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Database: UniProt
Entry: A0A0X8CDN1_9BRAD
LinkDB: A0A0X8CDN1_9BRAD
Original site: A0A0X8CDN1_9BRAD 
ID   A0A0X8CDN1_9BRAD        Unreviewed;       438 AA.
AC   A0A0X8CDN1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00015132, ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=BCCGELA001_03675 {ECO:0000313|EMBL:AMA55458.1};
OS   Bradyrhizobium sp. CCGE-LA001.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1223566 {ECO:0000313|EMBL:AMA55458.1, ECO:0000313|Proteomes:UP000019052};
RN   [1] {ECO:0000313|EMBL:AMA55458.1, ECO:0000313|Proteomes:UP000019052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCGE-LA001 {ECO:0000313|EMBL:AMA55458.1,
RC   ECO:0000313|Proteomes:UP000019052};
RX   PubMed=24952318; DOI=10.1016/j.ympev.2014.06.006;
RA   Servin-Garciduenas L.E., Zayas-Del Moral A., Ormeno-Orrillo E., Rogel M.A.,
RA   Delgado-Salinas A., Sanchez F., Martinez-Romero E.;
RT   "Symbiont shift towards Rhizobium nodulation in a group of phylogenetically
RT   related Phaseolus species.";
RL   Mol. Phylogenet. Evol. 79:1-11(2014).
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; CP013949; AMA55458.1; -; Genomic_DNA.
DR   RefSeq; WP_008542631.1; NZ_CP013949.1.
DR   AlphaFoldDB; A0A0X8CDN1; -.
DR   STRING; 1223566.BCCGELA001_03675; -.
DR   KEGG; brc:BCCGELA001_03675; -.
DR   UniPathway; UPA00038; UER00491.
DR   Proteomes; UP000019052; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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          317..418
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
FT   ACT_SITE        263
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         122
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         152..155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         252..256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         266
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         331
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
SQ   SEQUENCE   438 AA;  47306 MW;  3B839370E8E1125B CRC64;
     MRIAMIGTGY VGLVSGACFA DFGHDVTCVD KDEKKIAALH RGEIPIYEPG LEELVANNVR
     AKRLEFTTDL SKPVADADAV FIAVGTPSRR GDGHADLSYV YAAAKEIAQS LQGFTVVVTK
     STVPVGTGDE VERIIREANP KADVVVASNP EFLREGAAIR DFKFPDRVVV GTSDERGRKV
     MGDIYRPLSL NQAPLMFTAR RTAEMIKYAA NAFLATKITF INEIADLSEK AGANVQEVAR
     GIGLDNRIGT KFLHAGPGFG GSCFPKDTKA LIKIAQDYDV NLRIVESVLA VNENRKRAMA
     RKVSQALGGS LRGKTIAVLG LTFKPDTDDM RDAPSIPLVT GLIDMGAAVK AFDPVGMEQA
     KSELPSITYC EDAYSCAQGA DALVIVTEWV QFRALDLDRL KATMAQPVVV DLRNIYRPEE
     MEAAGFVYES VGRPAVQG
//
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