ID Q6KCZ8_ECOLX Unreviewed; 392 AA.
AC Q6KCZ8;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
GN Name=kfiD {ECO:0000313|EMBL:CAE55820.1};
GN ORFNames=BKL28_004751 {ECO:0000313|EMBL:EFH0045867.1}, FPI65_27440
GN {ECO:0000313|EMBL:NDR94936.1}, GRC73_19960
GN {ECO:0000313|EMBL:HAH4526256.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:CAE55820.1};
RN [1] {ECO:0000313|EMBL:CAE55820.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nissle 1917 {ECO:0000313|EMBL:CAE55820.1};
RX PubMed=15292145; DOI=10.1128/JB.186.16.5432-5441.2004;
RA Grozdanov L., Raasch C., Schulze J., Sonnenborn U., Gottschalk G.,
RA Hacker J., Dobrindt U.;
RT "Analysis of the genome structure of the nonpathogenic probiotic
RT Escherichia coli strain Nissle 1917.";
RL J. Bacteriol. 186:5432-5441(2004).
RN [2] {ECO:0000313|EMBL:HAH4526256.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC00763 {ECO:0000313|EMBL:HAH4526256.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [3] {ECO:0000313|EMBL:EFH0045867.1, ECO:0000313|Proteomes:UP000528199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PNUSAE004760 {ECO:0000313|EMBL:EFH0045867.1,
RC ECO:0000313|Proteomes:UP000528199};
RG PulseNet: The National Subtyping Network for Foodborne Disease Surveillance;
RA Tarr C.L., Trees E., Katz L.S., Carleton-Romer H.A., Stroika S.,
RA Kucerova Z., Roache K.F., Sabol A.L., Besser J., Gerner-Smidt P.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:HAH4526256.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EC00763 {ECO:0000313|EMBL:HAH4526256.1};
RG NCBI Pathogen Detection Project;
RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:NDR94936.1, ECO:0000313|Proteomes:UP000471490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11230 {ECO:0000313|EMBL:NDR94936.1,
RC ECO:0000313|Proteomes:UP000471490};
RX PubMed=32021174;
RA Kedziora A., Wernecki M., Korzekwa K., Speruda M., Gerasymchuk Y.,
RA Lukowiak A., Bugla-Ploskonska G.;
RT "Consequences Of Long-Term Bacteria's Exposure To Silver Nanoformulations
RT With Different PhysicoChemical Properties.";
RL Int J Nanomedicine 15:199-213(2020).
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 Evidence={ECO:0000256|ARBA:ARBA00000874,
CC ECO:0000256|PIRNR:PIRNR000124};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate
CC biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step
CC 1/1. {ECO:0000256|ARBA:ARBA00004701}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00006601, ECO:0000256|PIRNR:PIRNR000124}.
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DR EMBL; AJ586888; CAE55820.1; -; Genomic_DNA.
DR EMBL; AASUOH010000056; EFH0045867.1; -; Genomic_DNA.
DR EMBL; DABBJX010000027; HAH4526256.1; -; Genomic_DNA.
DR EMBL; VLTB01000450; NDR94936.1; -; Genomic_DNA.
DR RefSeq; WP_001305084.1; NZ_WSZB01000003.1.
DR OMA; CQDTQLN; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000471490; Unassembled WGS sequence.
DR Proteomes; UP000528199; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
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; 2.
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 {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000124};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000124}.
FT DOMAIN 304..391
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 257
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 146..149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 246..250
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 260
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
SQ SEQUENCE 392 AA; 44108 MW; 69E15A27FCD25C79 CRC64;
MFGTLKITVS GAGYVGLSNG ILMAQNHEVV AFDTHQKKVD LLNDKLSPIE DKEIENYLST
KILNFRATTN KYEAYKNANY VIIATPTNYD PGSNYFDTSS VEAVIRDVTE INPNAIMVVK
STVPVGFTKT IKEHLGINNI IFSPEFLREG RALYDNLHPS RIIIGECSER AERLAVLFQE
GAIKQNIPVL FTDSTEAEAI KLFSNTYLAM RVAFFNELDS YAESFGLNTR QIIDGVCLDP
RIGNYYNNPS FGYGGYCLPK DTKQLLANYQ SVPNKLISAI VDANRTRKDF ITNVILKHRP
QVVGVYRLIM KSGSDNFRDS SILGIIKRIK KKGVKVIIYE PLISGDTFFN SPLERELAIF
KGKADIIITN RMSEELNDVV DKVYSRDLFK CD
//
