UDG_SALTY
ID UDG_SALTY Reviewed; 388 AA.
AC Q04873;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 141.
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=pagA, pmrE; OrderedLocusNames=STM2080;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=7682279; DOI=10.1111/j.1365-2958.1993.tb01163.x;
RA Bastin D.A., Stevenson G., Brown P.K., Haase A., Reeves P.R.;
RT "Repeat unit polysaccharides of bacteria: a model for polymerization
RT resembling that of ribosomes and fatty acid synthetase, with a novel
RT mechanism for determining chain length.";
RL Mol. Microbiol. 7:725-734(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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 -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; Z17278; CAA78945.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20984.1; -; Genomic_DNA.
DR RefSeq; NP_461025.1; NC_003197.2.
DR RefSeq; WP_000704831.1; NC_003197.2.
DR AlphaFoldDB; Q04873; -.
DR SMR; Q04873; -.
DR STRING; 99287.STM2080; -.
DR PaxDb; Q04873; -.
DR PRIDE; Q04873; -.
DR EnsemblBacteria; AAL20984; AAL20984; STM2080.
DR GeneID; 1253601; -.
DR KEGG; stm:STM2080; -.
DR PATRIC; fig|99287.12.peg.2202; -.
DR HOGENOM; CLU_023810_2_0_6; -.
DR OMA; EDFTRPD; -.
DR PhylomeDB; Q04873; -.
DR BioCyc; SENT99287:STM2080-MON; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000001014; 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; 1.10.1040.10; -; 1.
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 Pfam; PF00984; UDPG_MGDP_dh; 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..388
FT /note="UDP-glucose 6-dehydrogenase"
FT /id="PRO_0000074047"
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; 43634 MW; 04184EEE5DAA80F7 CRC64;
MKITISGTGY VGLSNGLLIA QHHDVVALDI VPSRVELLND RISPIVDKEI QQFLKEDNIR
FRATLDKFDA YQNADYVIIA TPTDYDPKTN YFNTSSVESV MQDVISINPA AVMIIKSTVP
VGFTAAMRQK FATENIIFSP EFLREGKALY DNLYPSRIVI GEQSERAREF AALLQEGAIK
QEIPTLFTDS TEAEAIKLFA NTYLAMRVAY FNELDSYAET LGLNTRQIIE GVCLDPRIGN
HYNNPSFGYG GYCLPKDTKQ LLANYQSVPN NIISAIVEAN RTRKDFIADA ILARKPKVVG
IYRLIMKSGS DNFRASSIQG IMKRIKAKGV EVIIYEPVME EDTFFNSRLE RDLHCFKQQA
DVIISNRMAA ELLDVAEKVY TRDLFGSD
