ID   MTLD_CALS4              Reviewed;         386 AA.
AC   Q8RCS0;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   04-NOV-2026, entry version 118.
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=TTE0342;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
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; AE008691; AAM23634.1; -; Genomic_DNA.
DR   RefSeq; WP_011024796.1; NC_003869.1.
DR   AlphaFoldDB; Q8RCS0; -.
DR   SMR; Q8RCS0; -.
DR   STRING; 273068.TTE0342; -.
DR   KEGG; tte:TTE0342; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_2_0_9; -.
DR   OMA; AAALCYK; -.
DR   OrthoDB; 271711at2; -.
DR   Proteomes; UP000000555; 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   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; NF002652; PRK02318.2-5; 1.
DR   NCBIfam; NF002653; PRK02318.2-6; 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..386
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000170728"
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;  44022 MW;  251DDC8448736BEC CRC64;
     MLKALHFGAG NIGRGFIGYL LNKSGYEVTF VDISKEIVDN INKYKKYNVI ILKEPVEKEE
     VKEVKALHLE EEDKVLDAFL EADMVTTSVG VSNLSSIGGR LKKYLKARKE KNEKPLDIMA
     CENALFATDV LRERVVKEED DDFITYLNLK VGFPNTAVDR IVPAVKIDKK LPVDVAVEEF
     FEWDIEKNKI KGNLQIEGVE LVDDLKPYIE RKLFLLNGAH ATTAYLGYLR GYTYIHQAIK
     DDNIRAIVKG MQEEISTALS KKYDVDKESL MAYAEKVIKR FENPYLQDEV TRVGREPLRK
     LSSEDRLIAP LKLCSEVGIT PNFILYGIAA GLLFDYKEDA QAVKMREYVE QFGIKKAVNV
     ITGLEEESDL VEEIEKRYFE LKGKLI
//