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Protein

Mannitol 2-dehydrogenase

Gene

AFUA_4G14450

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

D-mannitol + NAD+ = D-fructose + NADH.

Kineticsi

  1. KM=13 mM for D-mannitol (in the presence of NAD+)1 Publication
  2. KM=82 mM for D-mannitol (in the presence of NADP+)1 Publication
  3. KM=60 mM for D-fructose (in the presence of NADH)1 Publication
  4. KM=159 mM for D-fructose (in the presence of NADPH)1 Publication
  5. KM=0.019 mM for NADH1 Publication
  6. KM=0.15 mM for NAD+1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi37 – 4812NADBy similarityAdd
    BLAST

    GO - Molecular functioni

    • mannitol 2-dehydrogenase activity Source: UniProtKB
    • NAD binding Source: UniProtKB
    • NADP binding Source: UniProtKB

    GO - Biological processi

    • mannitol metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD, NADP

    Enzyme and pathway databases

    BRENDAi1.1.1.67. 508.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannitol 2-dehydrogenase (EC:1.1.1.67)
    Short name:
    M2DH
    Short name:
    MDH
    Gene namesi
    ORF Names:AFUA_4G14450
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530 Componenti: Chromosome 4

    Organism-specific databases

    EuPathDBiFungiDB:Afu4g14450.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 502502Mannitol 2-dehydrogenasePRO_0000371540Add
    BLAST

    Proteomic databases

    PRIDEiQ4WQY4.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WQY4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the mannitol dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG0246.
    HOGENOMiHOG000202982.
    InParanoidiQ4WQY4.
    KOiK00045.
    OMAiCHNPATG.
    OrthoDBiEOG7PCJRT.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR000669. Mannitol_DH.
    IPR013118. Mannitol_DH_C.
    IPR013131. Mannitol_DH_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01232. Mannitol_dh. 1 hit.
    PF08125. Mannitol_dh_C. 1 hit.
    [Graphical view]
    PRINTSiPR00084. MTLDHDRGNASE.
    SUPFAMiSSF48179. SSF48179. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q4WQY4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAPLKLNSRN LSQIAAAGGA LVKIPTYQRG RAVKEGIVHI GVGGFHRAHL
    60 70 80 90 100
    AVYIDQLMQK HGVNDYAICG VGLQPFDSAM RDALASQDHL YTLIERSAKG
    110 120 130 140 150
    SFAHVIGSIN SYLFAPDNRE AVIAKMAHPD TKIVSLTITE SGYYYNENTH
    160 170 180 190 200
    ELQSEHPDIQ FDLDPANEKA PRTTFGFLYA GLTRRYQQGL KPFTVMSCDN
    210 220 230 240 250
    MQKNGSITRH MLESFARLRN PEVAEWIAEE GAFPNAMVDR ITPQTSETDK
    260 270 280 290 300
    TALAEKFGIV DSWPVVTEPF TQWVIEDQFS DGRPPFEKVG VQVVKDVHAV
    310 320 330 340 350
    EQFEKHKLRL LNGSHSALGY PGQLAGFQYV HEVMANPLFR KFVWQMMQEE
    360 370 380 390 400
    VKPLLPEIPG VDIDEYCNTL IERFTNPTIM DQLPRICLNA SGKIPQFIMP
    410 420 430 440 450
    SIAEAIWETG PFRRLCFVAA AWFHYIKGVD DRGKPFEVVD PMREELQAKA
    460 470 480 490 500
    RAGGNDPSEL LSIKSLFGDD LRNDERFLRE ITTAMNDIAR DGIMKTLPKY

    IN
    Length:502
    Mass (Da):56,475
    Last modified:July 5, 2005 - v1
    Checksum:i230384292D807EB1
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AAHF01000005 Genomic DNA. Translation: EAL89350.1.
    RefSeqiXP_751388.1. XM_746295.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00008043; CADAFUAP00008043; CADAFUAG00008043.
    GeneIDi3509495.
    KEGGiafm:AFUA_4G14450.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AAHF01000005 Genomic DNA. Translation: EAL89350.1.
    RefSeqiXP_751388.1. XM_746295.1.

    3D structure databases

    ProteinModelPortaliQ4WQY4.
    ModBaseiSearch...
    MobiDBiSearch...

    Proteomic databases

    PRIDEiQ4WQY4.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiCADAFUAT00008043; CADAFUAP00008043; CADAFUAG00008043.
    GeneIDi3509495.
    KEGGiafm:AFUA_4G14450.

    Organism-specific databases

    EuPathDBiFungiDB:Afu4g14450.

    Phylogenomic databases

    eggNOGiCOG0246.
    HOGENOMiHOG000202982.
    InParanoidiQ4WQY4.
    KOiK00045.
    OMAiCHNPATG.
    OrthoDBiEOG7PCJRT.

    Enzyme and pathway databases

    BRENDAi1.1.1.67. 508.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR000669. Mannitol_DH.
    IPR013118. Mannitol_DH_C.
    IPR013131. Mannitol_DH_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01232. Mannitol_dh. 1 hit.
    PF08125. Mannitol_dh_C. 1 hit.
    [Graphical view]
    PRINTSiPR00084. MTLDHDRGNASE.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
      Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
      , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
      Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
    2. "Polyol-specific long-chain dehydrogenases/reductases of mannitol metabolism in Aspergillus fumigatus: biochemical characterization and pH studies of mannitol 2-dehydrogenase and mannitol-1-phosphate 5-dehydrogenase."
      Krahulec S., Armao G.C., Bubner P., Klimacek M., Nidetzky B.
      Chem. Biol. Interact. 178:274-282(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiM2DH_ASPFU
    AccessioniPrimary (citable) accession number: Q4WQY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 5, 2009
    Last sequence update: July 5, 2005
    Last modified: June 24, 2015
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. 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.