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Avenacosidase 1 (EC 3.2.1.188) (26-desgluco-avenacosidase 1) (Protein As-Glu1) (Protein As-P60)

 AVCO1_AVESA             Reviewed;         574 AA.
Q38786;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-MAY-2017, entry version 82.
RecName: Full=Avenacosidase 1;
EC=3.2.1.188;
AltName: Full=26-desgluco-avenacosidase 1;
AltName: Full=Protein As-Glu1;
AltName: Full=Protein As-P60;
Flags: Precursor;
Name=P60A; Synonyms=GLU1;
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], PROTEIN SEQUENCE OF 56-68; 180-187;
191-197 AND 208-217, AND FUNCTION.
PubMed=8013661; DOI=10.1016/0014-5793(94)00503-6;
Gus-Mayer S., Brunner H., Schneider-Poetsch H.A., Lottspeich F.,
Eckerskorn C., Grimm R., Rudiger W.;
"The amino acid sequence previously attributed to a protein kinase or
a TCP1-related molecular chaperone and co-purified with phytochrome is
a beta-glucosidase.";
FEBS Lett. 347:51-54(1994).
[2]
PROTEIN SEQUENCE OF 56-71; 74-78; 180-187; 191-197; 208-217; 272-281;
346-348; 373-377 AND 439-448, SEQUENCE REVISION TO 100, FUNCTION,
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE
SPECIFICITY.
STRAIN=cv. Pirol;
PubMed=8000004; DOI=10.1007/BF00028858;
Gus-Mayer S., Brunner H., Schneider-Poetsch H.A., Rudiger W.;
"Avenacosidase from oat: purification, sequence analysis and
biochemical characterization of a new member of the BGA family of
beta-glucosidases.";
Plant Mol. Biol. 26:909-921(1994).
[3]
PROTEIN SEQUENCE OF 56-75, SUBUNIT, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
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).
[4]
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).
[5]
3D-STRUCTURE MODELING, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=15797725; DOI=10.1016/j.jsb.2004.07.007;
Kim S.Y., Kim Y.W., Hegerl R., Cyrklaff M., Kim I.S.;
"Novel type of enzyme multimerization enhances substrate affinity of
oat beta-glucosidase.";
J. Struct. Biol. 150:1-10(2005).
-!- 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.
{ECO:0000269|PubMed:24226684, ECO:0000269|PubMed:8000004,
ECO:0000269|PubMed:8013661}.
-!- CATALYTIC ACTIVITY: Avenacoside B + H(2)O = 26-desgluco-
avenacoside B + D-glucose. {ECO:0000269|PubMed:15797725,
ECO:0000269|PubMed:24226684, ECO:0000269|PubMed:8000004,
ECO:0000269|PubMed:9858780}.
-!- ENZYME REGULATION: Inhibited by N-(3-Dimethylaminopropyl)-N'-
ethylcarbodiimide hydrochloride (EDC).
{ECO:0000269|PubMed:9858780}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.2 mM for p-nitrophenyl-beta-D-glucopyranoside (with native
enzyme) {ECO:0000269|PubMed:15797725,
ECO:0000269|PubMed:24226684, ECO:0000269|PubMed:9858780};
KM=1.57 mM for p-nitrophenyl-beta-D-glucopyranoside (with
homomultimeric recombinant enzyme) {ECO:0000269|PubMed:15797725,
ECO:0000269|PubMed:24226684, ECO:0000269|PubMed:9858780};
KM=1.48 mM for p-nitrophenyl-beta-D-glucopyranoside (with
heteromultimeric recombinant enzyme)
{ECO:0000269|PubMed:15797725, ECO:0000269|PubMed:24226684,
ECO:0000269|PubMed:9858780};
KM=12 uM for avenacosides (with native enzyme)
{ECO:0000269|PubMed:15797725, ECO:0000269|PubMed:24226684,
ECO:0000269|PubMed:9858780};
KM=0.4 mM for genistin (with native enzyme)
{ECO:0000269|PubMed:15797725, ECO:0000269|PubMed:24226684,
ECO:0000269|PubMed:9858780};
Note=The activity increases with rising aggregation of the
enzyme. kcat is 982000 sec(-1) with avenacosides as substrate.
kcat is 3090 sec(-1) with p-nitrophenyl-beta-D-glucopyranoside
as substrate. kcat is 290 sec(-1) with genistin as substrate.;
pH dependence:
Optimum pH is 6.0. {ECO:0000269|PubMed:15797725,
ECO:0000269|PubMed:24226684, ECO:0000269|PubMed:9858780};
-!- SUBUNIT: Homo- and heteromultimer with P60B in a 1:1
stoichiometry. Aggregates to form the fibrilar stromacentre.
{ECO:0000269|PubMed:8000004, ECO:0000269|PubMed:9858780}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000269|PubMed:24226684, ECO:0000269|PubMed:8000004}.
Note=Found in a fibrillar spherulite called stromacentre.
-!- TISSUE SPECIFICITY: Expressed in caryopses, coleoptiles, primary
leaves, and etiolated and green seedlings, but not in roots.
{ECO:0000269|PubMed:8000004}.
-!- MISCELLANEOUS: Long fibrillar homomultimers are formed by linear
stacking of trimeric units. The multimerization of the enzyme
promotes formation of a long central channel with narrow openings
at the sides. The active sites are localized inside the tunnels,
constraining the accessibility of substrates and products.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
{ECO:0000305}.
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EMBL; X78433; CAA55196.1; -; mRNA.
PIR; S43128; S43128.
PIR; S45723; S45723.
PIR; S50756; S50756.
ProteinModelPortal; Q38786; -.
SMR; Q38786; -.
CAZy; GH1; Glycoside Hydrolase Family 1.
KEGG; ag:CAA55196; -.
KO; K20835; -.
BRENDA; 3.2.1.186; 588.
GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
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 55 Chloroplast. {ECO:0000269|PubMed:8000004,
ECO:0000269|PubMed:8013661,
ECO:0000269|PubMed:9858780}.
CHAIN 56 574 Avenacosidase 1.
/FTId=PRO_5000146241.
REGION 512 513 Substrate binding. {ECO:0000250}.
ACT_SITE 238 238 Proton donor. {ECO:0000250}.
ACT_SITE 454 454 Nucleophile. {ECO:0000250}.
BINDING 88 88 Substrate. {ECO:0000250}.
BINDING 237 237 Substrate. {ECO:0000250}.
BINDING 505 505 Substrate. {ECO:0000250}.
DISULFID 258 264 {ECO:0000250}.
SEQUENCE 574 AA; 65041 MW; 5C6312DCAF251631 CRC64;
MALLCSALSN STHPSFRSHI GANSENLWHL SADPAQKSKR RCNLTLSSRA ARISSALESA
KQVKPWQVPK RDWFPPEFMF GAASAAYQIE GAWNEGGKGP SSWDNFCHSH PDRIMDKSNA
DVAANSYYMY KEDVRMLKEI GMDSYRFSIS WPRILPKGTL DGGINHEGIQ YYNDLLDCLI
ENGIKPYITL FHWDTPQALA DEYKDFLDRR IVKDYTDYAT VCFEHFGDKV KNWFTFNEPH
SFCGLGYGTG LHAPGARCSA GMTCVIPEED ALRNPYIVGH NLLLAHAETV DVYNKFYKGD
DGQIGMVLDV MAYEPYGNNF LDQQAQERAI DFHIGWFLEP MVRGDYPFSM RSLVGDRLPF
FTKSEQEKLV SSYDFVGINY YTSRFAKHID ISPEFIPKIN TDDVYSNPEV NDSNGIPIGP
DVGMYFIYSY PKGLKNILLR MKEKYGNPPI YITENGTADM DGWGNPPMTD PLDDPLRIEY
LQQHMTAIKE AIDLGRRTLR GHFTWSLIDN FEWSLGYLSR FGIVYIDRND GCKRIMKKSA
KWLKEFNGAT KKLNNKILGA SSCCSGVTHG GGTA


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