SAT5_ARATH
ID SAT5_ARATH Reviewed; 312 AA.
AC Q42538; Q0WSF3; Q8LFG6;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Serine acetyltransferase 5;
DE Short=AtSAT-5;
DE EC=2.3.1.30;
DE AltName: Full=AtSERAT1;1;
DE AltName: Full=SAT-c;
GN Name=SAT5; Synonyms=SAT52; OrderedLocusNames=At5g56760; ORFNames=MIK19.23;
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=9048879; DOI=10.1016/s0167-4781(96)00213-8;
RA Howarth J.R., Roberts M.A., Wray J.L.;
RT "Cysteine biosynthesis in higher plants: a new member of the Arabidopsis
RT thaliana serine acetyltransferase small gene-family obtained by functional
RT complementation of an Escherichia coli cysteine auxotroph.";
RL Biochim. Biophys. Acta 1350:123-127(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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].
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 [6]
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 [7]
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, 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.
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 [9]
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).
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 -!- ACTIVITY REGULATION: Feedback inhibitions by L-Ser and acetyl-CoA.
CC {ECO:0000269|PubMed:9830017}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.71 mM for L-Ser (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9830017};
CC KM=0.28 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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9830017}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems, flowers and siliques.
CC Localized in vascular tissues, particularly in phloem.
CC {ECO:0000269|PubMed:12650624, ECO:0000269|PubMed:15579666}.
CC -!- INDUCTION: By cadmium (Cd). Not induced 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}.
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DR EMBL; U30298; AAC49655.1; -; mRNA.
DR EMBL; AB013392; BAB09894.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96804.1; -; Genomic_DNA.
DR EMBL; AY039612; AAK62667.1; -; mRNA.
DR EMBL; AY133674; AAM91504.1; -; mRNA.
DR EMBL; AK227979; BAE99945.1; -; mRNA.
DR EMBL; AY084861; AAM61424.1; -; mRNA.
DR PIR; S71207; S71207.
DR RefSeq; NP_200487.1; NM_125059.3.
DR AlphaFoldDB; Q42538; -.
DR SMR; Q42538; -.
DR BioGRID; 21022; 9.
DR IntAct; Q42538; 1.
DR STRING; 3702.AT5G56760.1; -.
DR iPTMnet; Q42538; -.
DR PaxDb; Q42538; -.
DR PRIDE; Q42538; -.
DR ProteomicsDB; 226618; -.
DR EnsemblPlants; AT5G56760.1; AT5G56760.1; AT5G56760.
DR GeneID; 835778; -.
DR Gramene; AT5G56760.1; AT5G56760.1; AT5G56760.
DR KEGG; ath:AT5G56760; -.
DR Araport; AT5G56760; -.
DR TAIR; locus:2164996; AT5G56760.
DR eggNOG; KOG4750; Eukaryota.
DR HOGENOM; CLU_051638_0_1_1; -.
DR InParanoid; Q42538; -.
DR OMA; HPKIRHG; -.
DR OrthoDB; 1337060at2759; -.
DR PhylomeDB; Q42538; -.
DR BioCyc; ARA:AT5G56760-MON; -.
DR BioCyc; MetaCyc:AT5G56760-MON; -.
DR BRENDA; 2.3.1.30; 399.
DR SABIO-RK; Q42538; -.
DR UniPathway; UPA00136; UER00199.
DR PRO; PR:Q42538; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q42538; baseline and differential.
DR Genevisible; Q42538; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009001; F:serine O-acetyltransferase activity; IBA:GO_Central.
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 Acyltransferase; Amino-acid biosynthesis; Cytoplasm; Reference proteome;
KW Transferase.
FT CHAIN 1..312
FT /note="Serine acetyltransferase 5"
FT /id="PRO_0000068693"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 23
FT /note="S -> F (in Ref. 5; AAM61424)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="S -> A (in Ref. 5; AAM61424)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 32770 MW; 15835510FF314A08 CRC64;
MPPAGELRHQ SPSKEKLSSV TQSDEAEAAS AAISAAAADA EAAGLWTQIK AEARRDAEAE
PALASYLYST ILSHSSLERS ISFHLGNKLC SSTLLSTLLY DLFLNTFSSD PSLRNATVAD
LRAARVRDPA CISFSHCLLN YKGFLAIQAH RVSHKLWTQS RKPLALALHS RISDVFAVDI
HPAAKIGKGI LLDHATGVVV GETAVIGNNV SILHHVTLGG TGKACGDRHP KIGDGCLIGA
GATILGNVKI GAGAKVGAGS VVLIDVPCRG TAVGNPARLV GGKEKPTIHD EECPGESMDH
TSFISEWSDY II
