XOATD_ORYSJ
ID XOATD_ORYSJ Reviewed; 502 AA.
AC Q2QYU2; Q0IQQ7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Xylan O-acetyltransferase 13 {ECO:0000303|PubMed:29569182};
DE EC=2.3.1.- {ECO:0000269|PubMed:29569182};
DE AltName: Full=Protein trichome birefringence-like 1 {ECO:0000303|PubMed:27864442};
DE Short=OsTBL1 {ECO:0000303|PubMed:27864442};
GN Name=XOAT13 {ECO:0000303|PubMed:29569182};
GN Synonyms=TBL1 {ECO:0000303|PubMed:27864442};
GN OrderedLocusNames=Os12g0106300 {ECO:0000312|EMBL:BAT15503.1},
GN LOC_Os12g01560 {ECO:0000312|EMBL:ABA95618.1};
GN ORFNames=OsJ_34935 {ECO:0000312|EMBL:EEE52607.1};
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=29569182; DOI=10.1007/s00425-018-2882-1;
RA Zhong R., Cui D., Dasher R.L., Ye Z.H.;
RT "Biochemical characterization of rice xylan O-acetyltransferases.";
RL Planta 247:1489-1498(2018).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, GENE FAMILY,
RP NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RX PubMed=27864442; DOI=10.1104/pp.16.01618;
RA Gao Y., He C., Zhang D., Liu X., Xu Z., Tian Y., Liu X.H., Zang S.,
RA Pauly M., Zhou Y., Zhang B.;
RT "Two trichome birefringence-like proteins mediate xylan acetylation, which
RT is essential for leaf blight resistance in rice.";
RL Plant Physiol. 173:470-481(2017).
CC -!- FUNCTION: Xylan acetyltransferase required for 2-O- and 3-O-
CC monoacetylation of xylosyl residues in xylan (PubMed:29569182,
CC PubMed:27864442). Catalyzes the 2-O-acetylation of xylan, followed by
CC nonenzymatic acetyl migration to the O-3 position, resulting in
CC products that are monoacetylated at both O-2 and O-3 positions (By
CC similarity). {ECO:0000250|UniProtKB:Q9LY46,
CC ECO:0000269|PubMed:27864442, ECO:0000269|PubMed:29569182}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.56 mM for xylohexaose {ECO:0000269|PubMed:29569182};
CC KM=4.98 mM for xylopentaose {ECO:0000269|PubMed:27864442};
CC Vmax=47.4 pmol/min/mg enzyme with xylohexaose as substrate
CC {ECO:0000269|PubMed:29569182};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:29569182}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Stunted growth and reduced plant height
CC (PubMed:27864442). The double mutants tbl1 and tbl2 exhibit increased
CC susceptibility to the bacterial pathogen Xanthomonas oryzae pv oryzae
CC (Xoo) (PubMed:27864442). {ECO:0000269|PubMed:27864442}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
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DR EMBL; MH037027; AVR54517.1; -; mRNA.
DR EMBL; DP000011; ABA95618.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT15503.1; -; Genomic_DNA.
DR EMBL; CM000149; EEE52607.1; -; Genomic_DNA.
DR EMBL; AK060755; BAG87557.1; -; mRNA.
DR RefSeq; XP_015618634.1; XM_015763148.1.
DR AlphaFoldDB; Q2QYU2; -.
DR SMR; Q2QYU2; -.
DR STRING; 4530.OS12T0106300-01; -.
DR PaxDb; Q2QYU2; -.
DR PRIDE; Q2QYU2; -.
DR EnsemblPlants; Os12t0106300-01; Os12t0106300-01; Os12g0106300.
DR GeneID; 4351267; -.
DR Gramene; Os12t0106300-01; Os12t0106300-01; Os12g0106300.
DR KEGG; osa:4351267; -.
DR eggNOG; ENOG502SHUB; Eukaryota.
DR HOGENOM; CLU_020953_3_1_1; -.
DR InParanoid; Q2QYU2; -.
DR OMA; KQNCYGE; -.
DR OrthoDB; 886886at2759; -.
DR Proteomes; UP000007752; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016413; F:O-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:1990538; F:xylan O-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1990937; P:xylan acetylation; IDA:UniProtKB.
DR InterPro; IPR026057; PC-Esterase.
DR InterPro; IPR029962; TBL.
DR InterPro; IPR025846; TBL_N.
DR PANTHER; PTHR32285; PTHR32285; 1.
DR Pfam; PF13839; PC-Esterase; 1.
DR Pfam; PF14416; PMR5N; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Membrane; Plant defense;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..502
FT /note="Xylan O-acetyltransferase 13"
FT /id="PRO_0000454036"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 54..76
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..502
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 226..228
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT MOTIF 478..481
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT ACT_SITE 228
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 478
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 481
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 152..203
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 174..239
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 183..483
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 399..479
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 502 AA; 57631 MW; 8C515124CDDEE851 CRC64;
MWSALFSHLR EVHKRSGVKE EKLIMKSPPA AGEAGCHKPQ ATATNKMTVL QSPLGLRTIL
TSLVAFFIVV SSVSLLFDRG QDAQAQLAVE QHQHQEVLLK QKPASAAVGE QKSVVVDQSS
LRSQEAQVQW TSELQDVATD SGDGGFDGEE DCNWSLGRWV YDNASRPLYS GLKCSFIFDE
VACDKYGRND TKYQHWRWQP HGCNLPRFNA TKFLEKLRNK RLVFVGDSVN RNQWVSMVCM
VEHFIPDGRK MRVYNGSLIS FKAFEYNATI DFYWSPLLLE SNSDNPIIHR VEYRIIRADR
IEKHANVWKD ADFIVFNSYL WWRKQRDGMM MKVMYGSFED GDAKLDEVQM VDGYEIALKK
LTEYLGANIN KNKTRIFFAG SSPAHSWASN WGGDDNNKCL NETEPIQIED YRSATTDYGM
MDKAKEIFGT LEPKGIHVQI LNITQLSEYR KDAHPTIFRR QYVPLTKEQI ANPSIYADCT
HWCLPGVPDV WNEFLYAYIM HK
