UXS1_ARATH
ID UXS1_ARATH Reviewed; 435 AA.
AC Q8VZC0; Q3EAK3; Q9LFG7;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=UDP-glucuronic acid decarboxylase 1 {ECO:0000303|PubMed:12481102};
DE EC=4.1.1.35 {ECO:0000269|PubMed:12481102};
DE AltName: Full=UDP-XYL synthase 1 {ECO:0000303|PubMed:12481102};
DE AltName: Full=UDP-glucuronate decarboxylase 1 {ECO:0000303|PubMed:12481102};
DE Short=UGD {ECO:0000303|PubMed:12481102};
DE Short=UXS-1 {ECO:0000303|PubMed:12481102};
GN Name=UXS1 {ECO:0000303|PubMed:12481102};
GN OrderedLocusNames=At3g53520 {ECO:0000312|Araport:AT3G53520};
GN ORFNames=F4P12.220 {ECO:0000312|EMBL:CAB67659.1};
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] (ISOFORM 2), GENE FAMILY, FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, COFACTOR, 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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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] (ISOFORM 1).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
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}.
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 Evidence={ECO:0000269|PubMed:12481102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23917;
CC Evidence={ECO:0000269|PubMed:12481102};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={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. {ECO:0000269|PubMed:12481102}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:Q5PQX0}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VZC0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VZC0-2; Sequence=VSP_046296;
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; AF387787; AAK70880.1; -; mRNA.
DR EMBL; AL132966; CAB67659.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79100.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79101.1; -; Genomic_DNA.
DR EMBL; AY065075; AAL38251.1; -; mRNA.
DR EMBL; BT003355; AAO29973.1; -; mRNA.
DR PIR; T45892; T45892.
DR RefSeq; NP_190920.3; NM_115212.3. [Q8VZC0-2]
DR RefSeq; NP_850694.2; NM_180363.3. [Q8VZC0-1]
DR AlphaFoldDB; Q8VZC0; -.
DR SMR; Q8VZC0; -.
DR STRING; 3702.AT3G53520.4; -.
DR iPTMnet; Q8VZC0; -.
DR SwissPalm; Q8VZC0; -.
DR ProteomicsDB; 228542; -. [Q8VZC0-1]
DR EnsemblPlants; AT3G53520.1; AT3G53520.1; AT3G53520. [Q8VZC0-1]
DR EnsemblPlants; AT3G53520.2; AT3G53520.2; AT3G53520. [Q8VZC0-2]
DR GeneID; 824520; -.
DR Gramene; AT3G53520.1; AT3G53520.1; AT3G53520. [Q8VZC0-1]
DR Gramene; AT3G53520.2; AT3G53520.2; AT3G53520. [Q8VZC0-2]
DR KEGG; ath:AT3G53520; -.
DR Araport; AT3G53520; -.
DR eggNOG; KOG1429; Eukaryota.
DR InParanoid; Q8VZC0; -.
DR OMA; LGIRACY; -.
DR PhylomeDB; Q8VZC0; -.
DR BioCyc; MetaCyc:AT3G53520-MON; -.
DR BRENDA; 4.1.1.35; 399.
DR SABIO-RK; Q8VZC0; -.
DR UniPathway; UPA00796; UER00771.
DR PRO; PR:Q8VZC0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VZC0; baseline and differential.
DR Genevisible; Q8VZC0; 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; IDA:UniProtKB.
DR GO; GO:0042732; P:D-xylose metabolic process; IDA:UniProtKB.
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; Decarboxylase; Golgi apparatus; Lyase; Membrane; NAD;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..435
FT /note="UDP-glucuronic acid decarboxylase 1"
FT /id="PRO_0000421982"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..435
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 262
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8NBZ7"
FT BINDING 150..175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8NBZ7"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NBZ7"
FT BINDING 262..266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8NBZ7"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NBZ7"
FT BINDING 303
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8NBZ7"
FT BINDING 304..308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NBZ7"
FT BINDING 321..328
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NBZ7"
FT BINDING 388..392
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NBZ7"
FT VAR_SEQ 337..338
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12481102"
FT /id="VSP_046296"
SQ SEQUENCE 435 AA; 48631 MW; DCCD1F47F9E56042 CRC64;
MKQLHKQMSS KRDEETIPMS QSSPYSPKTL KHPRSLPRSL HYLFREQRLL FILVGILIGS
TFFILQPSLS RLGAAESTSL ITRSVSYAVT DSPPSRSTFN SGGGGGRTGR VPVGIGRKRL
RIVVTGGAGF VGSHLVDKLI GRGDEVIVID NFFTGRKENL VHLFSNPRFE LIRHDVVEPI
LLEVDQIYHL ACPASPVHYK YNPVKTIKTN VMGTLNMLGL AKRVGARFLL TSTSEVYGDP
LEHPQKETYW GNVNPIGERS CYDEGKRTAE TLAMDYHRGA GVEVRIARIF NTYGPRMCLD
DGRVVSNFVA QTIRKHPMTV YGDGKQTRSF QYVSDLVEGL VALMENDHVG PFNLGNPGEF
TMLELAEVVK EVIDPSATIE FKPNTADDPH KRKPDISKAK EQLNWEPKIS LREGLPRMVS
DFRNRILNED EGKGL
