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P49235

- HGGL1_MAIZE

UniProt

P49235 - HGGL1_MAIZE

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Protein
4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplastic
Gene
GLU1
Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.2 Publications
(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.2 Publications
(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.2 Publications

Enzyme regulationi

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).2 Publications

Kineticsi

  1. KM=0.14 mM for 4-methylumbelliferyl beta-D-glucopyranoside (MUG)5 Publications
  2. KM=0.64 mM for p-nitrophenyl beta-D-glucopyranoside (PNPG)
  3. KM=0.41 mM for p-nitrophenyl beta-D-glucopyranoside (PNPG) (with recombinant enzyme)
  4. KM=98 µM for DIMBOA-beta-D-glucoside
  5. KM=0.251 mM for n-octyl-beta-D-glucopyranoside
  6. KM=0.394 mM for p-nitrophenyl beta-D-xyloside
  7. KM=0.648 mM for p-nitrophenyl beta-D-fucopyranoside
  8. KM=0.674 mM for p-nitrophenyl beta-D-cellobioside
  9. KM=0.769 mM for p-nitrophenyl beta-D-mannopyranoside
  10. KM=1.64 mM for o-nitrophenyl beta-D-glucopyranoside
  11. KM=1.42 mM for o-nitrophenyl beta-D-glucopyranoside (with recombinant enzyme)
  12. 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 dependencei

Optimum pH is 5.8.

Temperature dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921Substrate
Binding sitei196 – 1961Substrate
Binding sitei244 – 2441Substrate
Active sitei245 – 2451Proton donor By similarity
Binding sitei387 – 3871Substrate
Active sitei460 – 4601Nucleophile By similarity
Binding sitei511 – 5111Substrate

GO - Molecular functioni

  1. beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. cytokinin-activated signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cytokinin signaling pathway

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-10621.
SABIO-RKP49235.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended 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 (EC:3.2.1.21)
Short name:
ZmGlu1
Gene namesi
Name:GLU1
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Organism-specific databases

GrameneiP49235.
MaizeGDBi13870.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi245 – 2451E → D or Q: Loss of activity. 3 Publications
Mutagenesisi252 – 2521F → I, W or Y: Reduced substrate affinity. 1 Publication
Mutagenesisi264 – 2641C → A, D, R or S: Loss of activity due to impaired dimerization.
Mutagenesisi270 – 2701C → A, D, R or S: Loss of activity due to impaired dimerization.
Mutagenesisi317 – 3171M → F, I or V: No effect. 1 Publication
Mutagenesisi460 – 4601E → D: Loss of activity and impaired dimerization. 1 Publication
Mutagenesisi460 – 4601E → Q: Loss of activity. 1 Publication
Mutagenesisi463 – 4631I → D: Loss of activity due to impaired dimerization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5454Chloroplast2 Publications
Add
BLAST
Chaini55 – 5665124-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplastic
PRO_0000011763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi264 ↔ 2703 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP49235.
ProMEXiP49235.

Expressioni

Tissue specificityi

Expressed in all seedling parts. Most abundant in the coleoptile.1 Publication

Interactioni

Subunit structurei

Homo- and heterodimer.3 Publications

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi69 – 713
Helixi75 – 773
Beta strandi83 – 875
Helixi90 – 934
Helixi99 – 1013
Helixi106 – 1138
Helixi115 – 1173
Helixi130 – 14314
Beta strandi147 – 1526
Helixi155 – 1584
Turni164 – 1663
Helixi170 – 18516
Beta strandi189 – 1979
Helixi201 – 2077
Helixi209 – 2113
Helixi217 – 23317
Turni234 – 2363
Beta strandi239 – 2446
Helixi246 – 2538
Beta strandi268 – 2725
Turni277 – 2793
Helixi280 – 30223
Beta strandi309 – 32517
Helixi326 – 33914
Helixi341 – 3499
Helixi354 – 3607
Helixi361 – 3633
Helixi369 – 3757
Beta strandi380 – 39415
Helixi406 – 4105
Beta strandi412 – 4176
Beta strandi423 – 4253
Beta strandi429 – 4324
Helixi438 – 44912
Beta strandi456 – 4605
Beta strandi469 – 4713
Helixi475 – 4795
Helixi482 – 50019
Beta strandi505 – 5117
Helixi519 – 5213
Beta strandi524 – 5263
Beta strandi529 – 5335
Turni534 – 5374
Beta strandi538 – 5425
Helixi544 – 55411

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP49235.
SMRiP49235. Positions 61-555.

Miscellaneous databases

EvolutionaryTraceiP49235.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni325 – 36137Dimerization
Add
BLAST
Regioni394 – 40512Dimerization
Add
BLAST
Regioni450 – 4534Dimerization
Regioni518 – 5192Substrate binding

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000088630.
KOiK01188.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49235-1 [UniParc]FASTAAdd to Basket

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MAPLLAAAMN HAAAHPGLRS HLVGPNNESF SRHHLPSSSP QSSKRRCNLS    50
FTTRSARVGS QNGVQMLSPS EIPQRDWFPS DFTFGAATSA YQIEGAWNED 100
GKGESNWDHF CHNHPERILD GSNSDIGANS YHMYKTDVRL LKEMGMDAYR 150
FSISWPRILP KGTKEGGINP DGIKYYRNLI NLLLENGIEP YVTIFHWDVP 200
QALEEKYGGF LDKSHKSIVE DYTYFAKVCF DNFGDKVKNW LTFNEPQTFT 250
SFSYGTGVFA PGRCSPGLDC AYPTGNSLVE PYTAGHNILL AHAEAVDLYN 300
KHYKRDDTRI GLAFDVMGRV PYGTSFLDKQ AEERSWDINL GWFLEPVVRG 350
DYPFSMRSLA RERLPFFKDE QKEKLAGSYN MLGLNYYTSR FSKNIDISPN 400
YSPVLNTDDA YASQEVNGPD GKPIGPPMGN PWIYMYPEGL KDLLMIMKNK 450
YGNPPIYITE NGIGDVDTKE TPLPMEAALN DYKRLDYIQR HIATLKESID 500
LGSNVQGYFA WSLLDNFEWF AGFTERYGIV YVDRNNNCTR YMKESAKWLK 550
EFNTAKKPSK KILTPA 566
Length:566
Mass (Da):64,237
Last modified:February 1, 1996 - v1
Checksum:i4EA241258AE3641B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti477 – 4771A → D in CAA52293. 1 Publication
Sequence conflicti551 – 5511E → Q in CAA52293. 1 Publication
Sequence conflicti554 – 5541T → A in CAA52293. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U25157 mRNA. Translation: AAA65946.1.
X74217 mRNA. Translation: CAA52293.1.
PIRiA48860.
RefSeqiNP_001105454.1. NM_001111984.1.
UniGeneiZm.94498.

Genome annotation databases

GeneIDi542414.
KEGGizma:542414.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U25157 mRNA. Translation: AAA65946.1 .
X74217 mRNA. Translation: CAA52293.1 .
PIRi A48860.
RefSeqi NP_001105454.1. NM_001111984.1.
UniGenei Zm.94498.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E1E X-ray 2.50 A/B 55-566 [» ]
1E1F X-ray 2.60 A/B 55-566 [» ]
1E4L X-ray 2.20 A/B 55-566 [» ]
1E4N X-ray 2.10 A/B 55-566 [» ]
1E55 X-ray 2.00 A/B 55-566 [» ]
1E56 X-ray 2.10 A/B 55-566 [» ]
1H49 X-ray 1.90 A/B 55-566 [» ]
1HXJ X-ray 2.05 A/B 60-566 [» ]
1V08 X-ray 1.90 A/B 55-566 [» ]
ProteinModelPortali P49235.
SMRi P49235. Positions 61-555.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

Proteomic databases

PRIDEi P49235.
ProMEXi P49235.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 542414.
KEGGi zma:542414.

Organism-specific databases

Gramenei P49235.
MaizeGDBi 13870.

Phylogenomic databases

HOGENOMi HOG000088630.
KOi K01188.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-10621.
SABIO-RK P49235.

Miscellaneous databases

EvolutionaryTracei P49235.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10353. PTHR10353. 1 hit.
Pfami PF00232. Glyco_hydro_1. 1 hit.
[Graphical view ]
PRINTSi PR00131. GLHYDRLASE1.
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiHGGL1_MAIZE
AccessioniPrimary (citable) accession number: P49235
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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