Reviewed, UniProtKB/Swiss-Prot O58690 (MPGP_PYRHO)

Names and origin

Protein names

Recommended name:
    Mannosyl-3-phosphoglycerate phosphatase
      Short name=MPGP
    EC=3.1.3.70

Gene names

Name:	mngB
Ordered Locus Names:	PH0926

Organism

Pyrococcus horikoshii [Complete proteome] [HAMAP]

Taxonomic identifier

53953 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	243 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes mannosyl-3-phosphoglycerate (MPG) to form the osmolyte mannosylglycerate (MG). The enzyme is absolutely specific for MPG. HAMAP MF_00617
Catalytic activity	2(alpha-D-mannosyl)-3-phosphoglycerate + H2O = 2(alpha-D-mannosyl)-D-glycerate + phosphate. HAMAP MF_00617
Cofactor	Magnesium. HAMAP MF_00617
Pathway	Carbohydrate biosynthesis; mannosylglycerate biosynthesis; 2(alpha-D-mannosyl)-D-glycerate from GDP-D-mannose (MPG route): step 2/2. HAMAP MF_00617
Subcellular location	Cytoplasm. HAMAP MF_00617
Sequence similarities	Belongs to the HAD-like hydrolase superfamily. MPGP family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	mannosylglycerate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW mannosyl-3-phosphoglycerate 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 – 243

243

Mannosyl-3-phosphoglycerate phosphatase HAMAP MF_00617

PRO_0000184973

Secondary structure

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243

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Turn

11 – 13

3

Beta strand

14 – 17

4

Helix

20 – 22

3

Helix

23 – 31

9

Beta strand

34 – 39

6

Helix

44 – 54

11

Beta strand

60 – 62

3

Turn

63 – 66

4

Beta strand

67 – 70

4

Beta strand

88 – 91

4

Helix

96 – 110

15

Helix

115 – 117

3

Helix

120 – 127

8

Helix

131 – 133

3

Helix

134 – 137

4

Beta strand

141 – 146

6

Beta strand

150 – 152

3

Helix

154 – 160

7

Beta strand

164 – 167

4

Beta strand

169 – 175

7

Helix

180 – 192

13

Beta strand

197 – 203

7

Helix

206 – 208

3

Helix

209 – 212

4

Beta strand

215 – 223

9

Beta strand

230 – 233

4

Helix

235 – 242

8

Sequences

	Sequence		Length	Mass (Da)
	O58690-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: FE5EE94DCAAD3636	FASTA	243	27,959
	10 20 30 40 50 60 MIRLIFLDID KTLIPGYEPD PAKPIIEELK DMGFEIIFNS SKTRAEQEYY RKELEVETPF 70 80 90 100 110 120 ISENGSAIFI PKGYFPFDVK GKEVGNYIVI ELGIRVEKIR EELKKLENIY GLKYYGNSTK 130 140 150 160 170 180 EEIEKFTGMP PELVPLAMER EYSETIFEWS RDGWEEVLVE GGFKVTMGSR FYTVHGNSDK 190 200 210 220 230 240 GKAAKILLDF YKRLGQIESY AVGDSYNDFP MFEVVDKAFI VGSLKHKKAQ NVSSIIDVLE VIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: OT3.
[2]	"Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes." Empadinhas N., Marugg J.D., Borges N., Santos H., da Costa M.S. J. Biol. Chem. 276:43580-43588(2001) [PubMed: 11562374] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

BA000001 Genomic DNA. Translation: BAA30022.1.

PIR

H71082.

RefSeq

NP_142849.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WZC	X-ray	1.90	A/B	1-243	[»]
2ZOS	X-ray	1.70	A/B	1-243	[»]

ModBase

Search...

Genome annotation databases

GeneID

1443251.

GenomeReviews

Gene locus PH0926 in contig BA000001_GR.

KEGG

pho:PH0926.

NMPDR

fig|70601.1.peg.904.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

O58690.

OMA

O58690. EYSETIF.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13379.

BRENDA

3.1.3.70. 74679.

Family and domain databases

HAMAP

MF_00617.
[Tree]

InterPro

IPR013200. HAD-SF_hydro-like_3.
IPR006379. HAD-SF_hydro_IIB.
IPR006381. HAD-SF_hydro_IIB_YedP.
IPR012813. Osmo_MPG_phos.
[Graphical view]

Pfam

PF08282. Hydrolase_3. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01484. HAD-SF-IIB. 1 hit.
TIGR01486. HAD-SF-IIB-MPGP. 1 hit.
TIGR02461. osmo_MPG_phos. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MPGP_PYRHO

Accession

Primary (citable) accession number: O58690

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	August 1, 1998
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)