SAT4_ARATH
ID SAT4_ARATH Reviewed; 355 AA.
AC Q8W2B8; O81795;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Serine acetyltransferase 4 {ECO:0000303|Ref.1};
DE Short=AtSAT-4 {ECO:0000303|Ref.1};
DE Short=AtSERAT3;2 {ECO:0000303|PubMed:15579666};
DE EC=2.3.1.30 {ECO:0000269|PubMed:15579666};
GN Name=SAT4 {ECO:0000303|Ref.1};
GN OrderedLocusNames=At4g35640 {ECO:0000312|Araport:AT4G35640};
GN ORFNames=F8D20.150 {ECO:0000312|EMBL:CAA20034.1};
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 [GENOMIC DNA].
RA Buisson S., Droux M.;
RT "Characterization of a new serine acetyltransferase (SAT4) from Arabidopsis
RT thaliana.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY,
RP PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, GENE FAMILY,
RP 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 -!- ACTIVITY REGULATION: Feedback inhibitions by L-Ser and acetyl-CoA.
CC {ECO:0000269|PubMed:15579666}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=39.5 mM for L-Ser (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:15579666};
CC KM=45.1 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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15579666}.
CC -!- TISSUE SPECIFICITY: Localized in vascular tissues, particularly in
CC phloem. {ECO:0000269|PubMed:15579666}.
CC -!- INDUCTION: By cadmium (Cd). Induced in roots and shoots under sulfur-
CC deficient conditions. {ECO:0000269|PubMed:15579666}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA20034.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80280.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF331847; AAL37489.1; -; Genomic_DNA.
DR EMBL; AL031135; CAA20034.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161587; CAB80280.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86543.1; -; Genomic_DNA.
DR EMBL; BT004080; AAO42107.1; -; mRNA.
DR EMBL; BT005047; AAO50580.1; -; mRNA.
DR PIR; T04669; T04669.
DR RefSeq; NP_195289.3; NM_119729.4.
DR AlphaFoldDB; Q8W2B8; -.
DR SMR; Q8W2B8; -.
DR BioGRID; 14998; 2.
DR STRING; 3702.AT4G35640.1; -.
DR iPTMnet; Q8W2B8; -.
DR PaxDb; Q8W2B8; -.
DR PRIDE; Q8W2B8; -.
DR ProteomicsDB; 226688; -.
DR EnsemblPlants; AT4G35640.1; AT4G35640.1; AT4G35640.
DR GeneID; 829716; -.
DR Gramene; AT4G35640.1; AT4G35640.1; AT4G35640.
DR KEGG; ath:AT4G35640; -.
DR Araport; AT4G35640; -.
DR TAIR; locus:2127978; AT4G35640.
DR eggNOG; KOG4750; Eukaryota.
DR HOGENOM; CLU_051638_0_0_1; -.
DR InParanoid; Q8W2B8; -.
DR OMA; HSIRLDI; -.
DR OrthoDB; 1337060at2759; -.
DR PhylomeDB; Q8W2B8; -.
DR BRENDA; 2.3.1.30; 399.
DR SABIO-RK; Q8W2B8; -.
DR UniPathway; UPA00136; UER00199.
DR PRO; PR:Q8W2B8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W2B8; baseline and differential.
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; 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; Cytoplasm; Reference proteome;
KW Transferase.
FT CHAIN 1..355
FT /note="Serine acetyltransferase 4"
FT /id="PRO_0000068692"
SQ SEQUENCE 355 AA; 38424 MW; 3BF39845776C0EC7 CRC64;
MACINGENRD FSSSSSLSSL PMIVSRNFSA RDDGETGDEF PFERIFPVYA RGTLNPVADP
VLLDFTNSSY DPIWDSIREE AKLEAEEEPV LSSFLYASIL SHDCLEQALS FVLANRLQNP
TLLATQLMDI FCNVMVHDRG IQSSIRLDVQ AFKDRDPACL SYSSAILHLK GYLALQAYRV
AHKLWKQGRK LLALALQSRV SEVFGIDIHP AARIGKGILL DHGTGVVIGE TAVIGDRVSI
LHGVTLGGTG KETGDRHPNI GDGALLGACV TILGNIKIGA GAMVAAGSLV LKDVPSHSMV
AGNPAKLIGF VDEQDPSMTM EHDATREFFQ NVAVAYRETI PNGSSVSGSC RERRH
