UGDH2_ARATH
ID UGDH2_ARATH Reviewed; 480 AA.
AC Q9LIA8; Q8L8N1; Q944R8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
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 {ECO:0000269|PubMed:18057039};
DE AltName: Full=At-UGD2;
GN Name=UGD2; Synonyms=UGD; OrderedLocusNames=At3g29360;
GN ORFNames=MUO10.18, MUO10_6;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clone.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10758504; DOI=10.1046/j.1365-313x.2000.00696.x;
RA Seitz B., Klos C., Wurm M., Tenhaken R.;
RT "Matrix polysaccharide precursors in Arabidopsis cell walls are synthesized
RT by alternate pathways with organ-specific expression patterns.";
RL Plant J. 21:537-546(2000).
RN [9]
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 [10]
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 [11]
RP GENE FAMILY, NOMENCLATURE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, PATHWAY, 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 [12]
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 [13]
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:10758504,
CC ECO:0000269|PubMed:18057039, ECO:0000269|PubMed:21949134,
CC 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 -!- ACTIVITY REGULATION: Inhibited by UDP-xylose.
CC {ECO:0000269|PubMed:18057039}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=43 uM for NAD(+) {ECO:0000269|PubMed:18057039};
CC KM=123 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. {ECO:0000305|PubMed:18057039}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in roots.
CC {ECO:0000269|PubMed:10758504}.
CC -!- DEVELOPMENTAL STAGE: Restricted expression to the primary root in young
CC seedlings. Later detected in hypocotyl, leaves but with the strongest
CC expression in the root system. {ECO:0000269|PubMed:10758504,
CC ECO:0000269|PubMed:18057039}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Displays smaller nematode-
CC induced syncytia. The UGD2 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 mutants display 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; AP001309; BAB02581.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77573.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77574.1; -; Genomic_DNA.
DR EMBL; AF424576; AAL11570.1; -; mRNA.
DR EMBL; BT021126; AAX22261.1; -; mRNA.
DR EMBL; AK226539; BAE98678.1; -; mRNA.
DR EMBL; BT029164; ABJ17099.1; -; mRNA.
DR EMBL; AY088902; AAM67208.1; -; mRNA.
DR RefSeq; NP_001030792.1; NM_001035715.1.
DR RefSeq; NP_189582.1; NM_113861.4.
DR AlphaFoldDB; Q9LIA8; -.
DR SMR; Q9LIA8; -.
DR BioGRID; 7923; 1.
DR IntAct; Q9LIA8; 2.
DR STRING; 3702.AT3G29360.1; -.
DR iPTMnet; Q9LIA8; -.
DR PaxDb; Q9LIA8; -.
DR PRIDE; Q9LIA8; -.
DR ProteomicsDB; 246390; -.
DR EnsemblPlants; AT3G29360.1; AT3G29360.1; AT3G29360.
DR EnsemblPlants; AT3G29360.2; AT3G29360.2; AT3G29360.
DR GeneID; 822594; -.
DR Gramene; AT3G29360.1; AT3G29360.1; AT3G29360.
DR Gramene; AT3G29360.2; AT3G29360.2; AT3G29360.
DR KEGG; ath:AT3G29360; -.
DR Araport; AT3G29360; -.
DR TAIR; locus:2093827; AT3G29360.
DR eggNOG; KOG2666; Eukaryota.
DR HOGENOM; CLU_023810_7_0_1; -.
DR InParanoid; Q9LIA8; -.
DR OMA; KGIRFQI; -.
DR OrthoDB; 915490at2759; -.
DR PhylomeDB; Q9LIA8; -.
DR BioCyc; ARA:AT3G29360-MON; -.
DR BRENDA; 1.1.1.22; 399.
DR SABIO-RK; Q9LIA8; -.
DR UniPathway; UPA00038; UER00491.
DR PRO; PR:Q9LIA8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIA8; baseline and differential.
DR Genevisible; Q9LIA8; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0099503; C:secretory vesicle; 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 2"
FT /id="PRO_0000312027"
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 CONFLICT 12
FT /note="V -> I (in Ref. 3; AAL11570)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="G -> R (in Ref. 3; AAL11570)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="N -> D (in Ref. 7; AAM67208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 53173 MW; D6281D20442CBADF CRC64;
MVKICCIGAG YVGGPTMAVI ALKCPDVEVA VVDISVPRIN AWNSDTLPIY EPGLDDVVKQ
CRGKNLFFST DVEKHVREAD IVFVSVNTPT KTRGLGAGKA ADLTYWESAA RMIADVSVSD
KIVVEKSTVP VKTAEAIEKI LTHNSKGIKF QILSNPEFLA EGTAIKDLFN PDRVLIGGRE
TPEGFKAVQT LKNVYAHWVP EGQIITTNLW SAELSKLAAN AFLAQRISSV NAMSALCEAT
GADVTQVSYA VGTDSRIGPK FLNSSVGFGG SCFQKDILNL VYICECNGLP EVAEYWKQVI
KINDYQKSRF VNRVVSSMFN SVSNKKIAVL GFAFKKDTGD TRETPAIDVC KGLLEDKARL
SIYDPQVTED QIQRDLSMNK FDWDHPLHLQ PMSPTTVKQV TVTWDAYEAT KDAHGICIMT
EWDEFKNLDF QKIFDNMQKP AFVFDGRNIM NLQKLREIGF IVYSIGKPLD DWLKDMPAVA
