ID   A0A094A5T1_9PEZI        Unreviewed;       415 AA.
AC   A0A094A5T1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000256|ARBA:ARBA00016219};
DE            EC=1.1.1.17 {ECO:0000256|ARBA:ARBA00012939};
GN   ORFNames=V493_06438 {ECO:0000313|EMBL:KFY22653.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY22653.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY22653.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:19661, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:61381; EC=1.1.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00000292};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006541}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY22653.1}.
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DR   EMBL; JPJV01002396; KFY22653.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094A5T1; -.
DR   STRING; 1420906.A0A094A5T1; -.
DR   HOGENOM; CLU_036089_0_1_1; -.
DR   OrthoDB; 1700931at2759; -.
DR   Proteomes; UP000029327; Unassembled WGS sequence.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019594; P:mannitol metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00196; Mannitol_dehydrog; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR023028; Mannitol_1_phos_5_DH.
DR   InterPro; IPR000669; Mannitol_DH.
DR   InterPro; IPR013118; Mannitol_DH_C.
DR   InterPro; IPR013131; Mannitol_DH_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR30524:SF0; ALTRONATE OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR30524; MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE; 1.
DR   Pfam; PF01232; Mannitol_dh; 1.
DR   Pfam; PF08125; Mannitol_dh_C; 1.
DR   PRINTS; PR00084; MTLDHDRGNASE.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029327}.
FT   DOMAIN          29..150
FT                   /note="Mannitol dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01232"
FT   DOMAIN          180..389
FT                   /note="Mannitol dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08125"
SQ   SEQUENCE   415 AA;  46380 MW;  06FA3EE5F8809EDF CRC64;
     MENLTIGNFE ENGINGHNNT GRVESDHKKA VHFGAGNIGR GFVGEFLHNS GYEVVFADVQ
     DSIIDQLNET DSYDVIQVGS DGEQRSQVRN YRAINSRLNE AALIKEITTA DVVTCSVGPR
     VLKFIAPAIA KGIDRRAAGL RPLSVIACEN AIGATDTLAE FIKKDVSPYR ILDLGTRARF
     ANSAIDRIVP AQDPNAGLDV RLEKFSEWVV DRTPFAPFSP PAIKGIKWVD DLVPFIERKL
     YTVNTGHAAA AYHGYYHNKQ TVFDAMQDPR IMKQVRRALD ETSTLIVGKH GIEAEEQNAY
     VERILNRISN PYLEDSVERV GRDPLRKLSR KERFIGPATE LAEMGHEYSA LLLAAEMTFR
     FQNVPDDKES EDLAKLMNST KDAKEIVEEI CDVERTHPLF DDLVRIIERV QGEAI
//