O58690 (MPGP_PYRHO) Reviewed, UniProtKB/Swiss-Prot

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 (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › Pyrococcus horikoshii

Protein attributes

Sequence length	243 AA.
Sequence status	Complete.
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-Rule MF_00617
Catalytic activity	2(alpha-D-mannosyl)-3-phosphoglycerate + H2O = 2(alpha-D-mannosyl)-D-glycerate + phosphate. HAMAP-Rule MF_00617
Cofactor	Magnesium.
Pathway	Carbohydrate biosynthesis; 2-(alpha-D-mannosyl)-D-glycerate biosynthesis; 2-(alpha-D-mannosyl)-D-glycerate from GDP-alpha-D-mannose (MPG route): step 2/2. HAMAP-Rule MF_00617
Subcellular location	Cytoplasm HAMAP-Rule 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	dephosphorylation Inferred from electronic annotation. Source: GOC mannosylglycerate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	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-Rule 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 – 69

3

Beta strand

89 – 91

3

Helix

96 – 110

15

Helix

115 – 117

3

Helix

120 – 127

8

Turn

131 – 133

3

Helix

134 – 138

5

Beta strand

144 – 148

5

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

229 – 234

6

Helix

235 – 243

9

Sequences

	Sequence		Length	Mass (Da)
	O58690 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[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] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. Translation: BAA30022.1.

PIR

H71082.

RefSeq

NP_142849.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O58690.

SMR

O58690. Positions 1-243.

ModBase

Search...

Protein-protein interaction databases

STRING

70601.PH0926.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAA30022; BAA30022; BAA30022.

GeneID

1443251.

KEGG

pho:PH0926.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG3769.

HOGENOM

HOG000224319.

KO

K07026.

OMA

GLKYYGN.

ProtClustDB

PRK00192.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13379.
PHOR70601:GJWR-919-MONOMER.

SABIO-RK

O58690.

UniPathway

UPA00130; UER00193.

Family and domain databases

Gene3D

3.40.50.1000. 2 hits.

HAMAP

MF_00617. MPGP_rel.

InterPro

IPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR006381. HAD-SF_hydro_IIB_YedP.
IPR012815. MPG_Pase.
IPR012813. Osmo_MPG_phos.
[Graphical view]

Pfam

PF08282. Hydrolase_3. 2 hits.
[Graphical view]

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

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

ProtoNet

Search...

Other

EvolutionaryTrace

O58690.

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:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program