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Protein

Phosphoenolpyruvate phosphomutase

Gene
N/A
Organism
Mytilus edulis (Blue mussel)
Status
Reviewed-Annotation score: 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: phosphonate biosynthesis

This protein is involved in the pathway phosphonate biosynthesis, which is part of Phosphorus metabolism.
View all proteins of this organism that are known to be involved in the pathway phosphonate biosynthesis and in Phosphorus metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei58NucleophileSequence analysis1
Metal bindingi58Magnesium1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16744.
BRENDAi5.4.2.9. 3544.
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)DescriptionActionsGraphical viewLength
Mutagenesisi58D → A or S: Abolishes enzyme activity. 2 Publications1
Mutagenesisi58D → N: Strongly reduces enzyme activity. 2 Publications1
Mutagenesisi85D → A: Strongly reduces enzyme activity and increases KM. 1 Publication1
Mutagenesisi87D → A: Strongly reduces enzyme activity. 1 Publication1
Mutagenesisi114E → A: Strongly reduces enzyme activity. 1 Publication1
Mutagenesisi122N → A or D: Strongly reduces enzyme activity. 1 Publication1
Mutagenesisi159R → A: Strongly reduces enzyme activity. 1 Publication1
Mutagenesisi190H → A: Strongly reduces enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000688242 – 295Phosphoenolpyruvate phosphomutaseAdd BLAST294

Proteomic databases

PRIDEiP56839.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Structurei

Secondary structure

1295
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 16Combined sources10
Beta strandi17 – 19Combined sources3
Beta strandi21 – 26Combined sources6
Helixi29 – 38Combined sources10
Beta strandi43 – 45Combined sources3
Helixi48 – 52Combined sources5
Turni58 – 60Combined sources3
Helixi65 – 76Combined sources12
Beta strandi82 – 85Combined sources4
Beta strandi90 – 92Combined sources3
Helixi93 – 105Combined sources13
Beta strandi110 – 114Combined sources5
Beta strandi126 – 128Combined sources3
Helixi135 – 148Combined sources14
Beta strandi155 – 160Combined sources6
Turni162 – 166Combined sources5
Helixi169 – 181Combined sources13
Beta strandi185 – 189Combined sources5
Beta strandi193 – 196Combined sources4
Helixi197 – 206Combined sources10
Beta strandi208 – 210Combined sources3
Beta strandi212 – 214Combined sources3
Turni218 – 221Combined sources4
Helixi224 – 230Combined sources7
Beta strandi234 – 237Combined sources4
Helixi240 – 259Combined sources20
Beta strandi260 – 262Combined sources3
Turni263 – 265Combined sources3
Helixi266 – 268Combined sources3
Helixi272 – 277Combined sources6
Helixi281 – 291Combined sources11

3D structure databases

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

Proteomic databases

PRIDEiP56839.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00960.
BioCyciMetaCyc:MONOMER-16744.
BRENDAi5.4.2.9. 3544.

Miscellaneous databases

EvolutionaryTraceiP56839.

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.
ProtoNetiSearch...

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 2, 2016
This is version 82 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

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.