O74382 (SERB_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable phosphoserine phosphatase
Short name=PSP
Short name=PSPase
EC=3.1.3.3

Alternative name(s):
O-phosphoserine phosphohydrolase

Gene names

ORF Names:

SPBC3H7.07c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

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.
Sequence similarities	Belongs to the serB family.
Sequence caution	The sequence BAA13922.1 differs from that shown. Reason: Frameshift at position 267.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Serine biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	L-serine biosynthetic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Cellular component	cytoplasm Inferred from sequence or structural similarity. 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 – 298	298	Probable phosphoserine phosphatase		PRO_0000156884
Regions
	Region	170 – 171	2	Substrate binding By similarity
Sites
	Active site	82	1	Nucleophile By similarity
	Active site	84	1	Proton donor By similarity
	Metal binding	82	1	Magnesium By similarity
	Metal binding	84	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	240	1	Magnesium By similarity
	Binding site	91	1	Substrate By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	217	1	Substrate By similarity
	Binding site	243	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O74382 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 4BCBCE73E9013CA5	FASTA	298	32,411
	10 20 30 40 50 60 MVNAAIVVSS NRPNVLEQIS SLFRDGKTRS LGEQWTLVSG QLKGTFEDAK DACNRISATE 70 80 90 100 110 120 NVDCNCLSEA TFSTKKKLVV FDMDSTLIQQ ECIDELAAEA GIQKEVATIT SLAMNGEIDF 130 140 150 160 170 180 QESLRRRVSL LQGLSVDVIN KVIGKITFTP GAKQLCHCLK QMGATLVVAS GGFVPMAEYV 190 200 210 220 230 240 KGQLDLDYAY ANVLEFSDDG KFLTGKVQGA IVDGQRKASI LREKREELGL NKLETMAVGD 250 260 270 280 290 GANDLVMMAE SGLGIAFKAK PKVQLLADSK INLPSLQNAL YLLGIDEQQQ KKLLENKN

References

[1]	"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: PR745.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D89261 mRNA. Translation: BAA13922.1. Frameshift. CU329671 Genomic DNA. Translation: CAA20303.1.
PIR	T40408. T43186.
RefSeq	NP_595768.1. NM_001021669.1.
3D structure databases
ProteinModelPortal	O74382.
ModBase	Search...
Protein-protein interaction databases
STRING	O74382.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC3H7.07c.1; SPBC3H7.07c.1:pep; SPBC3H7.07c.
GeneID	2540968.
KEGG	spo:SPBC3H7.07c.
NMPDR	fig|4896.1.peg.1634.
Organism-specific databases
GeneDB_Spombe	SPBC3H7.07c.
Phylogenomic databases
eggNOG	fuNOG08484.
GeneTree	EFGT00050000003887.
HOGENOM	HBG645339.
OMA	FVAEPIL.
OrthoDB	EOG46X2HS.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003848-MONOMER.
Gene expression databases
ArrayExpress	O74382.
Family and domain databases
InterPro	IPR005834. Dehalogen-like_hydro. 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.
Pfam	PF00702. Hydrolase. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01488. HAD-SF-IB. 1 hit. TIGR00338. SerB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SERB_SCHPO

Accession

Primary (citable) accession number: O74382
Secondary accession number(s): P78910

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2003
Last sequence update:	November 1, 1998
Last modified:	December 14, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program