UXS2_ARATH
ID UXS2_ARATH Reviewed; 445 AA.
AC Q9LZI2; Q39077;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=UDP-glucuronic acid decarboxylase 2;
DE EC=4.1.1.35 {ECO:0000269|PubMed:15655675};
DE AltName: Full=UDP-XYL synthase 2;
DE AltName: Full=UDP-glucuronate decarboxylase 2;
DE Short=UGD;
DE Short=UXS-2;
DE AltName: Full=dTDP-glucose 4-6-dehydratase homolog D18;
GN Name=UXS2; Synonyms=AUD1, D18; OrderedLocusNames=At3g62830;
GN ORFNames=F26K9_260;
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].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7479844; DOI=10.1073/pnas.92.23.10580;
RA Kushnir S., Babiychuk E., Kampfenkel K., Belles-Boix E., Van Montagu M.,
RA Inze D.;
RT "Characterization of Arabidopsis thaliana cDNAs that render yeasts tolerant
RT toward the thiol-oxidizing drug diamide.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10580-10584(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, FUNCTION, COFACTOR, AND TISSUE
RP 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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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:15655675}.
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:15655675};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23917;
CC Evidence={ECO:0000305|PubMed:15655675};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:12481102, ECO:0000269|PubMed:15655675};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.20 mM for UDP-D-glucuronate {ECO:0000269|PubMed:15655675};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:15655675};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:15655675};
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:0000305|PubMed:15655675}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15655675}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:15655675}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:15655675}.
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; Z49239; CAA89205.1; -; mRNA.
DR EMBL; AF387788; AAK70881.1; -; mRNA.
DR EMBL; AL162651; CAB83133.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80398.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80399.1; -; Genomic_DNA.
DR EMBL; AF361617; AAK32785.1; -; mRNA.
DR EMBL; AY143897; AAN28836.1; -; mRNA.
DR PIR; S58282; S58282.
DR PIR; T48072; T48072.
DR RefSeq; NP_001118893.1; NM_001125421.1.
DR RefSeq; NP_191842.1; NM_116148.3.
DR AlphaFoldDB; Q9LZI2; -.
DR SMR; Q9LZI2; -.
DR BioGRID; 10772; 1.
DR STRING; 3702.AT3G62830.1; -.
DR iPTMnet; Q9LZI2; -.
DR SwissPalm; Q9LZI2; -.
DR PaxDb; Q9LZI2; -.
DR PRIDE; Q9LZI2; -.
DR ProteomicsDB; 228543; -.
DR EnsemblPlants; AT3G62830.1; AT3G62830.1; AT3G62830.
DR EnsemblPlants; AT3G62830.2; AT3G62830.2; AT3G62830.
DR GeneID; 825458; -.
DR Gramene; AT3G62830.1; AT3G62830.1; AT3G62830.
DR Gramene; AT3G62830.2; AT3G62830.2; AT3G62830.
DR KEGG; ath:AT3G62830; -.
DR Araport; AT3G62830; -.
DR TAIR; locus:2081675; AT3G62830.
DR eggNOG; KOG1429; Eukaryota.
DR HOGENOM; CLU_007383_2_1_1; -.
DR InParanoid; Q9LZI2; -.
DR OMA; DHKTNVV; -.
DR OrthoDB; 848823at2759; -.
DR PhylomeDB; Q9LZI2; -.
DR BioCyc; ARA:AT3G62830-MON; -.
DR BioCyc; MetaCyc:AT3G62830-MON; -.
DR BRENDA; 4.1.1.35; 399.
DR UniPathway; UPA00796; UER00771.
DR PRO; PR:Q9LZI2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZI2; baseline and differential.
DR Genevisible; Q9LZI2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IDA:TAIR.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; ISS:TAIR.
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:0019305; P:dTDP-rhamnose biosynthetic process; ISS:TAIR.
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 Acetylation; Decarboxylase; Golgi apparatus; Lyase; Membrane; NAD;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..445
FT /note="UDP-glucuronic acid decarboxylase 2"
FT /id="PRO_0000421983"
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..445
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 261
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 149..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 261..265
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 303..307
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 320..327
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 387..391
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 279
FT /note="A -> S (in Ref. 1; CAA89205, 2; AAK70881 and 3;
FT AAK32785)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 49971 MW; E8F3334C00B6D7B2 CRC64;
MASELINRRH ETDQPTADAY YPKPIKPWFT VTRPMRYMLR EQRLIFVLVG IAIATLVFTI
FPRSTQSTPY SDPFSGYGIR PDESYVPAIQ AQRKPSLEYL NRIGATGGKI PLGLKRKGLR
VVVTGGAGFV GSHLVDRLMA RGDTVIVVDN FFTGRKENVM HHFSNPNFEM IRHDVVEPIL
LEVDQIYHLA CPASPVHYKF NPVKTIKTNV VGTLNMLGLA KRVGARFLLT STSEVYGDPL
QHPQVETYWG NVNPIGVRSC YDEGKRTAET LTMDYHRGAN VEVRIARIFN TYGPRMCIDD
GRVVSNFVAQ ALRKEPLTVY GDGKQTRSFQ FVSDLVEGLM RLMEGEHVGP FNLGNPGEFT
MLELAKVVQE TIDPNANIEF RPNTEDDPHK RKPDITKAKE LLGWEPKVSL RQGLPLMVKD
FRQRVFGDQK EGSSAAATTT KTTSA
