ID W9YNE1_9EURO Unreviewed; 389 AA.
AC W9YNE1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000256|ARBA:ARBA00016219};
DE EC=1.1.1.17 {ECO:0000256|ARBA:ARBA00012939};
GN ORFNames=A1O1_07406 {ECO:0000313|EMBL:EXJ83779.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ83779.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ83779.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ83779.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) 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:EXJ83779.1}.
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DR EMBL; AMWN01000006; EXJ83779.1; -; Genomic_DNA.
DR RefSeq; XP_007726465.1; XM_007728275.1.
DR AlphaFoldDB; W9YNE1; -.
DR STRING; 1182541.W9YNE1; -.
DR GeneID; 19162264; -.
DR eggNOG; ENOG502QVPN; Eukaryota.
DR HOGENOM; CLU_036089_0_1_1; -.
DR OrthoDB; 1700931at2759; -.
DR Proteomes; UP000019484; 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:UP000019484}.
FT DOMAIN 5..125
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 155..359
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 389 AA; 42919 MW; 232379A7FEBBD3C1 CRC64;
MPGVAVHFGG GNIGRGFIAE LLHESGFEVV FVDVVDDLID RINNAKSYKI TEVGADGEKS
KEITNFRAIN SKYNMDDVVK TIADADVVTC AVGPNVMKFI AKPIADGIAA RTKSKPLAVI
ACENMINATD ALKELITDPK NMKPEVLKDL DKKAEFGNSA IDRIVPTQPA DANLDVVIES
FYEWCVETKG FYSGHPDING IHWVGDLEPY IERKLYTVNT SHATAAYFGY NKGIKTIHEA
MADPDIKQEV HEALEETAHL ISGKHDITEE EQQKYVDTIV SRISNPHLED VCVRVGRAPL
RKLSRNERFI GPAAQLAERG YDVTALVRGV EMALRFQNVE GDDESVELAK ILKSMPAEEA
TTKLTGLDPD HPLYAKILDK VKLVQSDTK
//
