ID   XYN5L_ARATH             Reviewed;         570 AA.
AC   Q84WT5; O82111; Q9M070;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 143.
DE   RecName: Full=Endo-1,4-beta-xylanase 5-like {ECO:0000305};
DE            Short=AtXyn5-like {ECO:0000305};
DE            Short=Xylan endohydrolase 5-like {ECO:0000305};
DE            Short=Xylanase 5-like {ECO:0000305};
DE            EC=3.2.1.8 {ECO:0000255|PROSITE-ProRule:PRU01096};
DE   Flags: Precursor;
GN   OrderedLocusNames=At4g33820 {ECO:0000312|Araport:AT4G33820};
GN   ORFNames=F17I5.10 {ECO:0000312|EMBL:CAA19864.1};
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=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   [4]
RP   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).
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   -!- 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=CAA19864.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80099.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL031032; CAA19864.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161584; CAB80099.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86281.1; -; Genomic_DNA.
DR   EMBL; BT002790; AAO22618.1; -; mRNA.
DR   PIR; B85398; B85398.
DR   PIR; T05210; T05210.
DR   RefSeq; NP_680761.1; NM_148395.2.
DR   AlphaFoldDB; Q84WT5; -.
DR   SMR; Q84WT5; -.
DR   STRING; 3702.Q84WT5; -.
DR   CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   PaxDb; 3702-AT4G33820-1; -.
DR   ProteomicsDB; 242456; -.
DR   EnsemblPlants; AT4G33820.1; AT4G33820.1; AT4G33820.
DR   GeneID; 829524; -.
DR   Gramene; AT4G33820.1; AT4G33820.1; AT4G33820.
DR   KEGG; ath:AT4G33820; -.
DR   Araport; AT4G33820; -.
DR   TAIR; AT4G33820; -.
DR   eggNOG; ENOG502QSCW; Eukaryota.
DR   HOGENOM; CLU_008797_4_0_1; -.
DR   InParanoid; Q84WT5; -.
DR   OMA; MQPSWVK; -.
DR   OrthoDB; 1328474at2759; -.
DR   PhylomeDB; Q84WT5; -.
DR   BioCyc; ARA:AT4G33820-MONOMER; -.
DR   UniPathway; UPA00114; -.
DR   PRO; PR:Q84WT5; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q84WT5; baseline and differential.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF52; ENDO-1,4-BETA-XYLANASE 5-RELATED; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Signal; Xylan degradation.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..570
FT                   /note="Endo-1,4-beta-xylanase 5-like"
FT                   /id="PRO_5014311984"
FT   DOMAIN          202..501
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        332
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        439
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        490
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        515
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        537
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        545
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   570 AA;  64941 MW;  073B628D5A70FF78 CRC64;
     MNSIKNGFFL CMIFLLWCHV DSGVSIDPFS HSHSLNTECV MKPPRSSETK GLLQFSRSLE
     DDSDEEWKID GNGFIREMAQ RIQLHQGNIY SFSAWVKLRE GNDKKVGVVF RTENGRLVHG
     GEVRANQECW TLLKGGIVPD FSGPVDIFFE SENRGAKISA HNVLLKQFSK EEWKLKQDQL
     IEKIRKSKVR FEVTYENKTA VKGVVISLKQ TKSSFLLGCG MNFRILQSQG YRKWFASRFK
     ITSFTNEMKW YATEKARGQE NYTVADSMLK FAEDNGILVR GHTVLWDNPK MQPSWVKNIK
     DPNDVMNVTL NRINSVMKRY KGKLTGWDVV NENLHWDYFE KMLGANASTS FYNLAFKIDP
     DVRLFVNEYN TIENTKEFTA TPIKVKKMME EILAYPGNKN MKGAIGAQGH FGPTQPNLAY
     IRSALDTLGS LGLPIWLTEV DMPKCPNQAQ YVEDILREAY SHPAVKGIII FGGPEVSGFD
     KLTLADKDFN NTQTGDVIDK LLKEWQQKSS EIQTNFTADS DNEEEEVSLL HGHYNVNVSH
     PWIANLSTSF SLEVTKEMDQ DQVIRVVISA
//