Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoserine phosphatase

Gene

aay

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates (By similarity).By similarity

Catalytic activityi

O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Pathwayi: L-serine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-serine from 3-phospho-D-glycerate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Probable phosphoserine aminotransferase (CG11899)
  3. Phosphoserine phosphatase (aay)
This subpathway is part of the pathway L-serine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-serine from 3-phospho-D-glycerate, the pathway L-serine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei67 – 671NucleophileBy similarity
Metal bindingi67 – 671MagnesiumBy similarity
Active sitei69 – 691Proton donorBy similarity
Metal bindingi69 – 691Magnesium; via carbonyl oxygenBy similarity
Binding sitei76 – 761SubstrateBy similarity
Binding sitei112 – 1121SubstrateBy similarity
Binding sitei205 – 2051SubstrateBy similarity
Metal bindingi227 – 2271MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

  • axon guidance Source: FlyBase
  • behavioral response to ethanol Source: FlyBase
  • dephosphorylation Source: GOC
  • L-serine biosynthetic process Source: FlyBase
  • L-serine metabolic process Source: UniProtKB
  • male courtship behavior, veined wing generated song production Source: FlyBase
  • peripheral nervous system development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Serine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-DME-977347. Serine biosynthesis.
UniPathwayiUPA00135; UER00198.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoserine phosphatase (EC:3.1.3.3)
Short name:
PSP
Short name:
PSPase
Alternative name(s):
O-phosphoserine phosphohydrolase
Gene namesi
Name:aay
Synonyms:astray
ORF Names:CG3705
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0023129. aay.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270Phosphoserine phosphatasePRO_0000156883Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VSY6.
PRIDEiQ9VSY6.

Expressioni

Developmental stagei

Expressed in a complex banded pattern early in embryogenesis. During maturation of the embryo, expression becomes restricted to cells around and of the gut.1 Publication

Gene expression databases

BgeeiQ9VSY6.
ExpressionAtlasiQ9VSY6. differential.
GenevisibleiQ9VSY6. DM.

Interactioni

Protein-protein interaction databases

BioGridi64479. 2 interactions.
MINTiMINT-973405.
STRINGi7227.FBpp0076185.

Structurei

3D structure databases

ProteinModelPortaliQ9VSY6.
SMRiQ9VSY6. Positions 56-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni156 – 1572Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the SerB family.Curated

Phylogenomic databases

eggNOGiKOG1615. Eukaryota.
COG0560. LUCA.
GeneTreeiENSGT00390000003115.
InParanoidiQ9VSY6.
KOiK01079.
OMAiTDLEACP.
OrthoDBiEOG7CRTQD.
PhylomeDBiQ9VSY6.

Family and domain databases

Gene3Di1.10.150.210. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006383. HAD-SF_hydro_IB_PSP-like.
IPR023190. Pser_Pase_dom_2.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01488. HAD-SF-IB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9VSY6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGSVLSLAR PAAATNGHNL LTKQLNCNGN GTTGGAAKTT VASAITPPKQ
60 70 80 90 100
PQLAAKVIQQ SQIVCFDVDS TVICEEGIDE LAEYCGKGSE VARVTKEAMG
110 120 130 140 150
GAMTFQDALK IRLNIIRPTQ QQVRDFIQER PSTLSKNVKR FVSHLKAEGK
160 170 180 190 200
QVYLISGGFD CLIAPVANEL GIPLKNVYAN KMLFDYLGEY DSFDINQPTS
210 220 230 240 250
RSGGKAEAIA LIRKENSDDS LITMIGDGAT DLEAVPPANY FIGFGGNVVR
260 270
PEVYRRAQYY VTDFEQLMGQ
Length:270
Mass (Da):29,218
Last modified:May 1, 2000 - v1
Checksum:i5B9DC00608EB59FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221T → A in AAF14696 (PubMed:11102367).Curated
Sequence conflicti217 – 2171S → N in AAF14696 (PubMed:11102367).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191498 mRNA. Translation: AAF14696.1.
AE014296 Genomic DNA. Translation: AAF50274.1.
AY051689 mRNA. Translation: AAK93113.1.
RefSeqiNP_524001.2. NM_079277.3.
UniGeneiDm.2900.

Genome annotation databases

EnsemblMetazoaiFBtr0076457; FBpp0076185; FBgn0023129.
GeneIDi39085.
KEGGidme:Dmel_CG3705.
UCSCiCG3705-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191498 mRNA. Translation: AAF14696.1.
AE014296 Genomic DNA. Translation: AAF50274.1.
AY051689 mRNA. Translation: AAK93113.1.
RefSeqiNP_524001.2. NM_079277.3.
UniGeneiDm.2900.

3D structure databases

ProteinModelPortaliQ9VSY6.
SMRiQ9VSY6. Positions 56-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64479. 2 interactions.
MINTiMINT-973405.
STRINGi7227.FBpp0076185.

Proteomic databases

PaxDbiQ9VSY6.
PRIDEiQ9VSY6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076457; FBpp0076185; FBgn0023129.
GeneIDi39085.
KEGGidme:Dmel_CG3705.
UCSCiCG3705-RA. d. melanogaster.

Organism-specific databases

CTDi39085.
FlyBaseiFBgn0023129. aay.

Phylogenomic databases

eggNOGiKOG1615. Eukaryota.
COG0560. LUCA.
GeneTreeiENSGT00390000003115.
InParanoidiQ9VSY6.
KOiK01079.
OMAiTDLEACP.
OrthoDBiEOG7CRTQD.
PhylomeDBiQ9VSY6.

Enzyme and pathway databases

UniPathwayiUPA00135; UER00198.
ReactomeiR-DME-977347. Serine biosynthesis.

Miscellaneous databases

GenomeRNAii39085.
PROiQ9VSY6.

Gene expression databases

BgeeiQ9VSY6.
ExpressionAtlasiQ9VSY6. differential.
GenevisibleiQ9VSY6. DM.

Family and domain databases

Gene3Di1.10.150.210. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006383. HAD-SF_hydro_IB_PSP-like.
IPR023190. Pser_Pase_dom_2.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01488. HAD-SF-IB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations affecting the development of the peripheral nervous system in Drosophila: a molecular screen for novel proteins."
    Prokopenko S.N., He Y., Lu Y., Bellen H.J.
    Genetics 156:1691-1715(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiSERB_DROME
AccessioniPrimary (citable) accession number: Q9VSY6
Secondary accession number(s): Q9U4B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.