UGDH5_ORYSJ
ID UGDH5_ORYSJ Reviewed; 480 AA.
AC Q2QS13; A0A0N7KTZ5;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=UDP-glucose 6-dehydrogenase 5;
DE Short=UDP-Glc dehydrogenase 5;
DE Short=UDP-GlcDH 5;
DE Short=UDPGDH 5;
DE EC=1.1.1.22;
DE AltName: Full=Os-UGD5;
GN Name=UGD5; OrderedLocusNames=Os12g0443600, LOC_Os12g25700;
GN ORFNames=OsJ_35986;
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=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(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 GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DP000011; ABA97737.1; -; Genomic_DNA.
DR EMBL; DP000011; ABA97738.1; -; Genomic_DNA.
DR EMBL; DP000011; ABG22007.1; -; Genomic_DNA.
DR EMBL; AP008218; BAF29725.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT16994.1; -; Genomic_DNA.
DR EMBL; CM000149; EEE53159.1; -; Genomic_DNA.
DR EMBL; AK099096; BAG93921.1; -; mRNA.
DR EMBL; AK103919; BAG96319.1; -; mRNA.
DR RefSeq; XP_015620482.1; XM_015764996.1.
DR RefSeq; XP_015620483.1; XM_015764997.1.
DR RefSeq; XP_015620484.1; XM_015764998.1.
DR RefSeq; XP_015620486.1; XM_015765000.1.
DR AlphaFoldDB; Q2QS13; -.
DR SMR; Q2QS13; -.
DR STRING; 4530.OS12T0443600-01; -.
DR PaxDb; Q2QS13; -.
DR PRIDE; Q2QS13; -.
DR EnsemblPlants; Os12t0443600-01; Os12t0443600-01; Os12g0443600.
DR EnsemblPlants; Os12t0443600-02; Os12t0443600-02; Os12g0443600.
DR GeneID; 4352147; -.
DR Gramene; Os12t0443600-01; Os12t0443600-01; Os12g0443600.
DR Gramene; Os12t0443600-02; Os12t0443600-02; Os12g0443600.
DR KEGG; osa:4352147; -.
DR eggNOG; KOG2666; Eukaryota.
DR HOGENOM; CLU_023810_7_0_1; -.
DR InParanoid; Q2QS13; -.
DR OMA; CECLNLP; -.
DR OrthoDB; 915490at2759; -.
DR PlantReactome; R-OSA-1119452; Galactose degradation II.
DR PlantReactome; R-OSA-1119563; UDP-D-xylose biosynthesis.
DR PlantReactome; R-OSA-1119574; UDP-L-arabinose biosynthesis and transport.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000007752; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q2QS13; OS.
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..480
FT /note="UDP-glucose 6-dehydrogenase 5"
FT /id="PRO_0000422271"
FT ACT_SITE 272
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 157..161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 216..223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 256..269
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 272..275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 334..335
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 480 AA; 52919 MW; F3243A7DC0A422FA CRC64;
MVKICCIGAG YVGGPTMAVI ALKCPAIEVV VVDISKPRVD AWNSDQLPIY EPGLDEVVKE
CRGRNLFFST DVEKHVAEAD IIFVSVNTPT KTRGLGAGKA ADLTYWESAA RMIADVSKSD
KIVVEKSTVP VKTAEAIEKI LTHNSKGINY QILSNPEFLA EGTAIEDLFK PDRVLIGGRE
TPEGKKAVQA LKEVYAHWVP EDRIITTNLW SAELSKLAAN AFLAQRISSV NAISALCEAT
GANVSEVAYA VGKDTRIGPK FLNASVGFGG SCFQKDILNL VYICECNGLP EVANYWKQVI
KINDYQKSRF VNRVVASMFN TVSGKKIAVL GFAFKKDTGD TRETPAIDVC HGLLGDKAQI
SIYDPQVTED QIQRDLSMAK FDWDHPRHLQ PTSPTAFKQV SVVWDAYEAT KGAHGLCILT
EWDEFKTLDY QRIFDNMQKP AFVFDGRNVV DPEKLREIGF IVYSIGKPLD AWLKDMPAVA
