XOAT1_ORYSJ
ID XOAT1_ORYSJ Reviewed; 522 AA.
AC Q8S237; Q0JI16;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Xylan O-acetyltransferase 1 {ECO:0000303|PubMed:29569182};
DE EC=2.3.1.- {ECO:0000269|PubMed:29569182};
DE AltName: Full=Protein trichome birefringence-like 12 {ECO:0000303|PubMed:27864442};
DE Short=OsTBL12 {ECO:0000303|PubMed:27864442};
GN Name=XOAT1 {ECO:0000303|PubMed:29569182};
GN Synonyms=TBL12 {ECO:0000303|PubMed:29569182};
GN OrderedLocusNames=Os01g0830700 {ECO:0000312|EMBL:BAS75052.1},
GN LOC_Os01g61460 {ECO:0000305};
GN ORFNames=P0446G04.22 {ECO:0000312|EMBL:BAB89591.1};
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=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
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 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 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=39 uM for xylohexaose {ECO:0000269|PubMed:29569182};
CC Vmax=40.4 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 in roots, leaves and inflorescences.
CC {ECO:0000269|PubMed:29569182}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MH037015; AVR54505.1; -; mRNA.
DR EMBL; AP003252; BAB89591.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF06612.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS75052.1; -; Genomic_DNA.
DR EMBL; AK101671; BAG95179.1; -; mRNA.
DR RefSeq; XP_015618544.1; XM_015763058.1.
DR AlphaFoldDB; Q8S237; -.
DR SMR; Q8S237; -.
DR STRING; 4530.OS01T0830700-01; -.
DR PaxDb; Q8S237; -.
DR PRIDE; Q8S237; -.
DR EnsemblPlants; Os01t0830700-01; Os01t0830700-01; Os01g0830700.
DR EnsemblPlants; Os01t0830700-02; Os01t0830700-02; Os01g0830700.
DR GeneID; 4327430; -.
DR Gramene; Os01t0830700-01; Os01t0830700-01; Os01g0830700.
DR Gramene; Os01t0830700-02; Os01t0830700-02; Os01g0830700.
DR KEGG; osa:4327430; -.
DR eggNOG; ENOG502SJAQ; Eukaryota.
DR HOGENOM; CLU_020953_3_2_1; -.
DR InParanoid; Q8S237; -.
DR OMA; HISPQVW; -.
DR OrthoDB; 492414at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
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..522
FT /note="Xylan O-acetyltransferase 1"
FT /id="PRO_0000454025"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..522
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 111..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 245..247
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT MOTIF 494..497
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT COMPBIAS 135..153
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 494
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 497
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 286
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 171..222
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 193..258
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 202..499
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 414..495
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 522 AA; 59274 MW; 99335A09DCEFABA4 CRC64;
MANRRKFSQA GGGGGGGVFD PFGTKQAVSS LRKGGRLPVY VAGVFFVIFV IIMYGEDIRS
LTLDPIARAG TTPARIVEPV VTEERHVARV NPPRREVSSA EKAAALPLDV DERPKLATPT
PTEAAKEVPK VEKIRKPKKP KTTKKKPRKP RPAKKTVAAA AGGLLGVPET CDLSKGEWVF
DNTSYPLYRE EQCEFLTSQV TCMRNGRRDD TYQKWRWQPK DCSMPRFDAK LFMERLRGKR
FMFVGDSLNR NQWESMVCLV QSAMSPGKKY VTWEDQRVVF HAVEYNATVE FYWAPFLVES
NSDDPKIHSI QHRIIKADAI AAHAQNWRGV DYLVFNTYIW WMNTLNMKIM RPGGQSWEEH
DEVVRIEAYR KVLTTWASWV NDNIDPARTS VFFMSISPLH ISPEVWGNPG GIRCAKETMP
LLNWHGPIWL GTDWDMFHAA ANVSRTAATR VPITFVDVTT MSERRKDGHT SVHTIRQGKV
LTPEQQADPG TYADCIHWCL PGVPDIWNLI LYTRIMSRPQ LV
