Q9VSY6 (SERB_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoserine phosphatase
Short name=PSP
Short name=PSPase
EC=3.1.3.3

Alternative name(s):
O-phosphoserine phosphohydrolase

Gene names

Name:	aay
Synonyms:	astray
ORF Names:	CG3705

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Catalytic activity	O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
Developmental stage	Expressed in a complex banded pattern early in embryogenesis. During maturation of the embryo, expression becomes restricted to cells around and of the gut. Ref.1
Sequence similarities	Belongs to the serB family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Serine biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	L-serine biosynthetic process Inferred from Biological aspect of Ancestor. Source: RefGenome axon guidance Inferred from mutant phenotype Ref.1. Source: FlyBase behavioral response to ethanol Inferred from mutant phenotype. Source: FlyBase peripheral nervous system development Traceable author statement Ref.1. Source: FlyBase
Cellular component	cytoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB phosphoserine phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 270	270	Phosphoserine phosphatase		PRO_0000156883
Regions
	Region	156 – 157	2	Substrate binding By similarity
Sites
	Active site	67	1	Nucleophile By similarity
	Active site	69	1	Proton donor By similarity
	Metal binding	67	1	Magnesium By similarity
	Metal binding	69	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	227	1	Magnesium By similarity
	Binding site	76	1	Substrate By similarity
	Binding site	112	1	Substrate By similarity
	Binding site	205	1	Substrate By similarity
Experimental info
	Sequence conflict	22	1	T → A in AAF14696. Ref.1
	Sequence conflict	217	1	S → N in AAF14696. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9VSY6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 5B9DC00608EB59FA	FASTA	270	29,218
	10 20 30 40 50 60 MSGSVLSLAR PAAATNGHNL LTKQLNCNGN GTTGGAAKTT VASAITPPKQ PQLAAKVIQQ 70 80 90 100 110 120 SQIVCFDVDS TVICEEGIDE LAEYCGKGSE VARVTKEAMG GAMTFQDALK IRLNIIRPTQ 130 140 150 160 170 180 QQVRDFIQER PSTLSKNVKR FVSHLKAEGK QVYLISGGFD CLIAPVANEL GIPLKNVYAN 190 200 210 220 230 240 KMLFDYLGEY DSFDINQPTS RSGGKAEAIA LIRKENSDDS LITMIGDGAT DLEAVPPANY 250 260 270 FIGFGGNVVR PEVYRRAQYY VTDFEQLMGQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11102367] [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: 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. , 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. 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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF191498 mRNA. Translation: AAF14696.1. AE014296 Genomic DNA. Translation: AAF50274.1. AY051689 mRNA. Translation: AAK93113.1.
RefSeq	NP_524001.2. NM_079277.2.
UniGene	Dm.2900.
3D structure databases
ProteinModelPortal	Q9VSY6.
SMR	Q9VSY6. Positions 52-269.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-973405.
STRING	Q9VSY6.
Proteomic databases
PRIDE	Q9VSY6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0076457; FBpp0076185; FBgn0023129.
GeneID	39085.
KEGG	dme:Dmel_CG3705.
NMPDR	fig|7227.3.peg.9062.
UCSC	CG3705-RA. d. melanogaster.
Organism-specific databases
CTD	39085.
FlyBase	FBgn0023129. aay.
Phylogenomic databases
GeneTree	EMGT00050000017200.
InParanoid	Q9VSY6.
OMA	YAGFDES.
OrthoDB	EOG4TB2TF.
PhylomeDB	Q9VSY6.
Gene expression databases
ArrayExpress	Q9VSY6.
Bgee	Q9VSY6.
GermOnline	CG3705. Drosophila melanogaster.
Family and domain databases
InterPro	IPR023214. HAD-like_dom. IPR006383. HAD-SF_hydro_IB_PSP-like. IPR023190. Pser_Pase_dom_2. IPR004469. SerB. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 2 hits. G3DSA:1.10.150.210. Pser_Pase_dom_2. 1 hit.
KO	K01079.
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01488. HAD-SF-IB. 1 hit. TIGR00338. SerB. 1 hit.
ProtoNet	Search...
Other
NextBio	811837.

Entry information

Entry name

SERB_DROME

Accession

Primary (citable) accession number: Q9VSY6
Secondary accession number(s): Q9U4B0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project