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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: 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
  1. Vmax=225.4 µmol/h/µg enzyme with p-nitrophenyl beta-D-glucopyranoside as substrate (with recombinant enzyme)5 Publications
  2. 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)DescriptionActionsGraphical viewLength
Binding sitei92SubstrateCombined sources2 Publications1
Binding sitei196SubstrateCombined sources1 Publication1
Binding sitei244SubstrateCombined sources1 Publication1
Active sitei245Proton donorBy similarity1
Binding sitei387SubstrateCombined sources1 Publication1
Active sitei460NucleophileBy similarity1
Binding sitei511SubstrateCombined sources2 Publications1
Binding sitei527SubstrateCombined sources1 Publication1

GO - Molecular functioni

  • beta-glucosidase activity Source: UniProtKB
  • cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB
  • fucosidase activity Source: UniProtKB
  • galactosidase activity Source: UniProtKB
  • mannosidase activity Source: UniProtKB
  • scopolin beta-glucosidase activity Source: UniProtKB-EC
  • xylanase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cytokinin signaling pathway

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-10621.
BRENDAi3.2.1.182. 6752.
3.2.1.21. 6752.
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 cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Unplaced

Organism-specific databases

MaizeGDBi13870.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi245E → D or Q: Loss of activity. 3 Publications1
Mutagenesisi252F → I, W or Y: Reduced substrate affinity. 1 Publication1
Mutagenesisi264C → A, D, R or S: Loss of activity due to impaired dimerization. 1
Mutagenesisi270C → A, D, R or S: Loss of activity due to impaired dimerization. 1
Mutagenesisi317M → F, I or V: No effect. 1 Publication1
Mutagenesisi460E → D: Loss of activity and impaired dimerization. 1 Publication1
Mutagenesisi460E → Q: Loss of activity. 1 Publication1
Mutagenesisi463I → D: Loss of activity due to impaired dimerization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 54Chloroplast2 PublicationsAdd BLAST54
ChainiPRO_000001176355 – 5664-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplasticAdd BLAST512

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi264 ↔ 2703 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP49235.
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

Protein-protein interaction databases

STRINGi4577.GRMZM2G016890_P01.

Structurei

Secondary structure

1566
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi69 – 71Combined sources3
Helixi75 – 77Combined sources3
Beta strandi83 – 87Combined sources5
Helixi90 – 93Combined sources4
Helixi99 – 101Combined sources3
Helixi106 – 113Combined sources8
Helixi115 – 117Combined sources3
Helixi130 – 143Combined sources14
Beta strandi147 – 152Combined sources6
Helixi155 – 158Combined sources4
Turni164 – 166Combined sources3
Helixi170 – 185Combined sources16
Beta strandi189 – 197Combined sources9
Helixi201 – 207Combined sources7
Helixi209 – 211Combined sources3
Helixi217 – 233Combined sources17
Turni234 – 236Combined sources3
Beta strandi239 – 244Combined sources6
Helixi246 – 253Combined sources8
Beta strandi268 – 272Combined sources5
Turni277 – 279Combined sources3
Helixi280 – 302Combined sources23
Beta strandi309 – 325Combined sources17
Helixi326 – 339Combined sources14
Helixi341 – 349Combined sources9
Helixi354 – 360Combined sources7
Helixi361 – 363Combined sources3
Helixi369 – 375Combined sources7
Beta strandi380 – 394Combined sources15
Helixi406 – 410Combined sources5
Beta strandi412 – 417Combined sources6
Beta strandi423 – 425Combined sources3
Beta strandi429 – 432Combined sources4
Helixi438 – 449Combined sources12
Beta strandi456 – 460Combined sources5
Beta strandi469 – 471Combined sources3
Helixi475 – 479Combined sources5
Helixi482 – 500Combined sources19
Beta strandi505 – 511Combined sources7
Helixi519 – 521Combined sources3
Beta strandi524 – 526Combined sources3
Beta strandi529 – 533Combined sources5
Turni534 – 537Combined sources4
Beta strandi538 – 542Combined sources5
Helixi544 – 554Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49235.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni325 – 361DimerizationAdd BLAST37
Regioni394 – 405DimerizationAdd BLAST12
Regioni450 – 453Dimerization4
Regioni518 – 519Substrate bindingCombined sources2 Publications2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0626. Eukaryota.
COG2723. LUCA.
HOGENOMiHOG000088630.
KOiK01188.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR033132. Glyco_hydro_1_N_CS.
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)DescriptionActionsGraphical viewLength
Sequence conflicti477A → D in CAA52293 (PubMed:8235622).Curated1
Sequence conflicti551E → Q in CAA52293 (PubMed:8235622).Curated1
Sequence conflicti554T → A in CAA52293 (PubMed:8235622).Curated1

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

EnsemblPlantsiZm00001d023994_T002; Zm00001d023994_T002; Zm00001d023994.
GeneIDi542414.
GrameneiZm00001d023994_T002; Zm00001d023994_T002; Zm00001d023994.
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.
PIRiA48860.
RefSeqiNP_001105454.1. NM_001111984.1.
UniGeneiZm.94498.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM2G016890_P01.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbiP49235.
PRIDEiP49235.
ProMEXiP49235.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiZm00001d023994_T002; Zm00001d023994_T002; Zm00001d023994.
GeneIDi542414.
GrameneiZm00001d023994_T002; Zm00001d023994_T002; Zm00001d023994.
KEGGizma:542414.

Organism-specific databases

MaizeGDBi13870.

Phylogenomic databases

eggNOGiKOG0626. Eukaryota.
COG2723. LUCA.
HOGENOMiHOG000088630.
KOiK01188.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-10621.
BRENDAi3.2.1.182. 6752.
3.2.1.21. 6752.
SABIO-RKP49235.

Miscellaneous databases

EvolutionaryTraceiP49235.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR033132. Glyco_hydro_1_N_CS.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 116 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, Complete proteome, Direct protein sequencing, Reference proteome

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.