XYN4_ARATH
ID XYN4_ARATH Reviewed; 570 AA.
AC Q680B7; Q6NQ91; Q9ZVK8;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Endo-1,4-beta-xylanase 4 {ECO:0000303|PubMed:12154138};
DE Short=AtXyn4 {ECO:0000303|PubMed:12154138};
DE Short=Xylan endohydrolase 4 {ECO:0000303|PubMed:12154138};
DE Short=Xylanase 4 {ECO:0000303|PubMed:12154138};
DE EC=3.2.1.8 {ECO:0000255|PROSITE-ProRule:PRU01096};
DE Flags: Precursor;
GN Name=XYN4 {ECO:0000303|PubMed:12154138};
GN OrderedLocusNames=At2g14690 {ECO:0000312|Araport:AT2G14690};
GN ORFNames=T6B13.7 {ECO:0000312|EMBL:AAC69373.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] OF 42-570.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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=AAC69373.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005398; AAC69373.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06322.1; -; Genomic_DNA.
DR EMBL; BT010567; AAQ65190.1; -; mRNA.
DR EMBL; AK175950; BAD43713.1; -; mRNA.
DR PIR; C84520; C84520.
DR RefSeq; NP_179076.3; NM_127033.4.
DR AlphaFoldDB; Q680B7; -.
DR SMR; Q680B7; -.
DR STRING; 3702.AT2G14690.1; -.
DR CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR PaxDb; Q680B7; -.
DR PRIDE; Q680B7; -.
DR ProteomicsDB; 242697; -.
DR EnsemblPlants; AT2G14690.1; AT2G14690.1; AT2G14690.
DR GeneID; 815957; -.
DR Gramene; AT2G14690.1; AT2G14690.1; AT2G14690.
DR KEGG; ath:AT2G14690; -.
DR Araport; AT2G14690; -.
DR TAIR; locus:2064241; AT2G14690.
DR eggNOG; ENOG502RD7C; Eukaryota.
DR HOGENOM; CLU_008797_4_0_1; -.
DR InParanoid; Q680B7; -.
DR OMA; QWRLQQD; -.
DR OrthoDB; 829814at2759; -.
DR PhylomeDB; Q680B7; -.
DR BioCyc; ARA:AT2G14690-MON; -.
DR UniPathway; UPA00114; -.
DR PRO; PR:Q680B7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q680B7; baseline and differential.
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; 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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Repeat; Signal;
KW Xylan degradation.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..570
FT /note="Endo-1,4-beta-xylanase 4"
FT /id="PRO_5014310291"
FT DOMAIN 195..494
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 325
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 432
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 339
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; 64944 MW; 8A6E19F8E478CEBC CRC64;
MKRFNYGFFH LVLFLISLLL LGSGICMDPF SYDQSLKSEC LMEPPQTTAN TGGEGVKELK
INENGGIRNV VEGVDLREGN IYITSAWVKL RNESQRKVGM TFSEKNGRNV FGGEVMAKRG
CWSLLKGGIT ADFSGPIDIF FESDGLAGLE ISVQNVRMQR FHKTQWRLQQ DQVIEKIRKN
KVRFQMSFKN KSALEGSVIS IEQIKPSFLL GCAMNYRILE SDSYREWFVS RFRLTSFTNE
MKWYATEAVR GQENYKIADS MMQLAEENAI LVKGHTVLWD DKYWQPNWVK TITDPEDLKN
VTLNRMNSVM KRYKGRLIGW DVMNENVHFN YFENMLGGNA SAIVYSLASK LDPDIPLFLN
EFNTVEYDKD RVVSPVNVVK KMQEIVSFPG NNNIKGGIGA QGHFAPVQPN LAYMRYALDT
LGSLSFPVWL TEVDMFKCPD QVKYMEDILR EAYSHPAVKA IILYGGPEVS GFDKLTLADK
DFKNTQAGDL IDKLLQEWKQ EPVEIPIQHH EHNDEEGGRI IGFSPEISLL HGHYRVTVTN
PSMKNLSTRF SVEVTKESGH LQEVQLVIDA
