RGP1_ORYSJ
ID RGP1_ORYSJ Reviewed; 364 AA.
AC Q8H8T0; A0A0P0W0V3; O82705; Q10H67; Q9FUN9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=UDP-arabinopyranose mutase 1 {ECO:0000303|PubMed:17182701};
DE Short=OsUAM1 {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 1 {ECO:0000303|PubMed:17182701};
DE AltName: Full=UDP-L-arabinose mutase 1 {ECO:0000305};
GN Name=UAM1 {ECO:0000303|PubMed:17182701};
GN Synonyms=RGP1 {ECO:0000303|PubMed:17182701};
GN OrderedLocusNames=Os03g0599800 {ECO:0000312|EMBL:BAS85190.1},
GN LOC_Os03g40270 {ECO:0000312|EMBL:ABF97476.1};
GN ORFNames=OJ1523_A02.1 {ECO:0000312|EMBL:AAN08217.1},
GN OsJ_11657 {ECO:0000312|EMBL:EEE59464.1};
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 [MRNA].
RA Gupta P., Raghuvanshi S., Tyagi A.K.;
RT "PCR-Amplification and cloning of the coding region of a cDNA for a
RT reversibly glycosylated polypeptide from rice with possible involvement in
RT the biosynthesis of glucans.";
RL J. Plant Biochem. Biotechnol. 9:99-102(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Lemont;
RA Bligh H.F., Jackson D.A.;
RT "Characterization of reverse glycosylating proteins 1 and 2 of Oryza
RT sativa.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo; TISSUE=Seedling;
RA Yoon U.H., Kim Y.H.;
RT "Molecular cloning of the alpha-1,4-glucan protein synthase genes in
RT rice.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo; TISSUE=Seedling;
RA Yoon U.H., Kim Y.H.;
RT "Structural and expression analysis of germinating seed genes in Oryza
RT sativa L.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP PROTEIN SEQUENCE OF 152-165, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, DOMAIN, GLYCOSYLATION AT ARG-158, AND MUTAGENESIS OF
RP ASP-112; ARG-151; ARG-158 AND ARG-165.
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).
RN [12]
RP FUNCTION, SUBUNIT, AND GLYCOSYLATION.
RX PubMed=12011358; DOI=10.1104/pp.010720;
RA Langeveld S.M., Vennik M., Kottenhagen M., Van Wijk R., Buijk A.,
RA Kijne J.W., de Pater S.;
RT "Glucosylation activity and complex formation of two classes of reversibly
RT glycosylated polypeptides.";
RL Plant Physiol. 129:278-289(2002).
RN [13]
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 [14]
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).
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:12011358, ECO:0000269|PubMed:17182701,
CC ECO:0000269|PubMed:20057139, 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=22.8 uM for UDP-L-arabinofuranose {ECO:0000269|PubMed:20057139};
CC KM=45.4 uM for UDP-L-arabinopyranose {ECO:0000269|PubMed:20057139};
CC Vmax=0.688 umol/min/mg enzyme with UDP-L-arabinofuranose as substrate
CC {ECO:0000269|PubMed:20057139};
CC Vmax=0.269 umol/min/mg enzyme with UDP-L-arabinofuranose as substrate
CC {ECO:0000269|PubMed:20057139};
CC pH dependence:
CC Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:20057139};
CC -!- SUBUNIT: Heteromers with UAM2 and UAM3. {ECO:0000269|PubMed:12011358,
CC 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:0000269|PubMed:20149347}.
CC -!- PTM: Reversibly glycosylated in vitro at Arg-158 by UDP-glucose.
CC Reversibly glycosylated by UDP-xylose and UDP-galactose.
CC {ECO:0000269|PubMed:12011358, ECO:0000269|PubMed:17182701,
CC ECO:0000269|PubMed:20149347}.
CC -!- SIMILARITY: Belongs to the RGP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABF97477.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA09469.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF294725; AAG17438.1; -; mRNA.
DR EMBL; AJ011078; CAA09469.1; ALT_FRAME; mRNA.
DR EMBL; EU267966; ACA50488.1; -; mRNA.
DR EMBL; GQ848047; ADM86860.1; -; mRNA.
DR EMBL; AC090874; AAN08217.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF97476.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF97477.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008209; BAF12531.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS85190.1; -; Genomic_DNA.
DR EMBL; CM000140; EEE59464.1; -; Genomic_DNA.
DR EMBL; AK061813; BAG88123.1; -; mRNA.
DR EMBL; AK098933; BAG93819.1; -; mRNA.
DR RefSeq; XP_015631326.1; XM_015775840.1.
DR AlphaFoldDB; Q8H8T0; -.
DR BioGRID; 802430; 1.
DR STRING; 4530.OS03T0599800-01; -.
DR CAZy; GT75; Glycosyltransferase Family 75.
DR PaxDb; Q8H8T0; -.
DR PRIDE; Q8H8T0; -.
DR EnsemblPlants; Os03t0599800-01; Os03t0599800-01; Os03g0599800.
DR GeneID; 4333393; -.
DR Gramene; Os03t0599800-01; Os03t0599800-01; Os03g0599800.
DR KEGG; osa:4333393; -.
DR eggNOG; ENOG502QSDP; Eukaryota.
DR HOGENOM; CLU_061976_0_0_1; -.
DR InParanoid; Q8H8T0; -.
DR OMA; WIESWEE; -.
DR OrthoDB; 662486at2759; -.
DR BioCyc; MetaCyc:MON-15774; -.
DR BRENDA; 5.4.99.30; 4460.
DR PlantReactome; R-OSA-1119574; UDP-L-arabinose biosynthesis and transport.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q8H8T0; baseline and differential.
DR Genevisible; Q8H8T0; 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; Direct protein sequencing; Glycoprotein;
KW Golgi apparatus; Isomerase; Reference proteome.
FT CHAIN 1..364
FT /note="UDP-arabinopyranose mutase 1"
FT /id="PRO_0000410989"
FT MOTIF 110..112
FT /note="DXD motif"
FT /evidence="ECO:0000269|PubMed:20149347"
FT SITE 158
FT /note="Required for activity"
FT /evidence="ECO:0000269|PubMed:20149347"
FT SITE 165
FT /note="Required for activity"
FT /evidence="ECO:0000269|PubMed:20149347"
FT CARBOHYD 158
FT /note="N-linked (Glc...) arginine"
FT /evidence="ECO:0000269|PubMed:20149347"
FT MUTAGEN 112
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20149347"
FT MUTAGEN 151
FT /note="R->A: No effect on the activity."
FT /evidence="ECO:0000269|PubMed:20149347"
FT MUTAGEN 158
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20149347"
FT MUTAGEN 165
FT /note="R->A,K: Decreases activity 20-fold."
FT /evidence="ECO:0000269|PubMed:20149347"
FT CONFLICT 83
FT /note="A -> G (in Ref. 2; CAA09469)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 41349 MW; 8CB8E232A780934C CRC64;
MAGTVTVPSA SVPSTPLLKD ELDIVIPTIR NLDFLEMWRP FFQPYHLIIV QDGDPTKTIR
VPEGFDYELY NRNDINRILG PKASCISFKD SACRCFGYMV SKKKYVFTID DDCFVAKDPS
GKDINALEQH IKNLLSPSTP FFFNTLYDPY REGADFVRGY PFSLREGAKT AVSHGLWLNI
PDYDAPTQMV KPRERNSRYV DAVMTVPKGT LFPMCGMNLA FDRDLIGPAM YFGLMGDGQP
IGRYDDMWAG WCMKVICDHL SLGVKTGLPY IWHSKASNPF VNLKKEYKGI FWQEDIIPFF
QNATIPKECD TVQKCYLSLA EQVREKLGKI DPYFVKLADA MVTWIEAWDE LNPSTAAVEN
GKAK
