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   16-JUN-2009, entry version 51.
DE   RecName: Full=UDP-glucuronate 4-epimerase 1;
DE            EC=5.1.3.6;
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP   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
RT   from Arabidopsis.";
RL   Plant Physiol. 135:1221-1230(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
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   [5]
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   [6]
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.,
RA   Kossmann J., Reiter W.-D., Pauly M.;
RT   "Identification and characterization of a UDP-D-glucuronate 4-
RT   epimerase in Arabidopsis.";
RL   FEBS Lett. 569:327-331(2004).
RN   [7]
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
RT   cloning and characterization of Arabidopsis UDP-D-glucuronic acid 4-
RT   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
CC       components.
CC   -!- CATALYTIC ACTIVITY: UDP-glucuronate = UDP-D-galacturonate.
CC   -!- ENZYME REGULATION: Inhibited by UDP-Xylose.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.19 mM for UDP-glucuronate;
CC         Note=Equilibrium between UDP-glucuronate and UDP-D-galacturonate
CC         established at 1:1.3. No activity with UDP-Galactose, UDP-
CC         Glucose or UDP-Xylose;
CC       pH dependence:
CC         Optimum pH is 7.6. Active from pH 6 to 8.9;
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane;
CC       Multi-pass membrane protein (Potential).
CC   -!- TISSUE SPECIFICITY: In root stele, leaves, siliques, flowers,
CC       pollen and stems.
CC   -!- SIMILARITY: Belongs to the sugar epimerase family.
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DR   EMBL; AY661562; AAT77233.1; -; Genomic_DNA.
DR   EMBL; AL161577; CAB79762.1; -; 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   IPI; IPI00530645; -.
DR   PIR; A85356; A85356.
DR   RefSeq; NP_194773.1; -.
DR   UniGene; At.20969; -.
DR   UniGene; At.67043; -.
DR   HSSP; Q14376; 1I3K.
DR   PRIDE; Q9M0B6; -.
DR   GeneID; 829167; -.
DR   GenomeReviews; CT486007_GR; AT4G30440.
DR   KEGG; ath:AT4G30440; -.
DR   NMPDR; fig|3702.1.peg.21026; -.
DR   TAIR; At4g30440; -.
DR   OMA; Q9M0B6; HAILARS.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
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:0044237; P:cellular metabolic process; IEA:InterPro.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR008089; Nuc_sugar_epim.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   PRINTS; PR01713; NUCEPIMERASE.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Golgi apparatus;
KW   Isomerase; Membrane; NAD; Transmembrane.
FT   CHAIN         1    429       UDP-glucuronate 4-epimerase 1.
FT                                /FTId=PRO_0000292596.
FT   TRANSMEM     36     56       Potential.
FT   TRANSMEM     87    107       Potential.
FT   NP_BIND      89    120       NAD (By similarity).
FT   COMPBIAS    213    216       Poly-Ser.
FT   ACT_SITE    239    239       Proton acceptor (By similarity).
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
//