ID   MTLD_KLEP7              Reviewed;         382 AA.
AC   A6TFJ4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=KPN78578_39040; ORFNames=KPN_03943;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR79328.1; -; Genomic_DNA.
DR   RefSeq; WP_015959133.1; NC_009648.1.
DR   AlphaFoldDB; A6TFJ4; -.
DR   SMR; A6TFJ4; -.
DR   STRING; 272620.KPN_03943; -.
DR   jPOST; A6TFJ4; -.
DR   DNASU; 5340588; -.
DR   EnsemblBacteria; ABR79328; ABR79328; KPN_03943.
DR   KEGG; kpn:KPN_03943; -.
DR   HOGENOM; CLU_036089_2_0_6; -.
DR   OMA; GKKAVHF; -.
DR   Proteomes; UP000000265; 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..382
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_1000011801"
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;  5AE6C41420F2040A CRC64;
     MKALHFGAGN IGRGFIGKLL ADAGIELTFA DVNQTVLDAL NARHSYQVHV VGENEQVDTV
     SGVNAVSSIG DEVVDLIAEV DLVTTAVGPV VLERIAPAIA KGLAQRKAQG TERPLNIIAC
     ENMVRGTTQL KGHVFNALAE EHKAWVEAHI GFVDSAVDRI VPPSASATHD PLEVTVETFS
     EWIVDKTQFK GALPTIPGME LTDNLMAFVE RKLFTLNTGH AITAYLGKLA GHQTIRDAIL
     DEKIRAVVQG AMEESGAVLI KRYAFDPQKH AAYIQKILGR FENPYLKDDV ERVGRQPLRK
     LSAGDRLIKP LLGTLEYGLP HRNLVKGIAA AMHFRSEDDP QAQELAALIA DKGPQAALAQ
     ISGLDAASDV VAEAVNDYNA EK