XYN5_ARATH
ID XYN5_ARATH Reviewed; 569 AA.
AC A0A1P8B8F8; F4JJU5; O81897;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Endo-1,4-beta-xylanase 5 {ECO:0000303|PubMed:12154138};
DE Short=AtXyn5 {ECO:0000303|PubMed:12154138};
DE Short=Xylan endohydrolase 5 {ECO:0000303|PubMed:12154138};
DE Short=Xylanase 5 {ECO:0000303|PubMed:12154138};
DE EC=3.2.1.8 {ECO:0000255|PROSITE-ProRule:PRU01096};
DE Flags: Precursor;
GN Name=XYN5 {ECO:0000303|PubMed:12154138};
GN OrderedLocusNames=At4g33810 {ECO:0000312|EMBL:ANM67882.1};
GN ORFNames=T16L1.300 {ECO:0000312|EMBL:CAA20594.1};
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 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A1P8B8F8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A1P8B8F8-2; Sequence=VSP_059824;
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=CAA20594.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80098.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL031394; CAA20594.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161584; CAB80098.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86280.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67882.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67883.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67884.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67885.1; -; Genomic_DNA.
DR PIR; T04998; T04998.
DR RefSeq; NP_001329678.1; NM_001342235.1. [A0A1P8B8F8-1]
DR RefSeq; NP_001329679.1; NM_001342236.1. [A0A1P8B8F8-1]
DR RefSeq; NP_001329680.1; NM_001342238.1. [A0A1P8B8F8-2]
DR RefSeq; NP_001329681.1; NM_001342237.1. [A0A1P8B8F8-1]
DR RefSeq; NP_195107.2; NM_119539.3. [A0A1P8B8F8-2]
DR AlphaFoldDB; A0A1P8B8F8; -.
DR SMR; A0A1P8B8F8; -.
DR STRING; 3702.AT4G33810.1; -.
DR CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR ProteomicsDB; 243045; -. [A0A1P8B8F8-1]
DR EnsemblPlants; AT4G33810.1; AT4G33810.1; AT4G33810. [A0A1P8B8F8-2]
DR EnsemblPlants; AT4G33810.2; AT4G33810.2; AT4G33810. [A0A1P8B8F8-1]
DR EnsemblPlants; AT4G33810.3; AT4G33810.3; AT4G33810. [A0A1P8B8F8-1]
DR EnsemblPlants; AT4G33810.4; AT4G33810.4; AT4G33810. [A0A1P8B8F8-1]
DR EnsemblPlants; AT4G33810.5; AT4G33810.5; AT4G33810. [A0A1P8B8F8-2]
DR GeneID; 829523; -.
DR Gramene; AT4G33810.1; AT4G33810.1; AT4G33810. [A0A1P8B8F8-2]
DR Gramene; AT4G33810.2; AT4G33810.2; AT4G33810. [A0A1P8B8F8-1]
DR Gramene; AT4G33810.3; AT4G33810.3; AT4G33810. [A0A1P8B8F8-1]
DR Gramene; AT4G33810.4; AT4G33810.4; AT4G33810. [A0A1P8B8F8-1]
DR Gramene; AT4G33810.5; AT4G33810.5; AT4G33810. [A0A1P8B8F8-2]
DR KEGG; ath:AT4G33810; -.
DR Araport; AT4G33810; -.
DR TAIR; locus:2134293; AT4G33810.
DR eggNOG; ENOG502QSCW; Eukaryota.
DR HOGENOM; CLU_008797_4_0_1; -.
DR OrthoDB; 829814at2759; -.
DR UniPathway; UPA00114; -.
DR PRO; PR:A0A1P8B8F8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; A0A1P8B8F8; 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 InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Carbohydrate metabolism; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Signal;
KW Xylan degradation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..569
FT /note="Endo-1,4-beta-xylanase 5"
FT /id="PRO_5015267967"
FT DOMAIN 209..500
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 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform 2)"
FT /id="VSP_059824"
SQ SEQUENCE 569 AA; 64947 MW; 5304A07DB2A1367B CRC64;
MKNINNGFFL CMLLLLWCFV HSGISIDPFS PSDSLKTECV MKPPRSSETK GLLQFSRSVE
DDSDEEWKID GSGSIREMTQ RIQLHEGNIY SFSAWVKLRE GNNKKVGVVF RTENGRFVHG
GEVRAKKRCW TLLKGGIVPD VSGSVDIFFE SDDKEAKISA SDVSLKQFSK QEWKLKQDQL
IEKIRKSKVR FEVTYQNKTA VKGAVISIEQ TKPSFLLGCA MNFRILQSEG YRNWFASRFK
ITSFTNEMKW YTTEKERGHE NYTAADSMLK FAEENGILVR GHTVLWDDPL MQPTWVPKIE
DPNDLMNVTL NRINSVMTRY KGKLTGWDVV NENVHWDYFE KMLGANASSS FYNLAFKLDP
DVTMFVNEYN TIENRVEVTA TPVKVKEKME EILAYPGNMN IKGAIGAQGH FRPTQPNLAY
MRSALDTLGS LGLPIWLTEV DMPKCPNQEV YIEEILREAY SHPAVKGIII FAGPEVSGFD
KLTLADKYFN NTATGDVIDK LLKEWQQSSE IPKIFMTDSE NDEEEVSLLH GHYNVNVSHP
WMKNMSTSFS LEVTKEMGQR QVVRVVINA
