramene; AT3G13110.1; AT3G13110.1; AT3G13110.
DR KEGG; ath:AT3G13110; -.
DR Araport; AT3G13110; -.
DR TAIR; locus:2089974; AT3G13110.
DR eggNOG; KOG4750; Eukaryota.
DR HOGENOM; CLU_051638_0_2_1; -.
DR InParanoid; Q39218; -.
DR OMA; PICKNRE; -.
DR OrthoDB; 1337060at2759; -.
DR PhylomeDB; Q39218; -.
DR BioCyc; ARA:AT3G13110-MON; -.
DR BioCyc; MetaCyc:AT3G13110-MON; -.
DR BRENDA; 2.3.1.30; 399.
DR SABIO-RK; Q39218; -.
DR UniPathway; UPA00136; UER00199.
DR PRO; PR:Q39218; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39218; baseline and differential.
DR Genevisible; Q39218; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009001; F:serine O-acetyltransferase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0019344; P:cysteine biosynthetic process; IMP:TAIR.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR CDD; cd03354; LbH_SAT; 1.
DR Gene3D; 1.10.3130.10; -; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR045304; LbH_SAT.
DR InterPro; IPR010493; Ser_AcTrfase_N.
DR InterPro; IPR042122; Ser_AcTrfase_N_sf.
DR InterPro; IPR005881; Ser_O-AcTrfase.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF06426; SATase_N; 1.
DR SMART; SM00971; SATase_N; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR01172; cysE; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..391
FT /note="Serine acetyltransferase 3, mitochondrial"
FT /id="PRO_0000045777"
FT REGION 40..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 186
FT /note="V -> G (in Ref. 5; AAB02050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 42721 MW; A3ED09DEA53C10E2 CRC64;
MLPVTSRRHF TMSLYMLRSS SPHINHHSFL LPSFVSSKFK HHTLSPPPSP PPPPPMAACI
DTCRTGKPQI SPRDSSKHHD DESGFRYMNY FRYPDRSSFN GTQTKTLHTR PLLEDLDRDA
EVDDVWAKIR EEAKSDIAKE PIVSAYYHAS IVSQRSLEAA LANTLSVKLS NLNLPSNTLF
DLFSGVLQGN PDIVESVKLD LLAVKERDPA CISYVHCFLH FKGFLACQAH RIAHELWTQD
RKILALLIQN RVSEAFAVDF HPGAKIGTGI LLDHATAIVI GETAVVGNNV SILHNVTLGG
TGKQCGDRHP KIGDGVLIGA GTCILGNITI GEGAKIGAGS VVLKDVPPRT TAVGNPARLL
GGKDNPKTHD KIPGLTMDQT SHISEWSDYV I
