BXL3_ARATH
ID BXL3_ARATH Reviewed; 773 AA.
AC Q9LXD6; Q56WQ6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Beta-D-xylosidase 3;
DE Short=AtBXL3;
DE EC=3.2.1.-;
DE AltName: Full=Alpha-L-arabinofuranosidase;
DE EC=3.2.1.55;
DE Flags: Precursor;
GN Name=BXL3; Synonyms=XYL3; OrderedLocusNames=At5g09730; ORFNames=F17I14.80;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 [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 [5]
RP PROTEIN SEQUENCE OF 24-31, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16798843; DOI=10.1093/jxb/erj205;
RA Minic Z., Do C.-T., Rihouey C., Morin H., Lerouge P., Jouanin L.;
RT "Purification, functional characterization, cloning, and identification of
RT mutants of a seed-specific arabinan hydrolase in Arabidopsis.";
RL J. Exp. Bot. 57:2339-2351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 487-773.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION.
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).
CC -!- FUNCTION: Involved in the hydrolysis of arabinan. Can hydrolyze (1,3)-
CC alpha-, (1,2)-alpha-linked side group residues and non-reducing
CC terminal L-arabinofuranose residues of debranched (1,5)-alpha-L-
CC arabinan backbone. Acts also as a beta-D-xylosidase, releasing D-xylose
CC from arabinoxylan and xylan. {ECO:0000269|PubMed:16798843}.
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:16798843};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for p-nitrophenyl-beta-D-xylopyranoside (at 37 degrees
CC Celsius) {ECO:0000269|PubMed:16798843};
CC KM=3.52 mM for p-nitrophenyl-alpha-L-arabinofuranoside (at 37 degrees
CC Celsius) {ECO:0000269|PubMed:16798843};
CC KM=5.5 mM for (1,5)-alpha-L-arabinobiose (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:16798843};
CC pH dependence:
CC Optimum pH is 4.7. {ECO:0000269|PubMed:16798843};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.
CC {ECO:0000269|PubMed:16798843};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and siliques, in the early
CC stage of seed formation and not at seed maturation. Detected
CC exclusively in the endosperm of very young seeds when the embryo is at
CC the globular stage. {ECO:0000269|PubMed:16798843}.
CC -!- DISRUPTION PHENOTYPE: Reduced seeds size and delayed germination.
CC {ECO:0000269|PubMed:16798843}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; AB020752; BAB09531.1; -; Genomic_DNA.
DR EMBL; AL353994; CAB89357.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91439.1; -; Genomic_DNA.
DR EMBL; AY053409; AAK96639.1; -; mRNA.
DR EMBL; AK221979; BAD94522.1; -; mRNA.
DR PIR; T49925; T49925.
DR RefSeq; NP_196535.1; NM_121010.3.
DR AlphaFoldDB; Q9LXD6; -.
DR SMR; Q9LXD6; -.
DR STRING; 3702.AT5G09730.1; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR PaxDb; Q9LXD6; -.
DR PRIDE; Q9LXD6; -.
DR ProteomicsDB; 239129; -.
DR EnsemblPlants; AT5G09730.1; AT5G09730.1; AT5G09730.
DR GeneID; 830833; -.
DR Gramene; AT5G09730.1; AT5G09730.1; AT5G09730.
DR KEGG; ath:AT5G09730; -.
DR Araport; AT5G09730; -.
DR TAIR; locus:2144756; AT5G09730.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_3_1; -.
DR InParanoid; Q9LXD6; -.
DR OMA; PTINICR; -.
DR OrthoDB; 321444at2759; -.
DR PhylomeDB; Q9LXD6; -.
DR BioCyc; ARA:AT5G09730-MON; -.
DR PRO; PR:Q9LXD6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LXD6; baseline and differential.
DR Genevisible; Q9LXD6; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; IDA: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 Direct protein sequencing; Extracellular matrix; Glycoprotein; Glycosidase;
KW Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:16798843"
FT CHAIN 24..773
FT /note="Beta-D-xylosidase 3"
FT /id="PRO_0000384058"
FT ACT_SITE 298
FT /evidence="ECO:0000250"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 488
FT /note="A -> S (in Ref. 6; BAD94522)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="A -> P (in Ref. 6; BAD94522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 773 AA; 83222 MW; 3C98ED6D3876621C CRC64;
MASRNRALFS VSTLFLCFIV CISEQSNNQS SPVFACDVTG NPSLAGLRFC NAGLSIKARV
TDLVGRLTLE EKIGFLTSKA IGVSRLGIPS YKWWSEALHG VSNVGGGSRF TGQVPGATSF
PQVILTAASF NVSLFQAIGK VVSTEARAMY NVGSAGLTFW SPNVNIFRDP RWGRGQETPG
EDPTLSSKYA VAYVKGLQET DGGDPNRLKV AACCKHYTAY DIDNWRNVNR LTFNAVVNQQ
DLADTFQPPF KSCVVDGHVA SVMCSYNQVN GKPTCADPDL LSGVIRGQWQ LNGYIVSDCD
SVDVLFRKQH YAKTPEEAVA KSLLAGLDLN CDHFNGQHAM GAVKAGLVNE TAIDKAISNN
FATLMRLGFF DGDPKKQLYG GLGPKDVCTA DNQELARDGA RQGIVLLKNS AGSLPLSPSA
IKTLAVIGPN ANATETMIGN YHGVPCKYTT PLQGLAETVS STYQLGCNVA CVDADIGSAV
DLAASADAVV LVVGADQSIE REGHDRVDLY LPGKQQELVT RVAMAARGPV VLVIMSGGGF
DITFAKNDKK ITSIMWVGYP GEAGGLAIAD VIFGRHNPSG NLPMTWYPQS YVEKVPMSNM
NMRPDKSKGY PGRSYRFYTG ETVYAFADAL TYTKFDHQLI KAPRLVSLSL DENHPCRSSE
CQSLDAIGPH CENAVEGGSD FEVHLNVKNT GDRAGSHTVF LFTTSPQVHG SPIKQLLGFE
KIRLGKSEEA VVRFNVNVCK DLSVVDETGK RKIALGHHLL HVGSLKHSLN ISV
