GAE5_ARATH
ID GAE5_ARATH Reviewed; 436 AA.
AC Q9STI6; Q949N3;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=UDP-glucuronate 4-epimerase 5;
DE EC=5.1.3.6;
DE AltName: Full=UDP-glucuronic acid epimerase 5;
GN Name=GAE5; OrderedLocusNames=At4g12250; ORFNames=T4C9.90;
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 [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 [2]
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 [3]
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 [4]
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 [5]
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 [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., 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).
CC -!- FUNCTION: Involved in the synthesis of the negatively charged
CC monosaccharide that forms the backbone of pectic cell wall components.
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 -!- 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 leaves, pollen and siliques, but not in roots or
CC flowers. {ECO:0000269|PubMed:15225656, ECO:0000269|PubMed:15247385}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AL080318; CAB45972.1; -; Genomic_DNA.
DR EMBL; AL161533; CAB78268.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83108.1; -; Genomic_DNA.
DR EMBL; AY050993; AAK93670.1; -; mRNA.
DR EMBL; AY150403; AAN12948.1; -; mRNA.
DR PIR; T48135; T48135.
DR RefSeq; NP_192962.1; NM_117295.4.
DR AlphaFoldDB; Q9STI6; -.
DR SMR; Q9STI6; -.
DR BioGRID; 12131; 14.
DR IntAct; Q9STI6; 14.
DR STRING; 3702.AT4G12250.1; -.
DR PaxDb; Q9STI6; -.
DR PRIDE; Q9STI6; -.
DR ProteomicsDB; 228895; -.
DR EnsemblPlants; AT4G12250.1; AT4G12250.1; AT4G12250.
DR GeneID; 826833; -.
DR Gramene; AT4G12250.1; AT4G12250.1; AT4G12250.
DR KEGG; ath:AT4G12250; -.
DR Araport; AT4G12250; -.
DR TAIR; locus:2139134; AT4G12250.
DR eggNOG; KOG1371; Eukaryota.
DR HOGENOM; CLU_007383_1_2_1; -.
DR InParanoid; Q9STI6; -.
DR OMA; LHTPYQV; -.
DR OrthoDB; 662484at2759; -.
DR PhylomeDB; Q9STI6; -.
DR BRENDA; 5.1.3.6; 399.
DR PRO; PR:Q9STI6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STI6; baseline and differential.
DR Genevisible; Q9STI6; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005797; C:Golgi medial 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 InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Golgi apparatus; Isomerase; Membrane; NAD;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..436
FT /note="UDP-glucuronate 4-epimerase 5"
FT /id="PRO_0000292600"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 97..128
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 116
FT /note="R -> Q (in Ref. 3; AAK93670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 48165 MW; 2D9B645D80735C14 CRC64;
MSHLDDLPST PGKYKTDKVP PYGILHHHRY LRLSKLTLWA SLFLALFLFY LVLSPPPSPS
RRNLNDSSSI SAAKYGGSHW EKQVRKSARP RSHGGLTVLV TGASGFVGTH VSIALRRRGD
GVLGLDNFNR YYDPKLKRAR QGLLERSGVF VVEGDINDAV LLRKLFDVVL FTHVMHLAAQ
AGVRYAMQNP GSYVNSNIAG FVNLLEVSKS ANPQPAIVWA SSSSVYGLNS KVPFSEKDRT
DQPASLYAAT KKAGEGIAHT YNHIYGLSLT GLRFFTVYGP WGRPDMAYFF FTKDILKGKT
ITVFESPDKG SVARDFTYID DIVKGCLGAL DTAEKSTGSG GKKKGPAMFR IYNLGNTSPV
PVTKLVTILE KLLKMKAKKK IMPLPRNGDV EFTHANITLA QAELGYKPAV DLETGLKKFV
KWYMGFYTGS KKKSSW