SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P56839

- PEPM_MYTED

UniProt

P56839 - PEPM_MYTED

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Phosphoenolpyruvate phosphomutase

Gene
N/A
Organism
Mytilus edulis (Blue mussel)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).

Catalytic activityi

Phosphoenolpyruvate = 3-phosphonopyruvate.

Cofactori

Magnesium.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581Nucleophile Reviewed prediction
Metal bindingi58 – 581Magnesium

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphoenolpyruvate mutase activity Source: UniProtKB-EC

GO - Biological processi

  1. organic phosphonate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16744.
UniPathwayiUPA00960.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate phosphomutase (EC:5.4.2.9)
Short name:
PEP mutase
Short name:
PEP phosphomutase
Short name:
Phosphoenolpyruvate mutase
OrganismiMytilus edulis (Blue mussel)
Taxonomic identifieri6550 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaMytiloidaMytiloideaMytilidaeMytilinaeMytilus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581D → A or S: Abolishes enzyme activity. 2 Publications
Mutagenesisi58 – 581D → N: Strongly reduces enzyme activity. 2 Publications
Mutagenesisi85 – 851D → A: Strongly reduces enzyme activity and increases KM. 1 Publication
Mutagenesisi87 – 871D → A: Strongly reduces enzyme activity. 1 Publication
Mutagenesisi114 – 1141E → A: Strongly reduces enzyme activity. 1 Publication
Mutagenesisi122 – 1221N → A or D: Strongly reduces enzyme activity. 1 Publication
Mutagenesisi159 – 1591R → A: Strongly reduces enzyme activity. 1 Publication
Mutagenesisi190 – 1901H → A: Strongly reduces enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 295294Phosphoenolpyruvate phosphomutasePRO_0000068824Add
BLAST

Interactioni

Subunit structurei

Homotetramer.2 Publications

Structurei

Secondary structure

1
295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 1610
Beta strandi17 – 193
Beta strandi21 – 266
Helixi29 – 3810
Beta strandi43 – 453
Helixi48 – 525
Turni58 – 603
Helixi65 – 7612
Beta strandi82 – 854
Beta strandi90 – 923
Helixi93 – 10513
Beta strandi110 – 1145
Beta strandi126 – 1283
Helixi135 – 14814
Beta strandi155 – 1606
Turni162 – 1665
Helixi169 – 18113
Beta strandi185 – 1895
Beta strandi193 – 1964
Helixi197 – 20610
Beta strandi208 – 2103
Beta strandi212 – 2143
Turni218 – 2214
Helixi224 – 2307
Beta strandi234 – 2374
Helixi240 – 25920
Beta strandi260 – 2623
Turni263 – 2653
Helixi266 – 2683
Helixi272 – 2776
Helixi281 – 29111

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M1BX-ray2.25A/B1-295[»]
1PYMX-ray1.80A/B1-295[»]
1S2TX-ray2.00A/B1-295[»]
1S2UX-ray2.00A/B1-295[»]
1S2VX-ray2.10A/B/C/D1-295[»]
1S2WX-ray1.69A1-295[»]
ProteinModelPortaliP56839.
SMRiP56839. Positions 5-295.

Miscellaneous databases

EvolutionaryTraceiP56839.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR012698. PEnolPyrv_PMutase_core.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR02320. PEP_mutase. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P56839-1 [UniParc]FASTAAdd to Basket

« Hide

MSTKVKKTTQ LKQMLNSKDL EFIMEAHNGL SARIVQEAGF KGIWGSGLSV    50
SAQLGVRDSN EASWTQVVEV LEFMSDASDV PILLDADTGY GNFNNARRLV 100
RKLEDRGVAG ACLEDKLFPK TNSLHDGRAQ PLADIEEFAL KIKACKDSQT 150
DPDFCIVARV EAFIAGWGLD EALKRAEAYR NAGADAILMH SKKADPSDIE 200
AFMKAWNNQG PVVIVPTKYY KTPTDHFRDM GVSMVIWANH NLRASVSAIQ 250
QTTKQIYDDQ SLVNVEDKIV SVKEIFRLQR DDELVQAEDK YLPKN 295
Length:295
Mass (Da):32,912
Last modified:January 23, 2007 - v3
Checksum:iA8A7CC4FD6B031F8
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M1B X-ray 2.25 A/B 1-295 [» ]
1PYM X-ray 1.80 A/B 1-295 [» ]
1S2T X-ray 2.00 A/B 1-295 [» ]
1S2U X-ray 2.00 A/B 1-295 [» ]
1S2V X-ray 2.10 A/B/C/D 1-295 [» ]
1S2W X-ray 1.69 A 1-295 [» ]
ProteinModelPortali P56839.
SMRi P56839. Positions 5-295.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00960 .
BioCyci MetaCyc:MONOMER-16744.

Miscellaneous databases

EvolutionaryTracei P56839.

Family and domain databases

Gene3Di 3.20.20.60. 1 hit.
InterProi IPR012698. PEnolPyrv_PMutase_core.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view ]
SUPFAMi SSF51621. SSF51621. 1 hit.
TIGRFAMsi TIGR02320. PEP_mutase. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Insight into the mechanism of phosphoenolpyruvate mutase catalysis derived from site-directed mutagenesis studies of active site residues."
    Jia Y., Lu Z., Huang K., Herzberg O., Dunaway-Mariano D.
    Biochemistry 38:14165-14173(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16 AND 115-129, MUTAGENESIS OF ASP-58; ASP-85; ASP-87; GLU-114 AND ARG-159, HOMOTETRAMERIZATION.
  2. "Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate."
    Huang K., Li Z., Jia Y., Dunaway-Mariano D., Herzberg O.
    Structure 7:539-548(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MG(2+) AND AN OXALATE INHIBITOR, HOMOTETRAMERIZATION.
  3. "Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/sulfopyruvate complex and kinetic properties of mutants."
    Liu S., Lu Z., Jia Y., Dunaway-Mariano D., Herzberg O.
    Biochemistry 41:10270-10276(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 6-295 IN COMPLEX WITH SULFOPYRUVATE, MUTAGENESIS OF ASP-58; ASN-122 AND HIS-190.

Entry informationi

Entry nameiPEPM_MYTED
AccessioniPrimary (citable) accession number: P56839
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 74 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi