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UGDH2_ORYSJ
ID   UGDH2_ORYSJ             Reviewed;         482 AA.
AC   B7F958; A0A0P0W012; Q6AUY0;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=UDP-glucose 6-dehydrogenase 2;
DE            Short=UDP-Glc dehydrogenase 2;
DE            Short=UDP-GlcDH 2;
DE            Short=UDPGDH 2;
DE            EC=1.1.1.22;
DE   AltName: Full=Os-UGD2;
GN   Name=UGD2; OrderedLocusNames=Os03g0604200, LOC_Os03g40720;
GN   ORFNames=OSJNBa0004G03.9;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RG   The rice full-length cDNA consortium;
RT   "Oryza sativa full length cDNA.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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=AAT78767.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=ABF97514.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC109601; AAT78767.1; ALT_INIT; Genomic_DNA.
DR   EMBL; DP000009; ABF97514.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP008209; BAF12545.2; -; Genomic_DNA.
DR   EMBL; AP014959; BAS85214.1; -; Genomic_DNA.
DR   EMBL; AK241939; BAH01156.1; -; mRNA.
DR   RefSeq; XP_015629261.1; XM_015773775.1.
DR   AlphaFoldDB; B7F958; -.
DR   SMR; B7F958; -.
DR   STRING; 4530.OS03T0604200-01; -.
DR   PaxDb; B7F958; -.
DR   PRIDE; B7F958; -.
DR   EnsemblPlants; Os03t0604200-01; Os03t0604200-01; Os03g0604200.
DR   GeneID; 4333410; -.
DR   Gramene; Os03t0604200-01; Os03t0604200-01; Os03g0604200.
DR   KEGG; osa:4333410; -.
DR   eggNOG; KOG2666; Eukaryota.
DR   HOGENOM; CLU_023810_7_0_1; -.
DR   InParanoid; B7F958; -.
DR   OMA; YWRQVIR; -.
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   2: Evidence at transcript level;
KW   NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..482
FT                   /note="UDP-glucose 6-dehydrogenase 2"
FT                   /id="PRO_0000422267"
FT   ACT_SITE        274
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         159..163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         218..225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         258..271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         274..277
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         336..337
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         449
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         395
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   482 AA;  53114 MW;  EA428871F560C003 CRC64;
     MVKICCIGAG YVGGPTMAVI ALKCPDVEVV VVDISAPRIE GWNSERLPIY EPGLDDVVRQ
     CRGRNLFFST DVERHVADAG IVFVSVNTPT KTRGLGAGKA ADLTYWESAA RIIADVSRSD
     KIVVEKSTVP VKTAEAIEKI LAHNSKGGNI RYQILSNPEF LAEGTAIQDL FSPDRVLIGG
     RETPEGRAAV AALKSIYARW VPDDRIITTN LWSAELSKLA ANAFLAQRIS SVNAISALCE
     ATGADVTEVA NSIGKDSRIG PRFLSASVGF GGSCFQKDIL NLVYICECYG LPEVANYWHQ
     VIRINDYQKS RFVNRVVSSM FNTVAGKKVA VLGFAFKKDT GDTRETPAID VCKGLVGDKA
     VVSIYDPQVT EEQVQRDLVM NKFDWDHPRH LQPMSPSSAK HVAVSWDAYE AARGAHAVCI
     LTEWDEFRRL DYQRMYDAMH KPAFLFDGRN VVDPDKLRRI GFVVYSIGKP LDHWLRDMPA
     VA
 
 
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