Skip Header

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

Phosphomannomutase

Gene

PMM

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in ascorbic acid biosynthesis and in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.2 Publications

Catalytic activityi

Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.

Kineticsi

Requires glucose-1,6-bisphosphate for activity.
  1. KM=29.7 µM for mannose-1-phosphate1 Publication
  2. KM=65.4 µM for glucose-1-phosphate1 Publication
  1. Vmax=14.4 µmol/min/mg enzyme with mannose-1-phosphate as substrate1 Publication
  2. Vmax=1.4 µmol/min/mg enzyme with glucose-1-phosphate as substrate1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Temperature dependencei

Optimum temperature is 30 degrees Celsius.1 Publication

Pathwayi: GDP-alpha-D-mannose biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Mannose-6-phosphate isomerase 1 (PMI1), Mannose-6-phosphate isomerase 2 (PMI2)
  2. Phosphomannomutase (PMM), Phosphomannomutase (AXX17_At2g43390)
This subpathway is part of the pathway GDP-alpha-D-mannose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate, the pathway GDP-alpha-D-mannose biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei13NucleophileBy similarity1
Active sitei15Proton donor/acceptorSequence analysis1
Binding sitei22SubstrateBy similarity1
Binding sitei124SubstrateBy similarity1
Binding sitei135SubstrateBy similarity1
Binding sitei142SubstrateBy similarity1
Binding sitei180SubstrateBy similarity1
Binding sitei182SubstrateBy similarity1

GO - Molecular functioni

  • phosphomannomutase activity Source: TAIR

GO - Biological processi

  • GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  • L-ascorbic acid biosynthetic process Source: TAIR
  • mannose metabolic process Source: GO_Central
  • protein N-linked glycosylation Source: GO_Central
  • protein targeting to ER Source: GO_Central
  • response to salt stress Source: TAIR

Keywordsi

Molecular functionIsomerase

Enzyme and pathway databases

BioCyciARA:AT2G45790-MONOMER
MetaCyc:AT2G45790-MONOMER
BRENDAi5.4.2.8 399
ReactomeiR-ATH-446205 Synthesis of GDP-mannose
UniPathwayiUPA00126; UER00424

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase (EC:5.4.2.8)
Short name:
AtPMM
Gene namesi
Name:PMM
Ordered Locus Names:At2g45790
ORF Names:F4I18.23
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

AraportiAT2G45790
TAIRilocus:2050751 AT2G45790

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

The thermosensitive lethality of pmm-12 results from glycosylation defects rather than ascorbic acid depletion.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7G → R in pmm-1; 18% reduction of catalytic activity. In pmm-12/dgr1; 92% reduction of catalytic activity resulting in lethality when grown at restrictive temperature; when associated with Q-37. 1 Publication1
Mutagenesisi37R → Q in pmm-2; 86% reduction of catalytic activity. In pmm-12/dgr1; 92% reduction of catalytic activity resulting in lethality when grown at restrictive temperature; when associated with R-7. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001997001 – 246PhosphomannomutaseAdd BLAST246

Proteomic databases

PaxDbiO80840
PRIDEiO80840

PTM databases

iPTMnetiO80840

Expressioni

Tissue specificityi

Expressed in roots, stems, leaves, flower buds, flowers and immature fruits.1 Publication

Gene expression databases

ExpressionAtlasiO80840 differential
GenevisibleiO80840 AT

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi4523, 2 interactors
IntActiO80840, 1 interactor
STRINGi3702.AT2G45790.1

Structurei

3D structure databases

ProteinModelPortaliO80840
SMRiO80840
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic PMM family.Curated

Phylogenomic databases

eggNOGiKOG3189 Eukaryota
COG0561 LUCA
HOGENOMiHOG000181843
InParanoidiO80840
KOiK17497
OMAiTYCLQHL
OrthoDBiEOG09360J1K
PhylomeDBiO80840

Family and domain databases

CDDicd02585 HAD_PMM, 1 hit
Gene3Di3.40.50.1000, 2 hits
InterProiView protein in InterPro
IPR036412 HAD-like_sf
IPR006379 HAD-SF_hydro_IIB
IPR023214 HAD_sf
IPR005002 PMM
PANTHERiPTHR10466 PTHR10466, 1 hit
PfamiView protein in Pfam
PF03332 PMM, 1 hit
SFLDiSFLDG01143 C2.B.3:_Phosphomannomutase_Lik, 1 hit
SUPFAMiSSF56784 SSF56784, 1 hit
TIGRFAMsiTIGR01484 HAD-SF-IIB, 1 hit

Sequencei

Sequence statusi: Complete.

O80840-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAKIPGVIA LFDVDGTLTA PRKEATPELL DFIRELRKVV TIGVVGGSDL
60 70 80 90 100
SKISEQLGKT VTNDYDYCFS ENGLVAHKDG KSIGIQSLKL HLGDDKLKEL
110 120 130 140 150
INFTLHYIAD LDIPIKRGTF IEFRNGMLNV SPIGRNCSQE ERDEFERYDK
160 170 180 190 200
VQNIRPKMVA ELRERFAHLN LTFSIGGQIS FDVFPKGWDK TYCLQYLEDF
210 220 230 240
SEIHFFGDKT YEGGNDYEIY ESPKTIGHSV TSPDDTVAKC KALFMS
Length:246
Mass (Da):27,762
Last modified:November 1, 1998 - v1
Checksum:i52971A3F1AE08DF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ442991 mRNA Translation: ABD97870.1
AC004665 Genomic DNA Translation: AAC28545.1
CP002685 Genomic DNA Translation: AEC10601.1
AY050806 mRNA Translation: AAK92741.1
AY113964 mRNA Translation: AAM45012.1
AY088930 mRNA Translation: AAM67236.1
PIRiT02468
RefSeqiNP_182103.1, NM_130142.4
UniGeneiAt.20569
At.48595

Genome annotation databases

EnsemblPlantsiAT2G45790.1; AT2G45790.1; AT2G45790
GeneIDi819187
GrameneiAT2G45790.1; AT2G45790.1; AT2G45790
KEGGiath:AT2G45790

Similar proteinsi

Entry informationi

Entry nameiPMM_ARATH
AccessioniPrimary (citable) accession number: O80840
Secondary accession number(s): Q1W379
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1998
Last modified: May 23, 2018
This is version 134 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health