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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MAPLLAAAMN HAAAHPGLRS HLVGPNNESF SRHHLPSSSP QSSKRRCNLS
60 70 80 90 100
FTTRSARVGS QNGVQMLSPS EIPQRDWFPS DFTFGAATSA YQIEGAWNED
110 120 130 140 150
GKGESNWDHF CHNHPERILD GSNSDIGANS YHMYKTDVRL LKEMGMDAYR
160 170 180 190 200
FSISWPRILP KGTKEGGINP DGIKYYRNLI NLLLENGIEP YVTIFHWDVP
210 220 230 240 250
QALEEKYGGF LDKSHKSIVE DYTYFAKVCF DNFGDKVKNW LTFNEPQTFT
260 270 280 290 300
SFSYGTGVFA PGRCSPGLDC AYPTGNSLVE PYTAGHNILL AHAEAVDLYN
310 320 330 340 350
KHYKRDDTRI GLAFDVMGRV PYGTSFLDKQ AEERSWDINL GWFLEPVVRG
360 370 380 390 400
DYPFSMRSLA RERLPFFKDE QKEKLAGSYN MLGLNYYTSR FSKNIDISPN
410 420 430 440 450
YSPVLNTDDA YASQEVNGPD GKPIGPPMGN PWIYMYPEGL KDLLMIMKNK
460 470 480 490 500
YGNPPIYITE NGIGDVDTKE TPLPMEAALN DYKRLDYIQR HIATLKESID
510 520 530 540 550
LGSNVQGYFA WSLLDNFEWF AGFTERYGIV YVDRNNNCTR YMKESAKWLK
560
EFNTAKKPSK KILTPA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 29, 2014
This is version 101 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