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Q42538 (SAT5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine acetyltransferase 5

Short name=AtSAT-5
EC=2.3.1.30
Alternative name(s):
AtSERAT1;1
SAT-c
Gene names
Name:SAT5
Synonyms:SAT52
Ordered Locus Names:At5g56760
ORF Names:MIK19.23
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceEvidence 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.7

Pathway

Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.

Subunit structure

Homomultimer By similarity.

Subcellular location

Cytoplasm Ref.7.

Tissue specificity

Mostly expressed in stems, flowers and siliques. Localized in vascular tissues, particularly in phloem. Ref.8 Ref.9

Induction

By cadmium (Cd). Not induced under sulfur-deficient conditions. Ref.7 Ref.8 Ref.9

Sequence similarities

Belongs to the transferase hexapeptide repeat family.

Biophysicochemical properties

Kinetic parameters:

KM=2.71 mM for L-Ser (at pH 8 and 37 degrees Celsius) Ref.7

KM=0.28 mM for acetyl-CoA (at pH 8 and 37 degrees Celsius)

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcysteine biosynthetic process from serine

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol

Inferred from direct assay Ref.7. Source: TAIR

   Molecular functionserine O-acetyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Serine acetyltransferase 5
PRO_0000068693

Regions

Compositional bias26 – 6439Ala-rich

Experimental info

Sequence conflict231S → F in AAM61424. Ref.5
Sequence conflict301S → A in AAM61424. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q42538 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 15835510FF314A08

FASTA31232,770
        10         20         30         40         50         60 
MPPAGELRHQ SPSKEKLSSV TQSDEAEAAS AAISAAAADA EAAGLWTQIK AEARRDAEAE 

        70         80         90        100        110        120 
PALASYLYST ILSHSSLERS ISFHLGNKLC SSTLLSTLLY DLFLNTFSSD PSLRNATVAD 

       130        140        150        160        170        180 
LRAARVRDPA CISFSHCLLN YKGFLAIQAH RVSHKLWTQS RKPLALALHS RISDVFAVDI 

       190        200        210        220        230        240 
HPAAKIGKGI LLDHATGVVV GETAVIGNNV SILHHVTLGG TGKACGDRHP KIGDGCLIGA 

       250        260        270        280        290        300 
GATILGNVKI GAGAKVGAGS VVLIDVPCRG TAVGNPARLV GGKEKPTIHD EECPGESMDH 

       310 
TSFISEWSDY II 

« Hide

References

« Hide 'large scale' references
[1]"Cysteine biosynthesis in higher plants: a new member of the Arabidopsis thaliana serine acetyltransferase small gene-family obtained by functional complementation of an Escherichia coli cysteine auxotroph."
Howarth J.R., Roberts M.A., Wray J.L.
Biochim. Biophys. Acta 1350:123-127(1997) [PubMed: 9048879] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
DNA Res. 5:203-216(1998) [PubMed: 9734815] [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. expand/collapse author list , 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. expand/collapse author list , 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]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"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: ENZYME REGULATION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U30298 mRNA. Translation: AAC49655.1.
AB013392 Genomic DNA. Translation: BAB09894.1.
CP002688 Genomic DNA. Translation: AED96804.1.
AY039612 mRNA. Translation: AAK62667.1.
AY133674 mRNA. Translation: AAM91504.1.
AK227979 mRNA. Translation: BAE99945.1.
AY084861 mRNA. Translation: AAM61424.1.
IPIIPI00517479.
PIRS71207.
RefSeqNP_200487.1. NM_125059.2.
UniGeneAt.23802.

3D structure databases

ProteinModelPortalQ42538.
SMRQ42538. Positions 8-307.
ModBaseSearch...

Protein-protein interaction databases

IntActQ42538. 1 interaction.
STRINGQ42538.

Proteomic databases

PRIDEQ42538.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G56760.1; AT5G56760.1; AT5G56760.
GeneID835778.
GenomeReviewsGene locus AT5G56760 in contig BA000015_GR.
KEGGath:AT5G56760.
NMPDRfig|3702.1.peg.27616.

Organism-specific databases

GeneFarm5181. 495.
TAIRAt5g56760.

Phylogenomic databases

eggNOGKOG4750.
GeneTreeEPGT00050000004084.
HOGENOMHBG754554.
InParanoidQ42538.
OMALALHSRI.
PhylomeDBQ42538.
ProtClustDBPLN02694.

Enzyme and pathway databases

BRENDA2.3.1.30. 399.

Gene expression databases

GenevestigatorQ42538.
GermOnlineAT5G56760. Arabidopsis thaliana.

Family and domain databases

InterProIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010493. Ser_AcTrfase_N.
IPR005881. Ser_O-AcTrfase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
KOK00640.
PfamPF00132. Hexapep. 1 hit.
PF06426. SATase_N. 1 hit.
[Graphical view]
SMARTSM00971. SATase_N. 1 hit.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01172. CysE. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSAT5_ARATH
AccessionPrimary (citable) accession number: Q42538
Secondary accession number(s): Q0WSF3, Q8LFG6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families