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Entry version 101 (16 Oct 2019)
Sequence version 1 (05 Jul 2005)
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Protein

Mannitol-1-phosphate 5-dehydrogenase

Gene

mpdA

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway. Has a strong preference for NADH over NADPH.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.23 mM for D-mannitol 1-phosphate2 Publications
  2. KM=2.1 mM for D-fructose 6-phosphate2 Publications
  3. KM=0.016 mM for NADH2 Publications
  4. KM=0.75 mM for NAD+2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei2131

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi5 – 16NADBy similarityAdd BLAST12

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionOxidoreductase
    LigandNAD

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.1.1.17 508

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q4X1A4

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Mannitol-1-phosphate 5-dehydrogenase (EC:1.1.1.17)
    Short name:
    M1PDH
    Short name:
    MPD
    Short name:
    MPDH
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:mpdA
    ORF Names:AFUA_2G10660
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri330879 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002530 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componentsi: Chromosome 2, Unassembled WGS sequence

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    FungiDB:Afu2g10660

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi213K → A: Loss of catalytic activity. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003715201 – 388Mannitol-1-phosphate 5-dehydrogenaseAdd BLAST388

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q4X1A4

    PTM databases

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    Q4X1A4

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer.

    1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    746128.CADAFUBP00002584

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q4X1A4

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the mannitol dehydrogenase family.Curated

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000271391

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q4X1A4

    KEGG Orthology (KO)

    More...
    KOi
    K00009

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    INSRTHE

    Database of Orthologous Groups

    More...
    OrthoDBi
    1133390at2759

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.1040.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00196 Mannitol_dehydrog, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR008927 6-PGluconate_DH-like_C_sf
    IPR013328 6PGD_dom2
    IPR023028 Mannitol_1_phos_5_DH
    IPR000669 Mannitol_DH
    IPR013118 Mannitol_DH_C
    IPR013131 Mannitol_DH_N
    IPR036291 NAD(P)-bd_dom_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01232 Mannitol_dh, 1 hit
    PF08125 Mannitol_dh_C, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00084 MTLDHDRGNASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48179 SSF48179, 1 hit
    SSF51735 SSF51735, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    Q4X1A4-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MGKKAIQFGG GNIGRGFVAE FLHEAGYEVV FIDVVDKIID ALKSTPSYEV
    60 70 80 90 100
    TEVSEEGEKT KTITNYRAIN SKTNEEDVVK EIGTADVVTC AVGPNVLKFI
    110 120 130 140 150
    APVIAKGIDA RTASKPVAVI ACENAIGATD TLRGFIEQNT DKDRLSSMSE
    160 170 180 190 200
    RARFANSAID RIVPNQPPNA GLNVRIEKFY EWTVEQTPFG EFGHPDIPAI
    210 220 230 240 250
    HWVDDLKPYI ERKLFTVNTG HATTAYYGHM RGKKMIADAL ADAEIRQIVH
    260 270 280 290 300
    KVLEQTAKLI TTKHEITEQE QNEYVDTIVK RMSNPFLEDN VERVGRAPLR
    310 320 330 340 350
    KLSRNERFIG PASQLAEKGL PFDALLGSIE MALRFQNVPG DEESAELAKI
    360 370 380
    LKEMSAEEAT GKLTGLEKHH PLYEPVQNVI AKVQKDSK
    Length:388
    Mass (Da):43,004
    Last modified:July 5, 2005 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iEE8F7B90FAFC3B3F
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AAHF01000001 Genomic DNA Translation: EAL93361.1

    NCBI Reference Sequences

    More...
    RefSeqi
    XP_755399.1, XM_750306.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    EAL93361; EAL93361; AFUA_2G10660

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    3513687

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    afm:AFUA_2G10660

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AAHF01000001 Genomic DNA Translation: EAL93361.1
    RefSeqiXP_755399.1, XM_750306.1

    3D structure databases

    SMRiQ4X1A4
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi746128.CADAFUBP00002584

    PTM databases

    SwissPalmiQ4X1A4

    Proteomic databases

    PRIDEiQ4X1A4

    Genome annotation databases

    EnsemblFungiiEAL93361; EAL93361; AFUA_2G10660
    GeneIDi3513687
    KEGGiafm:AFUA_2G10660

    Organism-specific databases

    EuPathDBiFungiDB:Afu2g10660

    Phylogenomic databases

    HOGENOMiHOG000271391
    InParanoidiQ4X1A4
    KOiK00009
    OMAiINSRTHE
    OrthoDBi1133390at2759

    Enzyme and pathway databases

    BRENDAi1.1.1.17 508
    SABIO-RKiQ4X1A4

    Family and domain databases

    Gene3Di1.10.1040.10, 1 hit
    HAMAPiMF_00196 Mannitol_dehydrog, 1 hit
    InterProiView protein in InterPro
    IPR008927 6-PGluconate_DH-like_C_sf
    IPR013328 6PGD_dom2
    IPR023028 Mannitol_1_phos_5_DH
    IPR000669 Mannitol_DH
    IPR013118 Mannitol_DH_C
    IPR013131 Mannitol_DH_N
    IPR036291 NAD(P)-bd_dom_sf
    PfamiView protein in Pfam
    PF01232 Mannitol_dh, 1 hit
    PF08125 Mannitol_dh_C, 1 hit
    PRINTSiPR00084 MTLDHDRGNASE
    SUPFAMiSSF48179 SSF48179, 1 hit
    SSF51735 SSF51735, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMTLD_ASPFU
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q4X1A4
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 5, 2009
    Last sequence update: July 5, 2005
    Last modified: October 16, 2019
    This is version 101 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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