ID   B0RB67_CLASE            Unreviewed;       389 AA.
AC   B0RB67;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   04-NOV-2026, entry version 115.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000256|ARBA:ARBA00016219, ECO:0000256|HAMAP-Rule:MF_00196};
DE            EC=1.1.1.17 {ECO:0000256|ARBA:ARBA00012939, ECO:0000256|HAMAP-Rule:MF_00196};
GN   Name=mtlD {ECO:0000256|HAMAP-Rule:MF_00196,
GN   ECO:0000313|EMBL:CAQ00432.1};
GN   OrderedLocusNames=CMS0311 {ECO:0000313|EMBL:CAQ00432.1};
OS   Clavibacter sepedonicus (Clavibacter michiganensis subsp. sepedonicus).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ00432.1, ECO:0000313|Proteomes:UP000001318};
RN   [1] {ECO:0000313|EMBL:CAQ00432.1, ECO:0000313|Proteomes:UP000001318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / ICMP 2535 / C-1
RC   {ECO:0000313|Proteomes:UP000001318};
RX   PubMed=18192393; DOI=10.1128/JB.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00048615, ECO:0000256|HAMAP-
CC         Rule:MF_00196};
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006541, ECO:0000256|HAMAP-Rule:MF_00196}.
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DR   EMBL; AM849034; CAQ00432.1; -; Genomic_DNA.
DR   RefSeq; WP_012297774.1; NC_010407.1.
DR   AlphaFoldDB; B0RB67; -.
DR   STRING; 31964.CMS0311; -.
DR   GeneID; 29469784; -.
DR   KEGG; cms:CMS0311; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_0_1_11; -.
DR   OMA; AAALCYK; -.
DR   OrthoDB; 271711at2; -.
DR   Proteomes; UP000001318; 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; IPR013131; Mannitol_DH_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; NF002652; PRK02318.2-5; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00196};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00196}; Reference proteome {ECO:0000313|Proteomes:UP000001318}.
FT   DOMAIN          1..192
FT                   /note="Mannitol dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01232"
FT   DOMAIN          200..341
FT                   /note="Mannitol dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08125"
FT   BINDING         3..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00196"
SQ   SEQUENCE   389 AA;  41226 MW;  5EC921115868E2DF CRC64;
     MKAVHFGAGN IGRGFVGLIL HEAGYEVVFA DVNAELIGHL ASADSYRVTE VGPHARDWTV
     TGFRAIDSAA DGEALIAEIA TADVVTTAVG PNILRFVAPA IAAGLRARSA DLGPVAVMAC
     ENAINATDTL RDEIAKALGD ETDALGRAVF ANTAVDRIVP NQDPAAGLDV TVEDFSEWVV
     ERTPFGDAVP DIAGATFVDD LAPYIERKLF TVNTGHATVA YHGYARGAVS QSDAMAIPEV
     ADEVRQVLEE TSALLVAKHG LDESEQAAYR EKNLARFANA ALADTVERVG RQPLRKLSRE
     ERFVGPASQL AERGLPHDAL VRAVGQALRF DPAGDPQALE LQGLLATDTA ADLVRRVTGL
     DDQHPLTPDL VAVVDAAQAD RRSAPRHRA
//