AVCO2_AVESA
ID AVCO2_AVESA Reviewed; 578 AA.
AC Q9ZP27;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Avenacosidase 2;
DE EC=3.2.1.188;
DE AltName: Full=26-desgluco-avenacosidase 2;
DE AltName: Full=Protein As-Glu2;
DE Flags: Precursor;
GN Name=P60B; Synonyms=GLU2;
OS Avena sativa (Oat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Aveninae; Avena.
OX NCBI_TaxID=4498;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11061978; DOI=10.1006/jmbi.2000.4130;
RA Kim Y.W., Kang K.S., Kim S.Y., Kim I.S.;
RT "Formation of fibrillar multimers of oat beta-glucosidase isoenzymes is
RT mediated by the As-Glu1 monomer.";
RL J. Mol. Biol. 303:831-842(2000).
RN [2]
RP PROTEIN SEQUENCE OF 58-76, AND SUBUNIT.
RC STRAIN=cv. Garry;
RX PubMed=9858780; DOI=10.1016/s0167-4838(98)00209-x;
RA Kim Y.W., Kim I.S.;
RT "Subunit composition and oligomer stability of oat beta-glucosidase
RT isozymes.";
RL Biochim. Biophys. Acta 1388:457-464(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24226684; DOI=10.1007/bf00958960;
RA Nisius A.;
RT "The stromacentre in Avena plastids: an aggregation of beta-glucosidase
RT responsible for the activation of oat-leaf saponins.";
RL Planta 173:474-481(1988).
CC -!- FUNCTION: Beta-glucosidase acting as a preformed defense system.
CC Hydrolyzes the bisdesmosides avenacosides A and B to 26-desgluco-
CC avenacosides exhibiting fungicidal activity. Can use beta-fucoside >
CC beta-glucoside > beta-galactoside > beta-xyloside as substrates, but
CC not alpha-glycosides, beta-thioglucosides and disaccharides (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:24226684}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=avenacoside B + H2O = 26-desgluco-avenacoside B + D-glucose;
CC Xref=Rhea:RHEA:38911, ChEBI:CHEBI:2938, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:75931; EC=3.2.1.188;
CC Evidence={ECO:0000269|PubMed:11061978, ECO:0000269|PubMed:24226684};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.48 mM for p-nitrophenyl-beta-D-glucopyranoside (with
CC heteromultimeric recombinant enzyme) {ECO:0000269|PubMed:11061978,
CC ECO:0000269|PubMed:24226684};
CC KM=2.47 mM for p-nitrophenyl-beta-D-glucopyranoside (with homodimeric
CC recombinant enzyme) {ECO:0000269|PubMed:11061978,
CC ECO:0000269|PubMed:24226684};
CC -!- SUBUNIT: Heteromultimer with P60A in a 1:1 stoichiometry. Aggregates to
CC form the fibrillar stromacentre. {ECO:0000269|PubMed:11061978,
CC ECO:0000269|PubMed:9858780}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:24226684}. Note=Found in a fibrillar spherulite
CC called stromacentre.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AF082991; AAD02839.1; -; mRNA.
DR AlphaFoldDB; Q9ZP27; -.
DR SMR; Q9ZP27; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR SABIO-RK; Q9ZP27; -.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Disulfide bond; Glycosidase;
KW Hydrolase; Plant defense; Plastid; Transit peptide.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:9858780"
FT CHAIN 58..578
FT /note="Avenacosidase 2"
FT /id="PRO_0000428641"
FT ACT_SITE 239
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 454
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 504
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 511..512
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 258..264
FT /evidence="ECO:0000250"
SQ SEQUENCE 578 AA; 65693 MW; FA800D307BAEB7E8 CRC64;
MALLCSALSN STHPSFRSHI AGANSENLWH LSAHPAQKSK RRCNLTLSSR AAARISSALE
SGKLKPWQIP KRDWFPPEFT FGAASAAYQI EGAWNEGGKG PSSWDNFCHN YPERIMDGSN
WDVAANSYYM YKEDVRMLKE IGMDSYRFSI SWPRILPEGT LEGGINHEGI QYYNDLLDCL
IENGIKPYIT LFHWDTPQAL ADKYNDFLDR RIVKDYTDYA TVCFEHFGDK VKNWITFNEP
HSFCGLAYGT GLHAPGLCSP GMDCAIPQGD ALRQPYIVGH NLLLAHAETV DVYKKFYKGD
DGQIGMVMDV MAYEPYGNNF VDQQAQERSI DFHIGWFLEP MVRGDYPFSM RSLVGDRLPF
FTKSEQEKLV SSYDFVGINY YTARFSEHID ISPEIIPKLN TDDAYSTPEF NDSNGIPIGP
DLGMYWILSY PKGLKDILLL MKEKYGNPPI YITENGTADM DGWGNPPMTD PLDDPLRIEY
LQQHMTAIKE AIDLGADVRG HFTWSLIDNF EWSMGYLSRF GIVYIDRNDG FKRIMKKSAK
WLKEFNGATK EVNNKILGAS SCCSGELMWF LVQNPYGK
