UXS6_ARATH
ID UXS6_ARATH Reviewed; 343 AA.
AC Q9ZV36;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=UDP-glucuronic acid decarboxylase 6;
DE EC=4.1.1.35;
DE AltName: Full=UDP-XYL synthase 6;
DE AltName: Full=UDP-glucuronate decarboxylase 6;
DE Short=UGD;
DE Short=UXS-6;
GN Name=UXS6; OrderedLocusNames=At2g28760; ORFNames=F8N16.5;
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;
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 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: Cytoplasm {ECO:0000250}.
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; AC005727; AAC79582.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08167.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08168.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08169.1; -; Genomic_DNA.
DR EMBL; AY099703; AAM20554.1; -; mRNA.
DR EMBL; AY128899; AAM91299.1; -; mRNA.
DR PIR; F84688; F84688.
DR RefSeq; NP_001077972.1; NM_001084503.2.
DR RefSeq; NP_180443.1; NM_128436.5.
DR RefSeq; NP_973555.1; NM_201826.3.
DR AlphaFoldDB; Q9ZV36; -.
DR SMR; Q9ZV36; -.
DR BioGRID; 2776; 1.
DR STRING; 3702.AT2G28760.1; -.
DR MetOSite; Q9ZV36; -.
DR PaxDb; Q9ZV36; -.
DR PRIDE; Q9ZV36; -.
DR ProteomicsDB; 228540; -.
DR EnsemblPlants; AT2G28760.1; AT2G28760.1; AT2G28760.
DR EnsemblPlants; AT2G28760.2; AT2G28760.2; AT2G28760.
DR EnsemblPlants; AT2G28760.3; AT2G28760.3; AT2G28760.
DR GeneID; 817426; -.
DR Gramene; AT2G28760.1; AT2G28760.1; AT2G28760.
DR Gramene; AT2G28760.2; AT2G28760.2; AT2G28760.
DR Gramene; AT2G28760.3; AT2G28760.3; AT2G28760.
DR KEGG; ath:AT2G28760; -.
DR Araport; AT2G28760; -.
DR TAIR; locus:2053275; AT2G28760.
DR eggNOG; KOG1429; Eukaryota.
DR HOGENOM; CLU_007383_4_0_1; -.
DR InParanoid; Q9ZV36; -.
DR PhylomeDB; Q9ZV36; -.
DR BRENDA; 4.1.1.35; 399.
DR UniPathway; UPA00796; UER00771.
DR PRO; PR:Q9ZV36; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZV36; baseline and differential.
DR Genevisible; Q9ZV36; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IDA:TAIR.
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; Cytoplasm; Decarboxylase; Lyase; NAD; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9LZI2"
FT CHAIN 2..343
FT /note="UDP-glucuronic acid decarboxylase 6"
FT /id="PRO_0000421987"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 62..87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 174..178
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 216..220
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233..240
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 300..304
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9LZI2"
SQ SEQUENCE 343 AA; 38621 MW; 0FB7C4CAB5E55711 CRC64;
MASNSSNGTT TTKPPPMPSP LRNSKFFQSN MRILVTGGAG FIGSHLVDKL MQNEKNEVIV
ADNYFTGSKD NLKKWIGHPR FELIRHDVTE PLFVEVDQIY HLACPASPIF YKYNPVKTIK
TNVIGTLNML GLAKRVGARI LLTSTSEVYG DPLVHPQTES YWGNVNPIGV RSCYDEGKRV
AETLMFDYHR QHGIEIRIAR IFNTYGPRMN IDDGRVVSNF IAQALRGEAL TVQKPGTQTR
SFCYVSDMVE GLMRLMEGDQ TGPINIGNPG EFTMVELAET VKELIKPDVE IKMVENTPDD
PRQRKPDISK AKEVLGWEPK VKLREGLPLM EEDFRLRLGV PKK
