ID   MTLD_OCEIH              Reviewed;         386 AA.
AC   Q8EN87;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00196};
DE            EC=1.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00196};
GN   Name=mtlD {ECO:0000255|HAMAP-Rule:MF_00196}; OrderedLocusNames=OB2600;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00196};
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00196}.
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DR   EMBL; BA000028; BAC14556.1; -; Genomic_DNA.
DR   RefSeq; WP_011066993.1; NC_004193.1.
DR   AlphaFoldDB; Q8EN87; -.
DR   SMR; Q8EN87; -.
DR   STRING; 221109.22778286; -.
DR   EnsemblBacteria; BAC14556; BAC14556; BAC14556.
DR   KEGG; oih:OB2600; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_2_0_9; -.
DR   OMA; GKKAVHF; -.
DR   OrthoDB; 1442117at2; -.
DR   PhylomeDB; Q8EN87; -.
DR   Proteomes; UP000000822; Chromosome.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019594; P:mannitol metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1040.10; -; 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; IPR023027; Mannitol_DH_CS.
DR   InterPro; IPR013131; Mannitol_DH_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01232; Mannitol_dh; 1.
DR   Pfam; PF08125; Mannitol_dh_C; 1.
DR   PRINTS; PR00084; MTLDHDRGNASE.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..386
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000170714"
FT   BINDING         4..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ   SEQUENCE   386 AA;  43089 MW;  151842F9E829C594 CRC64;
     MKTAVHFGAG NIGRGFIGLL LYQSGYQTIF IDVNNQVIDE INKQKSYHVY LAGKEKQELT
     VNHITGINSI KEPDAVTEAI VKADVVTTAV GPTILPVIAK AISKGLQERT KQNNSPLNII
     ACENMVGGSS LLKEHVFESL EAHKIGEFDR LYGFPDAAVD RIVPNQTNKN LLDVMVEPYY
     EWVVEKKKIV GEVPPIFGIT YVDDLAPYIE RKLFTVNTGH AIPAYLGTHL GYDTIVEAMK
     DLRIDDTIYG ALAESGEALI HAYGFNREMH QEYVSKIIQR FQNPYISDDV KRVARGPIRK
     LGAKDRLVKP ALMYIEYTGK IPVYLAKTIA AALLFNNDED REAIELQKKI SATGYQQAFV
     EVSGCDSDSI LTKKVIEQLR LLQNKK