UGE3_ARATH
ID UGE3_ARATH Reviewed; 351 AA.
AC Q8LDN8; Q9CAM5;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 3;
DE EC=5.1.3.2 {ECO:0000305|PubMed:16644739, ECO:0000305|PubMed:17496119, ECO:0000305|PubMed:19754426};
DE EC=5.1.3.5 {ECO:0000269|PubMed:19754426};
DE AltName: Full=UDP-D-xylose 4-epimerase;
DE AltName: Full=UDP-L-arabinose 4-epimerase;
DE AltName: Full=UDP-galactose 4-epimerase 3;
DE AltName: Full=UDP-glucose 4-epimerase 3;
DE Short=AtUGE3 {ECO:0000303|PubMed:19754426};
GN Name=UGE3; OrderedLocusNames=At1g63180; ORFNames=F16M19.8;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION.
RA Verma R., Burget E.G., Reiter W.-D.;
RT "Genetic and biochemical characterization of UDP sugar 4-epimerases in
RT Arabidopsis thaliana.";
RL (In) Proceedings of the 12th international conference on Arabidopsis
RL research, abstract#156, Madison (2001).
RN [7]
RP GENE FAMILY.
RX PubMed=11554483; DOI=10.1023/a:1010671129803;
RA Reiter W.-D., Vanzin G.F.;
RT "Molecular genetics of nucleotide sugar interconversion pathways in
RT plants.";
RL Plant Mol. Biol. 47:95-113(2001).
RN [8]
RP GENE FAMILY, AND TISSUE SPECIFICITY.
RX PubMed=12419184; DOI=10.1016/s0960-9822(02)01260-5;
RA Seifert G.J., Barber C., Wells B., Dolan L., Roberts K.;
RT "Galactose biosynthesis in Arabidopsis: genetic evidence for substrate
RT channeling from UDP-D-galactose into cell wall polymers.";
RL Curr. Biol. 12:1840-1845(2002).
RN [9]
RP INDUCTION.
RX PubMed=14973160; DOI=10.1105/tpc.019661;
RA Seifert G.J., Barber C., Wells B., Roberts K.;
RT "Growth regulators and the control of nucleotide sugar flux.";
RL Plant Cell 16:723-730(2004).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=16644739; DOI=10.1074/jbc.m512727200;
RA Barber C., Roesti J., Rawat A., Findlay K., Roberts K., Seifert G.J.;
RT "Distinct properties of the five UDP-D-glucose/UDP-D-galactose 4-epimerase
RT isoforms of Arabidopsis thaliana.";
RL J. Biol. Chem. 281:17276-17285(2006).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17496119; DOI=10.1105/tpc.106.049619;
RA Roesti J., Barton C.J., Albrecht S., Dupree P., Pauly M., Findlay K.,
RA Roberts K., Seifert G.J.;
RT "UDP-glucose 4-epimerase isoforms UGE2 and UGE4 cooperate in providing UDP-
RT galactose for cell wall biosynthesis and growth of Arabidopsis thaliana.";
RL Plant Cell 19:1565-1579(2007).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19754426; DOI=10.1042/bj20091025;
RA Kotake T., Takata R., Verma R., Takaba M., Yamaguchi D., Orita T.,
RA Kaneko S., Matsuoka K., Koyama T., Reiter W.D., Tsumuraya Y.;
RT "Bifunctional cytosolic UDP-glucose 4-epimerases catalyse the
RT interconversion between UDP-D-xylose and UDP-L-arabinose in plants.";
RL Biochem. J. 424:169-177(2009).
CC -!- FUNCTION: Catalyzes the interconversion between UDP-glucose and UDP-
CC galactose and the interconversion between UDP-arabinose and UDP-xylose.
CC Cooperates with UGE2 in pollen development. May preferentially act in
CC the UDP-galactose to UDP-glucose direction, therefore displaying a role
CC in carbohydrate catabolism (Probable). {ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:17496119, ECO:0000269|PubMed:19754426,
CC ECO:0000269|Ref.6, ECO:0000305|PubMed:16644739}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose;
CC Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914;
CC EC=5.1.3.2; Evidence={ECO:0000305|PubMed:16644739,
CC ECO:0000305|PubMed:17496119, ECO:0000305|PubMed:19754426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-beta-L-arabinopyranose = UDP-alpha-D-xylose;
CC Xref=Rhea:RHEA:11320, ChEBI:CHEBI:57632, ChEBI:CHEBI:61457;
CC EC=5.1.3.5; Evidence={ECO:0000269|PubMed:19754426};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Strongly inhibited by UDP.
CC {ECO:0000269|PubMed:16644739}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.19 mM for UDP-glucose {ECO:0000269|PubMed:16644739};
CC KM=0.19 mM for UDP-galactose {ECO:0000269|PubMed:16644739};
CC KM=0.22 mM for UDP-galactose {ECO:0000269|PubMed:16644739};
CC KM=0.068 mM for UDP-galactose {ECO:0000269|PubMed:19754426};
CC KM=0.32 mM for UDP-xylose {ECO:0000269|PubMed:19754426};
CC Note=kcat is 19 sec(-1) with UDP-glucose as substrate
CC (PubMed:16644739). kcat is 42 sec(-1) with UDP-galactose as substrate
CC (PubMed:16644739). kcat is 57 sec(-1) with UDP-galactose as substrate
CC (PubMed:16644739). kcat is 66 sec(-1) with UDP-galactose as substrate
CC (PubMed:16644739). kcat is 27 sec(-1) with UDP-galactose as substrate
CC (PubMed:19754426). kcat is 13 sec(-1) with UDP-xylose as substrate
CC (PubMed:19754426). {ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:19754426};
CC pH dependence:
CC Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:19754426};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-L-arabinose biosynthesis;
CC UDP-L-arabinose from UDP-alpha-D-xylose: step 1/1.
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBUNIT: homodimer. Heterodimer. {ECO:0000269|PubMed:16644739}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12419184,
CC ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:17496119}.
CC -!- INDUCTION: Down-regulated by ethylene. {ECO:0000269|PubMed:14973160}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Uge2 and uge3 double mutant
CC is almost completely sterile (PubMed:17496119).
CC {ECO:0000269|PubMed:17496119}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51599.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010795; AAG51599.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34065.1; -; Genomic_DNA.
DR EMBL; AK117913; BAC42551.1; -; mRNA.
DR EMBL; BT024882; ABD85153.1; -; mRNA.
DR EMBL; AY085887; AAM63099.1; -; mRNA.
DR PIR; D96657; D96657.
DR RefSeq; NP_564811.1; NM_104996.6.
DR AlphaFoldDB; Q8LDN8; -.
DR SMR; Q8LDN8; -.
DR STRING; 3702.AT1G63180.1; -.
DR PaxDb; Q8LDN8; -.
DR PRIDE; Q8LDN8; -.
DR ProteomicsDB; 245260; -.
DR EnsemblPlants; AT1G63180.1; AT1G63180.1; AT1G63180.
DR GeneID; 842622; -.
DR Gramene; AT1G63180.1; AT1G63180.1; AT1G63180.
DR KEGG; ath:AT1G63180; -.
DR Araport; AT1G63180; -.
DR TAIR; locus:2015253; AT1G63180.
DR eggNOG; KOG1371; Eukaryota.
DR HOGENOM; CLU_007383_1_10_1; -.
DR InParanoid; Q8LDN8; -.
DR OMA; DTPDIGC; -.
DR OrthoDB; 662484at2759; -.
DR PhylomeDB; Q8LDN8; -.
DR BRENDA; 5.1.3.2; 399.
DR BRENDA; 5.1.3.5; 399.
DR SABIO-RK; Q8LDN8; -.
DR UniPathway; UPA00214; -.
DR UniPathway; UPA00797; UER00772.
DR UniPathway; UPA00963; -.
DR PRO; PR:Q8LDN8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LDN8; baseline and differential.
DR Genevisible; Q8LDN8; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IPI:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0050373; F:UDP-arabinose 4-epimerase activity; IDA:UniProtKB.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IDA:TAIR.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR GO; GO:0033358; P:UDP-L-arabinose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005886; UDP_G4E.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01179; galE; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Galactose metabolism; Isomerase; NAD; Reference proteome.
FT CHAIN 1..351
FT /note="Bifunctional UDP-glucose 4-epimerase and UDP-xylose
FT 4-epimerase 3"
FT /id="PRO_0000422185"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 8..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 351 AA; 38910 MW; 314BC1FA8DD091EF CRC64;
MGSSVEQNIL VTGGAGFIGT HTVVQLLNQG FKVTIIDNLD NSVVEAVHRV RELVGPDLST
KLEFNLGDLR NKGDIEKLFS NQRFDAVIHF AGLKAVGESV GNPRRYFDNN LVGTINLYET
MAKYNCKMMV FSSSATVYGQ PEIVPCVEDF ELQAMNPYGR TKLFLEEIAR DIHAAEPEWK
IILLRYFNPV GAHESGRIGE DPKGIPNNLM PYIQQVAVGR LPELNVFGHD YPTMDGSAVR
DYIHVMDLAD GHVAALNKLF SDSKIGCTAY NLGTGQGTSV LEMVSSFEKA SGKKIPIKLC
PRRAGDATAV YASTQKAEKE LGWKAKYGVD EMCRDQWNWA NKNPWGFQKK P
