ID UDG_SHIFL Reviewed; 372 AA. AC P37791; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 24-JAN-2024, entry version 134. DE RecName: Full=Putative 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; OrderedLocusNames=SF2090, S2211; OS Shigella flexneri. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=PE577 / Serotype 2a; RX PubMed=7507920; DOI=10.1128/jb.176.3.733-747.1994; RA Morona R., Mavris M., Fallarino A., Manning P.A.; RT "Characterization of the rfc region of Shigella flexneri."; RL J. Bacteriol. 176:733-747(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella flexneri RT serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). 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 -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AE005674; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AE014073; Type=Frameshift; Evidence={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; X71970; CAA50782.1; -; Genomic_DNA. DR EMBL; AE005674; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AE014073; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; P37791; -. DR SMR; P37791; -. DR UniPathway; UPA00030; -. DR UniPathway; UPA00038; UER00491. DR Proteomes; UP000001006; Chromosome. DR Proteomes; UP000002673; 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 5: Uncertain; KW NAD; Oxidoreductase; Reference proteome. FT CHAIN 1..372 FT /note="Putative UDP-glucose 6-dehydrogenase" FT /id="PRO_0000074048" 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 291 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 298 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT CONFLICT 213 FT /note="E -> D (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 325 FT /note="G -> E (in Ref. 2 and 3)" FT /evidence="ECO:0000305" SQ SEQUENCE 372 AA; 41886 MW; DCF6ABB03362AD8D CRC64; MKITISGTGY VGLSNGLLIA QNHEVVALDI LPSRVAMLND RISPIVDKEI QQFLQSDKIH FNATLDKNEA YRDADYVIIA TPTDYDPKTN YFNTSSVESV IKDVVEINPY AVMVIKSTVP VGFTAAMHKK YRTENIIFSP EFLREGKALY DNLHPSRIVI GERSERAERF AALLQEGAIK QNIPTLFTDS TEAEAIKLFA NTYLAMRVAY FNELDSYAES LGLNTRQIIE GVCLDPRIGN HYNNPSFGYG GYCLPKDTKQ LLANYQSVPN NLISAIVDAN RKWWVFIVIM KSGSDNFRAS SIQGIMKRIK AKGVEVIIYE PVMKGDSFFN SRLERDLATF KQQADVIISN RMAEELKDVA DKVYTRDLFG SD //