ID MTLD_MANSM Reviewed; 382 AA.
AC Q65VJ3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 119.
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=MS0410;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU37017.1; -; Genomic_DNA.
DR RefSeq; WP_011199592.1; NC_006300.1.
DR AlphaFoldDB; Q65VJ3; -.
DR SMR; Q65VJ3; -.
DR STRING; 221988.MS0410; -.
DR KEGG; msu:MS0410; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_036089_2_0_6; -.
DR OrthoDB; 271711at2; -.
DR Proteomes; UP000000607; 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; 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; IPR023027; Mannitol_DH_CS.
DR InterPro; IPR013131; Mannitol_DH_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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.
DR PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase.
FT CHAIN 1..382
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_1000011806"
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; 42344 MW; 1DB52CD506C77015 CRC64;
MKALHFGAGN IGRGFIGKLL ADSGMQVIFA DVNDSVIDLL KSRRSYGVKI VGDSINTVER
VTQVTGVNSK DETAIITLFN EVDLVTTAVG PNVLKIVAST FAKALEARIA GGNTKPLNII
ACENMVRGTS FLKEQVFTHL NPDYKDKVEQ LIGFVDSAVD RIVPPVKPDA EDPLLVTVEE
FSEWIVDQTQ FKGAIPDIKG MELTDNLMAF VERKLFTLNT GHAVTSYYGK FKGYKFVKES
IEDESVKAFV KSVMQESGAV LIKRYGFDPQ AHAAYIEKIL KRFANPYLVD DVDRVGREPL
RKLSYNDRLI KPLRGTIEYG LPNDNLIRAI ATALSYRNEN DPQALELAKS LAEAGVTQTI
KKYTELQDEN VIARIAKAYE TL
//
