UGE2_ARATH
ID UGE2_ARATH Reviewed; 350 AA.
AC Q9T0A7; Q541V9; Q8LFW1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=UDP-glucose 4-epimerase 2 {ECO:0000303|PubMed:11554483};
DE Short=AtUGE2 {ECO:0000303|PubMed:11554483};
DE EC=5.1.3.2 {ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
DE AltName: Full=UDP-galactose 4-epimerase 2 {ECO:0000303|PubMed:12419184};
GN Name=UGE2 {ECO:0000303|PubMed:11554483};
GN OrderedLocusNames=At4g23920 {ECO:0000312|Araport:AT4G23920};
GN ORFNames=T32A16.90 {ECO:0000312|EMBL:CAB43892.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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=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;
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 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 TISSUE SPECIFICITY, AND 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 FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [10]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, 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 (Ref.6, PubMed:16644739, PubMed:19754426). Cooperates with
CC UGE3 in pollen development and with UGE4 in cell wall carbohydrate
CC biosynthesis and growth (PubMed:17496119).
CC {ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:17496119,
CC ECO:0000269|PubMed:19754426, ECO:0000269|Ref.6}.
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:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:19754426};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
CC -!- ACTIVITY REGULATION: Enhanced activity by NaCl. Enhanced activity by
CC NAD(+). Strongly inhibited by UDP. {ECO:0000269|PubMed:16644739}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.09 mM for UDP-glucose {ECO:0000269|PubMed:16644739};
CC KM=0.1 mM for UDP-galactose {ECO:0000269|PubMed:16644739};
CC KM=0.095 mM for UDP-galactose {ECO:0000269|PubMed:19754426};
CC KM=0.34 mM for UDP-xylose {ECO:0000269|PubMed:19754426};
CC pH dependence:
CC Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:16644739};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:16644739};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism. {ECO:0000305}.
CC -!- SUBUNIT: Forms homodimers and heterodimers.
CC {ECO:0000269|PubMed:16644739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16644739}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:12419184, PubMed:16644739,
CC PubMed:17496119, Ref.6). Most highly expressed in stems and flowers
CC (PubMed:17496119). {ECO:0000269|PubMed:12419184,
CC ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:17496119,
CC ECO:0000269|Ref.6}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. Uge2 and uge3 double mutant is almost completely sterile.
CC Uge2 and uge4 double mutant displays a reduction in rosette and root
CC growth, hypocotyl elongation, and secondary hypocotyl thickening.
CC {ECO:0000269|PubMed:17496119}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AL078468; CAB43892.1; -; Genomic_DNA.
DR EMBL; AL161560; CAB81310.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84827.1; -; Genomic_DNA.
DR EMBL; AK118722; BAC43316.1; -; mRNA.
DR EMBL; BT008539; AAP40366.1; -; mRNA.
DR EMBL; AY084615; AAM61178.1; -; mRNA.
DR PIR; T08911; T08911.
DR RefSeq; NP_194123.1; NM_118524.3.
DR AlphaFoldDB; Q9T0A7; -.
DR SMR; Q9T0A7; -.
DR BioGRID; 13781; 3.
DR IntAct; Q9T0A7; 2.
DR STRING; 3702.AT4G23920.1; -.
DR PaxDb; Q9T0A7; -.
DR PRIDE; Q9T0A7; -.
DR ProteomicsDB; 245259; -.
DR EnsemblPlants; AT4G23920.1; AT4G23920.1; AT4G23920.
DR GeneID; 828492; -.
DR Gramene; AT4G23920.1; AT4G23920.1; AT4G23920.
DR KEGG; ath:AT4G23920; -.
DR Araport; AT4G23920; -.
DR TAIR; locus:2138121; AT4G23920.
DR eggNOG; KOG1371; Eukaryota.
DR HOGENOM; CLU_007383_1_10_1; -.
DR InParanoid; Q9T0A7; -.
DR OMA; GEHLICN; -.
DR OrthoDB; 662484at2759; -.
DR PhylomeDB; Q9T0A7; -.
DR BRENDA; 5.1.3.2; 399.
DR BRENDA; 5.1.3.5; 399.
DR SABIO-RK; Q9T0A7; -.
DR UniPathway; UPA00214; -.
DR PRO; PR:Q9T0A7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T0A7; baseline and differential.
DR Genevisible; Q9T0A7; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IDA:TAIR.
DR GO; GO:0042546; P:cell wall biogenesis; IMP:TAIR.
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:0006364; P:rRNA processing; IBA:GO_Central.
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; Cytoplasm;
KW Galactose metabolism; Isomerase; NAD; Reference proteome.
FT CHAIN 1..350
FT /note="UDP-glucose 4-epimerase 2"
FT /id="PRO_0000183195"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 12..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 33..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 63..64
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 129..131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 181..183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 202..204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 220..222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 297..300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT CONFLICT 54
FT /note="G -> R (in Ref. 5; AAM61178)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="V -> I (in Ref. 5; AAM61178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 38382 MW; 79BC9886F3126D5C CRC64;
MAKSVLVTGG AGYIGSHTVL QLLEGGYSAV VVDNYDNSSA ASLQRVKKLA GENGNRLSFH
QVDLRDRPAL EKIFSETKFD AVIHFAGLKA VGESVEKPLL YYNNNIVGTV TLLEVMAQYG
CKNLVFSSSA TVYGWPKEVP CTEESPISAT NPYGRTKLFI EEICRDVHRS DSEWKIILLR
YFNPVGAHPS GYIGEDPLGV PNNLMPYVQQ VAVGRRPHLT VFGTDYKTKD GTGVRDYIHV
MDLADGHIAA LRKLDDLKIS CEVYNLGTGN GTSVLEMVAA FEKASGKKIP LVMAGRRPGD
AEVVYASTEK AERELNWKAK NGIEEMCRDL WNWASNNPYG YNSSSNGSSS
