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Database: UniProt
Entry: A0A1G8SI11_9GAMM
LinkDB: A0A1G8SI11_9GAMM
Original site: A0A1G8SI11_9GAMM 
ID   A0A1G8SI11_9GAMM        Unreviewed;       434 AA.
AC   A0A1G8SI11;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00015132, ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=SAMN04487954_1048 {ECO:0000313|EMBL:SDJ28879.1};
OS   Halomonas gudaonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=376427 {ECO:0000313|EMBL:SDJ28879.1, ECO:0000313|Proteomes:UP000198525};
RN   [1] {ECO:0000313|EMBL:SDJ28879.1, ECO:0000313|Proteomes:UP000198525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6133 {ECO:0000313|EMBL:SDJ28879.1,
RC   ECO:0000313|Proteomes:UP000198525};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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|PIRNR:PIRNR000124};
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR   EMBL; FNES01000004; SDJ28879.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8SI11; -.
DR   STRING; 376427.SAMN04487954_1048; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000198525; 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   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; IPR028357; UDPglc_DH_bac.
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   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:UP000198525}.
FT   DOMAIN          303..408
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
FT   BINDING         114
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         141
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         238..242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
SQ   SEQUENCE   434 AA;  48464 MW;  76A8257FFF0C69DB CRC64;
     MRVEIHGSEL AAVTAAAALA WVGHRVHWVP HAGMPWASLV RADWLVREPQ LLARLEEGRQ
     QGALTIAGDD DRDAGTIDVL WLALSPEQRG DADTLVVAAL GERTRPLLLV NNSTFPVGET
     ERLGRLGAPV HAVALVDTLE EGRAWESFTR PGRWLLGRDD DWPEAQVREL LRAFNRRRDA
     FQCMPRRAAE LTKLATIGML ATRISYMNEI AGLADTLGVD VEYVRQGMGA DSRIGYEYLY
     PGCGFGGPNF SRDLMRLADV QEASGRHSAL LEQVLDINEQ KKETLFRKLW THFHGRLEGR
     TVAIWGAAFK PGSARIDHAP VLTLLEALWA QGVSVRVHDP VATPSLHAAV GNHPRLVLLD
     DDPYLACEGA DALMLVTEWK HYWNPDWERL SSLLNERLLL DGRNIYDPRH VADHGLIYRG
     IGRRADPGEQ RSRR
//
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