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UDP-arabinopyranose mutase 1 (OsUAM1) (EC 5.4.99.30) (Reversibly glycosylated polypeptide 1) (UDP-L-arabinose mutase 1)

 RGP1_ORYSJ              Reviewed;         364 AA.
Q8H8T0; A0A0P0W0V3; O82705; Q10H67; Q9FUN9;
28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
31-JAN-2018, entry version 97.
RecName: Full=UDP-arabinopyranose mutase 1 {ECO:0000303|PubMed:17182701};
Short=OsUAM1 {ECO:0000303|PubMed:17182701};
EC=5.4.99.30 {ECO:0000269|PubMed:17182701, ECO:0000269|PubMed:20057139, ECO:0000269|PubMed:20149347};
AltName: Full=Reversibly glycosylated polypeptide 1 {ECO:0000303|PubMed:17182701};
AltName: Full=UDP-L-arabinose mutase 1 {ECO:0000305};
Name=UAM1 {ECO:0000303|PubMed:17182701};
Synonyms=RGP1 {ECO:0000303|PubMed:17182701};
OrderedLocusNames=Os03g0599800 {ECO:0000312|EMBL:BAS85190.1},
LOC_Os03g40270 {ECO:0000312|EMBL:ABF97476.1};
ORFNames=OJ1523_A02.1 {ECO:0000312|EMBL:AAN08217.1},
OsJ_11657 {ECO:0000312|EMBL:EEE59464.1};
Oryza sativa subsp. japonica (Rice).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
NCBI_TaxID=39947;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Gupta P., Raghuvanshi S., Tyagi A.K.;
"PCR-Amplification and cloning of the coding region of a cDNA for a
reversibly glycosylated polypeptide from rice with possible
involvement in the biosynthesis of glucans.";
J. Plant Biochem. Biotechnol. 9:99-102(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Lemont;
Bligh H.F., Jackson D.A.;
"Characterization of reverse glycosylating proteins 1 and 2 of Oryza
sativa.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Ilpoombyeo; TISSUE=Seedling;
Yoon U.H., Kim Y.H.;
"Molecular cloning of the alpha-1,4-glucan protein synthase genes in
rice.";
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Ilpoombyeo; TISSUE=Seedling;
Yoon U.H., Kim Y.H.;
"Structural and expression analysis of germinating seed genes in Oryza
sativa L.";
Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=16109971; DOI=10.1101/gr.3869505;
The rice chromosome 3 sequencing consortium;
Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R.,
Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L.,
Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S., Johri S.,
Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S.,
Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J.,
de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H.,
Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F.,
Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A.,
Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J.,
Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L.,
Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A.,
Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W.,
Lee H.R., Jiang J., Jackson S.;
"Sequence, annotation, and analysis of synteny between rice chromosome
3 and diverged grass species.";
Genome Res. 15:1284-1291(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=16100779; DOI=10.1038/nature03895;
International rice genome sequencing project (IRGSP);
"The map-based sequence of the rice genome.";
Nature 436:793-800(2005).
[7]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=18089549; DOI=10.1093/nar/gkm978;
The rice annotation project (RAP);
"The rice annotation project database (RAP-DB): 2008 update.";
Nucleic Acids Res. 36:D1028-D1033(2008).
[8]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=24280374; DOI=10.1186/1939-8433-6-4;
Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H.,
McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
Buell C.R., Matsumoto T.;
"Improvement of the Oryza sativa Nipponbare reference genome using
next generation sequence and optical map data.";
Rice 6:4-4(2013).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H.,
Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
Samudrala R., Wang J., Wong G.K.-S., Yang H.;
"The genomes of Oryza sativa: a history of duplications.";
PLoS Biol. 3:266-281(2005).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Nipponbare;
PubMed=12869764; DOI=10.1126/science.1081288;
The rice full-length cDNA consortium;
"Collection, mapping, and annotation of over 28,000 cDNA clones from
japonica rice.";
Science 301:376-379(2003).
[11]
PROTEIN SEQUENCE OF 152-165, IDENTIFICATION BY MASS SPECTROMETRY,
FUNCTION, CATALYTIC ACTIVITY, DOMAIN, GLYCOSYLATION AT ARG-158, AND
MUTAGENESIS OF ASP-112; ARG-151; ARG-158 AND ARG-165.
PubMed=20149347; DOI=10.1016/j.carres.2010.01.008;
Konishi T., Ohnishi-Kameyama M., Funane K., Miyazaki Y., Konishi T.,
Ishii T.;
"An arginyl residue in rice UDP-L-arabinopyranose mutase is required
for catalytic activity and autoglycosylation.";
Carbohydr. Res. 345:787-791(2010).
[12]
FUNCTION, SUBUNIT, AND GLYCOSYLATION.
PubMed=12011358; DOI=10.1104/pp.010720;
Langeveld S.M., Vennik M., Kottenhagen M., Van Wijk R., Buijk A.,
Kijne J.W., de Pater S.;
"Glucosylation activity and complex formation of two classes of
reversibly glycosylated polypeptides.";
Plant Physiol. 129:278-289(2002).
[13]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, GLYCOSYLATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17182701; DOI=10.1093/glycob/cwl081;
Konishi T., Takeda T., Miyazaki Y., Ohnishi-Kameyama M., Hayashi T.,
O'Neill M.A., Ishii T.;
"A plant mutase that interconverts UDP-L-arabinofuranose and UDP-L-
arabinopyranose.";
Glycobiology 17:345-354(2007).
[14]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=20057139; DOI=10.1271/bbb.90619;
Konishi T., Miyazaki Y., Yamakawa S., Iwai H., Satoh S., Ishii T.;
"Purification and biochemical characterization of recombinant rice
UDP-L-arabinopyranose mutase generated in insect cells.";
Biosci. Biotechnol. Biochem. 74:191-194(2010).
-!- FUNCTION: UDP-L-arabinose mutase involved in the biosynthesis of
cell wall non-cellulosic polysaccharides. Catalyzes the
interconvertion of UDP-L-arabinopyranose (UDP-Arap) and UDP-L-
arabinofuranose (UDP-Araf). Preferentially catalyzes the formation
of UDP-Arap from UDP-Araf. At thermodynamic equilibrium in vitro
the ratio of the pyranose form over the furanose form is 90:10. Is
probably active as heteromer in vivo.
{ECO:0000269|PubMed:12011358, ECO:0000269|PubMed:17182701,
ECO:0000269|PubMed:20057139, ECO:0000269|PubMed:20149347}.
-!- CATALYTIC ACTIVITY: UDP-beta-L-arabinofuranose = UDP-beta-L-
arabinopyranose. {ECO:0000269|PubMed:17182701,
ECO:0000269|PubMed:20057139, ECO:0000269|PubMed:20149347}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:17182701};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17182701};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=22.8 uM for UDP-L-arabinofuranose
{ECO:0000269|PubMed:20057139};
KM=45.4 uM for UDP-L-arabinopyranose
{ECO:0000269|PubMed:20057139};
Vmax=0.688 umol/min/mg enzyme with UDP-L-arabinofuranose as
substrate {ECO:0000269|PubMed:20057139};
Vmax=0.269 umol/min/mg enzyme with UDP-L-arabinofuranose as
substrate {ECO:0000269|PubMed:20057139};
pH dependence:
Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:20057139};
-!- SUBUNIT: Heteromers with UAM2 and UAM3.
{ECO:0000269|PubMed:12011358, ECO:0000269|PubMed:17182701}.
-!- SUBCELLULAR LOCATION: Golgi apparatus
{ECO:0000250|UniProtKB:Q9SRT9}.
-!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
{ECO:0000269|PubMed:20149347}.
-!- PTM: Reversibly glycosylated in vitro at Arg-158 by UDP-glucose.
Reversibly glycosylated by UDP-xylose and UDP-galactose.
{ECO:0000269|PubMed:12011358, ECO:0000269|PubMed:17182701,
ECO:0000269|PubMed:20149347}.
-!- SIMILARITY: Belongs to the RGP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABF97477.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA09469.1; Type=Frameshift; Positions=315; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF294725; AAG17438.1; -; mRNA.
EMBL; AJ011078; CAA09469.1; ALT_FRAME; mRNA.
EMBL; EU267966; ACA50488.1; -; mRNA.
EMBL; GQ848047; ADM86860.1; -; mRNA.
EMBL; AC090874; AAN08217.1; -; Genomic_DNA.
EMBL; DP000009; ABF97476.1; -; Genomic_DNA.
EMBL; DP000009; ABF97477.1; ALT_INIT; Genomic_DNA.
EMBL; AP008209; BAF12531.1; -; Genomic_DNA.
EMBL; AP014959; BAS85190.1; -; Genomic_DNA.
EMBL; CM000140; EEE59464.1; -; Genomic_DNA.
EMBL; AK061813; BAG88123.1; -; mRNA.
EMBL; AK098933; BAG93819.1; -; mRNA.
RefSeq; XP_015631326.1; XM_015775840.1.
UniGene; Os.5039; -.
SMR; Q8H8T0; -.
STRING; 39947.LOC_Os03g40270.1; -.
CAZy; GT75; Glycosyltransferase Family 75.
PaxDb; Q8H8T0; -.
PRIDE; Q8H8T0; -.
EnsemblPlants; OS03T0599800-01; OS03T0599800-01; OS03G0599800.
GeneID; 4333393; -.
Gramene; OS03T0599800-01; OS03T0599800-01; OS03G0599800.
KEGG; osa:4333393; -.
eggNOG; ENOG410IHTP; Eukaryota.
eggNOG; ENOG411144T; LUCA.
HOGENOM; HOG000234443; -.
InParanoid; Q8H8T0; -.
KO; K13379; -.
OMA; TIPKECT; -.
OrthoDB; EOG09360C9G; -.
BioCyc; MetaCyc:MONOMER-15774; -.
BRENDA; 5.4.99.30; 4460.
Proteomes; UP000059680; Chromosome 3.
ExpressionAtlas; Q8H8T0; baseline and differential.
Genevisible; Q8H8T0; OS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
GO; GO:0016866; F:intramolecular transferase activity; IDA:UniProtKB.
GO; GO:0052691; F:UDP-arabinopyranose mutase activity; IBA:GO_Central.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
GO; GO:0009832; P:plant-type cell wall biogenesis; IBA:GO_Central.
GO; GO:0033356; P:UDP-L-arabinose metabolic process; IBA:GO_Central.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR004901; RGP.
InterPro; IPR037595; RGP_fam.
PANTHER; PTHR31682; PTHR31682; 1.
Pfam; PF03214; RGP; 1.
PIRSF; PIRSF016429; UPTG; 1.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
Cell wall biogenesis/degradation; Complete proteome;
Direct protein sequencing; Glycoprotein; Golgi apparatus; Isomerase;
Reference proteome.
CHAIN 1 364 UDP-arabinopyranose mutase 1.
/FTId=PRO_0000410989.
MOTIF 110 112 DXD motif. {ECO:0000269|PubMed:20149347}.
SITE 158 158 Required for activity.
{ECO:0000269|PubMed:20149347}.
SITE 165 165 Required for activity.
{ECO:0000269|PubMed:20149347}.
CARBOHYD 158 158 N-linked (Glc...) arginine.
{ECO:0000269|PubMed:20149347}.
MUTAGEN 112 112 D->N: Loss of activity.
{ECO:0000269|PubMed:20149347}.
MUTAGEN 151 151 R->A: No effect on the activity.
{ECO:0000269|PubMed:20149347}.
MUTAGEN 158 158 R->A: Loss of activity.
{ECO:0000269|PubMed:20149347}.
MUTAGEN 165 165 R->A,K: Decreases activity 20-fold.
{ECO:0000269|PubMed:20149347}.
CONFLICT 83 83 A -> G (in Ref. 2; CAA09469).
{ECO:0000305}.
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


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