ID   MTLD_VIBCH              Reviewed;         384 AA.
AC   Q9KKQ6;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=VC_A1046;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003853; AAF96940.1; -; Genomic_DNA.
DR   PIR; C82385; C82385.
DR   RefSeq; NP_233428.1; NC_002506.1.
DR   RefSeq; WP_000739122.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KKQ6; -.
DR   SMR; Q9KKQ6; -.
DR   STRING; 243277.VC_A1046; -.
DR   DNASU; 2612121; -.
DR   EnsemblBacteria; AAF96940; AAF96940; VC_A1046.
DR   GeneID; 57742397; -.
DR   KEGG; vch:VC_A1046; -.
DR   PATRIC; fig|243277.26.peg.3652; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_2_0_6; -.
DR   OMA; GKKAVHF; -.
DR   BioCyc; VCHO:VCA1046-MON; -.
DR   Proteomes; UP000000584; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0019592; P:mannitol catabolic process; IBA:GO_Central.
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..384
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000170729"
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