XYL2_ARATH
ID XYL2_ARATH Reviewed; 868 AA.
AC F4J6T7; Q9LZT7;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Putative alpha-xylosidase 2;
DE EC=3.2.1.177;
DE Flags: Precursor;
GN Name=XYL2; OrderedLocusNames=At3g45940; ORFNames=F16L2.150;
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=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 [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 IDENTIFICATION.
RC STRAIN=cv. Columbia;
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 [4]
RP IDENTIFICATION.
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).
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 {ECO:0000250}. Secreted,
CC extracellular space, apoplast {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. Inactivating mutations
CC are found throughout the sequence in cv. Wassilewskija
CC (PubMed:20801759) and no expression of the gene is detected in cv.
CC Columbia (PubMed:16267099). {ECO:0000305|PubMed:16267099,
CC ECO:0000305|PubMed:20801759}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB82818.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162459; CAB82818.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78092.1; -; Genomic_DNA.
DR PIR; T47534; T47534.
DR RefSeq; NP_190180.1; NM_114463.1.
DR AlphaFoldDB; F4J6T7; -.
DR SMR; F4J6T7; -.
DR STRING; 3702.AT3G45940.1; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR PaxDb; F4J6T7; -.
DR PRIDE; F4J6T7; -.
DR ProteomicsDB; 243089; -.
DR EnsemblPlants; AT3G45940.1; AT3G45940.1; AT3G45940.
DR GeneID; 823737; -.
DR Gramene; AT3G45940.1; AT3G45940.1; AT3G45940.
DR KEGG; ath:AT3G45940; -.
DR Araport; AT3G45940; -.
DR TAIR; locus:2077142; AT3G45940.
DR eggNOG; KOG1065; Eukaryota.
DR HOGENOM; CLU_000631_11_1_1; -.
DR InParanoid; F4J6T7; -.
DR OMA; CKYGYWD; -.
DR OrthoDB; 151244at2759; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J6T7; baseline and differential.
DR Genevisible; F4J6T7; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; 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:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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 5: Uncertain;
KW Apoplast; Carbohydrate metabolism; Cell wall;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..868
FT /note="Putative alpha-xylosidase 2"
FT /id="PRO_0000420414"
FT ACT_SITE 437
FT /evidence="ECO:0000250"
FT ACT_SITE 440
FT /evidence="ECO:0000250"
FT ACT_SITE 515
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 798
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 804
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 847
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 868 AA; 97450 MW; 8698A823FFB97355 CRC64;
MASCLSLLVA IILCFSSLQC SNAIGKGYRL ISMEKSPDDG SFIGYLQVKQ SNKIYGSDIT
ILRLFINYRT DHRLRVHITD AKKQRWEVPY NLLRREQPPN VIGKSRKSPV TVQEISGPEL
ILIFTVDPFS FAVRRRSNGE TIFNTSSSDE SFGEMVFKDQ YLEISTSLPK DASLYGFGEN
SQANGIKLVP NEPYTLFTED VSAFNLNTDL YGSHPVYMDL RNVSGKAYAH SVLLLNSHGM
DVFYRGDSLT YKVIGGVFDF YFFAGPSPLN VVDQYTSLIG RPAPMPYWSL GFHQCRWGYR
NVSVVKDVVD NYQKAKIPLD VIWNDADYMD GYKDFTLDLV NFPHAKLLSF LDRIHKMGMK
YVVIKDPGIG VNASYGVYQR GMASDVFIKY EGKPFLAQVW PGPVYFPDFL NPKTVSWWGD
EIRRFHELVP IDGLWIDMNE INATGHKASL GFKTIPTSAY HYNGVREYDA HSIYGFSEAI
ATHKALLAVQ GKRPFILSRS TFVGSGQYAA HWTGDNQGTW QSLQVSISTM LNFGIFGVPM
VGSDICGFFP PTPEELCNRW IEVGAFYPFS RDHADYYAPR KELYQWGTVA ESARNALGMR
YKLLPFLYTL NYEAHMSGAP IARPLFFSFP EFTECYGLSK QFLLGSSLMI SPVLEQGKTQ
VEALFPPGSW YHMFDMTQVV VSKNGRLFTL PAPFNVVNVH LYQNAILPMQ QVVAFPAGAS
EGYASGKLFL DDDELPEMKL GNGKSTYIDF YASVGNESVK IWSQVKEGQF ALSQGLVIEK
VIVLGLKGTW KVSEILLNGS SISNETKTIE VSSKEQMYVV GSEDEGESKS FMVELKGLEM
LVGKDFNISW KMASTNVLSM AGNEVIAR
