Reviewed, UniProtKB/Swiss-Prot Q42588 (SAT1_ARATH)

Names and origin

Protein names

Recommended name:
    Serine acetyltransferase 1
      Short name=AtSAT-1
    EC=2.3.1.30
Alternative name(s):
    SAT-p
    AtSERAT2;1

Gene names

Name:	SAT1
Synonyms:	SAT5
Ordered Locus Names:	At1g55920
ORF Names:	F14J16.18

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May be involved in detoxification process by mediating the production of glutathione.
Catalytic activity	Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine.
Pathway	Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
Subunit structure	Homomultimer By similarity. Interacts with OASA1 to form the cysteine synthase complex. Ref.10 Ref.11
Subcellular location	Plastid › chloroplast. Cytoplasm. Note: First chloroplastic and progressively cytoplasmic during aging. Ref.6
Tissue specificity	Mostly expressed in leaves. Localized in cortex, trichomes and vascular tissues, particularly in phloem. Ref.1 Ref.7 Ref.8 Ref.9
Induction	By cadmium (Cd). Not induced under sulfur-deficient conditions. Repressed in trichomes in response to NaCl treatment. Ref.7 Ref.8 Ref.9
Sequence similarities	Belongs to the transferase hexapeptide repeat family.
Biophysicochemical properties	Kinetic parameters: KM=1.64 mM for L-Ser (at pH 8 and 37 degrees Celsius) KM=0.16 mM for acetyl-CoA (at pH 8 and 37 degrees Celsius)

Ontologies

Keywords
Biological process	Amino-acid biosynthesis
Cellular component	Chloroplast Cytoplasm Plastid
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cellular response to sulfate starvation Inferred from expression pattern. Source: TAIR cysteine biosynthetic process from serine Inferred from electronic annotation. Source: InterPro response to cold Inferred from expression pattern. Source: TAIR
Cellular component	chloroplast Ref.6 Inferred from direct assay. Source: TAIR cytosol Ref.2 Traceable author statement. Source: TAIR nucleus Inferred from direct assay. Source: TAIR
Molecular function	serine O-acetyltransferase activity Ref.1 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 314	314	Serine acetyltransferase 1		PRO_0000068690
Experimental info
	Sequence conflict	6	1	D → H in AAC37474. Ref.1
	Sequence conflict	24 – 25	2	KN → NK in AAC37474. Ref.1
	Sequence conflict	54	1	E → K in AAC37474. Ref.1
	Sequence conflict	57	1	K → E in AAC37474. Ref.1
	Sequence conflict	85	1	A → G in AAC37474. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q42588-1 [UniParc]. Last modified January 24, 2006. Version 2. Checksum: 78FACE3DA5CE04B0	FASTA	314	34,251
	10 20 30 40 50 60 MATCIDTCRT GNTQDDDSRF CCIKNFFRPG FSVNRKIHHT QIEDDDDVWI KMLEEAKSDV 70 80 90 100 110 120 KQEPILSNYY YASITSHRSL ESALAHILSV KLSNLNLPSN TLFELFISVL EESPEIIEST 130 140 150 160 170 180 KQDLIAVKER DPACISYVHC FLGFKGFLAC QAHRIAHTLW KQNRKIVALL IQNRVSESFA 190 200 210 220 230 240 VDIHPGAKIG KGILLDHATG VVIGETAVVG DNVSILHGVT LGGTGKQSGD RHPKIGDGVL 250 260 270 280 290 300 IGAGSCILGN ITIGEGAKIG SGSVVVKDVP ARTTAVGNPA RLIGGKENPR KHDKIPCLTM 310 DQTSYLTEWS DYVI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Serine acetyltransferase from Arabidopsis thaliana can functionally complement the cysteine requirement of a cysE mutant strain of Escherichia coli." Murillo M., Foglia R., Diller A., Lee S., Leustek T. Cell. Mol. Biol. Res. 41:425-433(1995) [PubMed: 8867790] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: cv. Columbia.
[2]	"Subcellular distribution of serine acetyltransferase from Pisum sativum and characterization of an Arabidopsis thaliana putative cytosolic isoform." Ruffet M.-L., Lebrun M., Droux M., Douce R. Eur. J. Biochem. 227:500-509(1995) [PubMed: 7851429] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Isoform-dependent differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana." Noji M., Inoue K., Kimura N., Gouda A., Saito K. J. Biol. Chem. 273:32739-32745(1998) [PubMed: 9830017] [Abstract] Cited for: SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
[7]	"Glutathione biosynthesis in Arabidopsis trichome cells." Gutierrez-Alcala G., Gotor C., Meyer A.J., Fricker M., Vega J.M., Romero L.C. Proc. Natl. Acad. Sci. U.S.A. 97:11108-11113(2000) [PubMed: 10995473] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[8]	"The serine acetyltransferase gene family in Arabidopsis thaliana and the regulation of its expression by cadmium." Howarth J.R., Dominguez-Solis J.R., Gutierrez-Alcala G., Wray J.L., Romero L.C., Gotor C. Plant Mol. Biol. 51:589-598(2003) [PubMed: 12650624] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION. Strain: cv. Columbia.
[9]	"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: TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, NOMENCLATURE.
[10]	"Molecular basis of cysteine biosynthesis in plants: structural and functional analysis of o-acetylserine sulfhydrylase from Arabidopsis thaliana." Bonner E.R., Cahoon R.E., Knapke S.M., Jez J.M. J. Biol. Chem. 280:38803-38813(2005) [PubMed: 16166087] [Abstract] Cited for: INTERACTION WITH OASA1.
[11]	"Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex." Francois J.A., Kumaran S., Jez J.M. Plant Cell 18:3647-3655(2006) [PubMed: 17194764] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 307-314, INTERACTION WITH OASA1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L42212 mRNA. Translation: AAC37474.1.
L34076 Genomic RNA. Translation: AAA58608.1.
Z34888 Genomic DNA. Translation: CAA84371.1.
AC002304 Genomic DNA. Translation: AAF79319.1.
BT008309 mRNA. Translation: AAP37668.1.
AK227691 mRNA. Translation: BAE99678.1.

IPI

IPI00540020.

PIR

S67482.
S71181.

RefSeq

NP_175988.1.

UniGene

At.24052

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ISQ	X-ray	2.80	B	307-314	[»]

SMR

Q42588. Positions 46-283.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q42588. 3 interactions.

STRING

Q42588.

Proteomic databases

PRIDE

Q42588.

Genome annotation databases

GeneID

842043.

GenomeReviews

Gene locus AT1G55920 in contig CT485782_GR.

KEGG

ath:AT1G55920.

NMPDR

fig|3702.1.peg.5135.

Organism-specific databases

GeneFarm

5177. 495.

TAIR

At1g55920.

Phylogenomic databases

eggNOG

KOG4750.

HOGENOM

HBG754554.

InParanoid

Q42588.

OMA

ERDFALY.

PhylomeDB

Q42588.

Enzyme and pathway databases

BRENDA

2.3.1.30. 302.

Gene expression databases

Genevestigator

Q42588.

GermOnline

AT1G55920. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR018357. Hexapep_transf_CS.
IPR005881. Ser_O-AcTrfase.
IPR011004. Trimer_LpxA-like.
[Graphical view]

TIGRFAMs

TIGR01172. cysE. 1 hit.

PROSITE

PS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SAT1_ARATH

Accession

Primary (citable) accession number: Q42588
Secondary accession number(s): Q0WT70, Q43297

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	January 24, 2006
Last modified:	February 9, 2010
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)