GAE6_ARATH
ID GAE6_ARATH Reviewed; 460 AA.
AC Q9LIS3; Q8H7G2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=UDP-glucuronate 4-epimerase 6;
DE EC=5.1.3.6;
DE AltName: Full=UDP-glucuronic acid epimerase 6;
DE Short=AtUGlcAE2;
GN Name=GAE6; Synonyms=UGlcAE2; OrderedLocusNames=At3g23820;
GN ORFNames=F14O13.1;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15225656; DOI=10.1016/j.febslet.2004.06.005;
RA Usadel B., Schlueter U., Moelhoej M., Gipmans M., Verma R., Kossmann J.,
RA Reiter W.-D., Pauly M.;
RT "Identification and characterization of a UDP-D-glucuronate 4-epimerase in
RT Arabidopsis.";
RL FEBS Lett. 569:327-331(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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].
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP IDENTIFICATION, AND NOMENCLATURE.
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 IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=15247385; DOI=10.1104/pp.104.043745;
RA Moelhoej M., Verma R., Reiter W.-D.;
RT "The biosynthesis of D-galacturonate in plants. Functional cloning and
RT characterization of a membrane-anchored UDP-D-glucuronate 4-epimerase from
RT Arabidopsis.";
RL Plant Physiol. 135:1221-1230(2004).
RN [8]
RP IDENTIFICATION, TISSUE SPECIFICITY, AND NOMENCLATURE.
RX PubMed=15563616; DOI=10.1104/pp.104.052365;
RA Gu X., Bar-Peled M.;
RT "The biosynthesis of UDP-galacturonic acid in plants. Functional cloning
RT and characterization of Arabidopsis UDP-D-glucuronic acid 4-epimerase.";
RL Plant Physiol. 136:4256-4264(2004).
CC -!- FUNCTION: Involved in the synthesis of the negatively charged
CC monosaccharide that forms the backbone of pectic cell wall components.
CC {ECO:0000269|PubMed:15225656}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucuronate = UDP-alpha-D-galacturonate;
CC Xref=Rhea:RHEA:11404, ChEBI:CHEBI:57635, ChEBI:CHEBI:58052;
CC EC=5.1.3.6;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 mM for UDP-glucuronate {ECO:0000269|PubMed:15225656};
CC Note=No activity with UDP-Galactose, UDP- Glucose or UDP-Xylose.;
CC pH dependence:
CC Optimum pH is 7.9. Active from pH 6 to 8.9.
CC {ECO:0000269|PubMed:15225656};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9LIS3; Q38869: CPK4; NbExp=4; IntAct=EBI-2297116, EBI-979475;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In roots, leaf veins, siliques, flowers, pollen and
CC stems. {ECO:0000269|PubMed:15225656, ECO:0000269|PubMed:15247385,
CC ECO:0000269|PubMed:15563616}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AJ879893; CAI53858.1; -; Genomic_DNA.
DR EMBL; AP001297; BAB03000.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76818.1; -; Genomic_DNA.
DR EMBL; AF083691; AAN60250.1; -; mRNA.
DR EMBL; AF370210; AAK44025.1; -; mRNA.
DR EMBL; AY056117; AAL07003.1; -; mRNA.
DR EMBL; AY062625; AAL32703.1; -; mRNA.
DR EMBL; AY133771; AAM91705.1; -; mRNA.
DR RefSeq; NP_189024.1; NM_113287.3.
DR AlphaFoldDB; Q9LIS3; -.
DR SMR; Q9LIS3; -.
DR BioGRID; 7297; 1.
DR IntAct; Q9LIS3; 1.
DR STRING; 3702.AT3G23820.1; -.
DR iPTMnet; Q9LIS3; -.
DR PaxDb; Q9LIS3; -.
DR PRIDE; Q9LIS3; -.
DR ProteomicsDB; 230471; -.
DR EnsemblPlants; AT3G23820.1; AT3G23820.1; AT3G23820.
DR GeneID; 821965; -.
DR Gramene; AT3G23820.1; AT3G23820.1; AT3G23820.
DR KEGG; ath:AT3G23820; -.
DR Araport; AT3G23820; -.
DR TAIR; locus:2076066; AT3G23820.
DR eggNOG; KOG1371; Eukaryota.
DR HOGENOM; CLU_007383_1_2_1; -.
DR InParanoid; Q9LIS3; -.
DR OMA; GVRTSWG; -.
DR OrthoDB; 662484at2759; -.
DR PhylomeDB; Q9LIS3; -.
DR BRENDA; 5.1.3.6; 399.
DR PRO; PR:Q9LIS3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIS3; baseline and differential.
DR Genevisible; Q9LIS3; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0050378; F:UDP-glucuronate 4-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IGI:TAIR.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IGI:TAIR.
DR GO; GO:0033481; P:galacturonate biosynthetic process; IMP:TAIR.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Golgi apparatus; Isomerase; Membrane; NAD;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..460
FT /note="UDP-glucuronate 4-epimerase 6"
FT /id="PRO_0000292601"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 113..144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 460 AA; 50570 MW; 674B9F3E907DFF49 CRC64;
MPLSATADTS KTVKLERYNS YLRKIHSTKV LNASSKVLFR ATLLVALVLV LIFAINYPPL
SDSRAAAAHH LHRRSFLSTG LFSSSSSSSS IGGAAWEKRV RQSSTAKRPH GLSVLVTGAA
GFVGSHCSLA LRKRGDGVLG FDNFNDYYDP SLKRARQELL EKQQVFIVEG DLNDGPLLRK
LFDVVPFTHI LHLAAQAGVR YAMKNPQSYI ASNIAGFVNL LEVAKAANPQ PAIVWASSSS
VYGLNTENPF SEEHRTDQPA SLYAATKKAG EEIAHTYNHI YGLSLTGLRF FTVYGPWGRP
DMAYFFFTKD ILHGKSIDIY RTQDNQEVAR DFTYIDDIVK GCVGALDTAE KSTGSGGKKR
GQAQLRVYNL GNTSPVPVGR LVSILEGLLG TKAKKHLIKM PRNGDVPYTH ANVSLAYKDF
GYKPTTDLAA GLRKFVKWYV GYYGIQPRVK KETSHAEDSA
