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Q1XH05

- HGL1B_WHEAT

UniProt

Q1XH05 - HGL1B_WHEAT

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Protein
4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1b, chloroplastic
Gene
GLU1B
Organism
Triticum aestivum (Wheat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 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

Kineticsi

kcat is 214 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 1201 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 128.2 sec(-1) with p-nitrophenyl beta-D-glucopyranoside as substrate (with recombinant enzyme).

  1. KM=1.34 mM for DIBOA-beta-D-glucoside (with native hexamer)1 Publication
  2. KM=1.44 mM for DIBOA-beta-D-glucoside (with recombinant enzyme)
  3. KM=0.272 mM for DIMBOA-beta-D-glucoside (with native hexamer)
  4. KM=0.29 mM for DIMBOA-beta-D-glucoside (with recombinant enzyme)
  5. KM=2.02 mM for HBOA-beta-D-glucoside (with native hexamer)
  6. KM=0.320 mM for HMBOA-beta-D-glucoside (with native hexamer)
  7. KM=1.7 mM for p-nitrophenyl beta-D-glucopyranoside (with native hexamer)
  8. KM=2.16 mM for p-nitrophenyl beta-D-glucopyranoside (with recombinant enzyme)
  9. KM=1.78 mM for p-nitrophenyl beta-D-galactopyranoside (with native hexamer)
  10. KM=3.11 mM for p-nitrophenyl beta-D-xyloside (with native hexamer)
  11. KM=0.67 mM for p-nitrophenyl beta-D-fucoside (with native hexamer)
  12. KM=0.240 mM for esculin (with native hexamer)

Vmax=1060 nmol/sec/mg enzyme with DIBOA-beta-D-glucoside as substrate (with native hexamer)

Vmax=4100 nmol/sec/mg enzyme with DIMBOA-beta-D-glucoside as substrate (with native hexamer)

Vmax=220 nmol/sec/mg enzyme with HBOA-beta-D-glucoside as substrate (with native hexamer)

Vmax=540 nmol/sec/mg enzyme with HMBOA-beta-D-glucoside as substrate (with native hexamer)

Vmax=520 nmol/sec/mg enzyme with p-nitrophenyl beta-D-glucopyranoside as substrate (with native hexamer)

Vmax=47 nmol/sec/mg enzyme with p-nitrophenyl beta-D-galactopyranoside as substrate (with native hexamer)

Vmax=35 nmol/sec/mg enzyme with p-nitrophenyl beta-D-xyloside as substrate (with native hexamer)

Vmax=1080 nmol/sec/mg enzyme with p-nitrophenyl beta-D-fucoside as substrate (with native hexamer)

Vmax=320 nmol/sec/mg enzyme with esculin as substrate (with native hexamer)

pH dependencei

Optimum pH is 5.5.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921Substrate
Binding sitei239 – 2391Substrate
Active sitei240 – 2401Proton donor By similarity
Binding sitei243 – 2431Substrate
Active sitei456 – 4561Nucleophile By similarity
Binding sitei504 – 5041Substrate

GO - Molecular functioni

  1. beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

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 1b, chloroplastic (EC:3.2.1.182)
Alternative name(s):
Beta-glucosidase 1b (EC:3.2.1.21)
Short name:
Taglu1b
Gene namesi
Name:GLU1B
OrganismiTriticum aestivum (Wheat)
Taxonomic identifieri4565 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum
ProteomesiUP000019116: Unplaced

Organism-specific databases

GrameneiQ1XH05.

Subcellular locationi

Plastidchloroplast Reviewed prediction

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5050Chloroplast1 Publication
Add
BLAST
Chaini51 – 5695194-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1b, chloroplastic
PRO_0000424098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi259 ↔ 2651 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed in young seedlings early after germination.1 Publication

Developmental stagei

Peak of expression 36 to 48 hours after imbibition.1 Publication

Interactioni

Subunit structurei

Homo- and heterohexamers.2 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
Turni124 – 1285
Helixi130 – 14415
Beta strandi147 – 1526
Helixi155 – 1584
Beta strandi162 – 1654
Helixi168 – 18316
Beta strandi187 – 1959
Helixi199 – 2057
Helixi207 – 2093
Helixi213 – 22816
Turni229 – 2313
Beta strandi234 – 2396
Helixi241 – 2499
Beta strandi263 – 2675
Turni272 – 2743
Helixi275 – 29723
Beta strandi305 – 32117
Helixi322 – 33514
Helixi337 – 3459
Helixi350 – 3567
Helixi357 – 3593
Helixi365 – 3717
Beta strandi376 – 39015
Helixi402 – 4065
Beta strandi408 – 4136
Beta strandi419 – 4213
Helixi433 – 44513
Beta strandi452 – 4565
Helixi475 – 49319
Beta strandi498 – 5047
Helixi512 – 5176
Beta strandi522 – 5254
Turni527 – 5315
Beta strandi533 – 5353
Helixi537 – 5459

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DGAX-ray1.80A50-569[»]
3AIQX-ray1.90A50-569[»]
3AIRX-ray2.00A50-569[»]
3AISX-ray2.20A50-569[»]
ProteinModelPortaliQ1XH05.
SMRiQ1XH05. Positions 61-551.

Miscellaneous databases

EvolutionaryTraceiQ1XH05.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni319 – 3202Sulfate binding
Regioni511 – 5122Substrate binding

Sequence similaritiesi

Keywords - Domaini

Transit peptide

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.

Q1XH05-1 [UniParc]FASTAAdd to Basket

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MALLAAATLN PTTHLSLRSR AGRNSENLWL RSTASSQKSK GRFCNLTIRA    50
GTPSKPAEPI GPVFTKLKPW QIPKRDWFDK DFLFGASTSA YQIEGAWNED 100
GKGPSTWDHF CHTYPERISD MTNGDVAANS YHLYEEDVKA LKDMGMKVYR 150
FSISWSRILP DGTGKVNQAG IDYYNKLINS LIDNDIVPYV TIWHWDTPQA 200
LEDKYGGFLN RQIVDDYKQF AEVCFKNFGD RVKNWFTFNE PHTYCCFSYG 250
EGIHAPGRCS PGMDCAVPEG DSLREPYTAG HHILLAHAEA VQLFKARYNM 300
HGDSKIGMAF DVMGYEPYQD SFLDDQARER SIDYNMGWFL EPVVRGDYPF 350
SMRSLIGDRL PMFTKEEQEK LASSCDIMGL NYYTSRFSKH VDMSPDFTPT 400
LNTDDAYASS ETTGSDGNDI GPITGTYWIY MYPKGLTDLL LIMKEKYGNP 450
PVFITENGIA DVEGDESMPD PLDDWKRLDY LQRHISAVKD AIDQGADVRG 500
HFTWGLIDNF EWSLGYSSRF GLVYIDKNDG NKRKLKKSAK WFSKFNSVPK 550
PLLKTTNNNA TMTAASVSV 569
Length:569
Mass (Da):64,482
Last modified:May 2, 2006 - v1
Checksum:i44FAB6E047F86F85
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB236422 mRNA. Translation: BAE92259.1.
UniGeneiTa.24442.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB236422 mRNA. Translation: BAE92259.1 .
UniGenei Ta.24442.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DGA X-ray 1.80 A 50-569 [» ]
3AIQ X-ray 1.90 A 50-569 [» ]
3AIR X-ray 2.00 A 50-569 [» ]
3AIS X-ray 2.20 A 50-569 [» ]
ProteinModelPortali Q1XH05.
SMRi Q1XH05. Positions 61-551.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei Q1XH05.

Miscellaneous databases

EvolutionaryTracei Q1XH05.

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. "Molecular and structural characterization of hexameric beta-D-glucosidases in wheat and rye."
    Sue M., Yamazaki K., Yajima S., Nomura T., Matsukawa T., Iwamura H., Miyamoto T.
    Plant Physiol. 141:1237-1247(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, SUBUNIT, X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 50-569 IN COMPLEX WITH DIMBOA, DISULFIDE BOND.
    Strain: cv. Chinese Spring.
    Tissue: Shoot.
  2. "Purification and characterization of a hydroxamic acid glucoside beta-glucosidase from wheat (Triticum aestivum L.) seedlings."
    Sue M., Ishihara A., Iwamura H.
    Planta 210:432-438(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 51-62, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBUNIT, X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 50-569.
    Strain: cv. Asakazekomugi.
  3. "Active-site architecture of benzoxazinone-glucoside beta-D-glucosidases in Triticeae."
    Sue M., Nakamura C., Miyamoto T., Yajima S.
    Plant Sci. 180:268-275(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 50-569 IN COMPLEX WITH DIMBOA OR INHIBITOR.

Entry informationi

Entry nameiHGL1B_WHEAT
AccessioniPrimary (citable) accession number: Q1XH05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: May 2, 2006
Last modified: April 16, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Wheat is a hexaploid with three different genomes that contains at least four genes coding for GLU1: GLU1A (AC Q1XIR9), GLU1B (AC Q1XH05), GLU1C (AC Q1XH04) and GLU1D (AC D5MTF8). The monomers can aggregate in diverse combinations, reflecting the several isozymes found in the native enzyme described in 1 Publication. The hexameric structure is required for activity toward DIMBOA-beta-D-glucoside (1 Publication).

Keywords - Technical termi

3D-structure, Complete proteome, 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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