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P49235

- HGGL1_MAIZE

UniProt

P49235 - HGGL1_MAIZE

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
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    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.
    (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.
    (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.

    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)5 Publications
    3. KM=0.41 mM for p-nitrophenyl beta-D-glucopyranoside (PNPG) (with recombinant enzyme)5 Publications
    4. KM=98 µM for DIMBOA-beta-D-glucoside5 Publications
    5. KM=0.251 mM for n-octyl-beta-D-glucopyranoside5 Publications
    6. KM=0.394 mM for p-nitrophenyl beta-D-xyloside5 Publications
    7. KM=0.648 mM for p-nitrophenyl beta-D-fucopyranoside5 Publications
    8. KM=0.674 mM for p-nitrophenyl beta-D-cellobioside5 Publications
    9. KM=0.769 mM for p-nitrophenyl beta-D-mannopyranoside5 Publications
    10. KM=1.64 mM for o-nitrophenyl beta-D-glucopyranoside5 Publications
    11. KM=1.42 mM for o-nitrophenyl beta-D-glucopyranoside (with recombinant enzyme)5 Publications
    12. KM=4.32 mM for p-nitrophenyl beta-D-galactopyranoside5 Publications

    Vmax=225.4 µmol/h/µg enzyme with p-nitrophenyl beta-D-glucopyranoside as substrate (with recombinant enzyme)5 Publications

    Vmax=282.7 µmol/h/µg enzyme with o-nitrophenyl beta-D-glucopyranoside as substrate (with recombinant enzyme)5 Publications

    pH dependencei

    Optimum pH is 5.8.5 Publications

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius. Loses activity when is heated at 55 degrees Celsius.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei92 – 921Substrate
    Binding sitei196 – 1961Substrate
    Binding sitei244 – 2441Substrate
    Active sitei245 – 2451Proton donorBy similarity
    Binding sitei387 – 3871Substrate
    Active sitei460 – 4601NucleophilePROSITE-ProRule annotation
    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

    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

    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 PublicationsAdd
    BLAST
    Chaini55 – 5665124-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplasticPRO_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.6 Publications

    Structurei

    Secondary structure

    1
    566
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49235.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    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

    « Hide

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti477 – 4771A → D in CAA52293. (PubMed:8235622)Curated
    Sequence conflicti551 – 5511E → Q in CAA52293. (PubMed:8235622)Curated
    Sequence conflicti554 – 5541T → A in CAA52293. (PubMed:8235622)Curated

    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: October 1, 2014
    This is version 100 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