ID   MTLD_BUCAI              Reviewed;         385 AA.
AC   P57634;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            EC=1.1.1.17;
GN   Name=mtlD; OrderedLocusNames=BU571;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000003; BAB13261.1; -; Genomic_DNA.
DR   RefSeq; NP_240375.1; NC_002528.1.
DR   RefSeq; WP_010896168.1; NC_002528.1.
DR   AlphaFoldDB; P57634; -.
DR   SMR; P57634; -.
DR   STRING; 107806.10039227; -.
DR   EnsemblBacteria; BAB13261; BAB13261; BAB13261.
DR   KEGG; buc:BU571; -.
DR   PATRIC; fig|107806.10.peg.574; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_2_0_6; -.
DR   OMA; GKKAVHF; -.
DR   Proteomes; UP000001806; 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; 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; 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.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..385
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000170699"
FT   BINDING         3..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   385 AA;  43825 MW;  C8B2D91910E97E2F CRC64;
     MKALQFGAGN IGRGFIGKTL SESGFSVIFS DVNQNIVDAI NYNREYFVKI IGSNQNKTVN
     IKRVSAINSN DSNIKKIISS VDLITTAVGP TALEKIALII TQGIIFKIKN QFTKPLNIIA
     CENKIKSSSF LKQVVLKNLP IKYHDYLNKY IGFIDCSIDT IIPAINNKDD LFLTVEEFKE
     WIVNINQFKG AVPKIVDMKF SNNLDAFIER KLFTLNTGHA IAAYLGLIKN YKTIQDAISD
     KKIRVIVRSA MEESGSVLIK RYNFNKNDHL DYIEKIFLRF ENPFLSDKLE RIGRNPLQKL
     RREDRLIKPF LGAFEYNLPY SNLAKGIAAA FYYHNKNDLE SIELSSSIKK QGLESTIIKI
     CDLPVNSKEV YSIILEYNLI KKIIR