BXL1_ARATH
ID BXL1_ARATH Reviewed; 774 AA.
AC Q9FGY1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Beta-D-xylosidase 1;
DE Short=AtBXL1;
DE EC=3.2.1.-;
DE AltName: Full=Alpha-L-arabinofuranosidase;
DE EC=3.2.1.55;
DE Flags: Precursor;
GN Name=BXL1; Synonyms=XYL1; OrderedLocusNames=At5g49360; ORFNames=K7J8.3;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12609041; DOI=10.1046/j.1365-313x.2003.01654.x;
RA Goujon T., Minic Z., El Amrani A., Lerouxel O., Aletti E., Lapierre C.,
RA Joseleau J.-P., Jouanin L.;
RT "AtBXL1, a novel higher plant (Arabidopsis thaliana) putative beta-
RT xylosidase gene, is involved in secondary cell wall metabolism and plant
RT development.";
RL Plant J. 33:677-690(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=15181203; DOI=10.1104/pp.104.041269;
RA Minic Z., Rihouey C., Do C.T., Lerouge P., Jouanin L.;
RT "Purification and characterization of enzymes exhibiting beta-D-xylosidase
RT activities in stem tissues of Arabidopsis.";
RL Plant Physiol. 135:867-878(2004).
RN [6]
RP INDUCTION BY SUGAR STARVATION.
RX PubMed=17234672; DOI=10.1093/pcp/pcm009;
RA Lee E.-J., Matsumura Y., Soga K., Hoson T., Koizumi N.;
RT "Glycosyl hydrolases of cell wall are induced by sugar starvation in
RT Arabidopsis.";
RL Plant Cell Physiol. 48:405-413(2007).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19458117; DOI=10.1104/pp.109.138388;
RA Arsovski A.A., Popma T.M., Haughn G.W., Carpita N.C., McCann M.C.,
RA Western T.L.;
RT "AtBXL1 encodes a bifunctional beta-D-xylosidase/alpha-L-
RT arabinofuranosidase required for pectic arabinan modification in
RT arabidopsis mucilage secretory cells.";
RL Plant Physiol. 150:1219-1234(2009).
CC -!- FUNCTION: Involved in pectic arabinan modification in mucilage
CC secretory cells. Acts also as a beta-D-xylosidase during the remodeling
CC of xylans in vascular development. {ECO:0000269|PubMed:12609041,
CC ECO:0000269|PubMed:15181203, ECO:0000269|PubMed:19458117}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC Evidence={ECO:0000269|PubMed:15181203};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for p-nitrophenyl-beta-D-xylopyranoside
CC {ECO:0000269|PubMed:15181203};
CC pH dependence:
CC Optimum pH is 4.9. {ECO:0000269|PubMed:15181203};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:15181203};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, seedlings, roots,
CC inflorescences, siliques and developing seeds. Expressed in the
CC vasculature of the roots, leaves, flowers and silique. Expressed in
CC tissues undergoing secondary cell wall thickening such as protoxylem,
CC metaxylem, intrafascicular cambium and fibers.
CC {ECO:0000269|PubMed:12609041, ECO:0000269|PubMed:15181203,
CC ECO:0000269|PubMed:19458117}.
CC -!- INDUCTION: By sugar starvation. {ECO:0000269|PubMed:17234672}.
CC -!- DISRUPTION PHENOTYPE: Delayed seeds germination resulting from an
CC altered mucilage composition. No visible growth defects; probably due
CC to partial redundancy with BXL2. Bxl1 and bxl2 double mutants have
CC shortened siliques and curled leaf edges.
CC {ECO:0000269|PubMed:19458117}.
CC -!- MISCELLANEOUS: Might be processed at the C-terminus.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; AB023034; BAB09906.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95802.1; -; Genomic_DNA.
DR EMBL; AY120767; AAM53325.1; -; mRNA.
DR RefSeq; NP_199747.1; NM_124313.3.
DR AlphaFoldDB; Q9FGY1; -.
DR SMR; Q9FGY1; -.
DR BioGRID; 20242; 4.
DR STRING; 3702.AT5G49360.1; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR PaxDb; Q9FGY1; -.
DR PRIDE; Q9FGY1; -.
DR ProteomicsDB; 240440; -.
DR EnsemblPlants; AT5G49360.1; AT5G49360.1; AT5G49360.
DR GeneID; 834996; -.
DR Gramene; AT5G49360.1; AT5G49360.1; AT5G49360.
DR KEGG; ath:AT5G49360; -.
DR Araport; AT5G49360; -.
DR TAIR; locus:2157994; AT5G49360.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_3_1; -.
DR InParanoid; Q9FGY1; -.
DR OMA; FFANNNE; -.
DR OrthoDB; 321444at2759; -.
DR PhylomeDB; Q9FGY1; -.
DR BioCyc; ARA:AT5G49360-MON; -.
DR BRENDA; 3.2.1.37; 399.
DR SABIO-RK; Q9FGY1; -.
DR PRO; PR:Q9FGY1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGY1; baseline and differential.
DR Genevisible; Q9FGY1; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IDA:TAIR.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IBA:GO_Central.
DR GO; GO:0031222; P:arabinan catabolic process; IBA:GO_Central.
DR GO; GO:0010214; P:seed coat development; IMP:TAIR.
DR GO; GO:0045493; P:xylan catabolic process; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 1.
DR InterPro; IPR044993; BXL.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42721; PTHR42721; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
PE 1: Evidence at protein level;
KW Extracellular matrix; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..774
FT /note="Beta-D-xylosidase 1"
FT /id="PRO_0000384056"
FT ACT_SITE 296
FT /evidence="ECO:0000250"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 774 AA; 83524 MW; 77478F0F28A5DA51 CRC64;
MSCYNKALLI GNKVVVILVF LLCLVHSSES LRPLFACDPA NGLTRTLRFC RANVPIHVRV
QDLLGRLTLQ EKIRNLVNNA AAVPRLGIGG YEWWSEALHG ISDVGPGAKF GGAFPGATSF
PQVITTAASF NQSLWEEIGR VVSDEARAMY NGGVAGLTYW SPNVNILRDP RWGRGQETPG
EDPIVAAKYA ASYVRGLQGT AAGNRLKVAA CCKHYTAYDL DNWNGVDRFH FNAKVTQQDL
EDTYNVPFKS CVYEGKVASV MCSYNQVNGK PTCADENLLK NTIRGQWRLN GYIVSDCDSV
DVFFNQQHYT STPEEAAARS IKAGLDLDCG PFLAIFTEGA VKKGLLTEND INLALANTLT
VQMRLGMFDG NLGPYANLGP RDVCTPAHKH LALEAAHQGI VLLKNSARSL PLSPRRHRTV
AVIGPNSDVT ETMIGNYAGK ACAYTSPLQG ISRYARTLHQ AGCAGVACKG NQGFGAAEAA
AREADATVLV MGLDQSIEAE TRDRTGLLLP GYQQDLVTRV AQASRGPVIL VLMSGGPIDV
TFAKNDPRVA AIIWAGYPGQ AGGAAIANII FGAANPGGKL PMTWYPQDYV AKVPMTVMAM
RASGNYPGRT YRFYKGPVVF PFGFGLSYTT FTHSLAKSPL AQLSVSLSNL NSANTILNSS
SHSIKVSHTN CNSFPKMPLH VEVSNTGEFD GTHTVFVFAE PPINGIKGLG VNKQLIAFEK
VHVMAGAKQT VQVDVDACKH LGVVDEYGKR RIPMGEHKLH IGDLKHTILV QPQL
