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Q96255 (SERC_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 102. Feed History...

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

Names and origin

Protein namesRecommended name:
Phosphoserine aminotransferase, chloroplastic
Short name=PSAT
EC=2.6.1.52
Alternative name(s):
Phosphohydroxythreonine aminotransferase
Gene names
Ordered Locus Names:At4g35630
ORF Names:F8D20.140
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine By similarity.

Catalytic activity

O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate.

4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.

Subunit structure

Homodimer By similarity.

Subcellular location

Plastid › chloroplast.

Sequence similarities

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast Potential
Chain? – 430Phosphoserine aminotransferase, chloroplasticPRO_0000001282

Regions

Region145 – 1462Pyridoxal phosphate binding By similarity
Region306 – 3072Pyridoxal phosphate binding By similarity

Sites

Binding site1111L-glutamate By similarity
Binding site1711Pyridoxal phosphate By similarity
Binding site2211Pyridoxal phosphate By similarity
Binding site2411Pyridoxal phosphate By similarity
Binding site2641Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q96255 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: B3225CC8DE78BDE2

FASTA43047,359
        10         20         30         40         50         60 
MAATTNSFLV GSNNTQIPAL KPKSSSQSFL HLSKPNTVNF VSKTKPVAVR CVASTTQVQD 

        70         80         90        100        110        120 
GVRSGSVGSQ ERVFNFAAGP ATLPENVLLK AQADLYNWRG SGMSVMEMSH RGKEFLSIIQ 

       130        140        150        160        170        180 
KAESDLRQLL EIPQEYSVLF LQGGATTQFA ALPLNLCKSD DTVDFVVTGS WGDKAVKEAK 

       190        200        210        220        230        240 
KYCKTNVIWS GKSEKYTKVP SFEELEQTPD AKYLHICANE TIHGVEFKDY PVPKNGFLVA 

       250        260        270        280        290        300 
DMSSNFCSKP VDVSKFGVIY GGAQKNVGPS GVTIVIIRKD LIGNAQDITP VMLDYKIHDE 

       310        320        330        340        350        360 
NSSLYNTPPC FGIYMCGLVF EDLLEQGGLK EVEKKNQRKA DLLYNAIEES NGFFRCPVEK 

       370        380        390        400        410        420 
SVRSLMNVPF TLEKSELEAE FIKEAAKEKM VQLKGHRSVG GMRASIYNAM PLAGVEKLVA 

       430 
FMKDFQAKHA

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of plastidic phosphoserine aminotransferase in serine biosynthesis from Arabidopsis."
Ho C.-L., Noji M., Saito M., Yamazaki M., Saito K.
Plant J. 16:443-452(1998) [PubMed: 9881164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D88541 mRNA. Translation: BAA13640.1.
AB010408 Genomic DNA. Translation: BAA24441.1.
AL031135 Genomic DNA. Translation: CAA20033.1.
AL161587 Genomic DNA. Translation: CAB80279.1.
CP002687 Genomic DNA. Translation: AEE86542.1.
IPIIPI00536454.
PIRT04668.
RefSeqNP_195288.1. NM_119728.2.
UniGeneAt.19734.
At.71197.

3D structure databases

ProteinModelPortalQ96255.
SMRQ96255. Positions 73-429.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ96255.

Proteomic databases

PRIDEQ96255.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G35630.1; AT4G35630.1; AT4G35630.
GeneID829715.
GenomeReviewsGene locus AT4G35630 in contig CT486007_GR.
KEGGath:AT4G35630.
NMPDRfig|3702.1.peg.21648.

Organism-specific databases

GeneFarm2144. 226.
TAIRAt4g35630.

Phylogenomic databases

GeneTreeEPGT00050000013052.
HOGENOMHBG289982.
InParanoidQ96255.
OMAYEVLFLQ.
PhylomeDBQ96255.
ProtClustDBPLN02452.

Gene expression databases

GenevestigatorQ96255.
GermOnlineAT4G35630. Arabidopsis thaliana.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR003248. Pser_aminoTfrase_subgr.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KOK00831.
PANTHERPTHR21152:SF1. PTHR21152:SF1. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF000525. SerC. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01364. SerC_1. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_ARATH
AccessionPrimary (citable) accession number: Q96255
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: November 16, 2011
This is version 102 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents