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Database: UniProt
Entry: W6T3R0_9LACO
LinkDB: W6T3R0_9LACO
Original site: W6T3R0_9LACO 
ID   W6T3R0_9LACO            Unreviewed;       385 AA.
AC   W6T3R0;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
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   ORFNames=LFAB_17225 {ECO:0000313|EMBL:ETY72496.1};
OS   Lactiplantibacillus fabifermentans T30PCM01.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1400520 {ECO:0000313|EMBL:ETY72496.1, ECO:0000313|Proteomes:UP000019247};
RN   [1] {ECO:0000313|EMBL:ETY72496.1, ECO:0000313|Proteomes:UP000019247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T30PCM01 {ECO:0000313|EMBL:ETY72496.1,
RC   ECO:0000313|Proteomes:UP000019247};
RX   PubMed=24558238;
RA   Treu L., Vendramin V., Bovo B., Giacomini A., Corich V., Campanaro S.;
RT   "Genome Sequence of Lactobacillus fabifermentans Strain T30PCM01, Isolated
RT   from Fermenting Grape Marc.";
RL   Genome Announc. 2:e00060-e00014(2014).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000292, ECO:0000256|HAMAP-
CC         Rule:MF_00196};
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00196}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETY72496.1}.
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DR   EMBL; AWWK01000097; ETY72496.1; -; Genomic_DNA.
DR   RefSeq; WP_033615034.1; NZ_KK036541.1.
DR   AlphaFoldDB; W6T3R0; -.
DR   STRING; 1400520.LFAB_17225; -.
DR   PATRIC; fig|1400520.3.peg.3389; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_2_0_9; -.
DR   OrthoDB; 271711at2; -.
DR   Proteomes; UP000019247; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00196};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00196}.
FT   DOMAIN          1..125
FT                   /note="Mannitol dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01232"
FT   DOMAIN          151..372
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   385 AA;  43328 MW;  214003850569947E CRC64;
     MKAVHFGAGN IGRGFIGETL AANGFEINFV DVNETIIDAL NQRHGYEIEL ADESHKRISV
     HNVAGINNGK EPEKVVQAIV EADIVTTAIG PKILKFIAPL IADGIRARQN AAKTTPVDVI
     ACENMIGGSQ NLKKEVYSHL ADAEQDFADK YIGFPNAAVD RIVPQQKHDD PLFVSVEPFK
     EWVIDEHQMA NPSLKLESVH YAPDLEPYIE RKLFSVNTGH ATVAYTGKYL GYSDIGSAIA
     DPKVLQQLKR VLKETGDLLI AKWNFKRTEH EAYQHKIIGR FENKYLSDEI ARVGRTPIRK
     LGYDERFIRP IREAKERDLD YEALLETVGM IYTFDEPKDT ESQKLMELIK AKPIQEVIAT
     TTGLKDQALI NEIEESYQKA VKERK
//
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