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Protein

Phosphomannomutase

Gene
N/A
Organism
Triticum aestivum (Wheat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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.By similarity

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei15 – 151NucleophileBy similarity
Active sitei17 – 171Proton donor/acceptorSequence Analysis
Binding sitei24 – 241SubstrateBy similarity
Binding sitei126 – 1261SubstrateBy similarity
Binding sitei137 – 1371SubstrateBy similarity
Binding sitei144 – 1441SubstrateBy similarity
Binding sitei182 – 1821SubstrateBy similarity
Binding sitei184 – 1841SubstrateBy similarity

GO - Molecular functioni

  1. phosphomannomutase activity Source: UniProtKB-EC

GO - Biological processi

  1. GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  2. mannose biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase (EC:5.4.2.8)
Alternative name(s):
TaPMM
OrganismiTriticum aestivum (Wheat)
Taxonomic identifieri4565 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum
ProteomesiUP000019116 Componenti: Unplaced

Organism-specific databases

GrameneiQ1W374.

Subcellular locationi

  1. Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249PhosphomannomutasePRO_0000326497Add
BLAST

Proteomic databases

PRIDEiQ1W374.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ1W374.
SMRiQ1W374. Positions 11-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic PMM family.Curated

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]
PANTHERiPTHR10466. PTHR10466. 1 hit.
PfamiPF03332. PMM. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q1W374-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAARKDAGV LALFDVDGTL TAPRKEVTPE MLEFMKRLRE NVTVGVVGGS
60 70 80 90 100
DLVKISEQLG KSVITDYDYV FSENGLVAHK DGKLIGTQSL KTYLGDDQLK
110 120 130 140 150
EFINFTLHYI ADLDIPIKRG TFIEFRSGMI NVSPIGRNCS QEERDDFEKY
160 170 180 190 200
DKVHNVRPKM VSVLREKFAH LNLTFSIGGQ ISFDVFPQGW DKTYCLRYLE
210 220 230 240
EFKEIHFFGD KTYKGGNDHE IFESDRTVGH TVTSPNDTVQ QCKSIFLSE
Length:249
Mass (Da):28,252
Last modified:May 2, 2006 - v1
Checksum:iAB85F0AB97DCD566
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ442996 mRNA. Translation: ABD97875.1.
UniGeneiTa.3539.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ442996 mRNA. Translation: ABD97875.1.
UniGeneiTa.3539.

3D structure databases

ProteinModelPortaliQ1W374.
SMRiQ1W374. Positions 11-246.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ1W374.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiQ1W374.

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]
PANTHERiPTHR10466. PTHR10466. 1 hit.
PfamiPF03332. PMM. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular and functional analysis of phosphomannomutase (PMM) from higher plants and genetic evidence for the involvement of PMM in ascorbic acid biosynthesis in Arabidopsis and Nicotiana benthamiana."
    Qian W., Yu C., Qin H., Liu X., Zhang A., Johansen I.E., Wang D.
    Plant J. 49:399-413(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPMM_WHEAT
AccessioniPrimary (citable) accession number: Q1W374
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 2, 2006
Last modified: January 7, 2015
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.