ID   UXUB_ECOLI              Reviewed;         486 AA.
AC   P39160; Q2M5Z0;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=D-mannonate oxidoreductase;
DE            EC=1.1.1.57;
DE   AltName: Full=Fructuronate reductase;
GN   Name=uxuB; OrderedLocusNames=b4323, JW4286;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Mizobuchi K.;
RL   Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannonate + NAD(+) = H(+) + keto-D-fructuronate + NADH;
CC         Xref=Rhea:RHEA:15729, ChEBI:CHEBI:15378, ChEBI:CHEBI:17767,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:59881; EC=1.1.1.57;
CC   -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC       interconversion.
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family. UxuB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; D13329; BAA02591.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97219.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77279.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78316.1; -; Genomic_DNA.
DR   PIR; S56548; S56548.
DR   RefSeq; NP_418743.1; NC_000913.3.
DR   RefSeq; WP_000208205.1; NZ_LN832404.1.
DR   AlphaFoldDB; P39160; -.
DR   SMR; P39160; -.
DR   BioGRID; 4260999; 6.
DR   DIP; DIP-11109N; -.
DR   IntAct; P39160; 3.
DR   STRING; 511145.b4323; -.
DR   jPOST; P39160; -.
DR   PaxDb; 511145-b4323; -.
DR   EnsemblBacteria; AAC77279; AAC77279; b4323.
DR   GeneID; 946795; -.
DR   KEGG; ecj:JW4286; -.
DR   KEGG; eco:b4323; -.
DR   PATRIC; fig|1411691.4.peg.2369; -.
DR   EchoBASE; EB4150; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_027324_0_1_6; -.
DR   InParanoid; P39160; -.
DR   OMA; IVASWAR; -.
DR   OrthoDB; 271711at2; -.
DR   PhylomeDB; P39160; -.
DR   BioCyc; EcoCyc:MANNONOXIDOREDUCT-MONOMER; -.
DR   BioCyc; MetaCyc:MANNONOXIDOREDUCT-MONOMER; -.
DR   UniPathway; UPA00246; -.
DR   PRO; PR:P39160; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008866; F:fructuronate reductase activity; IMP:CACAO.
DR   GO; GO:0042840; P:D-glucuronate catabolic process; IMP:EcoCyc.
DR   GO; GO:0019594; P:mannitol metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
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; PTHR43362:SF7; D-MANNONATE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR43362; MANNITOL DEHYDROGENASE DSF1-RELATED; 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; Reference proteome.
FT   CHAIN           1..486
FT                   /note="D-mannonate oxidoreductase"
FT                   /id="PRO_0000170747"
FT   BINDING         25..36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   486 AA;  53580 MW;  7835638682AF7B87 CRC64;
     MTTIVDSNLP VARPSWDHSR LESRIVHLGC GAFHRAHQAL YTHHLLESTD SDWGICEVNL
     MPGNDRVLIE NLKKQQLLYT VAEKGAESTE LKIIGSMKEA LHPEIDGCEG ILNAMARPQT
     AIVSLTVTEK GYCADAASGQ LDLNNPLIKH DLENPTAPKS AIGYIVEALR LRREKGLKAF
     TVMSCDNVRE NGHVAKVAVL GLAQARDPQL AAWIEENVTF PCTMVDRIVP AATPETLQEI
     ADQLGVYDPC AIACEPFRQW VIEDNFVNGR PDWDKVGAQF VADVVPFEMM KLRMLNGSHS
     FLAYLGYLGG YETIADTVTN PAYRKAAFAL MMQEQAPTLS MPEGTDLNAY ATLLIERFSN
     PSLRHRTWQI AMDGSQKLPQ RLLDPVRLHL QNGGSWRHLA LGVAGWMRYT QGVDEQGNAI
     DVVDPMLAEF QKINAQYQGA DRVKALLGLS GIFADDLPQN ADFVGAVTAA YQQLCERGAR
     ECVAAL
//