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 27-MAR-2024, entry version 148. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 99287-STM2080; -. DR GeneID; 1253601; -. DR KEGG; stm:STM2080; -. DR PATRIC; fig|99287.12.peg.2202; -. DR HOGENOM; CLU_023810_2_0_6; -. DR OMA; LFMGFTE; -. DR PhylomeDB; Q04873; -. DR BioCyc; SENT99287:STM2080-MONOMER; -. 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; 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; 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 //