UXS5_ARATH
ID UXS5_ARATH Reviewed; 341 AA.
AC Q9SN95;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=UDP-glucuronic acid decarboxylase 5;
DE EC=4.1.1.35;
DE AltName: Full=UDP-XYL synthase 5;
DE AltName: Full=UDP-glucuronate decarboxylase 5;
DE Short=UGD;
DE Short=UXS-5;
GN Name=UXS5; OrderedLocusNames=At3g46440; ORFNames=F18L15.160;
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=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 [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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
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 [6]
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 [7]
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; AL133298; CAB62035.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78158.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78159.1; -; Genomic_DNA.
DR EMBL; AY072098; AAL59920.1; -; mRNA.
DR EMBL; AY096586; AAM20236.1; -; mRNA.
DR EMBL; AK228600; BAF00515.1; -; mRNA.
DR EMBL; AK317497; BAH20162.1; -; mRNA.
DR EMBL; AY087118; AAM64676.1; -; mRNA.
DR PIR; T45701; T45701.
DR RefSeq; NP_001030820.1; NM_001035743.2.
DR RefSeq; NP_190228.1; NM_114511.4.
DR AlphaFoldDB; Q9SN95; -.
DR SMR; Q9SN95; -.
DR BioGRID; 9114; 2.
DR STRING; 3702.AT3G46440.2; -.
DR iPTMnet; Q9SN95; -.
DR PaxDb; Q9SN95; -.
DR PRIDE; Q9SN95; -.
DR ProteomicsDB; 243244; -.
DR EnsemblPlants; AT3G46440.1; AT3G46440.1; AT3G46440.
DR EnsemblPlants; AT3G46440.2; AT3G46440.2; AT3G46440.
DR GeneID; 823794; -.
DR Gramene; AT3G46440.1; AT3G46440.1; AT3G46440.
DR Gramene; AT3G46440.2; AT3G46440.2; AT3G46440.
DR KEGG; ath:AT3G46440; -.
DR Araport; AT3G46440; -.
DR TAIR; locus:2078206; AT3G46440.
DR eggNOG; KOG1429; Eukaryota.
DR HOGENOM; CLU_007383_4_0_1; -.
DR InParanoid; Q9SN95; -.
DR OMA; IGIFERQ; -.
DR OrthoDB; 848823at2759; -.
DR PhylomeDB; Q9SN95; -.
DR BioCyc; ARA:AT3G46440-MON; -.
DR BRENDA; 4.1.1.35; 399.
DR UniPathway; UPA00796; UER00771.
DR PRO; PR:Q9SN95; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SN95; baseline and differential.
DR Genevisible; Q9SN95; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; 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 GO; GO:0045492; P:xylan biosynthetic process; IGI:TAIR.
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 Cytoplasm; Decarboxylase; Lyase; NAD; Reference proteome.
FT CHAIN 1..341
FT /note="UDP-glucuronic acid decarboxylase 5"
FT /id="PRO_0000421986"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 60..85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172..176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 214..218
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 231..238
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 298..302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 341 AA; 38389 MW; B9D621A514B36B04 CRC64;
MASSDKQTSP KPPPSPSPLR NSKFCQSNMR ILISGGAGFI GSHLVDKLME NEKNEVIVAD
NYFTGSKDNL KKWIGHPRFE LIRHDVTEPL LIEVDQIYHL ACPASPIFYK YNPVKTIKTN
VIGTLNMLGL AKRVGARILL TSTSEVYGDP LIHPQPESYW GNVNPIGVRS CYDEGKRVAE
TLMFDYHRQH GIEIRIARIF NTYGPRMNID DGRVVSNFIA QALRGEALTV QKPGTQTRSF
CYVSDMVDGL MRLMEGDDTG PINIGNPGEF TMVELAETVK ELINPSIEIK MVENTPDDPR
QRKPDITKAK EVLGWEPKVK LREGLPLMEE DFRLRLGVHK N
