SAT2_ARATH
ID SAT2_ARATH Reviewed; 323 AA.
AC Q8S895; Q29Q39; Q9STB0; Q9ZPJ4;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Serine acetyltransferase 2 {ECO:0000303|PubMed:15579666};
DE Short=AtSAT-2 {ECO:0000303|PubMed:15579666};
DE Short=AtSERAT3;1 {ECO:0000303|PubMed:15579666};
DE EC=2.3.1.30 {ECO:0000269|PubMed:15579666};
GN Name=SAT2 {ECO:0000303|PubMed:15579666};
GN Synonyms=SAT106 {ECO:0000303|PubMed:12650624};
GN OrderedLocusNames=At2g17640 {ECO:0000312|Araport:AT2G17640};
GN ORFNames=T17A5.1, T19E12.2 {ECO:0000312|EMBL:AAM15485.1};
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], INDUCTION, TISSUE SPECIFICITY, AND SUBUNIT.
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Ruffet M.-L., Lebrun M., Droux M., Douce R.;
RT "Gene sequence of serine acetyltransferase 2 from A. thaliana.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR
RP LOCATION, 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).
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:0000269|PubMed:15579666};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24561;
CC Evidence={ECO:0000269|PubMed:15579666};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=121.4 mM for L-Ser (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15579666};
CC KM=24.5 mM for acetyl-CoA (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15579666};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 1/2. {ECO:0000269|PubMed:15579666}.
CC -!- SUBUNIT: Homomultimer. {ECO:0000303|PubMed:12650624}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15579666}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels. Localized in
CC vascular tissues, particularly in phloem. {ECO:0000269|PubMed:12650624,
CC ECO:0000269|PubMed:15579666}.
CC -!- INDUCTION: By cadmium (Cd). Induced in roots under sulfur-deficient
CC conditions. {ECO:0000269|PubMed:12650624, ECO:0000269|PubMed:15579666}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD45614.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM15485.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF112303; AAD19963.1; -; mRNA.
DR EMBL; L78444; AAD45614.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007509; AAM15485.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06660.1; -; Genomic_DNA.
DR EMBL; AK176573; BAD44336.1; -; mRNA.
DR EMBL; BT024717; ABD59055.1; -; mRNA.
DR PIR; T08867; T08867.
DR RefSeq; NP_565421.1; NM_127318.5.
DR AlphaFoldDB; Q8S895; -.
DR SMR; Q8S895; -.
DR STRING; 3702.AT2G17640.1; -.
DR PaxDb; Q8S895; -.
DR PRIDE; Q8S895; -.
DR ProteomicsDB; 232686; -.
DR EnsemblPlants; AT2G17640.1; AT2G17640.1; AT2G17640.
DR GeneID; 816271; -.
DR Gramene; AT2G17640.1; AT2G17640.1; AT2G17640.
DR KEGG; ath:AT2G17640; -.
DR Araport; AT2G17640; -.
DR TAIR; locus:2057254; AT2G17640.
DR eggNOG; KOG4750; Eukaryota.
DR HOGENOM; CLU_051638_0_0_1; -.
DR InParanoid; Q8S895; -.
DR OMA; DVIMHDR; -.
DR OrthoDB; 1337060at2759; -.
DR PhylomeDB; Q8S895; -.
DR BRENDA; 2.3.1.30; 399.
DR SABIO-RK; Q8S895; -.
DR UniPathway; UPA00136; UER00199.
DR PRO; PR:Q8S895; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S895; baseline and differential.
DR Genevisible; Q8S895; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009001; F:serine O-acetyltransferase activity; IDA:TAIR.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; TAS:TAIR.
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 Acyltransferase; Amino-acid biosynthesis; Cytoplasm; Reference proteome;
KW Transferase.
FT CHAIN 1..323
FT /note="Serine acetyltransferase 2"
FT /id="PRO_0000068691"
FT REGION 302..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 34534 MW; 8CE538962B44E610 CRC64;
MNGDELPFES GFEVYAKGTH KSEFDSNLLD PRSDPIWDAI REEAKLEAEK EPILSSFLYA
GILAHDCLEQ ALGFVLANRL QNPTLLATQL LDIFYGVMMH DKGIQSSIRH DLQAFKDRDP
ACLSYSSAIL HLKGYHALQA YRVAHKLWNE GRKLLALALQ SRISEVFGID IHPAARIGEG
ILLDHGTGVV IGETAVIGNG VSILHGVTLG GTGKETGDRH PKIGEGALLG ACVTILGNIS
IGAGAMVAAG SLVLKDVPSH SVVAGNPAKL IRVMEEQDPS LAMKHDATKE FFRHVADGYK
GAQSNGPSLS AGDTEKGHTN STS
