UGDH3_ARATH
ID UGDH3_ARATH Reviewed; 480 AA.
AC Q9LF33;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=UDP-glucose 6-dehydrogenase 3;
DE Short=UDP-Glc dehydrogenase 3;
DE Short=UDP-GlcDH 3;
DE Short=UDPGDH 3;
DE EC=1.1.1.22 {ECO:0000269|PubMed:18057039};
DE AltName: Full=At-UGD3;
GN Name=UGD3; OrderedLocusNames=At5g15490; ORFNames=T20K14_100;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY.
RX PubMed=11554483; DOI=10.1023/a:1010671129803;
RA Reiter W.-D., Vanzin G.F.;
RT "Molecular genetics of nucleotide sugar interconversion pathways in
RT plants.";
RL Plant Mol. Biol. 47:95-113(2001).
RN [6]
RP REVIEW.
RX PubMed=15134748; DOI=10.1016/j.pbi.2004.03.004;
RA Seifert G.J.;
RT "Nucleotide sugar interconversions and cell wall biosynthesis: how to bring
RT the inside to the outside.";
RL Curr. Opin. Plant Biol. 7:277-284(2004).
RN [7]
RP GENE FAMILY, NOMENCLATURE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND DEVELOPMENTAL STAGE.
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).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21949134; DOI=10.1074/jbc.m111.255695;
RA Reboul R., Geserick C., Pabst M., Frey B., Wittmann D., Luetz-Meindl U.,
RA Leonard R., Tenhaken R.;
RT "Down-regulation of UDP-glucuronic acid biosynthesis leads to swollen plant
RT cell walls and severe developmental defects associated with changes in
RT pectic polysaccharides.";
RL J. Biol. Chem. 286:39982-39992(2011).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22848518; DOI=10.1371/journal.pone.0041515;
RA Siddique S., Sobczak M., Tenhaken R., Grundler F.M., Bohlmann H.;
RT "Cell wall ingrowths in nematode induced syncytia require UGD2 and UGD3.";
RL PLoS ONE 7:E41515-E41515(2012).
CC -!- FUNCTION: Involved in the biosynthesis of UDP-glucuronic acid (UDP-
CC GlcA), providing nucleotide sugars for cell-wall polymers. Required for
CC the formation of cell wall ingrowths on the outer cell walls of
CC nematode-induced syncytia. {ECO:0000269|PubMed:18057039,
CC ECO:0000269|PubMed:21949134, ECO:0000269|PubMed:22848518}.
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:0000269|PubMed:18057039};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23597;
CC Evidence={ECO:0000305|PubMed:18057039};
CC -!- ACTIVITY REGULATION: Inhibited by UDP-xylose.
CC {ECO:0000269|PubMed:18057039}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=42 uM for NAD(+) {ECO:0000269|PubMed:18057039};
CC KM=335 uM for UDP-glucose {ECO:0000269|PubMed:18057039};
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 -!- DEVELOPMENTAL STAGE: Restricted expression to the primary root in young
CC seedlings. Later detected in hypocotyl, leaves and flowers.
CC {ECO:0000269|PubMed:18057039}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Displays smaller nematode-
CC induced syncytia. Ugd2 and ugd3 double mutant displays a strong dwarf
CC phenotype and often develops seedlings with severe root defects; cell
CC walls have an altered sugar composition (PubMed:21949134). Ugd2 and
CC ugd3 double mutant displays abnormal nematode-induced syncytia
CC (PubMed:22848518). {ECO:0000269|PubMed:21949134,
CC ECO:0000269|PubMed:22848518}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AL391143; CAC01748.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92167.1; -; Genomic_DNA.
DR EMBL; AY056200; AAL07049.1; -; mRNA.
DR EMBL; BT015794; AAU90084.1; -; mRNA.
DR PIR; T51527; T51527.
DR RefSeq; NP_197053.1; NM_121553.4.
DR AlphaFoldDB; Q9LF33; -.
DR SMR; Q9LF33; -.
DR BioGRID; 16678; 3.
DR STRING; 3702.AT5G15490.1; -.
DR iPTMnet; Q9LF33; -.
DR PaxDb; Q9LF33; -.
DR PRIDE; Q9LF33; -.
DR ProteomicsDB; 233033; -.
DR EnsemblPlants; AT5G15490.1; AT5G15490.1; AT5G15490.
DR GeneID; 831402; -.
DR Gramene; AT5G15490.1; AT5G15490.1; AT5G15490.
DR KEGG; ath:AT5G15490; -.
DR Araport; AT5G15490; -.
DR TAIR; locus:2180872; AT5G15490.
DR eggNOG; KOG2666; Eukaryota.
DR HOGENOM; CLU_023810_7_0_1; -.
DR InParanoid; Q9LF33; -.
DR OMA; CECLNLP; -.
DR OrthoDB; 915490at2759; -.
DR PhylomeDB; Q9LF33; -.
DR BioCyc; ARA:AT5G15490-MON; -.
DR BRENDA; 1.1.1.22; 399.
DR SABIO-RK; Q9LF33; -.
DR UniPathway; UPA00038; UER00491.
DR PRO; PR:Q9LF33; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LF33; baseline and differential.
DR Genevisible; Q9LF33; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IGI:TAIR.
DR GO; GO:0052546; P:cell wall pectin metabolic process; IGI:TAIR.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..480
FT /note="UDP-glucose 6-dehydrogenase 3"
FT /id="PRO_0000422268"
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"
SQ SEQUENCE 480 AA; 53117 MW; 51CD42EAB2C57A77 CRC64;
MVKICCIGAG YVGGPTMAVI ALKCPSVEVA VVDISVPRIN AWNSDQLPIY EPGLDDVVKQ
CRGKNLFFST DVEKHVREAD IVFVSVNTPT KTRGLGAGKA ADLTYWESAA RMIADVSVSD
KIVVEKSTVP VKTAEAIEKI LTHNSKGIKF QILSNPEFLA EGTAIEDLFM PDRVLIGGRE
TTEGFAAVKA LKDIYAQWVP EERILTTNLW SAELSKLAAN AFLAQRISSV NAMSALCEAT
GANVSEVSYA VGKDSRIGPK FLNSSVGFGG SCFQKDILNL VYICECNGLP EVAEYWKQVI
KINDYQKTRF VNRIVSSMFN TVSNKKIAVL GFAFKKDTGD TRETPAIDVC KGLLGDKARL
SIYDPQVTEE QIQRDLTMNK FDWDHPLHLQ PMSPTTVKQV SVAWDAYTAT KDAHGICILT
EWDEFKKLDF QRIFENMQKP AFVFDGRNVV DADKLREIGF IVYSIGKPLD QWLKDMPALA
