XYN3_ARATH
ID XYN3_ARATH Reviewed; 752 AA.
AC F4JG10; Q8GYW5; Q9C5T7; Q9SYE3;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Endo-1,4-beta-xylanase 3 {ECO:0000303|PubMed:12154138};
DE Short=AtXyn3 {ECO:0000303|PubMed:12154138};
DE Short=Xylan endohydrolase 3 {ECO:0000303|PubMed:12154138};
DE Short=Xylanase 3 {ECO:0000303|PubMed:12154138};
DE EC=3.2.1.8 {ECO:0000255|PROSITE-ProRule:PRU01096};
GN Name=XYN3 {ECO:0000303|PubMed:12154138};
GN OrderedLocusNames=At4g08160 {ECO:0000312|Araport:AT4G08160};
GN ORFNames=F9M13.1 {ECO:0000312|EMBL:AAD27896.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-232, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12154138; DOI=10.1093/pcp/pcf088;
RA Suzuki M., Kato A., Nagata N., Komeda Y.;
RT "A xylanase, AtXyn1, is predominantly expressed in vascular bundles, and
RT four putative xylanase genes were identified in the Arabidopsis thaliana
RT genome.";
RL Plant Cell Physiol. 43:759-767(2002).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=16103214; DOI=10.1101/gad.1331305;
RA Kubo M., Udagawa M., Nishikubo N., Horiguchi G., Yamaguchi M., Ito J.,
RA Mimura T., Fukuda H., Demura T.;
RT "Transcription switches for protoxylem and metaxylem vessel formation.";
RL Genes Dev. 19:1855-1860(2005).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=15618413; DOI=10.1104/pp.104.055145;
RA Sawa S., Demura T., Horiguchi G., Kubo M., Fukuda H.;
RT "The ATE genes are responsible for repression of transdifferentiation into
RT xylem cells in Arabidopsis.";
RL Plant Physiol. 137:141-148(2005).
CC -!- FUNCTION: Binds to and hydrolyzes insoluble and soluble xylan
CC substrates. {ECO:0000250|UniProtKB:A3DH97}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000255|PROSITE-ProRule:PRU01096};
CC -!- PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-
CC ProRule:PRU01096}.
CC -!- TISSUE SPECIFICITY: Confined to immature xylems.
CC {ECO:0000269|PubMed:15618413, ECO:0000269|PubMed:16103214}.
CC -!- DEVELOPMENTAL STAGE: Observed in maturing tracheary elements (TE) in
CC the root maturation zone. {ECO:0000269|PubMed:15618413}.
CC -!- DOMAIN: The GH10 domain binds to xylan. {ECO:0000250|UniProtKB:A3DH97}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000255|PROSITE-ProRule:PRU01096}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27896.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81152.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006267; AAD27896.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161510; CAB81152.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82599.1; -; Genomic_DNA.
DR EMBL; AK117349; BAC42019.1; -; mRNA.
DR EMBL; BT005962; AAO64897.1; -; mRNA.
DR EMBL; AB057770; BAB39757.1; -; mRNA.
DR PIR; E85080; E85080.
DR RefSeq; NP_192556.2; NM_116885.4.
DR AlphaFoldDB; F4JG10; -.
DR SMR; F4JG10; -.
DR STRING; 3702.AT4G08160.1; -.
DR CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR PaxDb; F4JG10; -.
DR PRIDE; F4JG10; -.
DR ProteomicsDB; 242406; -.
DR EnsemblPlants; AT4G08160.1; AT4G08160.1; AT4G08160.
DR GeneID; 826365; -.
DR Gramene; AT4G08160.1; AT4G08160.1; AT4G08160.
DR KEGG; ath:AT4G08160; -.
DR Araport; AT4G08160; -.
DR TAIR; locus:2128833; AT4G08160.
DR eggNOG; ENOG502QSCW; Eukaryota.
DR InParanoid; F4JG10; -.
DR OMA; HAYGIIN; -.
DR OrthoDB; 829814at2759; -.
DR UniPathway; UPA00114; -.
DR PRO; PR:F4JG10; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JG10; baseline and differential.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; ISS:TAIR.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF02018; CBM_4_9; 2.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Repeat; Xylan degradation.
FT CHAIN 1..752
FT /note="Endo-1,4-beta-xylanase 3"
FT /id="PRO_0000445197"
FT DOMAIN 26..163
FT /note="CBM-cenC 1"
FT /evidence="ECO:0000255"
FT DOMAIN 197..344
FT /note="CBM-cenC 2"
FT /evidence="ECO:0000255"
FT DOMAIN 397..692
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 526
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 627
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT CONFLICT 54
FT /note="D -> N (in Ref. 3; BAC42019 and 4; AAO64897)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="I -> V (in Ref. 3; BAC42019 and 4; AAO64897)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="A -> V (in Ref. 3; BAC42019 and 4; AAO64897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 752 AA; 84552 MW; 098416F492C1DBF9 CRC64;
MEKNTNTNHT SDDNNDKNHT NEEQEKIILN PNFEDGLNNW TGRACKIVLH ESMDSGKIVP
LSGKVFAAAT QRKDTWNGIQ QEISGRFRRK RVYEVTAVVR IFGNNVTSAT VQATLWVLNA
NKREQYIVIA NVQATDKNWV ELKGKFVIHG SPSRVILYLE GPPPRADILL NSLVVQHAKR
NRPSPPPFYE NPGFGVNIVE NSEVLDGGTK PWFTLGNCKL SVGQGAPRTL PPMARDTLGP
HKPLGGNYIV VTNRTQTWMG PAQMITDKIK LFLTYQISAW VKLGVGVSGS SMSPQNVNIA
LSVDNQWVNG GQVEVTVGDT WHEIAGSFRL EKQPQNVMVY VQGPGAGIDL MIAALQIFPV
DRRERVRCLK RQVDEVRKRD IVLKFSGLND DESFDLFPYI VKVKQTYNSF PVGTCINRTD
IDNEDFVDFF TKNFNWAVFG NELKWYATEA ERGKVNYQDA DDMLDLCIGN NINVRGHCIF
WEVESTVQPW VRQLNKTDLM NAVQKRLTDL LTRYKGKFKH YDVNNEMLHG SFYQDRLGKG
VRALMFNIAH KLDPSPLLFV NDYHVEDGDD PRSSPEKYIK LVLDLEAQGA TVGGIGIQGH
IDSPVGAIVC SALDMLSVLG RPIWFTELDV SSSNEYVRGE DLEVMLWEAF AHPSVEGIML
WGFWELSMSR ENANLVEGEG EVNEAGKRFL EVKQEWLSHA YGIINDESEF TFRGYHGTYA
VEICTPAGIV LKTFVVEKGD TPLVISIDLS SL
