ID   MTLK_CERSP              Reviewed;         477 AA.
AC   P33216;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Mannitol 2-dehydrogenase;
DE            Short=M2DH;
DE            Short=MDH;
DE            EC=1.1.1.67;
GN   Name=mtlK;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-44.
RC   STRAIN=DSM 8371 / Si4;
RX   PubMed=8254318; DOI=10.1099/00221287-139-10-2475;
RA   Schneider K.-H., Giffhorn F., Kaplan S.;
RT   "Cloning, nucleotide sequence and characterization of the mannitol
RT   dehydrogenase gene from Rhodobacter sphaeroides.";
RL   J. Gen. Microbiol. 139:2475-2484(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 8371 / Si4;
RA   Schneider K.-H., Giffhorn F.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol + NAD(+) = D-fructose + H(+) + NADH;
CC         Xref=Rhea:RHEA:12084, ChEBI:CHEBI:15378, ChEBI:CHEBI:16899,
CC         ChEBI:CHEBI:37721, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.67;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AF018073; AAC45771.1; -; Genomic_DNA.
DR   AlphaFoldDB; P33216; -.
DR   SMR; P33216; -.
DR   GO; GO:0050086; F:mannitol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019594; P:mannitol metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
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   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8254318"
FT   CHAIN           2..477
FT                   /note="Mannitol 2-dehydrogenase"
FT                   /id="PRO_0000170734"
FT   BINDING         19..30
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   477 AA;  51538 MW;  F823623B7BA920E8 CRC64;
     MTRSVTRPSY DRKALTPGIV HIGVGNFHRA HQAVYLDDLF ALGEGHDWAI LGAGVRPTDA
     RMREALAAQD NLSTVIELDP AGHRARQVGA MVGFLPVEAD NAALIEAMSD PRIRIVSLTV
     TEGGYYVDAS GAFDPTHPDI VADAAHPARP ATAFGAILAA LRARRDAGVT PFTVMSCDNL
     PGNGHVTRNA VVGLAELYDA ELAGWVKAQV AFPNGMVDRI TPATGPHERE LAQGFGLADP
     VPVTCEPFRQ WVIEDHFPAG RPALEKVGVT FTPHVHAYEA MKIRILNGGH AVIAYPSALM
     DIQLVHAAMA HPLIAAFLHK VEVEEILPHV PPVPDTSIPD YLTLIESRFS NPEIADTTRR
     LCLDGSNRQP KFIVPSLRDN LAAGTVPKGL VLLSALWCRY CFGTTDSGVV VEPNDPNWTA
     LQDRARRAKE TPAEWLAMTE VYGDLAQNDL LAAEFAAALE AVWRDGAEAV LRRFLAA