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Database: UniProt
Entry: UDG_ECO57
LinkDB: UDG_ECO57
Original site: UDG_ECO57 
ID   UDG_ECO57               Reviewed;         388 AA.
AC   Q7DBF9; Q7ACQ7;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=UDP-glucose 6-dehydrogenase;
DE            Short=UDP-Glc dehydrogenase;
DE            Short=UDP-GlcDH;
DE            Short=UDPGDH;
DE            EC=1.1.1.22;
GN   Name=ugd; OrderedLocusNames=Z3190, ECs2829;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-
CC         alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22;
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate
CC       biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step
CC       1/1.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis.
CC   -!- PTM: Phosphorylated on a tyrosine residue. It results in a significant
CC       increase of the dehydrogenase activity (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG57087.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36252.1; -; Genomic_DNA.
DR   RefSeq; NP_310856.1; NC_002695.1.
DR   RefSeq; WP_000704871.1; NZ_VOAI01000013.1.
DR   AlphaFoldDB; Q7DBF9; -.
DR   SMR; Q7DBF9; -.
DR   STRING; 155864.Z3190; -.
DR   GeneID; 913058; -.
DR   KEGG; ece:Z3190; -.
DR   KEGG; ecs:ECs_2829; -.
DR   PATRIC; fig|386585.9.peg.2964; -.
DR   eggNOG; COG1004; Bacteria.
DR   HOGENOM; CLU_023810_2_0_6; -.
DR   OMA; LFMGFTE; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00038; UER00491.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR   GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR017476; UDP-Glc/GDP-Man.
DR   InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR   InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR   InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR   InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR   InterPro; IPR028357; UDPglc_DH_bac.
DR   NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR   PANTHER; PTHR43750:SF2; UDP-GLUCOSE 6-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43750; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1.
DR   Pfam; PF00984; UDPG_MGDP_dh; 1.
DR   Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR   Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR   PIRSF; PIRSF500134; UDPglc_DH_bac; 1.
DR   PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR   SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..388
FT                   /note="UDP-glucose 6-dehydrogenase"
FT                   /id="PRO_0000074042"
FT   ACT_SITE        253
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         2..19
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   BINDING         11
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         29
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         83
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         118
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         141..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         145
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         242..246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         252
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         256
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         314
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
SQ   SEQUENCE   388 AA;  43713 MW;  44492C5BF394D2B9 CRC64;
     MKITISGTGY VGLSNGLLIA QNHEVVALDI LPSRVAMLND RISPIVDKEI QQFLQSDKIH
     FNATLDKNEA YRDADYVIIA TPTDYDPKTN YFNTSSVESV IKDVVEINPY AVMVIKSTVP
     VGFTEAMHKK YRTENIIFSP EFLREGKALY DNLHPSRIVI GERSERAERF AALLQEGAIK
     QNIPTLFTDS TEAEAIKLFA NTYLAMRVAY FNELDSYAES LGLNSRQIIE GVCLDPRIGN
     HYNNPSFGYG GYCLPKDTKQ LLANYQSVPN NLISAIVDAN RTRKDFIADA ILSRKPQVVG
     IYRLIMKSGS DNFRASSIQG IMKRIKAKGV EVIIYEPVMK EDSFFNSRLE RDLATFKQQA
     DVIISNRMAE ELRDVADKVY TRDLFGSD
//
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