AVCO1_AVESA
ID AVCO1_AVESA Reviewed; 574 AA.
AC Q38786;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Avenacosidase 1;
DE EC=3.2.1.188;
DE AltName: Full=26-desgluco-avenacosidase 1;
DE AltName: Full=Protein As-Glu1;
DE AltName: Full=Protein As-P60;
DE Flags: Precursor;
GN Name=P60A; Synonyms=GLU1;
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], PROTEIN SEQUENCE OF 56-68; 180-187; 191-197 AND
RP 208-217, AND FUNCTION.
RX PubMed=8013661; DOI=10.1016/0014-5793(94)00503-6;
RA Gus-Mayer S., Brunner H., Schneider-Poetsch H.A., Lottspeich F.,
RA Eckerskorn C., Grimm R., Rudiger W.;
RT "The amino acid sequence previously attributed to a protein kinase or a
RT TCP1-related molecular chaperone and co-purified with phytochrome is a
RT beta-glucosidase.";
RL FEBS Lett. 347:51-54(1994).
RN [2]
RP PROTEIN SEQUENCE OF 56-71; 74-78; 180-187; 191-197; 208-217; 272-281;
RP 346-348; 373-377 AND 439-448, SEQUENCE REVISION TO 100, FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Pirol;
RX PubMed=8000004; DOI=10.1007/bf00028858;
RA Gus-Mayer S., Brunner H., Schneider-Poetsch H.A., Rudiger W.;
RT "Avenacosidase from oat: purification, sequence analysis and biochemical
RT characterization of a new member of the BGA family of beta-glucosidases.";
RL Plant Mol. Biol. 26:909-921(1994).
RN [3]
RP PROTEIN SEQUENCE OF 56-75, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
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 [4]
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).
RN [5]
RP 3D-STRUCTURE MODELING, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15797725; DOI=10.1016/j.jsb.2004.07.007;
RA Kim S.Y., Kim Y.W., Hegerl R., Cyrklaff M., Kim I.S.;
RT "Novel type of enzyme multimerization enhances substrate affinity of oat
RT beta-glucosidase.";
RL J. Struct. Biol. 150:1-10(2005).
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.
CC {ECO:0000269|PubMed:24226684, ECO:0000269|PubMed:8000004,
CC ECO:0000269|PubMed:8013661}.
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:15797725, ECO:0000269|PubMed:24226684,
CC ECO:0000269|PubMed:8000004, ECO:0000269|PubMed:9858780};
CC -!- ACTIVITY REGULATION: Inhibited by N-(3-Dimethylaminopropyl)-N'-
CC ethylcarbodiimide hydrochloride (EDC). {ECO:0000269|PubMed:9858780}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 mM for p-nitrophenyl-beta-D-glucopyranoside (with native
CC enzyme) {ECO:0000269|PubMed:15797725, ECO:0000269|PubMed:24226684,
CC ECO:0000269|PubMed:9858780};
CC KM=1.57 mM for p-nitrophenyl-beta-D-glucopyranoside (with
CC homomultimeric recombinant enzyme) {ECO:0000269|PubMed:15797725,
CC ECO:0000269|PubMed:24226684, ECO:0000269|PubMed:9858780};
CC KM=1.48 mM for p-nitrophenyl-beta-D-glucopyranoside (with
CC heteromultimeric recombinant enzyme) {ECO:0000269|PubMed:15797725,
CC ECO:0000269|PubMed:24226684, ECO:0000269|PubMed:9858780};
CC KM=12 uM for avenacosides (with native enzyme)
CC {ECO:0000269|PubMed:15797725, ECO:0000269|PubMed:24226684,
CC ECO:0000269|PubMed:9858780};
CC KM=0.4 mM for genistin (with native enzyme)
CC {ECO:0000269|PubMed:15797725, ECO:0000269|PubMed:24226684,
CC ECO:0000269|PubMed:9858780};
CC Note=The activity increases with rising aggregation of the enzyme.
CC kcat is 982000 sec(-1) with avenacosides as substrate. kcat is 3090
CC sec(-1) with p-nitrophenyl-beta-D-glucopyranoside as substrate. kcat
CC is 290 sec(-1) with genistin as substrate.;
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:15797725,
CC ECO:0000269|PubMed:24226684, ECO:0000269|PubMed:9858780};
CC -!- SUBUNIT: Homo- and heteromultimer with P60B in a 1:1 stoichiometry.
CC Aggregates to form the fibrillar stromacentre.
CC {ECO:0000269|PubMed:8000004, ECO:0000269|PubMed:9858780}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:24226684, ECO:0000269|PubMed:8000004}. Note=Found
CC in a fibrillar spherulite called stromacentre.
CC -!- TISSUE SPECIFICITY: Expressed in caryopses, coleoptiles, primary
CC leaves, and etiolated and green seedlings, but not in roots.
CC {ECO:0000269|PubMed:8000004}.
CC -!- MISCELLANEOUS: Long fibrillar homomultimers are formed by linear
CC stacking of trimeric units. The multimerization of the enzyme promotes
CC formation of a long central channel with narrow openings at the sides.
CC The active sites are localized inside the tunnels, constraining the
CC accessibility of substrates and products.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; X78433; CAA55196.1; -; mRNA.
DR PIR; S43128; S43128.
DR PIR; S45723; S45723.
DR PIR; S50756; S50756.
DR AlphaFoldDB; Q38786; -.
DR SMR; Q38786; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; ag:CAA55196; -.
DR BRENDA; 3.2.1.186; 588.
DR SABIO-RK; Q38786; -.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
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..55
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:8000004,
FT ECO:0000269|PubMed:8013661, ECO:0000269|PubMed:9858780"
FT CHAIN 56..574
FT /note="Avenacosidase 1"
FT /id="PRO_5000146241"
FT ACT_SITE 238
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 454
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 505
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 512..513
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 258..264
FT /evidence="ECO:0000250"
SQ 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
