XYN1_ARATH
ID XYN1_ARATH Reviewed; 945 AA.
AC A0A1P8AWH8; Q9C643; Q9SM08;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Endo-1,4-beta-xylanase 1 {ECO:0000303|PubMed:12154138};
DE Short=AtXyn1 {ECO:0000303|PubMed:12154138};
DE Short=Xylan endohydrolase 1 {ECO:0000303|PubMed:12154138};
DE Short=Xylanase 1 {ECO:0000303|PubMed:12154138};
DE EC=3.2.1.8 {ECO:0000255|PROSITE-ProRule:PRU01096, ECO:0000269|PubMed:12154138};
GN Name=XYN1 {ECO:0000303|PubMed:12154138};
GN Synonyms=RXF12 {ECO:0000303|PubMed:10548732};
GN OrderedLocusNames=At1g58370 {ECO:0000312|Araport:AT1G58370};
GN ORFNames=F19C14.2 {ECO:0000312|EMBL:AAF82251.1},
GN F9K23.10 {ECO:0000312|EMBL:AAG50641.1};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, 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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-945.
RC STRAIN=cv. Columbia;
RX PubMed=10548732; DOI=10.1016/s0378-1119(99)00403-5;
RA Kato A., Suzuki M., Kuwahara A., Ooe H., Higano-Inaba K., Komeda Y.;
RT "Isolation and analysis of cDNA within a 300 kb Arabidopsis thaliana
RT genomic region located around the 100 map unit of chromosome 1.";
RL Gene 239:309-316(1999).
CC -!- FUNCTION: Binds to and hydrolyzes insoluble and soluble xylan
CC substrates (By similarity). Exhibits xylanase activity
CC (PubMed:12154138). {ECO:0000250|UniProtKB:A3DH97,
CC ECO:0000269|PubMed:12154138}.
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 ECO:0000269|PubMed:12154138};
CC -!- PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-
CC ProRule:PRU01096, ECO:0000269|PubMed:12154138}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:12154138}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in vascular bundles, but
CC not in vessel cells. Mostly expressed in stems, at lower levels in
CC roots, and weakly in inflorescences and seedlings.
CC {ECO:0000269|PubMed:12154138}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, present in the root, hypocotyl and
CC cotyledon veins. In roots, excluded from the root tip, otherwise
CC observed in the endodermis, pericycles and vascular bundles, except
CC vessels. Expressed in the root differentiation zone, especially during
CC root hair formation. In mature plants, mostly detected in vascular
CC bundles, but not in vessel cells. {ECO:0000269|PubMed:12154138}.
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=AAF82251.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50641.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE33542.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA88262.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB83869.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB077822; BAB83869.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC008051; AAF82251.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC082643; AAG50641.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33542.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; ANM61018.1; -; Genomic_DNA.
DR EMBL; AB008015; BAA88262.1; ALT_INIT; mRNA.
DR PIR; D96617; D96617.
DR PIR; T52467; T52467.
DR RefSeq; NP_001323263.1; NM_001333829.1.
DR RefSeq; NP_176133.1; NM_104617.4.
DR AlphaFoldDB; A0A1P8AWH8; -.
DR SMR; A0A1P8AWH8; -.
DR STRING; 3702.AT1G58370.1; -.
DR CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR iPTMnet; A0A1P8AWH8; -.
DR ProteomicsDB; 242982; -.
DR EnsemblPlants; AT1G58370.2; AT1G58370.2; AT1G58370.
DR GeneID; 842206; -.
DR Gramene; AT1G58370.2; AT1G58370.2; AT1G58370.
DR KEGG; ath:AT1G58370; -.
DR Araport; AT1G58370; -.
DR TAIR; locus:2016595; AT1G58370.
DR eggNOG; ENOG502QSCW; Eukaryota.
DR HOGENOM; CLU_008797_0_0_1; -.
DR OrthoDB; 829814at2759; -.
DR UniPathway; UPA00114; -.
DR PRO; PR:A0A1P8AWH8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A0A1P8AWH8; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; IDA:UniProtKB.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IDA:UniProtKB.
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; 2.
DR Pfam; PF02018; CBM_4_9; 3.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF49785; SSF49785; 3.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Repeat; Secreted;
KW Xylan degradation.
FT CHAIN 1..945
FT /note="Endo-1,4-beta-xylanase 1"
FT /id="PRO_0000445195"
FT DOMAIN 57..197
FT /note="CBM-cenC 1"
FT /evidence="ECO:0000255"
FT DOMAIN 227..362
FT /note="CBM-cenC 2"
FT /evidence="ECO:0000255"
FT DOMAIN 397..541
FT /note="CBM-cenC 3"
FT /evidence="ECO:0000255"
FT DOMAIN 589..884
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT REGION 16..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 718
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 819
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 945 AA; 105768 MW; AC91848683227872 CRC64;
MKRFTVCCFS NKIHKNGDRN PDKKSRESME VSRKDNEEPE KQNNNNVASI IGSDRTNVIV
NHDFSSGMHS WHPNCCEAFV VTAESNVSHG VLDPSKCGSY VVVKNRKETW QGLEQDITNR
VKPCSLYKVS ATVAVSGPVH GLVEVMATLK LESQQSQTNY QFIAKTCVFK EKWVRLEGMF
SLPSLPEKVV FYLEGPSPGI DLLIQSVTIH RESEPELERV TAEDETIVVN PNFEDGLNNW
SGRSCKIVLH DSMADGKIVP ESGKVFASAT ERTQNWNGIQ QEITGKVQRK RVYEATAVVR
IYGNNVTTAT VQATLWVQNP NQRDQYIGIS TVQATDKEWI HLKGKFLLNG SASRVVIYIE
GPPPGTDILL NSLTVKHAEK IPPSPPPSIE NPAFGVNILT NSHLSDDTTN GWFSLGNCTL
SVAEGSPRIL PPMARDSLGA HERLSGRYIL VTNRTQTWMG PAQMITDKLK LFLTYQISVW
VKVGSGINSP QNVNVALGID SQWVNGGQVE INDDRWHEIG GSFRIEKNPS KALVYVQGPS
SGIDLMVAGL QIFPVDRLAR IKHLKRQCDK IRKRDVILKF AGVDSSKFSG ASVRVRQIRN
SFPVGTCISR SNIDNEDFVD FFLKNFNWAV FANELKWYWT EPEQGKLNYQ DADDMLNLCS
SNNIETRGHC IFWEVQATVQ QWIQNMNQTD LNNAVQNRLT DLLNRYKGKF KHYDVNNEML
HGSFYQDKLG KDIRVNMFKT AHQLDPSATL FVNDYHIEDG CDPKSCPEKY TEQILDLQEK
GAPVGGIGIQ GHIDSPVGPI VCSALDKLGI LGLPIWFTEL DVSSVNEHIR ADDLEVMMWE
AFGHPAVEGI MLWGFWELFM SRDNSHLVNA EGDVNEAGKR FLAVKKDWLS HANGHIDQNG
AFPFRGYSGN YAVEVITTSS SKVLKTFGVD KEDSSQVITV DLQGL
