UGE5_ARATH
ID UGE5_ARATH Reviewed; 351 AA.
AC Q9SN58; O81619; Q8LEA9; Q8VZ26;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=UDP-glucose 4-epimerase 5 {ECO:0000303|PubMed:11554483};
DE Short=AtUGE5 {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 5 {ECO:0000303|PubMed:12419184};
GN Name=UGE5 {ECO:0000303|PubMed:11554483};
GN OrderedLocusNames=At4g10960 {ECO:0000312|Araport:AT4G10960};
GN ORFNames=F25I24.170 {ECO:0000312|EMBL:CAB40064.1},
GN F8M12.10 {ECO:0000312|EMBL:AAC33955.1};
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=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].
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 [5]
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 [6]
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 [7]
RP FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, 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 [8]
RP 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 [9]
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. {ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426}.
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. Inhibited by UDP.
CC {ECO:0000269|PubMed:16644739}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for UDP-glucose {ECO:0000269|PubMed:16644739};
CC KM=0.17 mM for UDP-galactose {ECO:0000269|PubMed:16644739};
CC KM=0.15 mM for UDP-galactose {ECO:0000269|PubMed:19754426};
CC KM=0.16 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 35 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 -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12419184,
CC ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:17496119}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growht
CC conditions. {ECO:0000269|PubMed:17496119}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC33955.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM62752.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF080118; AAC33955.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL049525; CAB40064.1; -; Genomic_DNA.
DR EMBL; AL161518; CAB81197.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82951.1; -; Genomic_DNA.
DR EMBL; AY065354; AAL38795.1; -; mRNA.
DR EMBL; AY117180; AAM51255.1; -; mRNA.
DR EMBL; AY140073; AAM98214.1; -; mRNA.
DR EMBL; AY085528; AAM62752.1; ALT_INIT; mRNA.
DR PIR; T01881; T01881.
DR PIR; T04291; T04291.
DR RefSeq; NP_192834.1; NM_117166.3.
DR AlphaFoldDB; Q9SN58; -.
DR SMR; Q9SN58; -.
DR BioGRID; 11995; 1.
DR IntAct; Q9SN58; 1.
DR STRING; 3702.AT4G10960.1; -.
DR iPTMnet; Q9SN58; -.
DR PaxDb; Q9SN58; -.
DR PRIDE; Q9SN58; -.
DR ProteomicsDB; 245262; -.
DR EnsemblPlants; AT4G10960.1; AT4G10960.1; AT4G10960.
DR GeneID; 826696; -.
DR Gramene; AT4G10960.1; AT4G10960.1; AT4G10960.
DR KEGG; ath:AT4G10960; -.
DR Araport; AT4G10960; -.
DR TAIR; locus:2123466; AT4G10960.
DR eggNOG; KOG1371; Eukaryota.
DR HOGENOM; CLU_007383_1_10_1; -.
DR InParanoid; Q9SN58; -.
DR OMA; ITEDTPC; -.
DR OrthoDB; 662484at2759; -.
DR PhylomeDB; Q9SN58; -.
DR BRENDA; 5.1.3.2; 399.
DR BRENDA; 5.1.3.5; 399.
DR SABIO-RK; Q9SN58; -.
DR UniPathway; UPA00214; -.
DR PRO; PR:Q9SN58; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SN58; baseline and differential.
DR Genevisible; Q9SN58; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IDA:TAIR.
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; Galactose metabolism; Isomerase; NAD;
KW Reference proteome.
FT CHAIN 1..351
FT /note="UDP-glucose 4-epimerase 5"
FT /id="PRO_0000183194"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 13..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 34..38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 64..65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 130..132
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 182..184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 203..205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 221..223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 298..301
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT CONFLICT 344..345
FT /note="Missing (in Ref. 4; AAM62752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 38618 MW; 0AF46F64FDC0814A CRC64;
MMARNVLVSG GAGYIGSHTV LQLLLGGYSV VVVDNLDNSS AVSLQRVKKL AAEHGERLSF
HQVDLRDRSA LEKIFSETKF DAVIHFAGLK AVGESVEKPL LYYNNNLVGT ITLLEVMAQH
GCKNLVFSSS ATVYGSPKEV PCTEEFPISA LNPYGRTKLF IEEICRDVYG SDPEWKIILL
RYFNPVGAHP SGDIGEDPRG IPNNLMPFVQ QVAVGRRPHL TVFGNDYNTK DGTGVRDYIH
VIDLADGHIA ALRKLEDCKI GCEVYNLGTG NGTSVLEMVD AFEKASGKKI PLVIAGRRPG
DAEVVYASTE RAESELNWKA KYGIEEMCRD LWNWASNNPY GYDSSSEDNS H
