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UDP-glucose 4-epimerase 4 (AtUGE4) (EC 5.1.3.2) (Protein ROOT EPIDERMAL BULGER 1) (Protein ROOT HAIR DEFECTIVE 1) (UDP-galactose 4-epimerase 4)

 UGE4_ARATH              Reviewed;         348 AA.
Q9C7W7; Q9SGX0;
01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
23-MAY-2018, entry version 114.
RecName: Full=UDP-glucose 4-epimerase 4;
Short=AtUGE4;
EC=5.1.3.2;
AltName: Full=Protein ROOT EPIDERMAL BULGER 1;
AltName: Full=Protein ROOT HAIR DEFECTIVE 1;
AltName: Full=UDP-galactose 4-epimerase 4;
Name=UGE4; Synonyms=REB1, RHD1; OrderedLocusNames=At1g64440;
ORFNames=F15H21.11, F1N19.2;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[4]
DISRUPTION PHENOTYPE.
DOI=10.1071/PP9920427;
Baskin T.I., Betzner A.S., Hoggart R., Cork A., Williamson R.E.;
"Root morphology mutants in Arabidopsis thaliana.";
Aust. J. Plant Physiol. 19:427-437(1992).
[5]
DISRUPTION PHENOTYPE.
PubMed=9431677; DOI=10.1007/s004250050194;
Ding L., Zhu J.K.;
"A role for arabinogalactan-proteins in root epidermal cell
expansion.";
Planta 203:289-294(1997).
[6]
GENE FAMILY.
PubMed=11554483; DOI=10.1023/A:1010671129803;
Reiter W.-D., Vanzin G.F.;
"Molecular genetics of nucleotide sugar interconversion pathways in
plants.";
Plant Mol. Biol. 47:95-113(2001).
[7]
GENE FAMILY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES,
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=12419184; DOI=10.1016/S0960-9822(02)01260-5;
Seifert G.J., Barber C., Wells B., Dolan L., Roberts K.;
"Galactose biosynthesis in Arabidopsis: genetic evidence for substrate
channeling from UDP-D-galactose into cell wall polymers.";
Curr. Biol. 12:1840-1845(2002).
[8]
DISRUPTION PHENOTYPE.
PubMed=12355155; DOI=10.1007/s00425-002-0836-z;
Andeme-Onzighi C., Sivaguru M., Judy-March J., Baskin T.I.,
Driouich A.;
"The reb1-1 mutation of Arabidopsis alters the morphology of
trichoblasts, the expression of arabinogalactan-proteins and the
organization of cortical microtubules.";
Planta 215:949-958(2002).
[9]
FUNCTION.
PubMed=14973160; DOI=10.1105/tpc.019661;
Seifert G.J., Barber C., Wells B., Roberts K.;
"Growth regulators and the control of nucleotide sugar flux.";
Plant Cell 16:723-730(2004).
[10]
SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=16644739; DOI=10.1074/jbc.M512727200;
Barber C., Roesti J., Rawat A., Findlay K., Roberts K., Seifert G.J.;
"Distinct properties of the five UDP-D-glucose/UDP-D-galactose 4-
epimerase isoforms of Arabidopsis thaliana.";
J. Biol. Chem. 281:17276-17285(2006).
[11]
FUNCTION.
PubMed=16500990; DOI=10.1104/pp.105.074997;
Nguema-Ona E., Andeme-Onzighi C., Aboughe-Angone S., Bardor M.,
Ishii T., Lerouge P., Driouich A.;
"The reb1-1 mutation of Arabidopsis. Effect on the structure and
localization of galactose-containing cell wall polysaccharides.";
Plant Physiol. 140:1406-1417(2006).
[12]
TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=17496119; DOI=10.1105/tpc.106.049619;
Roesti J., Barton C.J., Albrecht S., Dupree P., Pauly M., Findlay K.,
Roberts K., Seifert G.J.;
"UDP-glucose 4-epimerase isoforms UGE2 and UGE4 cooperate in providing
UDP-galactose for cell wall biosynthesis and growth of Arabidopsis
thaliana.";
Plant Cell 19:1565-1579(2007).
[13]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19754426; DOI=10.1042/BJ20091025;
Kotake T., Takata R., Verma R., Takaba M., Yamaguchi D., Orita T.,
Kaneko S., Matsuoka K., Koyama T., Reiter W.D., Tsumuraya Y.;
"Bifunctional cytosolic UDP-glucose 4-epimerases catalyse the
interconversion between UDP-D-xylose and UDP-L-arabinose in plants.";
Biochem. J. 424:169-177(2009).
-!- FUNCTION: Catalyzes the interconversion between UDP-glucose and
UDP-galactose. Involved in channeling UDP-D-galactose (UDP-D-Gal)
into cell wall polymers. Required for the galactosylation of
xyloglucan (XyG) and type II arabinogalactan (AGII). Cooperates
with UGE2 in cell wall carbohydrate biosynthesis and growth.
{ECO:0000269|PubMed:12419184, ECO:0000269|PubMed:14973160,
ECO:0000269|PubMed:16500990, ECO:0000269|PubMed:16644739,
ECO:0000269|PubMed:17496119, ECO:0000269|PubMed:19754426}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose = UDP-alpha-D-galactose.
-!- COFACTOR:
Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Inhibited by NaCl. Enhanced activity by NAD(+).
Slightly inhibited by UDP. {ECO:0000269|PubMed:16644739}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.56 mM for UDP-glucose {ECO:0000269|PubMed:12419184,
ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
KM=0.23 mM for UDP-galactose {ECO:0000269|PubMed:12419184,
ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
KM=0.057 mM for UDP-galactose {ECO:0000269|PubMed:12419184,
ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
KM=0.42 mM for UDP-xylose {ECO:0000269|PubMed:12419184,
ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
Vmax=7.41 mmol/min/mg enzyme toward UDP-D-glucose
{ECO:0000269|PubMed:12419184, ECO:0000269|PubMed:16644739,
ECO:0000269|PubMed:19754426};
pH dependence:
Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:12419184,
ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
Temperature dependence:
Optimum temperature is 30 degrees Celsius.
{ECO:0000269|PubMed:12419184, ECO:0000269|PubMed:16644739,
ECO:0000269|PubMed:19754426};
-!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
-!- SUBUNIT: homodimer. Heterodimer. {ECO:0000269|PubMed:16644739}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16644739}.
Golgi apparatus, Golgi stack {ECO:0000269|PubMed:16644739}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12419184,
ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:17496119}.
-!- DISRUPTION PHENOTYPE: Root epidermal bulging. Partially deficient
in cell wall arabinogalactan-protein (AGP). Abnormal trichoblast
cell wall. Uge2 and uge4 double mutant displays a reduction in
rosette and root growth, hypocotyl elongation, and secondary
hypocotyl thickening (PubMed:17496119).
{ECO:0000269|PubMed:12355155, ECO:0000269|PubMed:12419184,
ECO:0000269|PubMed:17496119, ECO:0000269|PubMed:9431677,
ECO:0000269|Ref.4}.
-!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF19668.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AC009519; AAF19668.1; ALT_SEQ; Genomic_DNA.
EMBL; AC066689; AAG51709.1; -; Genomic_DNA.
EMBL; CP002684; AEE34241.1; -; Genomic_DNA.
EMBL; BT011226; AAR92262.1; -; mRNA.
EMBL; BT012154; AAS76249.1; -; mRNA.
RefSeq; NP_176625.1; NM_105119.5.
UniGene; At.25758; -.
ProteinModelPortal; Q9C7W7; -.
SMR; Q9C7W7; -.
STRING; 3702.AT1G64440.1; -.
PaxDb; Q9C7W7; -.
PRIDE; Q9C7W7; -.
EnsemblPlants; AT1G64440.1; AT1G64440.1; AT1G64440.
GeneID; 842752; -.
Gramene; AT1G64440.1; AT1G64440.1; AT1G64440.
KEGG; ath:AT1G64440; -.
Araport; AT1G64440; -.
TAIR; locus:2014235; AT1G64440.
eggNOG; KOG1371; Eukaryota.
eggNOG; COG1087; LUCA.
HOGENOM; HOG000168001; -.
InParanoid; Q9C7W7; -.
KO; K01784; -.
OMA; LADGHIC; -.
OrthoDB; EOG09360DIQ; -.
PhylomeDB; Q9C7W7; -.
BRENDA; 5.1.3.2; 399.
BRENDA; 5.1.3.5; 399.
Reactome; R-ATH-70370; Galactose catabolism.
SABIO-RK; Q9C7W7; -.
UniPathway; UPA00214; -.
PRO; PR:Q9C7W7; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9C7W7; baseline and differential.
Genevisible; Q9C7W7; AT.
GO; GO:0005795; C:Golgi stack; IDA:TAIR.
GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IDA:TAIR.
GO; GO:0042546; P:cell wall biogenesis; IMP:TAIR.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0009832; P:plant-type cell wall biogenesis; TAS:TAIR.
GO; GO:0010053; P:root epidermal cell differentiation; IMP:TAIR.
GO; GO:0009969; P:xyloglucan biosynthetic process; IMP:TAIR.
CDD; cd05247; UDP_G4E_1_SDR_e; 1.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR005886; UDP_G4E.
Pfam; PF16363; GDP_Man_Dehyd; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01179; galE; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Cell wall biogenesis/degradation;
Complete proteome; Cytoplasm; Galactose metabolism; Golgi apparatus;
Isomerase; NAD; Reference proteome.
CHAIN 1 348 UDP-glucose 4-epimerase 4.
/FTId=PRO_0000422186.
NP_BIND 4 35 NAD. {ECO:0000250}.
ACT_SITE 153 153 Proton acceptor. {ECO:0000250}.
BINDING 129 129 Substrate. {ECO:0000250}.
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


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