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Database: UniProt
Entry: A0A2D5Z2G7_9BACT
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ID   A0A2D5Z2G7_9BACT        Unreviewed;       325 AA.
AC   A0A2D5Z2G7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954};
DE            EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954};
DE   Flags: Fragment;
GN   ORFNames=CMJ18_03785 {ECO:0000313|EMBL:MAE63370.1};
OS   Phycisphaeraceae bacterium.
OC   Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC   Phycisphaeraceae.
OX   NCBI_TaxID=2026777 {ECO:0000313|EMBL:MAE63370.1, ECO:0000313|Proteomes:UP000222953};
RN   [1] {ECO:0000313|Proteomes:UP000222953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MAE63370.1}.
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DR   EMBL; NYZC01000052; MAE63370.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D5Z2G7; -.
DR   UniPathway; UPA00038; UER00491.
DR   Proteomes; UP000222953; 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; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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   NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR   PANTHER; PTHR43750; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1.
DR   PANTHER; PTHR43750:SF3; 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 {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          194..296
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
FT   ACT_SITE        132
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT   BINDING         21..24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         24
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         121..125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         135
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         208
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:MAE63370.1"
SQ   SEQUENCE   325 AA;  36275 MW;  C05573C28A048839 CRC64;
     VAAEIEARTE KPFRMASNPE FLKEGAAIND FNKPDRVVLG VEDEGTGRRL HELYEPFVRQ
     GNPIYVMDIA SAEMVKYAAN AMLATKISFI NEIAGLCEAY GADIDEVRLG MCSDRRIGNQ
     FLFPGLGYGG SCFPKDVLAC ISMGEDTQRQ THLLRAVHDV NQRQRDAFFR KIDEHFGAEA
     SGQTERGLDG RRIAVWGLAF KPGTDDVREA PSLTIIERLL DRGATVTAFD PVAREASARM
     LDRPIEYAEN MMDCLDGADA LVICTDWDEF RHPDLDAVRQ RMRQPVIFDG RNLYRSTTMT
     EYGFTYYSVG REAVAPQVGI RGLAG
//
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