ID   MTLD_VIBCM              Reviewed;         384 AA.
AC   C3LWV8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=VCM66_A1004;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP001234; ACP07963.1; -; Genomic_DNA.
DR   RefSeq; WP_000739122.1; NC_012580.1.
DR   AlphaFoldDB; C3LWV8; -.
DR   SMR; C3LWV8; -.
DR   EnsemblBacteria; ACP07963; ACP07963; VCM66_A1004.
DR   GeneID; 57742397; -.
DR   KEGG; vcm:VCM66_A1004; -.
DR   HOGENOM; CLU_036089_2_0_6; -.
DR   OMA; GKKAVHF; -.
DR   Proteomes; UP000001217; Chromosome II.
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.
FT   CHAIN           1..384
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_1000124395"
FT   BINDING         5..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ   SEQUENCE   384 AA;  42340 MW;  60D4F90913EF186D CRC64;
     MKKNAVHFGA GNIGRGFIGK LLADADIAVT FADVNEPLVD QLSHQQEYKV KVVGSECKME
     TVSHVTAVNS ASEALIERII KTDLVTTAVG PTVLDIIAKT IAKGLSARFA AGNTQPLNII
     ACENMVRGTT HLKQQVYQFL TTEEQQQADA LVGFVDSAVD RIVPPLQAAN DDPLEVTVES
     FSEWIVDEQQ FKGEIPQIEG MEKTDNLMAF VERKLFTLNT GHCVTAYLGC LKGHRTIREA
     IEDPCIHAQV KQAMQESGEV LIRRYGFDRA LHSAYIEKIL SRFANPYLVD EVDRVGRQPL
     RKLSANDRLI KPLLGTIEYG LPNGMLLKGI AAALKYRNSS DPQAVELQQS IEKEGVRSTL
     ARYTGLAAES VEAQQIEALY QQMD