XOAT2_ORYSJ
ID XOAT2_ORYSJ Reviewed; 500 AA.
AC B9FKP6; A0A0P0WNF8; Q0DHF2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Xylan O-acetyltransferase 2 {ECO:0000303|PubMed:29569182};
DE EC=2.3.1.- {ECO:0000269|PubMed:29569182};
DE AltName: Full=Protein trichome birefringence-like 11 {ECO:0000303|PubMed:27864442};
DE Short=OsTBL11 {ECO:0000303|PubMed:27864442};
GN Name=XOAT2 {ECO:0000303|PubMed:29569182};
GN Synonyms=TBL11 {ECO:0000303|PubMed:27864442};
GN OrderedLocusNames=Os05g0470000 {ECO:0000312|EMBL:BAS94482.1},
GN LOC_Os05g39350 {ECO:0000305};
GN ORFNames=OsJ_18877 {ECO:0000312|EMBL:EEE64048.1};
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,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(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=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 [5]
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 [6]
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 [7]
RP GENE FAMILY, AND NOMENCLATURE.
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 Catalyzes the 2-O-acetylation of xylan, followed by nonenzymatic acetyl
CC migration to the O-3 position, resulting in products that are
CC monoacetylated at both O-2 and O-3 positions (By similarity).
CC {ECO:0000250|UniProtKB:Q9LY46, ECO:0000269|PubMed:29569182}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=210 uM for xylohexaose {ECO:0000269|PubMed:29569182};
CC Vmax=38.2 pmol/min/mg enzyme with xylohexaose as substrate
CC {ECO:0000269|PubMed:29569182};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q2QYU2}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots and leaves.
CC {ECO:0000269|PubMed:29569182}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF17721.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; MH037016; AVR54506.1; -; mRNA.
DR EMBL; AP008211; BAF17721.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014961; BAS94482.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE64048.1; -; Genomic_DNA.
DR RefSeq; XP_015637498.1; XM_015782012.1.
DR AlphaFoldDB; B9FKP6; -.
DR SMR; B9FKP6; -.
DR STRING; 4530.OS05T0470000-01; -.
DR PaxDb; B9FKP6; -.
DR PRIDE; B9FKP6; -.
DR EnsemblPlants; Os05t0470000-01; Os05t0470000-01; Os05g0470000.
DR GeneID; 4339070; -.
DR Gramene; Os05t0470000-01; Os05t0470000-01; Os05g0470000.
DR KEGG; osa:4339070; -.
DR eggNOG; ENOG502SJAQ; Eukaryota.
DR HOGENOM; CLU_020953_3_2_1; -.
DR OMA; CEYLTAQ; -.
DR OrthoDB; 611228at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISS: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: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;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..500
FT /note="Xylan O-acetyltransferase 2"
FT /id="PRO_0000454026"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 26..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..500
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 84..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 218..220
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT MOTIF 467..470
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT COMPBIAS 102..116
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 467
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 470
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 143..194
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 165..231
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 174..472
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 388..468
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 500 AA; 56368 MW; 3DF42F435F583B59 CRC64;
MGLPGRRNPL LSARRAAASL RRSRRLPVYV AAVFFVASVL LMFRDEILYL TTARSPSSSL
PTTGGSAGGA GLARKEELVS VNKPVLLGHG GKPEKHHSVT ERHRPKVSAK RRPNKKAAKA
ARKKFMASPS VAAGAEVNVP ETCNLSKGKW VFDNATYPLY REQECEYLTA QVTCTRNGRR
DDGYQKWRWQ PRDCDLPLAF DARLFMERLR GKRLMFVGDS LNRNQWESMV CLVRPALSPG
KSYVTWWDGQ RVVLHAWEYN ATVEFYWAPF LVESNSDDPK AHSIRDRVIK PEAIAAHAGD
WVGVDYLVFN TYIWWMNTVN MKVVRPTGKT WEEYDEVGRI EAYRRVLDTW ATWVNDNVDP
ARTSVFFMSV SPLHISPEAW GNPGGVRCAK EDAPVQNWHG PLWLGTDWDM FRAARNASRA
AGRVPVTFVD VTAMSELRKD GHTSVHTIRQ GRVLTPEQQA DPATYADCIH WCLPGVPDVW
NLMLYARILS RPPAAAGHVA
