ASD1_ARATH
ID ASD1_ARATH Reviewed; 678 AA.
AC Q9SG80; Q56W72; Q570E2; Q84RC5; Q94JT7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alpha-L-arabinofuranosidase 1;
DE Short=AtASD1;
DE EC=3.2.1.55;
DE AltName: Full=Beta-D-xylosidase;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=ASD1; Synonyms=ARAF, ARAF1; OrderedLocusNames=At3g10740;
GN ORFNames=T7M13.18;
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 [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY HORMONES.
RC STRAIN=cv. Columbia;
RX PubMed=14512381; DOI=10.1093/jxb/erg269;
RA Fulton L.M., Cobbett C.S.;
RT "Two alpha-L-arabinofuranosidase genes in Arabidopsis thaliana are
RT differentially expressed during vegetative growth and flower development.";
RL J. Exp. Bot. 54:2467-2477(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 287-678.
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 [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18344421; DOI=10.1104/pp.107.110023;
RA Chavez Montes R.A., Ranocha P., Martinez Y., Minic Z., Jouanin L.,
RA Marquis M., Saulnier L., Fulton L.M., Cobbett C.S., Bitton F., Renou J.-P.,
RA Jauneau A., Goffner D.;
RT "Cell wall modifications in Arabidopsis plants with altered alpha-L-
RT arabinofuranosidase activity.";
RL Plant Physiol. 147:63-77(2008).
CC -!- FUNCTION: May be involved in the coordinated dissolution of the cell
CC wall matrix during abscission and in the secondary cell wall formation
CC in xylem vessels. Prefers arabinoxylan, but may also use pectic
CC arabinans as substrates. {ECO:0000269|PubMed:15181203,
CC ECO:0000269|PubMed:16798843, ECO:0000269|PubMed:18344421}.
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, ECO:0000269|PubMed:16798843};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.48 mM for p-nitrophenyl-beta-D-xylopyranoside
CC {ECO:0000269|PubMed:15181203, ECO:0000269|PubMed:16798843};
CC KM=5.2 mM for (1,5)-alpha-L-arabinobiose (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:15181203, ECO:0000269|PubMed:16798843};
CC pH dependence:
CC Optimum pH is 4.3. {ECO:0000269|PubMed:15181203,
CC ECO:0000269|PubMed:16798843};
CC Temperature dependence:
CC Optimum temperature is 67 degrees Celsius.
CC {ECO:0000269|PubMed:15181203, ECO:0000269|PubMed:16798843};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers, stems,
CC siliques and seedlings. Observed in zones of cell proliferation, the
CC vascular system and floral abscission zones. Expressed in the guard
CC cells in stems, in xylem vessels and parenchyma cells surrounding the
CC vessels, in the cambium and in the phloem, but not in the secondary
CC xylem. {ECO:0000269|PubMed:14512381, ECO:0000269|PubMed:15181203,
CC ECO:0000269|PubMed:18344421}.
CC -!- INDUCTION: Not induced by hormones or during leaf senescence.
CC {ECO:0000269|PubMed:14512381}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; even in asd1 and asd2
CC double mutant. {ECO:0000269|PubMed:18344421}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY243509; AAO92261.1; -; mRNA.
DR EMBL; AC011708; AAF19575.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74949.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64547.1; -; Genomic_DNA.
DR EMBL; AF372949; AAK50089.1; -; mRNA.
DR EMBL; AY143944; AAN28883.1; -; mRNA.
DR EMBL; AK222175; BAD95302.1; -; mRNA.
DR EMBL; AK220766; BAD93969.1; -; mRNA.
DR RefSeq; NP_001326566.1; NM_001337893.1.
DR RefSeq; NP_187685.1; NM_111911.5.
DR AlphaFoldDB; Q9SG80; -.
DR SMR; Q9SG80; -.
DR STRING; 3702.AT3G10740.1; -.
DR CAZy; GH51; Glycoside Hydrolase Family 51.
DR PaxDb; Q9SG80; -.
DR PRIDE; Q9SG80; -.
DR ProteomicsDB; 246496; -.
DR EnsemblPlants; AT3G10740.1; AT3G10740.1; AT3G10740.
DR EnsemblPlants; AT3G10740.3; AT3G10740.3; AT3G10740.
DR GeneID; 820243; -.
DR Gramene; AT3G10740.1; AT3G10740.1; AT3G10740.
DR Gramene; AT3G10740.3; AT3G10740.3; AT3G10740.
DR KEGG; ath:AT3G10740; -.
DR Araport; AT3G10740; -.
DR TAIR; locus:2103172; AT3G10740.
DR eggNOG; ENOG502QQEX; Eukaryota.
DR HOGENOM; CLU_010060_3_0_1; -.
DR InParanoid; Q9SG80; -.
DR OMA; MFEEMDH; -.
DR PhylomeDB; Q9SG80; -.
DR BioCyc; ARA:AT3G10740-MON; -.
DR SABIO-RK; Q9SG80; -.
DR PRO; PR:Q9SG80; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SG80; baseline and differential.
DR Genevisible; Q9SG80; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IDA:TAIR.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IDA:TAIR.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IDA:TAIR.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR010720; Alpha-L-AF_C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF06964; Alpha-L-AF_C; 1.
DR SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Extracellular matrix; Glycoprotein; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..678
FT /note="Alpha-L-arabinofuranosidase 1"
FT /id="PRO_0000384371"
FT DOMAIN 152..239
FT /note="CBM-cenC"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 251
FT /note="L -> P (in Ref. 4; AAN28883/AAK50089)"
FT /evidence="ECO:0000305"
FT CONFLICT 253..254
FT /note="QM -> HL (in Ref. 1; AAO92261)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="R -> G (in Ref. 1; AAO92261)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="E -> D (in Ref. 1; AAO92261)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 678 AA; 75045 MW; 8116546072E6CA9A CRC64;
MDMESWKLLR SVCVLSFLLG SCFVYQSLRV VDAQEDPKPA VTLQVDASNG GGRPIPETLF
GIFFEEINHA GAGGLWAELV SNRGFEAGGQ NTPSNIWPWS IVGDHSSIYV ATDRSSCFER
NKIALRMDVL CDSKGCPSGG VGVYNPGYWG MNIEEGKKYK VALYVRSTGD IDLSVSLTSS
NGSRTLASEK IIASASDVSK WIKKEVLLEA KATDPSARLQ LTTTKKGSIW IDQVSAMPVD
THKGHGFRND LFQMMADIKP RFIRFPGGCF VEGEWLSNAF RWKETVGPWE ERPGHFGDVW
KYWTDDGLGH FEFFQMAEDI GAAPIWVFNN GISHNDEVET ASIMPFVQEA LDGIEFARGD
ANSTWGSVRA KMGRQEPFEL KYVAIGNEDC GKTYYRGNYI VFYDAIKKAY PDIKIISNCD
GSSHPLDHPA DYYDYHIYTS ASNLFSMYHQ FDRTSRKGPK AFVSEYAVTG KDAGTGSLLA
SLAEAAFLIG LEKNSDIVEM ASYAPLFVNT NDRRWNPDAI VFNSSHLYGT PSYWVQRFFA
ESSGATLLTS TLKGNSTSLV ASAISWKNNG KDYIRIKAVN FGANSENMQV LVTGLDPNVM
RVSGSKKTVL TSTNVMDENS FSQPEKVVPH ESLLELAEED MTVVLPPHSF SSFDLLKESA
KIRMPISDSS SHQKTTTV
