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Avenacosidase 2 (EC 3.2.1.188) (26-desgluco-avenacosidase 2) (Protein As-Glu2)

 AVCO2_AVESA             Reviewed;         578 AA.
Q9ZP27;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
10-MAY-2017, entry version 74.
RecName: Full=Avenacosidase 2;
EC=3.2.1.188;
AltName: Full=26-desgluco-avenacosidase 2;
AltName: Full=Protein As-Glu2;
Flags: Precursor;
Name=P60B; Synonyms=GLU2;
Avena sativa (Oat).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Pooideae; Poodae; Poeae; Aveninae; Avena.
NCBI_TaxID=4498;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11061978; DOI=10.1006/jmbi.2000.4130;
Kim Y.W., Kang K.S., Kim S.Y., Kim I.S.;
"Formation of fibrillar multimers of oat beta-glucosidase isoenzymes
is mediated by the As-Glu1 monomer.";
J. Mol. Biol. 303:831-842(2000).
[2]
PROTEIN SEQUENCE OF 58-76, AND SUBUNIT.
STRAIN=cv. Garry;
PubMed=9858780; DOI=10.1016/S0167-4838(98)00209-X;
Kim Y.W., Kim I.S.;
"Subunit composition and oligomer stability of oat beta-glucosidase
isozymes.";
Biochim. Biophys. Acta 1388:457-464(1998).
[3]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBCELLULAR LOCATION.
PubMed=24226684; DOI=10.1007/BF00958960;
Nisius A.;
"The stromacentre in Avena plastids: an aggregation of beta-
glucosidase responsible for the activation of oat-leaf saponins.";
Planta 173:474-481(1988).
-!- FUNCTION: Beta-glucosidase acting as a preformed defense system.
Hydrolyzes the bisdesmosides avenacosides A and B to 26-desgluco-
avenacosides exhibiting fungicidal activity. Can use beta-fucoside
> beta-glucoside > beta-galactoside > beta-xyloside as substrates,
but not alpha-glycosides, beta-thioglucosides and disaccharides
(By similarity). {ECO:0000250, ECO:0000269|PubMed:24226684}.
-!- CATALYTIC ACTIVITY: Avenacoside B + H(2)O = 26-desgluco-
avenacoside B + D-glucose. {ECO:0000269|PubMed:11061978,
ECO:0000269|PubMed:24226684}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.48 mM for p-nitrophenyl-beta-D-glucopyranoside (with
heteromultimeric recombinant enzyme)
{ECO:0000269|PubMed:11061978, ECO:0000269|PubMed:24226684};
KM=2.47 mM for p-nitrophenyl-beta-D-glucopyranoside (with
homodimeric recombinant enzyme) {ECO:0000269|PubMed:11061978,
ECO:0000269|PubMed:24226684};
-!- SUBUNIT: Heteromultimer with P60A in a 1:1 stoichiometry.
Aggregates to form the fibrilar stromacentre.
{ECO:0000269|PubMed:11061978, ECO:0000269|PubMed:9858780}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000269|PubMed:24226684}. Note=Found in a fibrillar
spherulite called stromacentre.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
{ECO:0000305}.
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EMBL; AF082991; AAD02839.1; -; mRNA.
ProteinModelPortal; Q9ZP27; -.
SMR; Q9ZP27; -.
CAZy; GH1; Glycoside Hydrolase Family 1.
GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
InterPro; IPR001360; Glyco_hydro_1.
InterPro; IPR033132; Glyco_hydro_1_N_CS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR10353; PTHR10353; 1.
Pfam; PF00232; Glyco_hydro_1; 1.
PRINTS; PR00131; GLHYDRLASE1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
1: Evidence at protein level;
Chloroplast; Direct protein sequencing; Disulfide bond; Glycosidase;
Hydrolase; Plant defense; Plastid; Transit peptide.
TRANSIT 1 57 Chloroplast.
{ECO:0000269|PubMed:9858780}.
CHAIN 58 578 Avenacosidase 2.
/FTId=PRO_0000428641.
REGION 511 512 Substrate binding. {ECO:0000250}.
ACT_SITE 239 239 Proton donor. {ECO:0000250}.
ACT_SITE 454 454 Nucleophile. {ECO:0000250}.
BINDING 89 89 Substrate. {ECO:0000250}.
BINDING 238 238 Substrate. {ECO:0000250}.
BINDING 504 504 Substrate. {ECO:0000250}.
DISULFID 258 264 {ECO:0000250}.
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


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