ID Q39VR0_GEOMG Unreviewed; 450 AA.
AC Q39VR0;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
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=ugd {ECO:0000313|EMBL:ABB31664.1};
GN OrderedLocusNames=Gmet_1430 {ECO:0000313|EMBL:ABB31664.1};
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB31664.1, ECO:0000313|Proteomes:UP000007073};
RN [1] {ECO:0000313|EMBL:ABB31664.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABB31664.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RX PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT "The genome sequence of Geobacter metallireducens: features of metabolism,
RT physiology and regulation common and dissimilar to Geobacter
RT sulfurreducens.";
RL BMC Microbiol. 9:109-109(2009).
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; CP000148; ABB31664.1; -; Genomic_DNA.
DR RefSeq; WP_004511638.1; NC_007517.1.
DR AlphaFoldDB; Q39VR0; -.
DR STRING; 269799.Gmet_1430; -.
DR KEGG; gme:Gmet_1430; -.
DR eggNOG; COG1004; Bacteria.
DR HOGENOM; CLU_023810_1_2_7; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000007073; Chromosome.
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:UP000007073}.
FT DOMAIN 325..428
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT BINDING 30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 155..158
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 255..259
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 339
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
SQ SEQUENCE 450 AA; 49386 MW; 167593D7A5901815 CRC64;
MKICVIGSGY VGLVAGTCFA ESGNTVICVD VNQEKIEGLK QGILPIYEPG LKELVLRNSA
EGRLSFTTDL ASAVKESLIC FIAVGTPPGE DGSADLQHVL AVAREIGRNM EGFKIIVDKS
TVPVGTADKV RRAAQEELDR RGAAYEFDVV SNPEFLKEGA AIDDFMKPDR VVIGADNVRT
AEIMKELYSP FMRKTNRLIV MDVHSAEMTK YAANAMLATR ISFMNQIANL CERMGADVSA
VREGIGSDSR IGYDFLFPGV GYGGSCFPKD VKALIKTAEE CEYDFVLLKS VEEVNERQKA
ILIDKMIAHF SRDNGASPLA GKTIAIWGLS FKPRTDDMRE APSIVIISKL LEMGATVLAH
DPEAVKEAKK IFGDRITYTS TNQYEILKGA DALAIITEWN EYRNPDFERI SASLTAPVIF
DGRNLYNPRR MKEIGFTYHS IGRNGSAFTG
//
