UXS3_ARATH
ID UXS3_ARATH Reviewed; 342 AA.
AC Q9FIE8; Q94JQ5;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=UDP-glucuronic acid decarboxylase 3;
DE EC=4.1.1.35;
DE AltName: Full=UDP-XYL synthase 3;
DE AltName: Full=UDP-glucuronate decarboxylase 3;
DE Short=UGD;
DE Short=UXS-3;
GN Name=UXS3; OrderedLocusNames=At5g59290; ORFNames=MNC17.20;
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 [MRNA], GENE FAMILY, FUNCTION, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=12481102; DOI=10.1104/pp.009654;
RA Harper A.D., Bar-Peled M.;
RT "Biosynthesis of UDP-xylose. Cloning and characterization of a novel
RT Arabidopsis gene family, UXS, encoding soluble and putative membrane-bound
RT UDP-glucuronic acid decarboxylase isoforms.";
RL Plant Physiol. 130:2188-2198(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [3]
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 [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15655675; DOI=10.1007/s00425-004-1471-7;
RA Pattathil S., Harper A.D., Bar-Peled M.;
RT "Biosynthesis of UDP-xylose: characterization of membrane-bound AtUxs2.";
RL Planta 221:538-548(2005).
RN [7]
RP FUNCTION.
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).
CC -!- FUNCTION: Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic
CC acid to UDP-xylose. Necessary for the biosynthesis of the core
CC tetrasaccharide in glycosaminoglycan biosynthesis.
CC {ECO:0000269|PubMed:12481102, ECO:0000269|PubMed:16817893}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + UDP-alpha-D-glucuronate = CO2 + UDP-alpha-D-xylose;
CC Xref=Rhea:RHEA:23916, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57632, ChEBI:CHEBI:58052; EC=4.1.1.35;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:12481102};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.51 mM for UDP-D-glucuronate at 30 degrees Celsius
CC {ECO:0000269|PubMed:12481102};
CC pH dependence:
CC Optimum pH is 5.5 at 30 degrees Celsius.
CC {ECO:0000269|PubMed:12481102};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:12481102};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-xylose
CC biosynthesis; UDP-alpha-D-xylose from UDP-alpha-D-glucuronate: step
CC 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15655675}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FIE8-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12481102}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. UDP-glucuronic acid decarboxylase subfamily. {ECO:0000305}.
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DR EMBL; AF387789; AAK70882.1; -; mRNA.
DR EMBL; AB016890; BAB09774.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97166.1; -; Genomic_DNA.
DR EMBL; AF375442; AAK53026.1; -; mRNA.
DR EMBL; AY093958; AAM16219.1; -; mRNA.
DR EMBL; AY088443; AAM65979.1; -; mRNA.
DR RefSeq; NP_200737.1; NM_125319.3. [Q9FIE8-1]
DR AlphaFoldDB; Q9FIE8; -.
DR SMR; Q9FIE8; -.
DR BioGRID; 21291; 1.
DR STRING; 3702.AT5G59290.2; -.
DR iPTMnet; Q9FIE8; -.
DR PaxDb; Q9FIE8; -.
DR PRIDE; Q9FIE8; -.
DR ProteomicsDB; 243247; -. [Q9FIE8-1]
DR EnsemblPlants; AT5G59290.1; AT5G59290.1; AT5G59290. [Q9FIE8-1]
DR GeneID; 836047; -.
DR Gramene; AT5G59290.1; AT5G59290.1; AT5G59290. [Q9FIE8-1]
DR KEGG; ath:AT5G59290; -.
DR Araport; AT5G59290; -.
DR eggNOG; KOG1429; Eukaryota.
DR HOGENOM; CLU_007383_4_0_1; -.
DR PhylomeDB; Q9FIE8; -.
DR BioCyc; ARA:AT5G59290-MON; -.
DR BioCyc; MetaCyc:AT5G59290-MON; -.
DR BRENDA; 4.1.1.35; 399.
DR SABIO-RK; Q9FIE8; -.
DR UniPathway; UPA00796; UER00771.
DR PRO; PR:Q9FIE8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIE8; baseline and differential.
DR Genevisible; Q9FIE8; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0042732; P:D-xylose metabolic process; IBA:GO_Central.
DR GO; GO:0033320; P:UDP-D-xylose biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR044516; UXS.
DR PANTHER; PTHR43078; PTHR43078; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Decarboxylase; Lyase; NAD;
KW Reference proteome.
FT CHAIN 1..342
FT /note="UDP-glucuronic acid decarboxylase 3"
FT /id="PRO_0000421984"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 61..86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 173..177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 215..219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232..239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 299..303
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 46
FT /note="V -> D (in Ref. 4; AAK53026/AAM16219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 38569 MW; 5E2AA6C9A13CEBD8 CRC64;
MAATSEKQNT TKPPPSPSPL RNSKFCQPNM RILISGGAGF IGSHLVDKLM ENEKNEVVVA
DNYFTGSKEN LKKWIGHPRF ELIRHDVTEP LLIEVDRIYH LACPASPIFY KYNPVKTIKT
NVIGTLNMLG LAKRVGARIL LTSTSEVYGD PLIHPQPESY WGNVNPIGVR SCYDEGKRVA
ETLMFDYHRQ HGIEIRIARI FNTYGPRMNI DDGRVVSNFI AQALRGEALT VQKPGTQTRS
FCYVSDMVDG LIRLMEGNDT GPINIGNPGE FTMVELAETV KELINPSIEI KMVENTPDDP
RQRKPDISKA KEVLGWEPKV KLREGLPLME EDFRLRLNVP RN
