XOAT7_ORYSJ
ID XOAT7_ORYSJ Reviewed; 605 AA.
AC Q0D3C8; A0A0P0XAF8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Xylan O-acetyltransferase 7 {ECO:0000303|PubMed:29569182};
DE EC=2.3.1.- {ECO:0000269|PubMed:29569182};
DE AltName: Full=Protein trichome birefringence-like 14 {ECO:0000303|PubMed:27864442};
DE Short=OsTBL14 {ECO:0000303|PubMed:27864442};
GN Name=XOAT7 {ECO:0000303|PubMed:29569182};
GN Synonyms=TBL14 {ECO:0000303|PubMed:27864442};
GN OrderedLocusNames=Os07g0693600 {ECO:0000312|EMBL:BAT03359.1},
GN LOC_Os07g49280 {ECO:0000305};
GN ORFNames=OsJ_25693 {ECO:0000312|EMBL:EAZ41191.1};
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=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 [3]
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 [4]
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 [5]
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=60 uM for xylohexaose {ECO:0000269|PubMed:29569182};
CC Vmax=37.7 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}.
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DR EMBL; MH037021; AVR54511.1; -; mRNA.
DR EMBL; AP014963; BAT03359.1; -; Genomic_DNA.
DR EMBL; CM000144; EAZ41191.1; -; Genomic_DNA.
DR RefSeq; XP_015646517.1; XM_015791031.1.
DR AlphaFoldDB; Q0D3C8; -.
DR SMR; Q0D3C8; -.
DR STRING; 4530.OS07T0693600-01; -.
DR PaxDb; Q0D3C8; -.
DR PRIDE; Q0D3C8; -.
DR EnsemblPlants; Os07t0693600-01; Os07t0693600-01; Os07g0693600.
DR GeneID; 4344387; -.
DR Gramene; Os07t0693600-01; Os07t0693600-01; Os07g0693600.
DR KEGG; osa:4344387; -.
DR eggNOG; ENOG502QUBK; Eukaryota.
DR HOGENOM; CLU_020953_3_2_1; -.
DR InParanoid; Q0D3C8; -.
DR OMA; METQPIV; -.
DR OrthoDB; 492414at2759; -.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
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..605
FT /note="Xylan O-acetyltransferase 7"
FT /id="PRO_0000454031"
FT TOPO_DOM 1..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 125..145
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..605
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 86..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 319..321
FT /note="GDS motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT MOTIF 579..582
FT /note="DXXH motif"
FT /evidence="ECO:0000305|PubMed:29569182"
FT ACT_SITE 321
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 579
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT ACT_SITE 582
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 243..296
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 267..332
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 276..584
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
FT DISULFID 499..580
FT /evidence="ECO:0000250|UniProtKB:Q9LY46"
SQ SEQUENCE 605 AA; 68270 MW; BFD28C5A9AB2A4FF CRC64;
MKKKKNGMGA AADRGRLLAL AHHDKLNPTK PSEAQRRFKP SILLLLGSSL PRLVPPLPSS
FLPVVIKQTE FHQRWLVGDL NPPPPPCHLL PIQGQGQMQM QQRRKPPPAA APVAAKQPSP
RRTPGPLSFA GALLSLLVVA TFLYINDHGN MMPPHASPDP DLRLLQEAAH QKVNSILLSR
HAPAPPPRTN TNTSSSDQHL RLINIPMSSD LDLELGGNST SSSGVEIQFE QQQQQEEKNL
RGCELYKGRW VYDAAGREAP LYRESECGFL TEQVTCMRNG RRDDSYQRWR WQPEGCDLPS
FDARALLERL RNKRMMFVGD SLNRNQWESM VCLVQSAIPY GQKTLTKFVN NGSLNVFRAH
EYNATVEFYW APFLVQSNSD DPQVHSVRDR VIAWRSIAKH AANWKGVHYL VFNTYIWWLN
NFQIKVLKSR GAPFAGSGGW SSRYALVDRA IAYREVLKTW AKWVDRRIDP NKTHVFFMAM
SPNHFMPEAW GGSAGAVKCA METQPIVNRT SGGLDIGTDW RLHGVARGVL RSMRRVGVRF
VDITALSELR KDAHTSVHTL RQGKLLTPEQ QADPRTYADC IHWCLPGLPD TWNHFLYAHI
VAHAA
