XYL1_ARATH
ID XYL1_ARATH Reviewed; 915 AA.
AC Q9S7Y7; P80846; Q9ZP26;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Alpha-xylosidase 1;
DE EC=3.2.1.177;
DE Flags: Precursor;
GN Name=XYL1 {ECO:0000312|EMBL:AAD37363.1}; Synonyms=AXY3;
GN OrderedLocusNames=At1g68560; ORFNames=F24J5.20;
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] {ECO:0000305, ECO:0000312|EMBL:AAD37363.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia {ECO:0000269|PubMed:11402218};
RC TISSUE=Seedling hypocotyl {ECO:0000312|EMBL:AAD05539.1};
RX PubMed=11402218; DOI=10.1104/pp.126.2.910;
RA Sampedro J., Sieiro C., Revilla G., Gonzalez-Villa T., Zarra I.;
RT "Cloning and expression pattern of a gene encoding an alpha-xylosidase
RT active against xyloglucan oligosaccharides from Arabidopsis.";
RL Plant Physiol. 126:910-920(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD49987.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000269|PubMed:11130712};
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] {ECO:0000305, ECO:0000312|EMBL:AAO11591.1}
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] {ECO:0000305, ECO:0000312|EMBL:AAL09716.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia {ECO:0000269|PubMed:14593172};
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] {ECO:0000305}
RP PROTEIN SEQUENCE OF 28-36, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9188482; DOI=10.1074/jbc.272.25.15841;
RA Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P.,
RA Slabas A.R.;
RT "Differential extraction and protein sequencing reveals major differences
RT in patterns of primary cell wall proteins from plants.";
RL J. Biol. Chem. 272:15841-15848(1997).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16267099; DOI=10.1093/pcp/pci223;
RA Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G., Zarra I.;
RT "Apoplastic glycosidases active against xyloglucan oligosaccharides of
RT Arabidopsis thaliana.";
RL Plant Cell Physiol. 47:55-63(2006).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=20801759; DOI=10.1104/pp.110.163212;
RA Sampedro J., Pardo B., Gianzo C., Guitian E., Revilla G., Zarra I.;
RT "Lack of alpha-xylosidase activity in Arabidopsis alters xyloglucan
RT composition and results in growth defects.";
RL Plant Physiol. 154:1105-1115(2010).
RN [8]
RP FUNCTION, MUTAGENESIS OF GLU-630, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21170548; DOI=10.1007/s00425-010-1330-7;
RA Gunl M., Pauly M.;
RT "AXY3 encodes a alpha-xylosidase that impacts the structure and
RT accessibility of the hemicellulose xyloglucan in Arabidopsis plant cell
RT walls.";
RL Planta 233:707-719(2011).
CC -!- FUNCTION: Glycoside hydrolase releasing xylosyl residues from
CC xyloglucan oligosaccharides at the non-reducing end. Has alpha-
CC xylosidase activity against xylan oligosaccharides. Also has alpha-
CC glucosidase activity against p-nitrophenyl-alpha-D-glucopyranoside. No
CC activity against p-nitrophenyl-D-xyloside.
CC {ECO:0000269|PubMed:11402218, ECO:0000269|PubMed:20801759,
CC ECO:0000269|PubMed:21170548}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-xylose residues
CC with release of alpha-D-xylose.; EC=3.2.1.177;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall. Secreted, extracellular
CC space, apoplast.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. Expressed in cell types undergoing cell wall modifications,
CC including trichomes, vasculature, stomata, and elongating anther
CC filaments. Not detected in pollen. {ECO:0000269|PubMed:16267099,
CC ECO:0000269|PubMed:20801759}.
CC -!- DEVELOPMENTAL STAGE: Expressed at higher levels in younger, faster
CC growing leaves than in older, slower growing leaves.
CC {ECO:0000269|PubMed:11402218}.
CC -!- DISRUPTION PHENOTYPE: No visible growth or morphological phenotypes,
CC with the exception of shorter siliques. Loss of alpha-xylosidase
CC activity and altered xyloglucan composition.
CC {ECO:0000269|PubMed:16267099, ECO:0000269|PubMed:20801759,
CC ECO:0000269|PubMed:21170548}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000255}.
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DR EMBL; AF144078; AAD37363.1; -; Genomic_DNA.
DR EMBL; AF087483; AAD05539.1; -; mRNA.
DR EMBL; AC008075; AAD49987.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34811.1; -; Genomic_DNA.
DR EMBL; AY057482; AAL09716.1; -; mRNA.
DR EMBL; BT002675; AAO11591.1; -; mRNA.
DR PIR; H96709; H96709.
DR RefSeq; NP_177023.1; NM_105527.5.
DR AlphaFoldDB; Q9S7Y7; -.
DR SMR; Q9S7Y7; -.
DR BioGRID; 28406; 3.
DR IntAct; Q9S7Y7; 2.
DR STRING; 3702.AT1G68560.1; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR iPTMnet; Q9S7Y7; -.
DR PaxDb; Q9S7Y7; -.
DR PRIDE; Q9S7Y7; -.
DR ProteomicsDB; 242411; -.
DR EnsemblPlants; AT1G68560.1; AT1G68560.1; AT1G68560.
DR GeneID; 843185; -.
DR Gramene; AT1G68560.1; AT1G68560.1; AT1G68560.
DR KEGG; ath:AT1G68560; -.
DR Araport; AT1G68560; -.
DR TAIR; locus:2026895; AT1G68560.
DR eggNOG; KOG1065; Eukaryota.
DR HOGENOM; CLU_000631_11_1_1; -.
DR InParanoid; Q9S7Y7; -.
DR OMA; YDTYTRG; -.
DR OrthoDB; 151244at2759; -.
DR PhylomeDB; Q9S7Y7; -.
DR BioCyc; ARA:AT1G68560-MON; -.
DR BRENDA; 3.2.1.177; 399.
DR PRO; PR:Q9S7Y7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S7Y7; baseline and differential.
DR Genevisible; Q9S7Y7; AT.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0061634; F:alpha-D-xyloside xylohydrolase; IEA:UniProtKB-EC.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IDA:TAIR.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IDA:TAIR.
DR GO; GO:0080176; F:xyloglucan 1,6-alpha-xylosidase activity; IDA:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR GO; GO:0045493; P:xylan catabolic process; IDA:TAIR.
DR GO; GO:0010411; P:xyloglucan metabolic process; IMP:TAIR.
DR Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR Pfam; PF16863; NtCtMGAM_N; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE 1: Evidence at protein level;
KW Apoplast; Carbohydrate metabolism; Cell wall;
KW Cell wall biogenesis/degradation; Direct protein sequencing; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:9188482"
FT CHAIN 28..915
FT /note="Alpha-xylosidase 1"
FT /id="PRO_0000042740"
FT ACT_SITE 440
FT /evidence="ECO:0000250|UniProtKB:O04931"
FT ACT_SITE 443
FT /evidence="ECO:0000250|UniProtKB:O04931"
FT ACT_SITE 563
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O04931"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 888
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 907
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 630
FT /note="E->K: In axy3.1; Loss of activity and altered
FT xyloglucan composition."
FT /evidence="ECO:0000269|PubMed:21170548"
SQ SEQUENCE 915 AA; 102399 MW; 28F9610D8D7EA657 CRC64;
MASSSSSLAF SLSLLLALIL CFSPTQSYKT IGKGYRLVSI EESPDGGFIG YLQVKQKNKI
YGSDITTLRL FVKHETDSRL RVHITDAKQQ RWEVPYNLLP REQPPQVGKV IGKSRKSPIT
VQEISGSELI FSYTTDPFTF AVKRRSNHET LFNTTSSLVF KDQYLEISTS LPKEASLYGL
GENSQANGIK LVPNEPYTLY TEDVSAINLN TDLYGSHPMY MDLRNVGGKA YAHAVLLLNS
NGMDVFYRGD SLTYKVIGGV FDFYFIAGPS PLNVVDQYTQ LIGRPAPMPY WSLGFHQCRW
GYHNLSVVED VVDNYKKAKI PLDVIWNDDD HMDGHKDFTL NPVAYPRAKL LAFLDKIHKI
GMKYIVINDP GIGVNASYGT FQRAMAADVF IKYEGKPFLA QVWPGPVYFP DFLNPKTVSW
WGDEIKRFHD LVPIDGLWID MNEVSNFCSG LCTIPEGKQC PSGEGPGWVC CLDCKNITKT
RWDDPPYKIN ATGVVAPVGF KTIATSATHY NGVREYDAHS IYGFSETIAT HKGLLNVQGK
RPFILSRSTF VGSGQYAAHW TGDNQGTWQS LQVSISTMLN FGIFGVPMVG SDICGFYPQP
TEELCNRWIE VGAFYPFSRD HANYYSPRQE LYQWDTVADS ARNALGMRYK ILPFLYTLNY
EAHMTGAPIA RPLFFSFPEY TECYGNSRQF LLGSSFMISP VLEQGKTEVE ALFPPGSWYH
MFDMTQAVVS KNGKRVTLPA PLNFVNVHLY QNTILPTQQG GLISKDARTT PFSLVIAFPA
GASEGYATGK LYLDEDELPE MKLGNGQSTY VDFYASVGNG TMKMWSQVKE GKFALSKGWV
IEKVSVLGLR GAGQVSEIQI NGSPMTKKIE VSSKEHTYVI GLEDEEENKS VMVEVRGLEM
LVGKDFNMSW KMGIN
