GAE4_ARATH
ID GAE4_ARATH Reviewed; 437 AA.
AC O22141;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=UDP-glucuronate 4-epimerase 4;
DE EC=5.1.3.6;
DE AltName: Full=UDP-glucuronic acid epimerase 4;
DE Short=AtUGlcAE1;
GN Name=GAE4; Synonyms=UGlcAE1; OrderedLocusNames=At2g45310; ORFNames=F4L23;
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 [MRNA], ACTIVITY REGULATION, SUBUNIT, TISSUE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 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 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 [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).
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 -!- ACTIVITY REGULATION: Activated by glycerol, not effected by dimethyl
CC sulfoxide and inhibited by high concentration of monovalent salts, UDP-
CC xylose, UDP-arabinose or UDP. {ECO:0000269|PubMed:15563616}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.72 mM for UDP-glucuronate {ECO:0000269|PubMed:15563616};
CC Note=Equilibrium between UDP-glucuronate and UDP-D-galacturonate
CC established at 1:1.9. No activity with UDP-Galactose, UDP-Glucose,
CC UDP-arabinose, UDP-Xylose, CDP-glucose or GDP-manose.;
CC pH dependence:
CC Optimum pH is 7.5. Active from pH 6.8 to 8.2.
CC {ECO:0000269|PubMed:15563616};
CC Temperature dependence:
CC Active between 20 and 55 degrees Celsius.
CC {ECO:0000269|PubMed:15563616};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:15563616}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In roots, leaves, 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; AY594693; AAT06796.1; -; mRNA.
DR EMBL; AC002387; AAB82632.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10537.1; -; Genomic_DNA.
DR EMBL; BT005652; AAO64072.1; -; mRNA.
DR EMBL; BT004225; AAO42241.1; -; mRNA.
DR PIR; A84889; A84889.
DR RefSeq; NP_182056.1; NM_130094.2.
DR AlphaFoldDB; O22141; -.
DR SMR; O22141; -.
DR STRING; 3702.AT2G45310.1; -.
DR iPTMnet; O22141; -.
DR PaxDb; O22141; -.
DR PRIDE; O22141; -.
DR ProteomicsDB; 230008; -.
DR EnsemblPlants; AT2G45310.1; AT2G45310.1; AT2G45310.
DR GeneID; 819139; -.
DR Gramene; AT2G45310.1; AT2G45310.1; AT2G45310.
DR KEGG; ath:AT2G45310; -.
DR Araport; AT2G45310; -.
DR TAIR; locus:2050921; AT2G45310.
DR eggNOG; KOG1371; Eukaryota.
DR HOGENOM; CLU_007383_1_2_1; -.
DR InParanoid; O22141; -.
DR OMA; WSIVFFC; -.
DR OrthoDB; 662484at2759; -.
DR PhylomeDB; O22141; -.
DR BioCyc; ARA:AT2G45310-MON; -.
DR BioCyc; MetaCyc:AT2G45310-MON; -.
DR BRENDA; 5.1.3.6; 399.
DR SABIO-RK; O22141; -.
DR PRO; PR:O22141; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22141; differential.
DR Genevisible; O22141; AT.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Golgi apparatus; Isomerase; Membrane; NAD;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..437
FT /note="UDP-glucuronate 4-epimerase 4"
FT /id="PRO_0000292599"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 56..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 98..129
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 437 AA; 48536 MW; FF8D60C56550CB41 CRC64;
MSRLDDIPSS PGKFKMEKSS YLHRLRFQSS LTKFAFFSFF LLCLISLLFL RSPPSINPSS
PSDPSRRSLR TNTYGGPAWE KRLRSSARIR TSTNNGITVL VTGAAGFVGT HVSAALKRRG
DGVIGLDNFN DYYDPSLKRA RRALLERSGI FIVEGDINDV ELLRKLFKIV SFTHVMHLAA
QAGVRYAMEN PSSYVHSNIA GFVNLLEICK SVNPQPAIVW ASSSSVYGLN TKVPFSEKDK
TDQPASLYAA TKKAGEEIAH TYNHIYGLSL TGLRFFTVYG PWGRPDMAYF FFTKDILKGK
SISIFESANH GTVARDFTYI DDIVKGCLAA LDTAEKSTGS GGKKRGPAQL RVFNLGNTSP
VPVSDLVRIL ERQLKVKAKK NLIKMPRNGD VPFTHANISL AQRELGYKPT TDLQTGLKKF
VRWYLSYYSG DKKAAAR
