MTLD_BUCBP
ID MTLD_BUCBP Reviewed; 390 AA.
AC Q89A37;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=bbp_516;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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; AE016826; AAO27219.1; -; Genomic_DNA.
DR RefSeq; WP_011091620.1; NC_004545.1.
DR AlphaFoldDB; Q89A37; -.
DR SMR; Q89A37; -.
DR STRING; 224915.bbp_516; -.
DR EnsemblBacteria; AAO27219; AAO27219; bbp_516.
DR GeneID; 56471050; -.
DR KEGG; bab:bbp_516; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_036089_2_0_6; -.
DR OMA; GKKAVHF; -.
DR OrthoDB; 1442117at2; -.
DR Proteomes; UP000000601; 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..390
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000170701"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ SEQUENCE 390 AA; 44567 MW; B1037CA82DC02E8D CRC64;
MNALHFGAGN IGRGFIGPLL LKSGFNLTFV DNNQAIVDAI NRHQKYDITV VGNNFSYITT
VKKVKAIYIN DPNIYFKIAK INVITISVGV HAINSLVVFF EKLIRYKIET NDFVFLTIIA
CENVFRCASK LKENIKILLP GIYHKYLDKN ISFVDSVVDK IVCPNDKNNS DDINLSVKVE
KFSEWIVDCT QFKHDRPNII GMIYSNHLDA FFERKLFTLN TGHAIAAYLG LLIGYKNIYQ
AILDPLIFNI VYGAMKESGM VLIRKYNFFT DSEHKNYILK ILSRFKNIYL TDSLKRVGRN
PLQKLKKDDR LISPLIDTIK YNLPNANLMK GIAAALCYID EKDIEAKKLR NMIINKGIKY
VLSKISSLDS SLLIISEISI YFNIFMKVNI