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Q1W374

- PMM_WHEAT

UniProt

Q1W374 - PMM_WHEAT

Protein

Phosphomannomutase

Gene
N/A
Organism
Triticum aestivum (Wheat)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 33 (01 Oct 2014)
      Sequence version 1 (02 May 2006)
      Previous versions | rss
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    • Comment

    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

    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: Unplaced

    Organism-specific databases

    GrameneiQ1W374.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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

    MAAARKDAGV LALFDVDGTL TAPRKEVTPE MLEFMKRLRE NVTVGVVGGS    50
    DLVKISEQLG KSVITDYDYV FSENGLVAHK DGKLIGTQSL KTYLGDDQLK 100
    EFINFTLHYI ADLDIPIKRG TFIEFRSGMI NVSPIGRNCS QEERDDFEKY 150
    DKVHNVRPKM VSVLREKFAH LNLTFSIGGQ ISFDVFPQGW DKTYCLRYLE 200
    EFKEIHFFGD KTYKGGNDHE IFESDRTVGH TVTSPNDTVQ QCKSIFLSE 249
    Length:249
    Mass (Da):28,252
    Last modified:May 2, 2006 - v1
    Checksum:iAB85F0AB97DCD566
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ442996 mRNA. Translation: ABD97875.1.
    UniGeneiTa.3539.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ442996 mRNA. Translation: ABD97875.1 .
    UniGenei Ta.3539.

    3D structure databases

    ProteinModelPortali Q1W374.
    SMRi Q1W374. Positions 11-246.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q1W374.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei Q1W374.

    Enzyme and pathway databases

    UniPathwayi UPA00126 ; UER00424 .

    Family and domain databases

    Gene3Di 3.40.50.1000. 2 hits.
    InterProi IPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR005002. PMM.
    [Graphical view ]
    PANTHERi PTHR10466. PTHR10466. 1 hit.
    Pfami PF03332. PMM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR01484. HAD-SF-IIB. 1 hit.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 33 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