UGE4_ARATH
ID UGE4_ARATH Reviewed; 348 AA.
AC Q9C7W7; Q9SGX0;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=UDP-glucose 4-epimerase 4 {ECO:0000303|PubMed:12419184};
DE Short=AtUGE4 {ECO:0000303|PubMed:12419184};
DE EC=5.1.3.2 {ECO:0000269|PubMed:12419184, ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
DE AltName: Full=Protein ROOT EPIDERMAL BULGER 1 {ECO:0000303|PubMed:12355155, ECO:0000303|PubMed:9431677, ECO:0000303|Ref.4};
DE AltName: Full=Protein ROOT HAIR DEFECTIVE 1 {ECO:0000303|PubMed:12419184};
DE AltName: Full=UDP-galactose 4-epimerase 4 {ECO:0000303|PubMed:12419184};
GN Name=UGE4 {ECO:0000303|PubMed:12419184};
GN Synonyms=REB1 {ECO:0000303|PubMed:12355155, ECO:0000303|PubMed:9431677,
GN ECO:0000303|Ref.4}, RHD1 {ECO:0000303|PubMed:12419184};
GN OrderedLocusNames=At1g64440 {ECO:0000312|Araport:AT1G64440};
GN ORFNames=F15H21.11 {ECO:0000312|EMBL:AAG51709.1},
GN F1N19.2 {ECO:0000312|EMBL:AAF19668.1};
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=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;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DISRUPTION PHENOTYPE.
RX DOI=10.1071/PP9920427;
RA Baskin T.I., Betzner A.S., Hoggart R., Cork A., Williamson R.E.;
RT "Root morphology mutants in Arabidopsis thaliana.";
RL Aust. J. Plant Physiol. 19:427-437(1992).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=9431677; DOI=10.1007/s004250050194;
RA Ding L., Zhu J.-K.;
RT "A role for arabinogalactan-proteins in root epidermal cell expansion.";
RL Planta 203:289-294(1997).
RN [6]
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 [7]
RP GENE FAMILY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC
RP ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND FUNCTION.
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 [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=12355155; DOI=10.1007/s00425-002-0836-z;
RA Andeme-Onzighi C., Sivaguru M., Judy-March J., Baskin T.I., Driouich A.;
RT "The reb1-1 mutation of Arabidopsis alters the morphology of trichoblasts,
RT the expression of arabinogalactan-proteins and the organization of cortical
RT microtubules.";
RL Planta 215:949-958(2002).
RN [9]
RP FUNCTION.
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 SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, CATALYTIC
RP ACTIVITY, PATHWAY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
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.
RX PubMed=16500990; DOI=10.1104/pp.105.074997;
RA Nguema-Ona E., Andeme-Onzighi C., Aboughe-Angone S., Bardor M., Ishii T.,
RA Lerouge P., Driouich A.;
RT "The reb1-1 mutation of Arabidopsis. Effect on the structure and
RT localization of galactose-containing cell wall polysaccharides.";
RL Plant Physiol. 140:1406-1417(2006).
RN [12]
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 [13]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND PATHWAY.
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. Involved in channeling UDP-D-galactose (UDP-D-Gal) into cell
CC wall polymers. Required for the galactosylation of xyloglucan (XyG) and
CC type II arabinogalactan (AGII). Cooperates with UGE2 in cell wall
CC carbohydrate biosynthesis and growth. {ECO:0000269|PubMed:12419184,
CC ECO:0000269|PubMed:14973160, ECO:0000269|PubMed:16500990,
CC ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:17496119,
CC 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:12419184,
CC ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:Q14376};
CC -!- ACTIVITY REGULATION: Inhibited by NaCl. Enhanced activity by NAD(+).
CC Slightly inhibited by UDP. {ECO:0000269|PubMed:16644739}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.56 mM for UDP-glucose {ECO:0000269|PubMed:12419184,
CC ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
CC KM=0.23 mM for UDP-galactose {ECO:0000269|PubMed:12419184,
CC ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
CC KM=0.057 mM for UDP-galactose {ECO:0000269|PubMed:12419184,
CC ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
CC KM=0.42 mM for UDP-xylose {ECO:0000269|PubMed:12419184,
CC ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
CC Vmax=7.41 mmol/min/mg enzyme toward UDP-D-glucose
CC {ECO:0000269|PubMed:12419184, ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:19754426};
CC pH dependence:
CC Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:12419184,
CC ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:12419184, ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:19754426};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000269|PubMed:12419184, ECO:0000269|PubMed:16644739,
CC ECO:0000269|PubMed:19754426}.
CC -!- SUBUNIT: Homodimer. Heterodimer. {ECO:0000269|PubMed:16644739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16644739}. Golgi
CC apparatus, Golgi stack {ECO:0000269|PubMed:16644739}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12419184,
CC ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:17496119}.
CC -!- DISRUPTION PHENOTYPE: Root epidermal bulging. Partially deficient in
CC cell wall arabinogalactan-protein (AGP). Abnormal trichoblast cell
CC wall. Uge2 and uge4 double mutant displays a reduction in rosette and
CC root growth, hypocotyl elongation, and secondary hypocotyl thickening
CC (PubMed:17496119). {ECO:0000269|PubMed:12355155,
CC ECO:0000269|PubMed:12419184, ECO:0000269|PubMed:17496119,
CC ECO:0000269|PubMed:9431677, ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19668.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009519; AAF19668.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC066689; AAG51709.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34241.1; -; Genomic_DNA.
DR EMBL; BT011226; AAR92262.1; -; mRNA.
DR EMBL; BT012154; AAS76249.1; -; mRNA.
DR RefSeq; NP_176625.1; NM_105119.5.
DR AlphaFoldDB; Q9C7W7; -.
DR SMR; Q9C7W7; -.
DR STRING; 3702.AT1G64440.1; -.
DR PaxDb; Q9C7W7; -.
DR PRIDE; Q9C7W7; -.
DR ProteomicsDB; 245261; -.
DR EnsemblPlants; AT1G64440.1; AT1G64440.1; AT1G64440.
DR GeneID; 842752; -.
DR Gramene; AT1G64440.1; AT1G64440.1; AT1G64440.
DR KEGG; ath:AT1G64440; -.
DR Araport; AT1G64440; -.
DR TAIR; locus:2014235; AT1G64440.
DR eggNOG; KOG1371; Eukaryota.
DR HOGENOM; CLU_007383_1_10_1; -.
DR InParanoid; Q9C7W7; -.
DR OMA; WASNNPF; -.
DR OrthoDB; 662484at2759; -.
DR PhylomeDB; Q9C7W7; -.
DR BRENDA; 5.1.3.2; 399.
DR BRENDA; 5.1.3.5; 399.
DR SABIO-RK; Q9C7W7; -.
DR UniPathway; UPA00214; -.
DR PRO; PR:Q9C7W7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7W7; baseline and differential.
DR Genevisible; Q9C7W7; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005795; C:Golgi stack; IDA:TAIR.
DR GO; GO:0046983; F:protein dimerization activity; IPI:TAIR.
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: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:0009832; P:plant-type cell wall biogenesis; TAS:TAIR.
DR GO; GO:0010053; P:root epidermal cell differentiation; IMP:TAIR.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR GO; GO:0009969; P:xyloglucan biosynthetic process; IMP:TAIR.
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; Golgi apparatus; Isomerase; NAD; Reference proteome.
FT CHAIN 1..348
FT /note="UDP-glucose 4-epimerase 4"
FT /id="PRO_0000422186"
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"
SQ SEQUENCE 348 AA; 38123 MW; A98B6D334B6B779D CRC64;
MVGNILVTGG AGYIGSHTVL QLLLGGYNTV VIDNLDNSSL VSIQRVKDLA GDHGQNLTVH
QVDLRDKPAL EKVFSETKFD AVMHFAGLKA VGESVAKPLL YYNNNLIATI TLLEVMAAHG
CKKLVFSSSA TVYGWPKEVP CTEESPLSGM SPYGRTKLFI EDICRDVQRG DPEWRIIMLR
YFNPVGAHPS GRIGEDPCGT PNNLMPYVQQ VVVGRLPNLK IYGTDYTTKD GTGVRDYIHV
VDLADGHICA LQKLDDTEIG CEVYNLGTGK GTTVLEMVDA FEKASGMKIP LVKVGRRPGD
AETVYASTEK AERELNWKAN FGIEEMCRDQ WNWASNNPFG YGSSPNST
