SERB_DROME
ID SERB_DROME Reviewed; 270 AA.
AC Q9VSY6; Q9U4B0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Phosphoserine phosphatase;
DE Short=PSP;
DE Short=PSPase;
DE EC=3.1.3.3;
DE AltName: Full=O-phosphoserine phosphohydrolase;
GN Name=aay; Synonyms=astray; ORFNames=CG3705;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=11102367; DOI=10.1093/genetics/156.4.1691;
RA Prokopenko S.N., He Y., Lu Y., Bellen H.J.;
RT "Mutations affecting the development of the peripheral nervous system in
RT Drosophila: a molecular screen for novel proteins.";
RL Genetics 156:1691-1715(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Catalyzes the last step in the biosynthesis of serine from
CC carbohydrates. The reaction mechanism proceeds via the formation of a
CC phosphoryl-enzyme intermediates (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-serine = L-serine + phosphate;
CC Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-D-serine = D-serine + phosphate;
CC Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3.
CC -!- DEVELOPMENTAL STAGE: Expressed in a complex banded pattern early in
CC embryogenesis. During maturation of the embryo, expression becomes
CC restricted to cells around and of the gut.
CC {ECO:0000269|PubMed:11102367}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC {ECO:0000305}.
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DR EMBL; AF191498; AAF14696.1; -; mRNA.
DR EMBL; AE014296; AAF50274.1; -; Genomic_DNA.
DR EMBL; AY051689; AAK93113.1; -; mRNA.
DR RefSeq; NP_524001.2; NM_079277.3.
DR AlphaFoldDB; Q9VSY6; -.
DR SMR; Q9VSY6; -.
DR BioGRID; 64479; 2.
DR IntAct; Q9VSY6; 1.
DR STRING; 7227.FBpp0076185; -.
DR PaxDb; Q9VSY6; -.
DR PRIDE; Q9VSY6; -.
DR DNASU; 39085; -.
DR EnsemblMetazoa; FBtr0076457; FBpp0076185; FBgn0023129.
DR GeneID; 39085; -.
DR KEGG; dme:Dmel_CG3705; -.
DR UCSC; CG3705-RA; d. melanogaster.
DR CTD; 39085; -.
DR FlyBase; FBgn0023129; aay.
DR VEuPathDB; VectorBase:FBgn0023129; -.
DR eggNOG; KOG1615; Eukaryota.
DR GeneTree; ENSGT00390000003115; -.
DR HOGENOM; CLU_036368_2_1_1; -.
DR InParanoid; Q9VSY6; -.
DR OMA; RAQYYVT; -.
DR OrthoDB; 1009123at2759; -.
DR PhylomeDB; Q9VSY6; -.
DR Reactome; R-DME-977347; Serine biosynthesis.
DR UniPathway; UPA00135; UER00198.
DR BioGRID-ORCS; 39085; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39085; -.
DR PRO; PR:Q9VSY6; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0023129; Expressed in head capsule and 56 other tissues.
DR ExpressionAtlas; Q9VSY6; baseline and differential.
DR Genevisible; Q9VSY6; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004469; PSP.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00338; serB; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome; Serine biosynthesis.
FT CHAIN 1..270
FT /note="Phosphoserine phosphatase"
FT /id="PRO_0000156883"
FT ACT_SITE 67
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 69
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 156..157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 22
FT /note="T -> A (in Ref. 1; AAF14696)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="S -> N (in Ref. 1; AAF14696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 29218 MW; 5B9DC00608EB59FA CRC64;
MSGSVLSLAR PAAATNGHNL LTKQLNCNGN GTTGGAAKTT VASAITPPKQ PQLAAKVIQQ
SQIVCFDVDS TVICEEGIDE LAEYCGKGSE VARVTKEAMG GAMTFQDALK IRLNIIRPTQ
QQVRDFIQER PSTLSKNVKR FVSHLKAEGK QVYLISGGFD CLIAPVANEL GIPLKNVYAN
KMLFDYLGEY DSFDINQPTS RSGGKAEAIA LIRKENSDDS LITMIGDGAT DLEAVPPANY
FIGFGGNVVR PEVYRRAQYY VTDFEQLMGQ
