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Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 3 (EC 5.1.3.2) (EC 5.1.3.5) (UDP-D-xylose 4-epimerase) (UDP-L-arabinose 4-epimerase) (UDP-galactose 4-epimerase 3) (UDP-glucose 4-epimerase 3) (AtUGE3)

 UGE3_ARATH              Reviewed;         351 AA.
Q8LDN8; Q9CAM5;
01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-OCT-2017, entry version 114.
RecName: Full=Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 3;
EC=5.1.3.2;
EC=5.1.3.5;
AltName: Full=UDP-D-xylose 4-epimerase;
AltName: Full=UDP-L-arabinose 4-epimerase;
AltName: Full=UDP-galactose 4-epimerase 3;
AltName: Full=UDP-glucose 4-epimerase 3;
Short=AtUGE3;
Name=UGE3; OrderedLocusNames=At1g63180; ORFNames=F16M19.8;
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;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Shinn P., Chen H., Kim C.J., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION.
Verma R., Burget E.G., Reiter W.-D.;
"Genetic and biochemical characterization of UDP sugar 4-epimerases in
Arabidopsis thaliana.";
(In) Proceedings of the 12th international conference on Arabidopsis
research, abstract#156, Madison (2001).
[7]
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).
[8]
GENE FAMILY, AND TISSUE SPECIFICITY.
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).
[9]
INDUCTION.
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, 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]
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).
[12]
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 and the interconversion between UDP-arabinose and
UDP-xylose. Cooperates with UGE2 in pollen development.
{ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:17496119,
ECO:0000269|PubMed:19754426, ECO:0000269|Ref.6}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose = UDP-alpha-D-galactose.
-!- CATALYTIC ACTIVITY: UDP-L-arabinose = UDP-D-xylose.
-!- COFACTOR:
Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Strongly inhibited by UDP.
{ECO:0000269|PubMed:16644739}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.19 mM for UDP-glucose {ECO:0000269|PubMed:16644739,
ECO:0000269|PubMed:19754426};
KM=0.22 mM for UDP-galactose {ECO:0000269|PubMed:16644739,
ECO:0000269|PubMed:19754426};
KM=0.068 mM for UDP-galactose {ECO:0000269|PubMed:16644739,
ECO:0000269|PubMed:19754426};
KM=0.32 mM for UDP-xylose {ECO:0000269|PubMed:16644739,
ECO:0000269|PubMed:19754426};
pH dependence:
Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:16644739,
ECO:0000269|PubMed:19754426};
Temperature dependence:
Optimum temperature is 35 degrees Celsius.
{ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:19754426};
-!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
-!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-L-arabinose
biosynthesis; UDP-L-arabinose from UDP-alpha-D-xylose: step 1/1.
-!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide
biosynthesis.
-!- SUBUNIT: homodimer. Heterodimer. {ECO:0000269|PubMed:16644739}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12419184,
ECO:0000269|PubMed:16644739, ECO:0000269|PubMed:17496119}.
-!- INDUCTION: Down-regulated by ethylene.
{ECO:0000269|PubMed:14973160}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Uge2 and uge3 double
mutant is almost completely sterile (PubMed:17496119).
{ECO:0000269|PubMed:17496119}.
-!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG51599.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC010795; AAG51599.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE34065.1; -; Genomic_DNA.
EMBL; AK117913; BAC42551.1; -; mRNA.
EMBL; BT024882; ABD85153.1; -; mRNA.
EMBL; AY085887; AAM63099.1; -; mRNA.
PIR; D96657; D96657.
RefSeq; NP_564811.1; NM_104996.6.
UniGene; At.36168; -.
ProteinModelPortal; Q8LDN8; -.
SMR; Q8LDN8; -.
STRING; 3702.AT1G63180.1; -.
PaxDb; Q8LDN8; -.
EnsemblPlants; AT1G63180.1; AT1G63180.1; AT1G63180.
GeneID; 842622; -.
Gramene; AT1G63180.1; AT1G63180.1; AT1G63180.
KEGG; ath:AT1G63180; -.
Araport; AT1G63180; -.
TAIR; locus:2015253; AT1G63180.
eggNOG; KOG1371; Eukaryota.
eggNOG; COG1087; LUCA.
HOGENOM; HOG000168001; -.
InParanoid; Q8LDN8; -.
KO; K01784; -.
OMA; YNINGTM; -.
OrthoDB; EOG09360DIQ; -.
PhylomeDB; Q8LDN8; -.
BRENDA; 5.1.3.2; 399.
BRENDA; 5.1.3.5; 399.
Reactome; R-ATH-70370; Galactose catabolism.
SABIO-RK; Q8LDN8; -.
UniPathway; UPA00214; -.
UniPathway; UPA00797; UER00772.
UniPathway; UPA00963; -.
PRO; PR:Q8LDN8; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q8LDN8; baseline and differential.
Genevisible; Q8LDN8; AT.
GO; GO:0050373; F:UDP-arabinose 4-epimerase activity; IDA:UniProtKB.
GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IDA:TAIR.
GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0009555; P:pollen development; IMP:TAIR.
GO; GO:0033358; P:UDP-L-arabinose biosynthetic process; IEA:UniProtKB-UniPathway.
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; Galactose metabolism; Isomerase; NAD;
Reference proteome.
CHAIN 1 351 Bifunctional UDP-glucose 4-epimerase and
UDP-xylose 4-epimerase 3.
/FTId=PRO_0000422185.
NP_BIND 8 39 NAD. {ECO:0000250}.
ACT_SITE 158 158 Proton acceptor. {ECO:0000250}.
BINDING 134 134 Substrate. {ECO:0000250}.
SEQUENCE 351 AA; 38910 MW; 314BC1FA8DD091EF CRC64;
MGSSVEQNIL VTGGAGFIGT HTVVQLLNQG FKVTIIDNLD NSVVEAVHRV RELVGPDLST
KLEFNLGDLR NKGDIEKLFS NQRFDAVIHF AGLKAVGESV GNPRRYFDNN LVGTINLYET
MAKYNCKMMV FSSSATVYGQ PEIVPCVEDF ELQAMNPYGR TKLFLEEIAR DIHAAEPEWK
IILLRYFNPV GAHESGRIGE DPKGIPNNLM PYIQQVAVGR LPELNVFGHD YPTMDGSAVR
DYIHVMDLAD GHVAALNKLF SDSKIGCTAY NLGTGQGTSV LEMVSSFEKA SGKKIPIKLC
PRRAGDATAV YASTQKAEKE LGWKAKYGVD EMCRDQWNWA NKNPWGFQKK P


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