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Protein

Mannosyl-3-phosphoglycerate phosphatase

Gene

yedP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O = 2-O-(alpha-D-mannosyl)-D-glycerate + phosphate.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei13 – 131NucleophileUniRule annotationCurated
Metal bindingi13 – 131MagnesiumUniRule annotation
Metal bindingi15 – 151Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi214 – 2141MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7048-MONOMER.
ECOL316407:JW1938-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannosyl-3-phosphoglycerate phosphatase1 PublicationUniRule annotation (EC:3.1.3.70UniRule annotation1 Publication)
Short name:
MPGPUniRule annotation
Gene namesi
Name:yedP
Ordered Locus Names:b1955, JW1938
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14039. yedP.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Mannosyl-3-phosphoglycerate phosphatasePRO_0000184974Add
BLAST

Proteomic databases

PaxDbiP76329.
PRIDEiP76329.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
yedIP461251EBI-1126577,EBI-1126588

Protein-protein interaction databases

BioGridi4261051. 8 interactions.
DIPiDIP-11848N.
IntActiP76329. 3 interactions.
STRINGi511145.b1955.

Structurei

Secondary structure

1
271
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 136Combined sources
Turni15 – 173Combined sources
Helixi30 – 389Combined sources
Beta strandi43 – 464Combined sources
Helixi51 – 6010Combined sources
Beta strandi68 – 703Combined sources
Helixi71 – 733Combined sources
Beta strandi75 – 773Combined sources
Turni86 – 894Combined sources
Beta strandi90 – 923Combined sources
Helixi97 – 11115Combined sources
Beta strandi115 – 1173Combined sources
Helixi118 – 1203Combined sources
Helixi123 – 1308Combined sources
Helixi134 – 1418Combined sources
Beta strandi147 – 1515Combined sources
Helixi155 – 16713Combined sources
Beta strandi170 – 1745Combined sources
Beta strandi179 – 1835Combined sources
Helixi188 – 20316Combined sources
Beta strandi208 – 2158Combined sources
Helixi216 – 2183Combined sources
Helixi219 – 2235Combined sources
Beta strandi225 – 2306Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XVIX-ray2.26A/B1-271[»]
ProteinModelPortaliP76329.
SMRiP76329. Positions 1-234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP76329.

Family & Domainsi

Sequence similaritiesi

Belongs to the HAD-like hydrolase superfamily. MPGP family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108ZFX. Bacteria.
COG3769. LUCA.
HOGENOMiHOG000224319.
KOiK07026.
OMAiDHHTYSF.
OrthoDBiEOG62G5MV.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
HAMAPiMF_00617. MPGP_rel.
InterProiIPR023214. HAD-like_dom.
IPR006381. HAD-SF-IIB-MPGP.
IPR006379. HAD-SF_hydro_IIB.
IPR012815. MPG_Pase.
[Graphical view]
PfamiPF08282. Hydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
TIGR01486. HAD-SF-IIB-MPGP. 1 hit.

Sequencei

Sequence statusi: Complete.

P76329-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSIQQPLLV FSDLDGTLLD SHSYDWQPAA PWLTRLREAN VPVILCSSKT
60 70 80 90 100
SAEMLYLQKT LGLQGLPLIA ENGAVIQLAE QWQEIDGFPR IISGISHGEI
110 120 130 140 150
SLVLNTLREK EHFKFTTFDD VDDATIAEWT GLSRSQAALT QLHEASVTLI
160 170 180 190 200
WRDSDERMAQ FTARLNELGL QFMQGARFWH VLDASAGKDQ AANWIIATYQ
210 220 230 240 250
QLSGKRPTTL GLGDGPNDAP LLEVMDYAVI VKGLNREGVH LHDEDPARVW
260 270
RTQREGPEGW REGLDHFFSA R
Length:271
Mass (Da):30,439
Last modified:February 1, 1997 - v1
Checksum:i1192A5DC83F71816
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75021.1.
AP009048 Genomic DNA. Translation: BAE76555.1.
PIRiG64959.
RefSeqiNP_416464.1. NC_000913.3.
WP_000491520.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75021; AAC75021; b1955.
BAE76555; BAE76555; BAE76555.
GeneIDi946472.
KEGGiecj:JW1938.
eco:b1955.
PATRICi32119237. VBIEscCol129921_2033.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75021.1.
AP009048 Genomic DNA. Translation: BAE76555.1.
PIRiG64959.
RefSeqiNP_416464.1. NC_000913.3.
WP_000491520.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XVIX-ray2.26A/B1-271[»]
ProteinModelPortaliP76329.
SMRiP76329. Positions 1-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261051. 8 interactions.
DIPiDIP-11848N.
IntActiP76329. 3 interactions.
STRINGi511145.b1955.

Proteomic databases

PaxDbiP76329.
PRIDEiP76329.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75021; AAC75021; b1955.
BAE76555; BAE76555; BAE76555.
GeneIDi946472.
KEGGiecj:JW1938.
eco:b1955.
PATRICi32119237. VBIEscCol129921_2033.

Organism-specific databases

EchoBASEiEB3793.
EcoGeneiEG14039. yedP.

Phylogenomic databases

eggNOGiENOG4108ZFX. Bacteria.
COG3769. LUCA.
HOGENOMiHOG000224319.
KOiK07026.
OMAiDHHTYSF.
OrthoDBiEOG62G5MV.

Enzyme and pathway databases

BioCyciEcoCyc:G7048-MONOMER.
ECOL316407:JW1938-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP76329.
PROiP76329.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
HAMAPiMF_00617. MPGP_rel.
InterProiIPR023214. HAD-like_dom.
IPR006381. HAD-SF-IIB-MPGP.
IPR006379. HAD-SF_hydro_IIB.
IPR012815. MPG_Pase.
[Graphical view]
PfamiPF08282. Hydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
TIGR01486. HAD-SF-IIB-MPGP. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: CATALYTIC ACTIVITY, COFACTOR.
  4. "Crystal Structure of YedP, phosphatase-like domain protein from Escherichia coli K12."
    Kim Y., Joachimiak A., Cymborowski M., Skarina T., Savchenko A., Edwards A.
    Submitted (OCT-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS).

Entry informationi

Entry nameiMPGP_ECOLI
AccessioniPrimary (citable) accession number: P76329
Secondary accession number(s): Q2MB01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: April 13, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.