UXS4_ARATH
ID UXS4_ARATH Reviewed; 443 AA.
AC Q8S8T4;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=UDP-glucuronic acid decarboxylase 4;
DE EC=4.1.1.35;
DE AltName: Full=UDP-XYL synthase 4;
DE AltName: Full=UDP-glucuronate decarboxylase 4;
DE Short=UGD;
DE Short=UXS-4;
GN Name=UXS4; OrderedLocusNames=At2g47650; ORFNames=T30B22.31;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP GENE FAMILY.
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).
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 (By similarity).
CC {ECO:0000250}.
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; Evidence={ECO:0000250};
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: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
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=Q8S8T4-1; Sequence=Displayed;
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; AC002535; AAM14846.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10871.1; -; Genomic_DNA.
DR EMBL; BT022016; AAY25428.1; -; mRNA.
DR EMBL; AK316734; BAH19459.1; -; mRNA.
DR PIR; T00419; T00419.
DR RefSeq; NP_182287.1; NM_130333.4. [Q8S8T4-1]
DR AlphaFoldDB; Q8S8T4; -.
DR SMR; Q8S8T4; -.
DR STRING; 3702.AT2G47650.2; -.
DR PaxDb; Q8S8T4; -.
DR PRIDE; Q8S8T4; -.
DR ProteomicsDB; 228544; -. [Q8S8T4-1]
DR EnsemblPlants; AT2G47650.1; AT2G47650.1; AT2G47650. [Q8S8T4-1]
DR GeneID; 819378; -.
DR Gramene; AT2G47650.1; AT2G47650.1; AT2G47650. [Q8S8T4-1]
DR KEGG; ath:AT2G47650; -.
DR Araport; AT2G47650; -.
DR eggNOG; KOG1429; Eukaryota.
DR HOGENOM; CLU_007383_2_1_1; -.
DR InParanoid; Q8S8T4; -.
DR OMA; CEGFISL; -.
DR PhylomeDB; Q8S8T4; -.
DR UniPathway; UPA00796; UER00771.
DR PRO; PR:Q8S8T4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S8T4; baseline and differential.
DR Genevisible; Q8S8T4; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Decarboxylase; Golgi apparatus; Lyase;
KW Membrane; NAD; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9LZI2"
FT CHAIN 2..443
FT /note="UDP-glucuronic acid decarboxylase 4"
FT /id="PRO_0000421985"
FT TOPO_DOM 2..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..443
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 151..176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 263..267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 305..309
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 322..329
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 389..393
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9LZI2"
SQ SEQUENCE 443 AA; 49945 MW; CAD02A4FA5B57811 CRC64;
MASELTNRRH EIEQPEAESY YPKPIKPWFV AIRPIRYMLR EQRLVFVLVG IAIATLGFTI
FSKSSNHQPI PYDVDPLSGY GMRSESSYLP ATIHKKPSIE YMSRIGSAGG KIPLGLKRKV
LRVVVTGGAG FVGSHLVDRL MARGDNVIVV DNFFTGRKEN VMHHFNNPNF EMIRHDVVEP
ILLEVDQIYH LACPASPVHY KFNPVKTIKT NVVGTLNMLG LAKRVGARFL LTSTSEVYGD
PLQHPQVETY WGNVNPIGVR SCYDEGKRTA ETLTMDYHRG ANVEVRIARI FNTYGPRMCI
DDGRVVSNFV AQALRKEPLT VYGDGKQTRS FQFVSDLVEG LMRLMEGEHV GPFNLGNPGE
FTMLELAKVV QETIDPNAKI EFRPNTEDDP HKRKPDITKA KELLGWEPKV ALRQGLPLMV
KDFRQRVFGD QKQDSSTTSS STE
