Q8W2B8 (SAT4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine acetyltransferase 4
Short name=AtSAT-4
Short name=AtSERAT3;2
EC=2.3.1.30

Gene names

Name:	SAT4
Ordered Locus Names:	At4g35640
ORF Names:	F8D20.150

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine.
Enzyme regulation	Feedback inhibitions by L-Ser and acetyl-CoA. Ref.5
Pathway	Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
Subunit structure	Homomultimer By similarity.
Subcellular location	Cytoplasm Ref.5.
Tissue specificity	Localized in vascular tissues, particularly in phloem. Ref.5
Induction	By cadmium (Cd). Induced in roots and shoots under sulfur-deficient conditions. Ref.5
Sequence similarities	Belongs to the transferase hexapeptide repeat family.
Biophysicochemical properties	Kinetic parameters: KM=39.5 mM for L-Ser (at pH 8 and 30 degrees Celsius) Ref.5 KM=45.1 mM for acetyl-CoA (at pH 8 and 30 degrees Celsius)
Sequence caution	The sequence CAA20034.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB80280.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process from serine Inferred from electronic annotation. Source: InterPro sulfate assimilation Traceable author statement Ref.5. Source: TAIR
Cellular component	cytosol Inferred from direct assay Ref.5. Source: TAIR
Molecular function	serine O-acetyltransferase activity Inferred from direct assay Ref.5. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 355	355	Serine acetyltransferase 4		PRO_0000068692
Regions
	Compositional bias	12 – 19	8	Poly-Ser

Sequences

	Sequence		Length	Mass (Da)
	Q8W2B8 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 3BF39845776C0EC7	FASTA	355	38,424
	10 20 30 40 50 60 MACINGENRD FSSSSSLSSL PMIVSRNFSA RDDGETGDEF PFERIFPVYA RGTLNPVADP 70 80 90 100 110 120 VLLDFTNSSY DPIWDSIREE AKLEAEEEPV LSSFLYASIL SHDCLEQALS FVLANRLQNP 130 140 150 160 170 180 TLLATQLMDI FCNVMVHDRG IQSSIRLDVQ AFKDRDPACL SYSSAILHLK GYLALQAYRV 190 200 210 220 230 240 AHKLWKQGRK LLALALQSRV SEVFGIDIHP AARIGKGILL DHGTGVVIGE TAVIGDRVSI 250 260 270 280 290 300 LHGVTLGGTG KETGDRHPNI GDGALLGACV TILGNIKIGA GAMVAAGSLV LKDVPSHSMV 310 320 330 340 350 AGNPAKLIGF VDEQDPSMTM EHDATREFFQ NVAVAYRETI PNGSSVSGSC RERRH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a new serine acetyltransferase (SAT4) from Arabidopsis thaliana." Buisson S., Droux M. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Characterization and expression analysis of a serine acetyltransferase gene family involved in a key step of the sulfur assimilation pathway in Arabidopsis." Kawashima C.G., Berkowitz O., Hell R., Noji M., Saito K. Plant Physiol. 137:220-230(2005) [PubMed: 15579666] [Abstract] Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF331847 Genomic DNA. Translation: AAL37489.1. AL031135 Genomic DNA. Translation: CAA20034.1. Sequence problems. AL161587 Genomic DNA. Translation: CAB80280.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE86543.1. BT004080 mRNA. Translation: AAO42107.1. BT005047 mRNA. Translation: AAO50580.1.
IPI	IPI00533746.
PIR	T04669.
RefSeq	NP_195289.3. NM_119729.4.
UniGene	At.19734. At.71197.
3D structure databases
ProteinModelPortal	Q8W2B8.
SMR	Q8W2B8. Positions 67-341.
ModBase	Search...
Proteomic databases
PRIDE	Q8W2B8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G35640.1; AT4G35640.1; AT4G35640.
GeneID	829716.
GenomeReviews	Gene locus AT4G35640 in contig CT486007_GR.
KEGG	ath:AT4G35640.
NMPDR	fig|3702.1.peg.21649.
Organism-specific databases
GeneFarm	5180. 495.
TAIR	At4g35640.
Phylogenomic databases
eggNOG	KOG4750.
GeneTree	EPGT00070000030470.
HOGENOM	HBG754554.
InParanoid	Q8W2B8.
OMA	DPLLYFK.
PhylomeDB	Q8W2B8.
ProtClustDB	PLN02739.
Gene expression databases
Genevestigator	Q8W2B8.
Family and domain databases
InterPro	IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. IPR010493. Ser_AcTrfase_N. IPR005881. Ser_O-AcTrfase. IPR011004. Trimer_LpxA-like. [Graphical view]
KO	K00640.
Pfam	PF00132. Hexapep. 1 hit. PF06426. SATase_N. 1 hit. [Graphical view]
SMART	SM00971. SATase_N. 1 hit. [Graphical view]
SUPFAM	SSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMs	TIGR01172. CysE. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SAT4_ARATH

Accession

Primary (citable) accession number: Q8W2B8
Secondary accession number(s): O81795

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	March 1, 2002
Last modified:	November 16, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program