RGP3_ORYSJ
ID RGP3_ORYSJ Reviewed; 366 AA.
AC Q6Z4G3; A0A0P0X8G9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=UDP-arabinopyranose mutase 3 {ECO:0000303|PubMed:17182701};
DE Short=OsUAM3 {ECO:0000303|PubMed:17182701};
DE EC=5.4.99.30 {ECO:0000269|PubMed:17182701, ECO:0000269|PubMed:20057139, ECO:0000269|PubMed:20149347};
DE AltName: Full=Reversibly glycosylated polypeptide 3 {ECO:0000303|PubMed:17182701};
DE AltName: Full=UDP-L-arabinose mutase 3 {ECO:0000305};
GN Name=UAM3 {ECO:0000303|PubMed:17182701};
GN Synonyms=RGP3 {ECO:0000303|PubMed:17182701};
GN OrderedLocusNames=Os07g0604800 {ECO:0000312|EMBL:BAT02557.1},
GN LOC_Os07g41360 {ECO:0000305};
GN ORFNames=OsJ_25044 {ECO:0000312|EMBL:EAZ40585.1},
GN OSJNBb0040H10.21 {ECO:0000312|EMBL:BAC83877.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, GLYCOSYLATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17182701; DOI=10.1093/glycob/cwl081;
RA Konishi T., Takeda T., Miyazaki Y., Ohnishi-Kameyama M., Hayashi T.,
RA O'Neill M.A., Ishii T.;
RT "A plant mutase that interconverts UDP-L-arabinofuranose and UDP-L-
RT arabinopyranose.";
RL Glycobiology 17:345-354(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20057139; DOI=10.1271/bbb.90619;
RA Konishi T., Miyazaki Y., Yamakawa S., Iwai H., Satoh S., Ishii T.;
RT "Purification and biochemical characterization of recombinant rice UDP-L-
RT arabinopyranose mutase generated in insect cells.";
RL Biosci. Biotechnol. Biochem. 74:191-194(2010).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-149; ARG-156 AND
RP ARG-163.
RX PubMed=20149347; DOI=10.1016/j.carres.2010.01.008;
RA Konishi T., Ohnishi-Kameyama M., Funane K., Miyazaki Y., Konishi T.,
RA Ishii T.;
RT "An arginyl residue in rice UDP-L-arabinopyranose mutase is required for
RT catalytic activity and autoglycosylation.";
RL Carbohydr. Res. 345:787-791(2010).
CC -!- FUNCTION: UDP-L-arabinose mutase involved in the biosynthesis of cell
CC wall non-cellulosic polysaccharides. Catalyzes the interconvertion of
CC UDP-L-arabinopyranose (UDP-Arap) and UDP-L-arabinofuranose (UDP-Araf).
CC Preferentially catalyzes the formation of UDP-Arap from UDP-Araf. At
CC thermodynamic equilibrium in vitro the ratio of the pyranose form over
CC the furanose form is 90:10. Is probably active as heteromer in vivo.
CC {ECO:0000269|PubMed:17182701, ECO:0000269|PubMed:20057139,
CC ECO:0000269|PubMed:20149347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose;
CC Xref=Rhea:RHEA:28350, ChEBI:CHEBI:61457, ChEBI:CHEBI:61463;
CC EC=5.4.99.30; Evidence={ECO:0000269|PubMed:17182701,
CC ECO:0000269|PubMed:20057139, ECO:0000269|PubMed:20149347};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17182701};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17182701};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=84.8 uM for UDP-L-arabinofuranose {ECO:0000269|PubMed:20057139};
CC KM=210 uM for UDP-L-arabinopyranose {ECO:0000269|PubMed:20057139};
CC Vmax=2.82 umol/min/mg enzyme with UDP-L-arabinofuranose as substrate
CC {ECO:0000269|PubMed:20057139};
CC Vmax=1.36 umol/min/mg enzyme with UDP-L-arabinofuranose as substrate
CC {ECO:0000269|PubMed:20057139};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:20057139};
CC -!- SUBUNIT: Heteromers with UAM1 and UAM2. {ECO:0000269|PubMed:17182701}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q9SRT9}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250|UniProtKB:Q8H8T0}.
CC -!- PTM: Reversibly glycosylated in vitro by UDP-glucose, UDP-xylose and
CC UDP-galactose. {ECO:0000269|PubMed:17182701}.
CC -!- SIMILARITY: Belongs to the RGP family. {ECO:0000305}.
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DR EMBL; AP005175; BAC83877.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF22138.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT02557.1; -; Genomic_DNA.
DR EMBL; CM000144; EAZ40585.1; -; Genomic_DNA.
DR EMBL; AK061294; BAG87841.1; -; mRNA.
DR RefSeq; XP_015647980.1; XM_015792494.1.
DR AlphaFoldDB; Q6Z4G3; -.
DR STRING; 4530.OS07T0604800-01; -.
DR CAZy; GT75; Glycosyltransferase Family 75.
DR PaxDb; Q6Z4G3; -.
DR PRIDE; Q6Z4G3; -.
DR EnsemblPlants; Os07t0604800-01; Os07t0604800-01; Os07g0604800.
DR GeneID; 4343849; -.
DR Gramene; Os07t0604800-01; Os07t0604800-01; Os07g0604800.
DR KEGG; osa:4343849; -.
DR eggNOG; ENOG502QSDP; Eukaryota.
DR HOGENOM; CLU_061976_0_0_1; -.
DR InParanoid; Q6Z4G3; -.
DR OMA; DSVQQCY; -.
DR OrthoDB; 662486at2759; -.
DR BRENDA; 5.4.99.30; 4460.
DR PlantReactome; R-OSA-1119574; UDP-L-arabinose biosynthesis and transport.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q6Z4G3; OS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016866; F:intramolecular transferase activity; IDA:UniProtKB.
DR GO; GO:0052691; F:UDP-arabinopyranose mutase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IBA:GO_Central.
DR GO; GO:0033356; P:UDP-L-arabinose metabolic process; IBA:GO_Central.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR004901; RGP.
DR InterPro; IPR037595; RGP_fam.
DR PANTHER; PTHR31682; PTHR31682; 1.
DR Pfam; PF03214; RGP; 1.
DR PIRSF; PIRSF016429; UPTG; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Glycoprotein; Golgi apparatus; Isomerase;
KW Reference proteome.
FT CHAIN 1..366
FT /note="UDP-arabinopyranose mutase 3"
FT /id="PRO_0000410991"
FT MOTIF 108..110
FT /note="DXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT SITE 156
FT /note="Required for activity"
FT /evidence="ECO:0000269|PubMed:20149347"
FT SITE 163
FT /note="Required for activity"
FT /evidence="ECO:0000269|PubMed:20149347"
FT CARBOHYD 156
FT /note="N-linked (Glc...) arginine"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT MUTAGEN 149
FT /note="R->A: No effect on the activity."
FT /evidence="ECO:0000269|PubMed:20149347"
FT MUTAGEN 156
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20149347"
FT MUTAGEN 163
FT /note="R->A: Decreases activity 50-fold."
FT /evidence="ECO:0000269|PubMed:20149347"
SQ SEQUENCE 366 AA; 41279 MW; 6DBC4B6769966C44 CRC64;
MASSDAAAAQ AATPLLKDEL DIVIPTIRNL DFLEMWRPFF QPYHLIIVQD GDPKKTIRVP
EGFDYELYNR DDINRILGPR ASCISFKDSA CRCFGYMVSK KKYIYTIDDD CFVAKDPSGK
DINALEQHIK NLLNPSTPFF FNTLYDPYRD GADFVRGYPF SLREGAPTAV SHGLWLNIPD
YDAPTQLVKP LERNSRYVDA VMTIPKGTLF PMCGMNLAFD RDLIGPAMYF GLMGDGQPIG
RYDDMWAGWC TKVITDHLGL GVKTGLPYIW HSKASNPFVN LKKEYNGIFW QEELIPFFQS
ASLPKEADTV QKCYLELAKQ VRAKLGKVDG YFNKLADSMV TWIEAWDQLN PPKGAVATAN
GTAKSK
