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Reviewed, UniProtKB/Swiss-Prot P49235 (BGLC_MAIZE)

Last modified November 25, 2008. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Beta-glucosidase, chloroplastic
    EC=3.2.1.21
Alternative name(s):
    Gentiobiase
    Cellobiase
    Beta-D-glucoside glucohydrolase
Gene names
Name: GLU1
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACCAD clade › Panicoideae › Andropogoneae › Zea

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Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Is implicated in many functions such as ABA metabolism, hydrolysis of conjugated gibberellins, conversion of storage forms of cytokinins to active forms. Also acts in defense of young plant parts against pests via the production of hydroxamic acids from hydroxamic acid glucosides. Enzymatic activity is highly correlated with plant growth.

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.

Enzyme regulation

Reversibly inhibited by micromolar concentrations of Hg(2+) or Ag(+), but irreversibly inhibited by alkylation in presence of urea. Competitive inhibition by p-nitrophenyl beta-D-thioglucoside (pNPTGlc), glucotetrazole, and para-hydroxy-S-mandelonitrile beta-glucoside (dhurrin).

Subunit structure

Homodimer.

Subcellular location

Plastid › chloroplast.

Tissue specificity

Most abundant in the coleoptile.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.14 mM for 4-methylumbelliferyl beta-D-glucopyranoside (MUG)

KM=0.64 mM for p-nitrophenyl beta-D-glucopyranoside (PNPG)

KM=98 µM for DIMBOA-beta-D-glucoside

pH dependence:

Optimum pH is 5.8.

Temperature dependence:

Optimum temperature is 50 degrees Celsius. Loses activity when is heated at 55 degrees Celsius.

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Ontologies

Keywords

   Biological processCytokinin signaling pathway
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cytokinin mediated signaling

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbeta-glucosidase activity

Inferred from electronic annotation. Source: EC

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5454Chloroplast
Chain55 – 566512Beta-glucosidase, chloroplastic
PRO_0000011763

Regions

Region325 – 36137Dimerization
Region394 – 40512Dimerization
Region450 – 4534Dimerization
Region518 – 5192Substrate binding

Sites

Active site2451Proton donor
Active site4601Nucleophile
Binding site921Substrate
Binding site3871Substrate
Binding site5111Substrate

Amino acid modifications

Disulfide bond264 ↔ 270

Experimental info

Mutagenesis2451E → D or Q: Loss of activity
Mutagenesis2521F → I, W or Y: Reduced substrate affinity
Mutagenesis2641C → A, D, R or S: Loss of activity due to impaired dimerization
Mutagenesis2701C → A, D, R or S: Loss of activity due to impaired dimerization
Mutagenesis3171M → F, I or V: No effect
Mutagenesis4601E → D: Loss of activity and impaired dimerization
Mutagenesis4601E → Q: Loss of activity
Mutagenesis4631I → D: Loss of activity due to impaired dimerization
Sequence conflict4771A → D in CAA52293. Ref.2
Sequence conflict5511E → Q in CAA52293. Ref.2
Sequence conflict5541T → A in CAA52293. Ref.2

Secondary structure

1 ................................................................................... 566
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P49235-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 4EA241258AE3641B

FASTA56664,237
        10         20         30         40         50         60 
MAPLLAAAMN HAAAHPGLRS HLVGPNNESF SRHHLPSSSP QSSKRRCNLS FTTRSARVGS 

        70         80         90        100        110        120 
QNGVQMLSPS EIPQRDWFPS DFTFGAATSA YQIEGAWNED GKGESNWDHF CHNHPERILD 

       130        140        150        160        170        180 
GSNSDIGANS YHMYKTDVRL LKEMGMDAYR FSISWPRILP KGTKEGGINP DGIKYYRNLI 

       190        200        210        220        230        240 
NLLLENGIEP YVTIFHWDVP QALEEKYGGF LDKSHKSIVE DYTYFAKVCF DNFGDKVKNW 

       250        260        270        280        290        300 
LTFNEPQTFT SFSYGTGVFA PGRCSPGLDC AYPTGNSLVE PYTAGHNILL AHAEAVDLYN 

       310        320        330        340        350        360 
KHYKRDDTRI GLAFDVMGRV PYGTSFLDKQ AEERSWDINL GWFLEPVVRG DYPFSMRSLA 

       370        380        390        400        410        420 
RERLPFFKDE QKEKLAGSYN MLGLNYYTSR FSKNIDISPN YSPVLNTDDA YASQEVNGPD 

       430        440        450        460        470        480 
GKPIGPPMGN PWIYMYPEGL KDLLMIMKNK YGNPPIYITE NGIGDVDTKE TPLPMEAALN 

       490        500        510        520        530        540 
DYKRLDYIQR HIATLKESID LGSNVQGYFA WSLLDNFEWF AGFTERYGIV YVDRNNNCTR 

       550        560 
YMKESAKWLK EFNTAKKPSK KILTPA

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References

[1]Esen A., Shahid M.
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Inbred line K55.
Tissue: Shoot.
[2]"Release of active cytokinin by a beta-glucosidase localized to the maize root meristem."
Brzobohaty B., Moore I., Kristoffersen P., Bako L., Campos N., Schell J., Palme K.
Science 262:1051-1054(1993) [PubMed: 8235622] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. MUTIN.
Tissue: Coleoptile.
[3]"Purification and partial characterization of Maize (Zea Mays L.) beta-glucosidase."
Esen A.
Plant Physiol. 98:174-182(1992) [PubMed: 16668611] [Abstract]
Cited for: PROTEIN SEQUENCE OF 55-74, CHARACTERIZATION.
Strain: cv. Inbred line K55.
[4]"The maize two dimensional gel protein database: towards an integrated genome analysis program."
Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., Pernollet J.-C., Zivy M., de Vienne D.
Theor. Appl. Genet. 93:997-1005(1996) [Agricola: IND20551642]
Cited for: PROTEIN SEQUENCE OF 55-69; 165-174; 207-213 AND 217-235.
Tissue: Coleoptile.
[5]"Expression, single-step purification, and matrix-assisted refolding of a maize cytokinin glucoside-specific beta-glucosidase."
Zouhar J., Nanak E., Brzobohaty B.
Protein Expr. Purif. 17:153-162(1999) [PubMed: 10497081] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[6]"Crystal structure of a monocotyledon (maize ZMGlu1) beta-glucosidase and a model of its complex with p-nitrophenyl beta-D-thioglucoside."
Czjzek M., Cicek M., Zamboni V., Burmeister W.P., Bevan D.R., Henrissat B., Esen A.
Biochem. J. 354:37-46(2001) [PubMed: 11171077] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 55-566 IN COMPLEX WITH THE INHIBITOR P-NITROPHENYL BETA-D-THIOGLUCOSIDE, ENZYME REGULATION, HOMODIMER, DISULFID BONDS.
[7]"The mechanism of substrate (aglycone) specificity in beta -glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes."
Czjzek M., Cicek M., Zamboni V., Bevan D.R., Henrissat B., Esen A.
Proc. Natl. Acad. Sci. U.S.A. 97:13555-13560(2000) [PubMed: 11106394] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 55-566 IN COMPLEX WITH SUBSTRATES AND THE INHIBITOR PARA-HYDROXY-S-MANDELONITRILE BETA-GLUCOSIDE, MUTAGENESIS OF GLU-245, ENZYME REGULATION.
[8]"Insights into the functional architecture of the catalytic center of a maize beta-glucosidase Zm-p60.1."
Zouhar J., Vevodova J., Marek J., Damborsky J., Su X.-D., Brzobohaty B.
Plant Physiol. 127:973-985(2001) [PubMed: 11706179] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 60-566, MUTAGENESIS OF GLU-245; PHE-252; MET-317; GLU-460 AND ILE-463, HOMODIMER, DISULFID BONDS.
[9]"Structural determinants of substrate specificity in family 1 beta-glucosidases: novel insights from the crystal structure of sorghum dhurrinase-1, a plant beta-glucosidase with strict specificity, in complex with its natural substrate."
Verdoucq L., Moriniere J., Bevan D.R., Esen A., Vasella A., Henrissat B., Czjzek M.
J. Biol. Chem. 279:31796-31803(2004) [PubMed: 15148317] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 55-566 IN COMPLEX WITH SUBSTRATES AND THE INHIBITOR GLUCOTETRAZOLE, MUTAGENESIS OF GLU-245, BIOPHYSICOCHEMICAL PROPERTIES, DISULFID BONDS.

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Cross-references

Sequence databases

U25157 mRNA. Translation: AAA65946.1.
X74217 mRNA. Translation: CAA52293.1.
PIRA48860.
RefSeqNP_001105454.1.
UniGeneZm.94498

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1E1EX-ray2.50A/B55-566[»]