Q58989 (SERB_METJA) 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

Ordered Locus Names:

MJ1594

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate. Ref.2
Cofactor	Binds 1 magnesium ion per subunit. Ref.4
Pathway	Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
Sequence similarities	Belongs to the serB family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.5. Ref.4 Temperature dependence: Optimum temperature is 70 degrees Celsius.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Serine biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	L-serine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoserine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 211

211

Phosphoserine phosphatase

PRO_0000156891

Regions

Region

99 – 100

2

Substrate binding

Sites

Active site

11

1

Nucleophile

Active site

13

1

Proton donor

Metal binding

11

1

Magnesium

Metal binding

13

1

Magnesium; via carbonyl oxygen

Metal binding

167

1

Magnesium

Binding site

20

1

Substrate

Binding site

56

1

Substrate

Binding site

144

1

Substrate

Binding site

170

1

Substrate

Experimental info

Mutagenesis

11

1

D → N: Loss of activity. Ref.4

Secondary structure

1

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211

Helix Strand Turn

Details...

Beta strand

6 – 11

6

Helix

12 – 16

5

Beta strand

17 – 19

3

Helix

21 – 28

8

Helix

32 – 43

12

Helix

49 – 58

10

Turn

59 – 62

4

Helix

65 – 73

9

Helix

81 – 90

10

Beta strand

93 – 102

10

Helix

103 – 113

11

Beta strand

116 – 126

11

Beta strand

129 – 135

7

Helix

143 – 155

13

Helix

159 – 161

3

Beta strand

162 – 166

5

Helix

169 – 171

3

Helix

172 – 177

6

Beta strand

179 – 185

7

Helix

188 – 191

4

Beta strand

195 – 198

4

Helix

203 – 209

7

Sequences

	Sequence		Length	Mass (Da)
	Q58989 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 8573E6D92D883AA6	FASTA	211	23,594
	10 20 30 40 50 60 MEKKKKLILF DFDSTLVNNE TIDEIAREAG VEEEVKKITK EAMEGKLNFE QSLRKRVSLL 70 80 90 100 110 120 KDLPIEKVEK AIKRITPTEG AEETIKELKN RGYVVAVVSG GFDIAVNKIK EKLGLDYAFA 130 140 150 160 170 180 NRLIVKDGKL TGDVEGEVLK ENAKGEILEK IAKIEGINLE DTVAVGDGAN DISMFKKAGL 190 200 210 KIAFCAKPIL KEKADICIEK RDLREILKYI K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase." Cho H., Wang W., Kim R., Yokota H., Damo S., Kim S.H., Wemmer D., Kustu S., Yan D. Proc. Natl. Acad. Sci. U.S.A. 98:8525-8530(2001) [PubMed: 11438683] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH BEF3 AND MAGNESIUM ION, CATALYTIC ACTIVITY.
[3]	"Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 A resolution." Wang W., Kim R., Jancarik J., Yokota H., Kim S.-H. Structure 9:65-71(2001) [PubMed: 11342136] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND PHOSPHATE.
[4]	"Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic 'snapshots' of intermediate states." Wang W., Cho H.S., Kim R., Jancarik J., Yokota H., Nguyen H.H., Grigoriev I.V., Wemmer D.E., Kim S.-H. J. Mol. Biol. 319:421-431(2002) [PubMed: 12051918] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM; SUBSTRATE; PHOSPHATE AND TRANSITION STATE ANALOG, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME MECHANISM, COFACTOR, MUTAGENESIS OF ASP-11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L77117 Genomic DNA. Translation: AAB99612.1.

PIR

A64499.

RefSeq

NP_248603.1. NC_000909.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F5S	X-ray	1.80	A/B	1-211	[»]
1J97	X-ray	1.50	A/B	1-211	[»]
1L7M	X-ray	1.48	A/B	1-211	[»]
1L7N	X-ray	1.80	A/B	1-211	[»]
1L7O	X-ray	2.20	A/B	1-211	[»]
1L7P	X-ray	1.90	A/B	1-211	[»]

ProteinModelPortal

Q58989.

SMR

Q58989. Positions 2-211.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1452502.

GenomeReviews

Gene locus MJ1594 in contig L77117_GR.

KEGG

mja:MJ_1594.

NMPDR

fig|243232.1.peg.1640.

TIGR

MJ1594.

Phylogenomic databases

HOGENOM

HBG645339.

OMA

INIECVD.

ProtClustDB

CLSK876636.

Enzyme and pathway databases

BioCyc

MJAN243232:MJ_1594-MONOMER.

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_METJA

Accession

Primary (citable) accession number: Q58989

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	November 16, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program