ID S8FEY0_9BACT Unreviewed; 418 AA.
AC S8FEY0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=HMPREF9012_0382 {ECO:0000313|EMBL:EPT34536.1};
OS Bacteroidetes bacterium oral taxon 272 str. F0290.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=888054 {ECO:0000313|EMBL:EPT34536.1, ECO:0000313|Proteomes:UP000015345};
RN [1] {ECO:0000313|EMBL:EPT34536.1, ECO:0000313|Proteomes:UP000015345}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0290 {ECO:0000313|EMBL:EPT34536.1,
RC ECO:0000313|Proteomes:UP000015345};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (JUL-2013) 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 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}.
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:EPT34536.1}.
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DR EMBL; AUTU01000007; EPT34536.1; -; Genomic_DNA.
DR AlphaFoldDB; S8FEY0; -.
DR PATRIC; fig|888054.3.peg.318; -.
DR OrthoDB; 9803238at2; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000015345; 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|PIRNR:PIRNR000124};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000124};
KW Reference proteome {ECO:0000313|Proteomes:UP000015345}.
FT DOMAIN 323..417
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 270
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT BINDING 35
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 124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 157..160
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 259..263
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 337
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
SQ SEQUENCE 418 AA; 46751 MW; 62D7415EA90E5BCB CRC64;
MVITIFGLGF VGLTTALGFA EYGHKIYGIE TDEERLHTVR SGSLPFLEPG LDEALARHLQ
RDFFPIALPD LEEAIAESDC IYYCVGTPYG KDGQAELSYL FEAIDQTLAR IRDERFRVLV
VKSTVPPSTC AKQIVPYLED KGVKLGDKIG LANNPEFLRE GHCWDDFMGA DRIVLGVNDA
QSQELLCRLY ASVDVPLFCV SLNTGEFIKY LSNALLATLI SFSNEMSMVA DTVGDIDVAR
AFRILHLDKR WGGCDMASYV YPGCGYGGYC LPKDTNALYA VLKTMGFEAN LLREVIVVND
TMPQVIVRRI DQAVKGNKQV KLGFLGLSFK PGSDDVRDAP SAKIIRYLLD EGYSNILAYD
PVANEEFKKH YTLTIDYVDQ YPKILEQADA FVITTAWPEF RHIESETTKP VVDCRYML
//
