XOAT5_ORYSJ
ID XOAT5_ORYSJ Reviewed; 531 AA.
AC A0A0P0WL81; Q0DIX3; Q5W782;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Xylan O-acetyltransferase 5 {ECO:0000303|PubMed:29569182};
DE EC=2.3.1.- {ECO:0000269|PubMed:29569182};
DE AltName: Full=Protein trichome birefringence-like 13 {ECO:0000303|PubMed:27864442};
DE Short=OsTBL13 {ECO:0000303|PubMed:27864442};
GN Name=XOAT5 {ECO:0000303|PubMed:29569182};
GN Synonyms=TBL13 {ECO:0000303|PubMed:27864442};
GN OrderedLocusNames=Os05g0354400 {ECO:0000312|EMBL:BAS93559.1},
GN LOC_Os05g28630 {ECO:0000305};
GN ORFNames=OJ1537_B05.7 {ECO:0000312|EMBL:AAV43889.1};
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 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=350 uM for xylohexaose {ECO:0000269|PubMed:29569182};
CC Vmax=71.3 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 stems.
CC {ECO:0000269|PubMed:29569182}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV43889.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF17200.1; Type=Erroneous gene model prediction; Evidence={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; MH037019; AVR54509.1; -; mRNA.
DR EMBL; AC104281; AAV43889.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008211; BAF17200.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014961; BAS93559.1; -; Genomic_DNA.
DR RefSeq; XP_015640655.1; XM_015785169.1.
DR AlphaFoldDB; A0A0P0WL81; -.
DR SMR; A0A0P0WL81; -.
DR STRING; 4530.OS05T0354400-01; -.
DR PaxDb; A0A0P0WL81; -.
DR EnsemblPlants; Os05t0354400-01; Os05t0354400-01; Os05g0354400.
DR GeneID; 4338512; -.
DR Gramene; Os05t0354400-01; Os05t0354400-01; Os05g0354400.
DR KEGG; osa:4338512; -.
DR eggNOG; ENOG502QUBK; Eukaryota.
DR HOGENOM; CLU_020953_3_2_1; -.
DR OMA; PEMKILH; -.
DR OrthoDB; 492414at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; A0A0P0WL81; baseline and differential.
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..531
FT /note="Xylan O-acetyltransferase 5"
FT /id="PRO_0000454029"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..531
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 50..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 242..244
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT MOTIF 492..495
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT COMPBIAS 122..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 244
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 492
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 495
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 168..219
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 190..255
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 199..497
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 413..493
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 531 AA; 58841 MW; 1003F455831A7FEE CRC64;
MRIPRRKGGA GPLVGAPSRR AQVAAVFALA LLLGVSVLYD SAHIAASLRR HGVGGGGSSG
GGGGGGGDGA RAYTNTKLSA TTEEAEAEAA EVRSPPAQGV ESAVEATDRG EAPPEQPVAA
DSGASSAETP PSLLEQVTET PPPSPSSSSA AAAAAEAQVG GDHGGESCDV YKGRWVYDEA
NAPLYKESAC EFLTEQVTCM RNGRRDDDYQ KWRWQPDGCD LPRFDAKLLL EKLRNKRLMF
VGDSLNRNQW ESMVCLVQSE APWEKKSLVK NDSLNVFRLE EYNATIEFYW SPFLVESNSD
DPNMHSIVDR IIKPTSIAKH AANWEGVDYL IFNTYIWWMN TPEMKILHGG SFSKKPVKYD
EMERVAAYRK VLKTWSRWVE KHVDPKRSTV FFMSVSPVHM QSEGWGKPDA IKCFSETQPA
INYTKKLEVG TDWDLFSTAH HVTKAMKRVP VHFINITALS EIRKDAHTSV NTLRQGKLLT
KEQKANPRKF ADCIHWCLPG LPDTWNEFIY GHIVSSPQRR PVEPIENQPQ R
