SAT1_ARATH
ID SAT1_ARATH Reviewed; 314 AA.
AC Q42588; Q0WT70; Q43297;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Serine acetyltransferase 1, chloroplastic;
DE Short=AtSAT-1;
DE EC=2.3.1.30 {ECO:0000305|PubMed:7851429, ECO:0000305|PubMed:9830017};
DE AltName: Full=AtSERAT2;1 {ECO:0000303|PubMed:15579666};
DE AltName: Full=SAT-p {ECO:0000303|PubMed:9830017};
GN Name=SAT1; Synonyms=SAT5 {ECO:0000303|PubMed:7851429};
GN OrderedLocusNames=At1g55920; ORFNames=F14J16.18;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8867790;
RA Murillo M., Foglia R., Diller A., Lee S., Leustek T.;
RT "Serine acetyltransferase from Arabidopsis thaliana can functionally
RT complement the cysteine requirement of a cysE mutant strain of Escherichia
RT coli.";
RL Cell. Mol. Biol. Res. 41:425-433(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=7851429; DOI=10.1111/j.1432-1033.1995.tb20416.x;
RA Ruffet M.-L., Lebrun M., Droux M., Douce R.;
RT "Subcellular distribution of serine acetyltransferase from Pisum sativum
RT and characterization of an Arabidopsis thaliana putative cytosolic
RT isoform.";
RL Eur. J. Biochem. 227:500-509(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP 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 [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10995473; DOI=10.1073/pnas.190334497;
RA Gutierrez-Alcala G., Gotor C., Meyer A.J., Fricker M., Vega J.M.,
RA Romero L.C.;
RT "Glutathione biosynthesis in Arabidopsis trichome cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:11108-11113(2000).
RN [9]
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 [10]
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 [11]
RP INTERACTION WITH OASA1.
RX PubMed=16166087; DOI=10.1074/jbc.m505313200;
RA Bonner E.R., Cahoon R.E., Knapke S.M., Jez J.M.;
RT "Molecular basis of cysteine biosynthesis in plants: structural and
RT functional analysis of o-acetylserine sulfhydrylase from Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 280:38803-38813(2005).
RN [12]
RP INTERACTION WITH CYP20-3.
RX PubMed=18845687; DOI=10.1073/pnas.0808204105;
RA Dominguez-Solis J.R., He Z., Lima A., Ting J., Buchanan B.B., Luan S.;
RT "A cyclophilin links redox and light signals to cysteine biosynthesis and
RT stress responses in chloroplasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:16386-16391(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 307-314, AND INTERACTION WITH
RP OASA1.
RX PubMed=17194764; DOI=10.1105/tpc.106.047316;
RA Francois J.A., Kumaran S., Jez J.M.;
RT "Structural basis for interaction of O-acetylserine sulfhydrylase and
RT serine acetyltransferase in the Arabidopsis cysteine synthase complex.";
RL Plant Cell 18:3647-3655(2006).
CC -!- FUNCTION: Serine acetyltransferase which catalyzes the formation of O-
CC acetyl-L-serine from acetyl-CoA and L-serine (PubMed:7851429,
CC PubMed:9830017). Also displays O-acetylserine (thio1)-lyase activity in
CC vitro (PubMed:7851429). May be involved in detoxification process by
CC mediating the production of glutathione. {ECO:0000269|PubMed:7851429,
CC ECO:0000269|PubMed:9830017}.
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 Evidence={ECO:0000305|PubMed:7851429, ECO:0000305|PubMed:9830017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24561;
CC Evidence={ECO:0000305|PubMed:7851429, ECO:0000305|PubMed:9830017};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.64 mM for L-Ser (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9830017};
CC KM=0.16 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 OASA1 and CYP20-
CC 3. Component of the cysteine synthase complex (CSC) composed of two
CC OAS-TL dimers and one SAT hexamer. {ECO:0000250,
CC ECO:0000269|PubMed:16166087, ECO:0000269|PubMed:17194764,
CC ECO:0000269|PubMed:18845687}.
CC -!- INTERACTION:
CC Q42588; P34791: CYP20-3; NbExp=3; IntAct=EBI-1633480, EBI-449385;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:9830017}. Cytoplasm {ECO:0000269|PubMed:9830017}.
CC Note=First chloroplastic and progressively cytoplasmic during aging.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves. Localized in cortex,
CC trichomes and vascular tissues, particularly in phloem.
CC {ECO:0000269|PubMed:10995473, ECO:0000269|PubMed:12650624,
CC ECO:0000269|PubMed:15579666, ECO:0000269|PubMed:8867790}.
CC -!- INDUCTION: By cadmium (Cd). Not induced under sulfur-deficient
CC conditions. Repressed in trichomes in response to NaCl treatment.
CC {ECO:0000269|PubMed:10995473, ECO:0000269|PubMed:12650624,
CC ECO:0000269|PubMed:15579666}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L42212; AAC37474.1; -; mRNA.
DR EMBL; L34076; AAA58608.1; -; Genomic_RNA.
DR EMBL; Z34888; CAA84371.1; -; Genomic_DNA.
DR EMBL; AC002304; AAF79319.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33320.1; -; Genomic_DNA.
DR EMBL; BT008309; AAP37668.1; -; mRNA.
DR EMBL; AK227691; BAE99678.1; -; mRNA.
DR PIR; S67482; S67482.
DR PIR; S71181; S71181.
DR RefSeq; NP_175988.1; NM_104470.3.
DR PDB; 2ISQ; X-ray; 2.80 A; B=307-314.
DR PDBsum; 2ISQ; -.
DR AlphaFoldDB; Q42588; -.
DR SMR; Q42588; -.
DR BioGRID; 27268; 2.
DR DIP; DIP-40647N; -.
DR IntAct; Q42588; 2.
DR STRING; 3702.AT1G55920.1; -.
DR PaxDb; Q42588; -.
DR PRIDE; Q42588; -.
DR ProteomicsDB; 232759; -.
DR EnsemblPlants; AT1G55920.1; AT1G55920.1; AT1G55920.
DR GeneID; 842043; -.
DR Gramene; AT1G55920.1; AT1G55920.1; AT1G55920.
DR KEGG; ath:AT1G55920; -.
DR Araport; AT1G55920; -.
DR TAIR; locus:2012085; AT1G55920.
DR eggNOG; KOG4750; Eukaryota.
DR HOGENOM; CLU_051638_0_1_1; -.
DR InParanoid; Q42588; -.
DR OMA; SHITEWS; -.
DR OrthoDB; 1337060at2759; -.
DR PhylomeDB; Q42588; -.
DR BioCyc; ARA:AT1G55920-MON; -.
DR BioCyc; MetaCyc:AT1G55920-MON; -.
DR BRENDA; 2.3.1.30; 399.
DR SABIO-RK; Q42588; -.
DR UniPathway; UPA00136; UER00199.
DR EvolutionaryTrace; Q42588; -.
DR PRO; PR:Q42588; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42588; baseline and differential.
DR Genevisible; Q42588; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009001; F:serine O-acetyltransferase activity; IDA:TAIR.
DR GO; GO:0009970; P:cellular response to sulfate starvation; IEP: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; 2.
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 3D-structure; Acyltransferase; Amino-acid biosynthesis; Chloroplast;
KW Cytoplasm; Plastid; Reference proteome; Transferase.
FT CHAIN 1..314
FT /note="Serine acetyltransferase 1, chloroplastic"
FT /id="PRO_0000068690"
FT CONFLICT 6
FT /note="D -> H (in Ref. 1; AAC37474)"
FT /evidence="ECO:0000305"
FT CONFLICT 24..25
FT /note="KN -> NK (in Ref. 1; AAC37474)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="E -> K (in Ref. 1; AAC37474)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="K -> E (in Ref. 1; AAC37474)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="A -> G (in Ref. 1; AAC37474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 34251 MW; 78FACE3DA5CE04B0 CRC64;
MATCIDTCRT GNTQDDDSRF CCIKNFFRPG FSVNRKIHHT QIEDDDDVWI KMLEEAKSDV
KQEPILSNYY YASITSHRSL ESALAHILSV KLSNLNLPSN TLFELFISVL EESPEIIEST
KQDLIAVKER DPACISYVHC FLGFKGFLAC QAHRIAHTLW KQNRKIVALL IQNRVSESFA
VDIHPGAKIG KGILLDHATG VVIGETAVVG DNVSILHGVT LGGTGKQSGD RHPKIGDGVL
IGAGSCILGN ITIGEGAKIG SGSVVVKDVP ARTTAVGNPA RLIGGKENPR KHDKIPCLTM
DQTSYLTEWS DYVI
