O58689 (MPGS_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mannosyl-3-phosphoglycerate synthase
Short name=MPG synthase
Short name=MPGS
EC=2.4.1.217

Gene names

Name:	mngA
Ordered Locus Names:	PH0927

Organism

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

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transfers a mannosyl group from GDP-mannose to phosphoglycerate to form mannosyl-3-phosphoglycerate (MPG). The enzyme is absolutely specific for GDP-mannose and 3-phosphoglycerate, and transfers the mannosyl group with retention of configuration.
Catalytic activity	GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate.
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 1/2.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium
Molecular function	Glycosyltransferase Transferase
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	mannosyl-3-phosphoglycerate synthase 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 – 394

394

Mannosyl-3-phosphoglycerate synthase

PRO_0000059287

Secondary structure

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394

Helix Strand Turn

Details...

Beta strand

2 – 4

3

Beta strand

9 – 11

3

Beta strand

16 – 18

3

Beta strand

21 – 26

6

Beta strand

38 – 40

3

Helix

43 – 49

7

Beta strand

55 – 61

7

Helix

64 – 67

4

Helix

71 – 73

3

Beta strand

80 – 84

5

Helix

93 – 108

16

Beta strand

112 – 116

5

Helix

123 – 128

6

Helix

154 – 158

5

Helix

177 – 185

9

Beta strand

193 – 201

9

Helix

221 – 237

17

Beta strand

252 – 255

4

Helix

256 – 259

4

Helix

270 – 281

12

Helix

289 – 291

3

Helix

292 – 296

5

Beta strand

300 – 305

6

Helix

318 – 332

15

Helix

339 – 351

13

Helix

375 – 382

8

Beta strand

390 – 392

3

Sequences

	Sequence		Length	Mass (Da)
	O58689 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 6C2FB4141D2CC807	FASTA	394	45,210
	10 20 30 40 50 60 MLLEAPVYKE IFGAVTIHEV QKVIKMDTET EEVPIYTISN IPREKIYDLL GKMAVIVPMK 70 80 90 100 110 120 NEKLHLVDGV LKAIPHKCPI IIVSNSKREG PNRYKLEVDL IRHFYNLTHS KIIMIHQKDP 130 140 150 160 170 180 GLAKAFKEVG YTDILDENGM IRSGKGEGML VGLLLAKAIG AEYVGFVDAD NYIPGAVNEY 190 200 210 220 230 240 VKDYAAGFLM SESEYTMVRL HWRHKPKVTK GTLYFKKWGR VSEITNHYLN LLVSEHTAFE 250 260 270 280 290 300 TTIMVTGNAG EHAMTMKLAE ILPFSTGYSI EPYEIVYILE RFGKWENVEE FKDVFDQGIE 310 320 330 340 350 360 IFQIETLNPH FHEDKGKEHV KEMLLLSLAT IYHSKLATDN LRKRILKDLR DHGILGENEE 370 380 390 PPKPLVMRPI KEIPIKEWMD IVEGNSETLL RFEL

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: 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: 11562374] [Abstract] Cited for: CHARACTERIZATION. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. Translation: BAA30023.1.

PIR

A71083.

RefSeq

NP_142850.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ZU7	X-ray	2.50	A/B	1-394	[»]
2ZU8	X-ray	2.40	A/B	1-394	[»]
2ZU9	X-ray	2.00	A/B	1-394	[»]

ProteinModelPortal

O58689.

ModBase

Search...

Protein family/group databases

CAZy

GT55. Glycosyltransferase Family 55.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000001600; EBPYRP00000001600; EBPYRG00000001600.

GeneID

1443252.

GenomeReviews

Gene locus PH0927 in contig BA000001_GR.

KEGG

pho:PH0927.

NMPDR

fig|70601.1.peg.905.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000022714.

HOGENOM

HBG297698.

OMA

RVSEITN.

ProtClustDB

PRK14503.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13380.
PHOR70601:PH0927-MONOMER.

Family and domain databases

InterPro

IPR012812. Osmo_MPG_synth.
[Graphical view]

KO

K05947.

Pfam

PF09488. Osmo_MPGsynth. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02460. Osmo_MPGsynth. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MPGS_PYRHO

Accession

Primary (citable) accession number: O58689

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	August 1, 1998
Last modified:	November 16, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program