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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581NucleophileSequence Analysis
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 – 1610Combined sources
Beta strandi17 – 193Combined sources
Beta strandi21 – 266Combined sources
Helixi29 – 3810Combined sources
Beta strandi43 – 453Combined sources
Helixi48 – 525Combined sources
Turni58 – 603Combined sources
Helixi65 – 7612Combined sources
Beta strandi82 – 854Combined sources
Beta strandi90 – 923Combined sources
Helixi93 – 10513Combined sources
Beta strandi110 – 1145Combined sources
Beta strandi126 – 1283Combined sources
Helixi135 – 14814Combined sources
Beta strandi155 – 1606Combined sources
Turni162 – 1665Combined sources
Helixi169 – 18113Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi193 – 1964Combined sources
Helixi197 – 20610Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi212 – 2143Combined sources
Turni218 – 2214Combined sources
Helixi224 – 2307Combined sources
Beta strandi234 – 2374Combined sources
Helixi240 – 25920Combined sources
Beta strandi260 – 2623Combined sources
Turni263 – 2653Combined sources
Helixi266 – 2683Combined sources
Helixi272 – 2776Combined sources
Helixi281 – 29111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MSTKVKKTTQ LKQMLNSKDL EFIMEAHNGL SARIVQEAGF KGIWGSGLSV
60 70 80 90 100
SAQLGVRDSN EASWTQVVEV LEFMSDASDV PILLDADTGY GNFNNARRLV
110 120 130 140 150
RKLEDRGVAG ACLEDKLFPK TNSLHDGRAQ PLADIEEFAL KIKACKDSQT
160 170 180 190 200
DPDFCIVARV EAFIAGWGLD EALKRAEAYR NAGADAILMH SKKADPSDIE
210 220 230 240 250
AFMKAWNNQG PVVIVPTKYY KTPTDHFRDM GVSMVIWANH NLRASVSAIQ
260 270 280 290
QTTKQIYDDQ SLVNVEDKIV SVKEIFRLQR DDELVQAEDK YLPKN
Length:295
Mass (Da):32,912
Last modified:January 23, 2007 - v3
Checksum:iA8A7CC4FD6B031F8
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 77 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