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P49235 (HGGL1_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplastic

EC=3.2.1.182
Alternative name(s):
Beta-D-glucoside glucohydrolase
Beta-glucosidase 1
Short name=ZmGlu1
EC=3.2.1.21
Gene names
Name:GLU1
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

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

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. The preferred substrate is DIMBOA-beta-D-glucoside. Hydrolyzes the chromogenic substrate 6-bromo-2-naphthyl-beta-D-glucoside (6BNGlc) and various artificial aryl beta-glucosides. No activity with cellobiose, arbutin, gentiobiose, linamarin or dhurrin as substrates. Ref.3 Ref.5 Ref.6

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Ref.5 Ref.6

(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside + H2O = 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one + D-glucose. Ref.5 Ref.6

(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside + H2O = 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one + D-glucose. Ref.5 Ref.6

Enzyme regulation

Reversibly inhibited by micromolar concentrations of Hg2+ 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). Ref.8 Ref.9

Subunit structure

Homo- and heterodimer. Ref.3 Ref.6 Ref.10

Subcellular location

Plastidchloroplast.

Tissue specificity

Expressed in all seedling parts. Most abundant in the coleoptile. Ref.6

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.14 mM for 4-methylumbelliferyl beta-D-glucopyranoside (MUG) Ref.3 Ref.5 Ref.6 Ref.7 Ref.11

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

KM=0.41 mM for p-nitrophenyl beta-D-glucopyranoside (PNPG) (with recombinant enzyme)

KM=98 µM for DIMBOA-beta-D-glucoside

KM=0.251 mM for n-octyl-beta-D-glucopyranoside

KM=0.394 mM for p-nitrophenyl beta-D-xyloside

KM=0.648 mM for p-nitrophenyl beta-D-fucopyranoside

KM=0.674 mM for p-nitrophenyl beta-D-cellobioside

KM=0.769 mM for p-nitrophenyl beta-D-mannopyranoside

KM=1.64 mM for o-nitrophenyl beta-D-glucopyranoside

KM=1.42 mM for o-nitrophenyl beta-D-glucopyranoside (with recombinant enzyme)

KM=4.32 mM for p-nitrophenyl beta-D-galactopyranoside

Vmax=225.4 µmol/h/µg enzyme with p-nitrophenyl beta-D-glucopyranoside as substrate (with recombinant enzyme)

Vmax=282.7 µmol/h/µg enzyme with o-nitrophenyl beta-D-glucopyranoside as substrate (with recombinant enzyme)

pH dependence:

Optimum pH is 5.8.

Temperature dependence:

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

Ontologies

Keywords
   Biological processCytokinin signaling pathway
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cytokinin-activated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5454Chloroplast Ref.3 Ref.4
Chain55 – 5665124-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplastic
PRO_0000011763

Regions

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

Sites

Active site2451Proton donor By similarity
Active site4601Nucleophile By similarity
Binding site921Substrate
Binding site1961Substrate
Binding site2441Substrate
Binding site3871Substrate
Binding site5111Substrate

Amino acid modifications

Disulfide bond264 ↔ 270 Ref.8 Ref.10 Ref.11

Experimental info

Mutagenesis2451E → D or Q: Loss of activity. Ref.9 Ref.10 Ref.11
Mutagenesis2521F → I, W or Y: Reduced substrate affinity. Ref.10
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. Ref.10
Mutagenesis4601E → D: Loss of activity and impaired dimerization. Ref.10
Mutagenesis4601E → Q: Loss of activity. Ref.10
Mutagenesis4631I → D: Loss of activity due to impaired dimerization. Ref.10
Sequence conflict4771A → D in CAA52293. Ref.2
Sequence conflict5511E → Q in CAA52293. Ref.2
Sequence conflict5541T → A in CAA52293. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P49235 [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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 55-74, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
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] [Europe PMC]
Cited for: PROTEIN SEQUENCE OF 55-69; 165-174; 207-213 AND 217-235.
Tissue: Coleoptile.
[5]"Substrate specificity of maize beta-glucosidase."
Babcock G.D., Esen A.
Plant Sci. 101:31-39(1994)
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"Expression of soluble and catalytically active plant (monocot) beta-glucosidases in E. coli."
Cicek M., Esen A.
Biotechnol. Bioeng. 63:392-400(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBUNIT, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[7]"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] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[8]"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] [Europe PMC] [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, DISULFIDE BONDS.
[9]"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] [Europe PMC] [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.
[10]"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] [Europe PMC] [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, SUBUNIT, DISULFIDE BONDS.
[11]"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] [Europe PMC] [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, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U25157 mRNA. Translation: AAA65946.1.
X74217 mRNA. Translation: CAA52293.1.
PIRA48860.
RefSeqNP_001105454.1. NM_001111984.1.
UniGeneZm.94498.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E1EX-ray2.50A/B55-566[»]
1E1FX-ray2.60A/B55-566[»]
1E4LX-ray2.20A/B55-566[»]
1E4NX-ray2.10A/B55-566[»]
1E55X-ray2.00A/B55-566[»]
1E56X-ray2.10A/B55-566[»]
1H49X-ray1.90A/B55-566[»]
1HXJX-ray2.05A/B60-566[»]
1V08X-ray1.90A/B55-566[»]
ProteinModelPortalP49235.
SMRP49235. Positions 61-555.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PRIDEP49235.
ProMEXP49235.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID542414.
KEGGzma:542414.

Organism-specific databases

GrameneP49235.
MaizeGDB13870.

Phylogenomic databases

HOGENOMHOG000088630.
KOK01188.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-10621.
SABIO-RKP49235.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP49235.

Entry information

Entry nameHGGL1_MAIZE
AccessionPrimary (citable) accession number: P49235
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries