XYN2_ARATH
ID XYN2_ARATH Reviewed; 1063 AA.
AC O80596;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Endo-1,4-beta-xylanase 2 {ECO:0000303|PubMed:12154138};
DE Short=AtXyn2 {ECO:0000303|PubMed:12154138};
DE Short=Xylan endohydrolase 2 {ECO:0000303|PubMed:12154138};
DE Short=Xylanase 2 {ECO:0000303|PubMed:12154138};
DE EC=3.2.1.8 {ECO:0000255|PROSITE-ProRule:PRU01096};
GN Name=XYN2 {ECO:0000303|PubMed:12154138};
GN OrderedLocusNames=At1g10050 {ECO:0000312|Araport:AT1G10050};
GN ORFNames=T27I1.7 {ECO:0000312|EMBL:AAC34334.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 -!- 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}.
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DR EMBL; AC004122; AAC34334.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28533.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60238.1; -; Genomic_DNA.
DR PIR; T00624; T00624.
DR RefSeq; NP_001322538.1; NM_001331878.1.
DR RefSeq; NP_172476.1; NM_100879.2.
DR AlphaFoldDB; O80596; -.
DR SMR; O80596; -.
DR STRING; 3702.AT1G10050.1; -.
DR CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR iPTMnet; O80596; -.
DR PaxDb; O80596; -.
DR PRIDE; O80596; -.
DR EnsemblPlants; AT1G10050.1; AT1G10050.1; AT1G10050.
DR EnsemblPlants; AT1G10050.2; AT1G10050.2; AT1G10050.
DR GeneID; 837540; -.
DR Gramene; AT1G10050.1; AT1G10050.1; AT1G10050.
DR Gramene; AT1G10050.2; AT1G10050.2; AT1G10050.
DR KEGG; ath:AT1G10050; -.
DR Araport; AT1G10050; -.
DR TAIR; locus:2201911; AT1G10050.
DR HOGENOM; CLU_008797_0_0_1; -.
DR InParanoid; O80596; -.
DR OMA; NIITNHD; -.
DR PhylomeDB; O80596; -.
DR UniPathway; UPA00114; -.
DR PRO; PR:O80596; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80596; 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; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 3.
DR Pfam; PF02018; CBM_4_9; 4.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF49785; SSF49785; 4.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Repeat; Xylan degradation.
FT CHAIN 1..1063
FT /note="Endo-1,4-beta-xylanase 2"
FT /id="PRO_0000445196"
FT DOMAIN 5..146
FT /note="CBM-cenC 1"
FT /evidence="ECO:0000255"
FT DOMAIN 183..313
FT /note="CBM-cenC 2"
FT /evidence="ECO:0000255"
FT DOMAIN 348..482
FT /note="CBM-cenC 3"
FT /evidence="ECO:0000255"
FT DOMAIN 517..662
FT /note="CBM-cenC 4"
FT /evidence="ECO:0000255"
FT DOMAIN 711..1006
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 840
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 941
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
SQ SEQUENCE 1063 AA; 118371 MW; 78F24C1749ACB841 CRC64;
MADLNIVMNG DFFAGIEPWY PNGCEAFVVS SDPFSSEVMS ADSSSGGYVV VTNRKETWQG
LEQDITTRVA SGMNYTVSTC VGVSGPFNES AEVLSTVRLE HEDSPTEYLC IGKTYASRDK
WVDLEGTFSI SNMPDRVVLY LEGPAPGKDL LIRSVTVRSS TSSDFQETEK NTDASNVFPL
ALNIIKNHDF SDGLYSWNTN GCDSFVVSSN DCNLESNAVV NNRSETWQGL EQDITDNVSP
GFSYKVSASV SVSGPVLGSA QVLATLKLEH KSSATEFQLI GKTYASKDIW KTLEGTFEVS
GRPDRVVFFL EGPPPGIDLL VKSVTIHCES DNQFERSREF CSAPESDNHI FLNSSFSDGL
NHWSGRGCNL MLHESLADGK ILPDSGTCFA SASERTHKWS GIEQDITERV QRKLIYEASS
VVRLSHSHHT VQATLYVQYL DQREEYIGIS SVQGTHDDWV ELKGKFLLNG SPARAVVYIE
GPPPGIDVFV DHFAVKPAEK ETPSGRPYIE SHAFGMNIVS NSHLSDGTIE GWFPLGDCHL
KVGDGSPRIL PPLARDSLRK TQGYLSGRYV LATNRSGTWM GPAQTITDKV KLFVTYQVSA
WVKIGSGGRT SPQDVNIALS VDGNWVNGGK VEVDDGDWHE VVGSFRIEKE AKEVMLHVQG
PSPGVDLMVA GLQIFAVDRK ARLSYLRGQA DVVRKRNVCL KFSGLDPSEL SGATVKIRQT
RNSFPLGSCI SRSNIDNEDF VDFFLNNFDW AVFGYELKWY WTEPEQGNFN YRDANEMIEF
CERYNIKTRG HCIFWEVESA IQPWVQQLTG SKLEAAVENR VTDLLTRYNG KFRHYDVNNE
MLHGSFYRDR LDSDARANMF KTAHELDPLA TLFLNEYHIE DGFDSRSSPE KYIKLVHKLQ
KKGAPVGGIG IQGHITSPVG HIVRSALDKL STLGLPIWFT ELDVSSTNEH IRGDDLEVML
WEAFAHPAVE GVMLWGFWEL FMSREHSHLV NADGEVNEAG KRFLEIKREW LSFVDGEIED
GGGLEFRGYH GSYTVEVVTS ESKYVTNFVV DKGNSPVDVI IDL
