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Reviewed, UniProtKB/Swiss-Prot Q9VAN0 (SERC_DROME)

Last modified February 9, 2010. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable phosphoserine aminotransferase
      Short name=PSAT
    EC=2.6.1.52
Alternative name(s):
    Phosphohydroxythreonine aminotransferase
Gene names
ORF Names: CG11899
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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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.

Tissue specificity

Expressed in ovary and head. Ref.1

Sequence similarities

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

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

PHGPxQ9VZQ81EBI-83690,EBI-97554
SelRQ8INK9-11EBI-83690,EBI-218847

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364Probable phosphoserine aminotransferase
PRO_0000150139

Regions

Region74 – 752Pyridoxal phosphate binding By similarity
Region235 – 2362Pyridoxal phosphate binding By similarity

Sites

Binding site401L-glutamate By similarity
Binding site1001Pyridoxal phosphate By similarity
Binding site1491Pyridoxal phosphate By similarity
Binding site1701Pyridoxal phosphate By similarity
Binding site1931Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1941N6-(pyridoxal phosphate)lysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9VAN0-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: DAEA4E2F5BD4DB74

FASTA36439,540
        10         20         30         40         50         60 
MVINFAAGPA KLPEEVLKEV QENLVNCNGS GISVMEMSHR SSNYAKIHDA TISDLRELLN 

        70         80         90        100        110        120 
VPSNYKILLM QGGGTGQFAA VALNLIGKTG TADYVITGSW SAKAAKEAAQ YGTVNAVLPK 

       130        140        150        160        170        180 
LAKYTTVPRQ ETWKLDPNAS YVYYCDNETV EGVEFDFVPE VPAGVPLVAD MSSNFLSRPF 

       190        200        210        220        230        240 
DVSKFGVIYA GAQKNIGPAG TTVIIVRDDL IGKHLKITPS ILNFEQMDKN NSLLNTPPTF 

       250        260        270        280        290        300 
GIYVMGLVFK WIKRNGGVAG MAKLAAAKSK LIYDTINQSN GFYYCPVDVN VRSRMNVPFR 

       310        320        330        340        350        360 
IGSASGDDAL EKEFLSKAEA EGMIQLKGHR SVGGIRASLY NAVTLAETQQ LANLMLAFYK 


NNKN

« Hide

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References

« Hide 'large scale' references
[1]"Rapidly evolving genes of Drosophila: differing levels of selective pressure in testis, ovary, and head tissues between sibling species."
Jagadeeshan S., Singh R.S.
Mol. Biol. Evol. 22:1793-1801(2005) [PubMed: 15917496] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Head.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Ovary.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DQ062790 mRNA. Translation: AAY56663.1.
AE014297 Genomic DNA. Translation: AAF56874.1.
AY119560 mRNA. Translation: AAM50214.1.
RefSeqNP_652046.1.
UniGeneDm.11354

3D structure databases

SMRQ9VAN0. Positions 2-362.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-17047N.
IntActQ9VAN0. 8 interactions.
STRINGQ9VAN0.

Proteomic databases

PRIDEQ9VAN0.

Genome annotation databases

EnsemblFBtr0085390; FBpp0084759; FBgn0014427; Drosophila melanogaster. [Genome view]
GeneID46391.
KEGGdme:Dmel_CG11899.
NMPDRfig|7227.3.peg.15201.
UCSCCG11899-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0014427. CG11899.

Phylogenomic databases

eggNOGinNOG04441.
InParanoidQ9VAN0.
OMATFAWYLA.
OrthoDBEOG9K0QW1.
PhylomeDBQ9VAN0.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-013935-MONOMER.
BRENDA2.6.1.52. 48.

Gene expression databases

GermOnlineCG11899. Drosophila melanogaster.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR003248. Pser_amintransf.
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.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
TIGRFAMsTIGR01364. serC_1. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio838831.

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Entry information

Entry nameSERC_DROME
AccessionPrimary (citable) accession number: Q9VAN0
Secondary accession number(s): Q3YMT6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: February 9, 2010
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents