ID   UGDH1_ORYSJ             Reviewed;         481 AA.
AC   Q75GS4; A0A0P0VYX6; Q0DR19; Q10JC3;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=UDP-glucose 6-dehydrogenase 1;
DE            Short=UDP-Glc dehydrogenase 1;
DE            Short=UDP-GlcDH 1;
DE            Short=UDPGDH 1;
DE            EC=1.1.1.22;
DE   AltName: Full=Os-UGD1;
GN   Name=UGD1; OrderedLocusNames=Os03g0425600, LOC_Os03g31210;
GN   ORFNames=OSJNBa0020H02.10;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18057039; DOI=10.1093/jxb/erm209;
RA   Klinghammer M., Tenhaken R.;
RT   "Genome-wide analysis of the UDP-glucose dehydrogenase gene family in
RT   Arabidopsis, a key enzyme for matrix polysaccharides in cell walls.";
RL   J. Exp. Bot. 58:3609-3621(2007).
CC   -!- FUNCTION: Involved in the biosynthesis of UDP-glucuronic acid (UDP-
CC       GlcA), providing nucleotide sugars for cell-wall polymers.
CC       {ECO:0000250}.
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   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate
CC       biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step
CC       1/1.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABF96712.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF12319.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC137999; AAS07200.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF96712.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008209; BAF12319.2; ALT_INIT; Genomic_DNA.
DR   EMBL; AP014959; BAS84780.1; -; Genomic_DNA.
DR   RefSeq; XP_015630087.1; XM_015774601.1.
DR   AlphaFoldDB; Q75GS4; -.
DR   SMR; Q75GS4; -.
DR   STRING; 4530.OS03T0425600-00; -.
DR   PRIDE; Q75GS4; -.
DR   EnsemblPlants; Os03t0425600-00; Os03t0425600-00; Os03g0425600.
DR   GeneID; 4333156; -.
DR   Gramene; Os03t0425600-00; Os03t0425600-00; Os03g0425600.
DR   KEGG; osa:4333156; -.
DR   eggNOG; KOG2666; Eukaryota.
DR   HOGENOM; CLU_023810_7_0_1; -.
DR   InParanoid; Q75GS4; -.
DR   OMA; RDGVGFQ; -.
DR   OrthoDB; 915490at2759; -.
DR   PlantReactome; R-OSA-1119574; UDP-L-arabinose biosynthesis and transport.
DR   UniPathway; UPA00038; UER00491.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006024; P:glycosaminoglycan biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR028356; UDPglc_DH_euk.
DR   PANTHER; PTHR11374; PTHR11374; 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; PIRSF500133; UDPglc_DH_euk; 1.
DR   PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR   SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52413; SSF52413; 1.
DR   TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..481
FT                   /note="UDP-glucose 6-dehydrogenase 1"
FT                   /id="PRO_0000422266"
FT   ACT_SITE        273
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         8..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         86..90
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         127..128
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         158..162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         217..224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         257..270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         273..276
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         335..336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         448
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         394
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   481 AA;  52297 MW;  CB144A401CDDC0CD CRC64;
     MVKICCLGAG YVGGPTMAVI ALKCPDVEVV VVDISAARID AWNSDALPIY EPGLDDVVRR
     CRGRNLFFSS DVERHVGEAD IVFVSVNTPT KARGLGAGKA ADLTYWESAA RMIAAVATSD
     KVVVEKSTVP VKTAEAIEKI LDHNGRDGVG FQILSNPEFL AEGTAIRDLL APDRVLIGGR
     ETAAGRAAVQ ALKDVYTRWV PEERILTTNL WSAELSKLAA NAFLAQRISS VNAMSALCEA
     TGADVAEVAY AVGKDSRIGA KFLNASVGFG GSCFQKDILN LVYICECNGL PEVANYWKQV
     IKINDYQKSR FVNRVVSSMF NTVAGKKIAV LGFAFKKDTG DTRETPAIDV CKGLIGDKAK
     VSIYDPQVTE DQVQRDLAMS KFDWDHPVHL QPMSPTAIKQ VSVAWDAYEA ARAAHGVCIL
     TEWDEFRSLD YARIYGGMQK PAFVFDGRNV VDAEKLREIG FIVYSIGKPL DAWLKDMPAV
     A