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MTLD_VIBVY
ID   MTLD_VIBVY              Reviewed;         382 AA.
AC   Q7MP60;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=VV0504;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000037; BAC93268.1; -; Genomic_DNA.
DR   RefSeq; WP_011149418.1; NC_005139.1.
DR   AlphaFoldDB; Q7MP60; -.
DR   SMR; Q7MP60; -.
DR   STRING; 672.VV93_v1c04720; -.
DR   PRIDE; Q7MP60; -.
DR   EnsemblBacteria; BAC93268; BAC93268; BAC93268.
DR   KEGG; vvy:VV0504; -.
DR   PATRIC; fig|196600.6.peg.528; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_2_0_6; -.
DR   OMA; GKKAVHF; -.
DR   OrthoDB; 1442117at2; -.
DR   Proteomes; UP000002675; Chromosome I.
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_0000170732"
FT   BINDING         4..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ   SEQUENCE   382 AA;  41985 MW;  EA93806949B1C482 CRC64;
     MKNAVHFGAG NIGRGFIGKL LADANVSVTF ADVDAPLVDQ LSHRQEYKVK VVGSECQIDT
     VTHVTAVNSA SEEVIDRIVQ TDLVTTAVGP NVLDIIAKTI AQGIAKRFAA GNLAPLNIIA
     CENMVRGTTH LKGEVYKHLD ASLHAQVDEL VGFVDSAVDR IVPPAEAAND DPLEVTVESF
     SEWIVDEQQF KGEVPSIAGM EKTHNLMAFV ERKLFTLNTG HCITAYLGCL QGHRTIREAI
     ENPAICDQVK QAMMESGEVL IRRYGFDREM HQAYIEKILA RFANPFLVDE VDRVGRQPIR
     KLGMNDRLIK PLLGTIEFGT ANQHLLKGIA AALKYQNDSD PQAVELQRSL QQVGVKKTLA
     KYTSLAEDSV EVAKIETLYN QL
 
 
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