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   27-MAR-2024, entry version 121.
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;
GN   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.Q9LXD6; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GlyCosmos; Q9LXD6; 4 sites, No reported glycans.
DR   PaxDb; 3702-AT5G09730-1; -.
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; AT5G09730; BXL3.
DR   eggNOG; ENOG502QQ55; Eukaryota.
DR   HOGENOM; CLU_004542_5_3_1; -.
DR   InParanoid; Q9LXD6; -.
DR   OMA; WTTHAGA; -.
DR   OrthoDB; 649069at2759; -.
DR   PhylomeDB; Q9LXD6; -.
DR   BioCyc; ARA:AT5G09730-MONOMER; -.
DR   PRO; PR:Q9LXD6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LXD6; baseline and differential.
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; IEA:InterPro.
DR   GO; GO:0031222; P:arabinan catabolic process; IDA:TAIR.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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:SF20; BETA-D-XYLOSIDASE 3; 1.
DR   PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   Genevisible; Q9LXD6; AT.
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
//