ID   MTLD_ERWT9              Reviewed;         382 AA.
AC   B2VCH7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   18-JUN-2025, entry version 87.
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};
GN   OrderedLocusNames=ETA_34190;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC         + NADH + H(+); 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; CU468135; CAO98465.1; -; Genomic_DNA.
DR   RefSeq; WP_012443088.1; NC_010694.1.
DR   AlphaFoldDB; B2VCH7; -.
DR   SMR; B2VCH7; -.
DR   STRING; 465817.ETA_34190; -.
DR   KEGG; eta:ETA_34190; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_2_0_6; -.
DR   OrthoDB; 271711at2; -.
DR   Proteomes; UP000001726; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019592; P:mannitol catabolic process; IEA:TreeGrafter.
DR   FunFam; 1.10.1040.10:FF:000009; Mannitol-1-phosphate 5-dehydrogenase; 1.
DR   FunFam; 3.40.50.720:FF:000075; Mannitol-1-phosphate 5-dehydrogenase; 1.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR023027; Mannitol_DH_CS.
DR   InterPro; IPR013131; Mannitol_DH_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; NF002646; PRK02318.1-2; 1.
DR   NCBIfam; NF002647; PRK02318.1-3; 1.
DR   NCBIfam; NF002650; PRK02318.2-2; 1.
DR   NCBIfam; NF002652; PRK02318.2-5; 1.
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.
DR   PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..382
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_1000099192"
FT   BINDING         3..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ   SEQUENCE   382 AA;  41195 MW;  45104C836AD4D935 CRC64;
     MKALHFGAGN IGRGFIGKLL ADAGVQLTFA DVNQAVLDAL NARGTYPVHV VGEQAQIEIV
     NGVNAVHSSS DDIIALIAEV DIVTTAVGPQ ILERIAAGMA QGIAKRSDNA NSRPLNIIAC
     ENMVRGTTQL KAHVLKALPE RYHAWLEEHV GFVDSAVDRI VPPSAADSSD PLEVTVETFS
     EWIVDKTQFK GEPPTIPGME LTDNLMAFVE RKLFTLNTGH AIAAYLGQLA GHKTIREAIM
     DKKVRAIVQG AMEESGAVLI KRYGFAADKH AAYIQKIINR FENPYLIDDV ERVGRQPLRK
     LSAGDRLIKP TLGTLEYHLP NNNLVTGIAA ALLYRNEGDP QAIELAGLLS RQDVATTLVH
     ISGLDKDSDV VKAVVKAVNA LA
//