UGE1_ARATH
ID UGE1_ARATH Reviewed; 351 AA.
AC Q42605; B9DI57; Q9LPX1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 1;
DE EC=5.1.3.2 {ECO:0000305|PubMed:16644739, ECO:0000305|PubMed:17496119, ECO:0000305|PubMed:19754426, ECO:0000305|PubMed:8615692};
DE EC=5.1.3.5 {ECO:0000305|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 1;
DE AltName: Full=UDP-glucose 4-epimerase 1;
DE Short=AtUGE1;
GN Name=UGE1; OrderedLocusNames=At1g12780; ORFNames=F13K23.3;
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8615692; DOI=10.1006/abbi.1996.0088;
RA Doermann P., Benning C.;
RT "Functional expression of uridine 5'-diphospho-glucose 4-epimerase (EC
RT 5.1.3.2) from Arabidopsis thaliana in Saccharomyces cerevisiae and
RT Escherichia coli.";
RL Arch. Biochem. Biophys. 327:27-34(1996).
RN [2]
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 [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].
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] OF 136-351.
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
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 INDUCTION, AND FUNCTION.
RX PubMed=9681006; DOI=10.1046/j.1365-313x.1998.00067.x;
RA Doermann P., Benning C.;
RT "The role of UDP-glucose epimerase in carbohydrate metabolism of
RT Arabidopsis.";
RL Plant J. 13:641-652(1998).
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, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
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 [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 (PubMed:8615692, PubMed:17496119). Plays a role in D-galactose
CC detoxification. {ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:17496119, ECO:0000269|PubMed:19754426,
CC ECO:0000269|PubMed:8615692, ECO:0000269|PubMed:9681006}.
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 ECO:0000305|PubMed:8615692};
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:0000305|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=0.11 mM for UDP-glucose {ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:19754426, ECO:0000269|PubMed:8615692};
CC KM=0.76 mM for UDP-glucose {ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:19754426, ECO:0000269|PubMed:8615692};
CC KM=0.19 mM for UDP-galactose {ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:19754426, ECO:0000269|PubMed:8615692};
CC KM=0.087 mM for UDP-galactose {ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:19754426, ECO:0000269|PubMed:8615692};
CC KM=0.43 mM for UDP-xylose {ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:19754426, ECO:0000269|PubMed:8615692};
CC Vmax=3.96 mmol/min/mg enzyme {ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:19754426, ECO:0000269|PubMed:8615692};
CC pH dependence:
CC Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:19754426, ECO:0000269|PubMed:8615692};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426,
CC ECO:0000269|PubMed:8615692};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16644739}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression in stems
CC and roots. {ECO:0000269|PubMed:12419184, ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:17496119, ECO:0000269|PubMed:8615692}.
CC -!- INDUCTION: Not induced by galactose. Down-regulated by ethylene.
CC {ECO:0000269|PubMed:14973160, ECO:0000269|PubMed:9681006}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17496119}.
CC -!- MISCELLANEOUS: Does not seem to need NAD for activity.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; Z54214; CAA90941.1; -; mRNA.
DR EMBL; AC012187; AAF78483.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28928.1; -; Genomic_DNA.
DR EMBL; AF334724; AAG50102.1; -; mRNA.
DR EMBL; AY054207; AAL06868.1; -; mRNA.
DR EMBL; AY120709; AAM53267.1; -; mRNA.
DR EMBL; BT000032; AAN15351.1; -; mRNA.
DR EMBL; AK317768; BAH20424.1; -; mRNA.
DR PIR; B86261; B86261.
DR PIR; S62783; S62783.
DR RefSeq; NP_172738.1; NM_101148.4.
DR AlphaFoldDB; Q42605; -.
DR SMR; Q42605; -.
DR BioGRID; 23074; 2.
DR IntAct; Q42605; 1.
DR STRING; 3702.AT1G12780.1; -.
DR iPTMnet; Q42605; -.
DR PaxDb; Q42605; -.
DR PRIDE; Q42605; -.
DR ProteomicsDB; 245258; -.
DR EnsemblPlants; AT1G12780.1; AT1G12780.1; AT1G12780.
DR GeneID; 837834; -.
DR Gramene; AT1G12780.1; AT1G12780.1; AT1G12780.
DR KEGG; ath:AT1G12780; -.
DR Araport; AT1G12780; -.
DR TAIR; locus:2010371; AT1G12780.
DR eggNOG; KOG1371; Eukaryota.
DR HOGENOM; CLU_007383_1_10_1; -.
DR InParanoid; Q42605; -.
DR OMA; KVMTGQY; -.
DR OrthoDB; 662484at2759; -.
DR PhylomeDB; Q42605; -.
DR BioCyc; ARA:AT1G12780-MON; -.
DR BioCyc; MetaCyc:AT1G12780-MON; -.
DR BRENDA; 5.1.3.2; 399.
DR BRENDA; 5.1.3.5; 399.
DR SABIO-RK; Q42605; -.
DR UniPathway; UPA00214; -.
DR UniPathway; UPA00797; UER00772.
DR UniPathway; UPA00963; -.
DR PRO; PR:Q42605; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42605; baseline and differential.
DR Genevisible; Q42605; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA: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: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; Cytoplasm;
KW Galactose metabolism; Isomerase; NAD; Reference proteome.
FT CHAIN 1..351
FT /note="Bifunctional UDP-glucose 4-epimerase and UDP-xylose
FT 4-epimerase 1"
FT /id="PRO_0000183193"
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"
FT CONFLICT 102..103
FT /note="NP -> KG (in Ref. 1; CAA90941)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="N -> F (in Ref. 1; CAA90941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 39158 MW; FDE640FB26A1DD1D CRC64;
MGSSVEQNIL VTGGAGFIGT HTVVQLLKDG FKVSIIDNFD NSVIEAVDRV RELVGPDLSK
KLDFNLGDLR NKGDIEKLFS KQRFDAVIHF AGLKAVGESV ENPRRYFDNN LVGTINLYET
MAKYNCKMMV FSSSATVYGQ PEKIPCMEDF ELKAMNPYGR TKLFLEEIAR DIQKAEPEWR
IILLRYFNPV GAHESGSIGE DPKGIPNNLM PYIQQVAVGR LPELNVYGHD YPTEDGSAVR
DYIHVMDLAD GHIAALRKLF ADPKIGCTAY NLGTGQGTSV LEMVAAFEKA SGKKIPIKLC
PRRSGDATAV YASTEKAEKE LGWKAKYGVD EMCRDQWKWA NNNPWGYQNK L
