GAE1_ARATH
ID GAE1_ARATH Reviewed; 429 AA.
AC Q9M0B6;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=UDP-glucuronate 4-epimerase 1;
DE EC=5.1.3.6 {ECO:0000269|PubMed:15247385};
DE AltName: Full=UDP-glucuronic acid epimerase 1;
DE Short=AtUGlcAE3;
GN Name=GAE1; Synonyms=UGlcAE3; OrderedLocusNames=At4g30440;
GN ORFNames=F17I23.220;
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, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
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 [2]
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 [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].
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 [5]
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 [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 TISSUE SPECIFICITY.
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 [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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: UDP-D-glucuronate 4-epimerase involved in the synthesis of
CC the negatively charged monosaccharide that forms the backbone of pectic
CC cell wall components. {ECO:0000269|PubMed:15247385}.
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; Evidence={ECO:0000269|PubMed:15247385};
CC -!- ACTIVITY REGULATION: Inhibited by UDP-Xylose.
CC {ECO:0000269|PubMed:15247385}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.19 mM for UDP-glucuronate {ECO:0000269|PubMed:15247385};
CC Note=Equilibrium between UDP-glucuronate and UDP-D-galacturonate
CC established at 1:1.3. {ECO:0000269|PubMed:15247385};
CC pH dependence:
CC Optimum pH is 7.6. Active from pH 6 to 8.9.
CC {ECO:0000269|PubMed:15247385};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In root stele, leaves, siliques, flowers, pollen
CC and 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; AY661562; AAT77233.1; -; Genomic_DNA.
DR EMBL; AL161577; CAB79762.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85765.1; -; Genomic_DNA.
DR EMBL; AY056303; AAL07152.1; -; mRNA.
DR EMBL; AY099855; AAM20706.1; -; mRNA.
DR EMBL; BT000308; AAN15627.1; -; mRNA.
DR EMBL; AY085505; AAM62729.1; -; mRNA.
DR PIR; A85356; A85356.
DR RefSeq; NP_194773.1; NM_119190.4.
DR AlphaFoldDB; Q9M0B6; -.
DR SMR; Q9M0B6; -.
DR STRING; 3702.AT4G30440.1; -.
DR iPTMnet; Q9M0B6; -.
DR SwissPalm; Q9M0B6; -.
DR PaxDb; Q9M0B6; -.
DR PRIDE; Q9M0B6; -.
DR ProteomicsDB; 230470; -.
DR EnsemblPlants; AT4G30440.1; AT4G30440.1; AT4G30440.
DR GeneID; 829167; -.
DR Gramene; AT4G30440.1; AT4G30440.1; AT4G30440.
DR KEGG; ath:AT4G30440; -.
DR Araport; AT4G30440; -.
DR TAIR; locus:2118711; AT4G30440.
DR eggNOG; KOG1371; Eukaryota.
DR HOGENOM; CLU_007383_1_2_1; -.
DR InParanoid; Q9M0B6; -.
DR OMA; EPIKVFN; -.
DR OrthoDB; 662484at2759; -.
DR PhylomeDB; Q9M0B6; -.
DR BRENDA; 5.1.3.6; 399.
DR SABIO-RK; Q9M0B6; -.
DR PRO; PR:Q9M0B6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0B6; baseline and differential.
DR Genevisible; Q9M0B6; 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; IDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
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; IGI: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..429
FT /note="UDP-glucuronate 4-epimerase 1"
FT /id="PRO_0000292596"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 89..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 429 AA; 47458 MW; 1FDD14BC3FDABCD4 CRC64;
MPSIEDELFP STPGKFKIDR SNRQLHRCFA STSTMFLWAL FLIALTASYL SFQSFVDSGS
RYLTASWGGI QWEKQVRTSA QIHRSGGISV LVTGATGFVG SHVSLALRKR GDGVVGLDNF
NNYYDPSLKR ARRSLLSSRG IFVVEGDLND AKLLAKLFDV VAFTHVMHLA AQAGVRYALE
NPQSYVHSNI AGLVNLLEIC KAANPQPAIV WASSSSVYGL NEKVPFSESD RTDQPASLYA
ATKKAGEEIT HTYNHIYGLA ITGLRFFTVY GPWGRPDMAY FSFTRNILQG KPITIYRGKN
RVDLARDFTY IDDIVKGCLG SLDSSGKSTG SGGKKRGAAP YRIFNLGNTS PVTVPILVDI
LEKHLKVKAK RNFVEMPGNG DVPFTHANIS SARNEFGYKP TTDLETGLKK FVRWYLSYYG
YNTKAKLVH
