UGDH1_ARATH
ID UGDH1_ARATH Reviewed; 481 AA.
AC Q9FZE1; Q8LG68;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
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 {ECO:0000269|PubMed:16817893};
DE AltName: Full=At-UGD1;
GN Name=UGD1; Synonyms=UGD4; OrderedLocusNames=At1g26570; ORFNames=T1K7.6;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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 [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 FUNCTION, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=16817893; DOI=10.1111/j.1742-4658.2006.05281.x;
RA Oka T., Jigami Y.;
RT "Reconstruction of de novo pathway for synthesis of UDP-glucuronic acid and
RT UDP-xylose from intrinsic UDP-glucose in Saccharomyces cerevisiae.";
RL FEBS J. 273:2645-2657(2006).
RN [8]
RP GENE FAMILY, NOMENCLATURE, 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 [9]
RP DISRUPTION PHENOTYPE, AND INDUCTION.
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.
CC {ECO:0000269|PubMed:16817893}.
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:16817893};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23597;
CC Evidence={ECO:0000305|PubMed:16817893};
CC -!- ACTIVITY REGULATION: Inhibited by UDP-xylose.
CC {ECO:0000269|PubMed:16817893}.
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:16817893}.
CC -!- DEVELOPMENTAL STAGE: Restricted expression to the primary shoot in
CC young seedlings. Later detected in hypocotyl, leaves and flowers.
CC {ECO:0000269|PubMed:18057039}.
CC -!- INDUCTION: Specifically induced by H.schachtii (cyst nematodes) in
CC nematode-induced syncytia. {ECO:0000269|PubMed:22848518}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:22848518}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000305}.
CC -!- CAUTION: Was originally assigned as UGD4.
CC {ECO:0000305|PubMed:11554483}.
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DR EMBL; AC013427; AAF98561.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30705.1; -; Genomic_DNA.
DR EMBL; AY070758; AAL50096.1; -; mRNA.
DR EMBL; AY143922; AAN28861.1; -; mRNA.
DR EMBL; AY084436; AAM61009.1; -; mRNA.
DR PIR; G86392; G86392.
DR RefSeq; NP_173979.1; NM_102419.4.
DR AlphaFoldDB; Q9FZE1; -.
DR SMR; Q9FZE1; -.
DR BioGRID; 24433; 3.
DR IntAct; Q9FZE1; 2.
DR STRING; 3702.AT1G26570.1; -.
DR PaxDb; Q9FZE1; -.
DR PRIDE; Q9FZE1; -.
DR ProteomicsDB; 245296; -.
DR EnsemblPlants; AT1G26570.1; AT1G26570.1; AT1G26570.
DR GeneID; 839197; -.
DR Gramene; AT1G26570.1; AT1G26570.1; AT1G26570.
DR KEGG; ath:AT1G26570; -.
DR Araport; AT1G26570; -.
DR TAIR; locus:2197945; AT1G26570.
DR eggNOG; KOG2666; Eukaryota.
DR HOGENOM; CLU_023810_7_0_1; -.
DR InParanoid; Q9FZE1; -.
DR OMA; YASNCFL; -.
DR OrthoDB; 915490at2759; -.
DR PhylomeDB; Q9FZE1; -.
DR BioCyc; ARA:AT1G26570-MON; -.
DR UniPathway; UPA00038; UER00491.
DR PRO; PR:Q9FZE1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZE1; baseline and differential.
DR Genevisible; Q9FZE1; AT.
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; IDA:UniProtKB.
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..481
FT /note="UDP-glucose 6-dehydrogenase 1"
FT /id="PRO_0000422265"
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 448
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 114
FT /note="A -> P (in Ref. 4; AAM61009)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 52972 MW; B36F0F7AE3676BC0 CRC64;
MVKICCIGAG YVGGPTMAVM ALKCPEIEVV VVDISEPRIN AWNSDRLPIY EPGLEDVVKQ
CRGKNLFFST DVEKHVFESD IVFVSVNTPT KTQGLGAGKA ADLTYWESAA RMIADVSKSS
KIVVEKSTVP VRTAEAIEKI LTHNSKGIEF QILSNPEFLA EGTAIKDLYN PDRVLIGGRD
TAAGQKAIKA LRDVYAHWVP VEQIICTNLW SAELSKLAAN AFLAQRISSV NAMSALCEAT
GADVTQVAHA VGTDTRIGPK FLNASVGFGG SCFQKDILNL IYICECNGLP EAANYWKQVV
KVNDYQKIRF ANRVVSSMFN TVSGKKIAIL GFAFKKDTGD TRETPAIDVC NRLVADKAKL
SIYDPQVLEE QIRRDLSMAR FDWDHPVPLQ QIKAEGISEQ VNVVSDAYEA TKDAHGLCVL
TEWDEFKSLD FKKIFDNMQK PAFVFDGRNV VDAVKLREIG FIVYSIGKPL DSWLKDMPAV
A
