UDG_PSEAE
ID UDG_PSEAE Reviewed; 453 AA.
AC O86422; Q9I292;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 2.
DT 03-AUG-2022, entry version 137.
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=udg; Synonyms=ugd; OrderedLocusNames=PA2022;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Peng H.L., Chang J.T., Lee J.H., Chang H.Y.;
RT "Organization of UDP glucose dehydrogenase and UDP glucose
RT pyrophosphorylase gene cluster in Pseudomonas aeruginosa PAO1.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA09327.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ010734; CAA09327.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE004091; AAG05410.1; -; Genomic_DNA.
DR PIR; H83393; H83393.
DR RefSeq; NP_250712.1; NC_002516.2.
DR RefSeq; WP_003113510.1; NZ_QZGE01000026.1.
DR AlphaFoldDB; O86422; -.
DR SMR; O86422; -.
DR STRING; 287.DR97_5825; -.
DR PaxDb; O86422; -.
DR PRIDE; O86422; -.
DR EnsemblBacteria; AAG05410; AAG05410; PA2022.
DR GeneID; 879866; -.
DR KEGG; pae:PA2022; -.
DR PATRIC; fig|208964.12.peg.2107; -.
DR PseudoCAP; PA2022; -.
DR HOGENOM; CLU_023810_1_2_6; -.
DR InParanoid; O86422; -.
DR OMA; YWRQVIR; -.
DR PhylomeDB; O86422; -.
DR BioCyc; PAER208964:G1FZ6-2060-MON; -.
DR BRENDA; 1.1.1.22; 5087.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000002438; 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 InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
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 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; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52413; SSF52413; 1.
DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..453
FT /note="UDP-glucose 6-dehydrogenase"
FT /id="PRO_0000074049"
FT ACT_SITE 266
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 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 154..158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 255..259
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 334
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT CONFLICT 81
FT /note="F -> L (in Ref. 1; CAA09327)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="A -> R (in Ref. 1; CAA09327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 49690 MW; A8E7954D0D11557D CRC64;
MRLCVIGAGY VGLVTAACFA EMGNQVRCVE RDRERVARLR RGEMPIYEPG LESILRDQLD
AARLTFTASL AEGLADAEVV FIAVGTPCGE DGSADLSHVL AVAEQLGAQL RQACIVVNKS
TVPVGTAERV EEIIRLGLAR RRKRFRVAVA SNPEFLKEGS AVDDFRRPDR VIIGSAETQA
GETLRQLYAP FLRNHERVLL MGRREAEFSK YAANAFLATK ISFMNEMAGL CALTGVDIED
VRRGMGSDKR IGTHFIYAGC GYGGSCFPKD VRALIRSAEQ QGYDSQILRA VEARNARQKE
LLFETLGELF QGRWQGRTVA LWGLAFKPGT DDLREAPSLV LLEALLRHGV RVRAHDPVAN
AGVAARYPEA VACARLTLHD SPYAAVEGAD ALVLVTEWKQ FRQPDFQKIR GSMRTPLLVD
GRNLYAPARM AELGFIYQGI GRPRAGHCKA SAA
