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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.
(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.

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

Vmax=1060 nmol/sec/mg enzyme with DIBOA-beta-D-glucoside as substrate (with native hexamer)1 Publication

Vmax=4100 nmol/sec/mg enzyme with DIMBOA-beta-D-glucoside as substrate (with native hexamer)1 Publication

Vmax=220 nmol/sec/mg enzyme with HBOA-beta-D-glucoside as substrate (with native hexamer)1 Publication

Vmax=540 nmol/sec/mg enzyme with HMBOA-beta-D-glucoside as substrate (with native hexamer)1 Publication

Vmax=520 nmol/sec/mg enzyme with p-nitrophenyl beta-D-glucopyranoside as substrate (with native hexamer)1 Publication

Vmax=47 nmol/sec/mg enzyme with p-nitrophenyl beta-D-galactopyranoside as substrate (with native hexamer)1 Publication

Vmax=35 nmol/sec/mg enzyme with p-nitrophenyl beta-D-xyloside as substrate (with native hexamer)1 Publication

Vmax=1080 nmol/sec/mg enzyme with p-nitrophenyl beta-D-fucoside as substrate (with native hexamer)1 Publication

Vmax=320 nmol/sec/mg enzyme with esculin as substrate (with native hexamer)1 Publication

pH dependencei

Optimum pH is 5.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921Substrate
Binding sitei239 – 2391Substrate
Active sitei240 – 2401Proton donorBy similarity
Binding sitei243 – 2431Substrate
Active sitei456 – 4561NucleophilePROSITE-ProRule annotation
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 Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

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

Structurei

Secondary structure

1
569
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
Turni124 – 1285Combined sources
Helixi130 – 14415Combined sources
Beta strandi147 – 1526Combined sources
Helixi155 – 1584Combined sources
Beta strandi162 – 1654Combined sources
Helixi168 – 18316Combined sources
Beta strandi187 – 1959Combined sources
Helixi199 – 2057Combined sources
Helixi207 – 2093Combined sources
Helixi213 – 22816Combined sources
Turni229 – 2313Combined sources
Beta strandi234 – 2396Combined sources
Helixi241 – 2499Combined sources
Beta strandi263 – 2675Combined sources
Turni272 – 2743Combined sources
Helixi275 – 29723Combined sources
Beta strandi305 – 32117Combined sources
Helixi322 – 33514Combined sources
Helixi337 – 3459Combined sources
Helixi350 – 3567Combined sources
Helixi357 – 3593Combined sources
Helixi365 – 3717Combined sources
Beta strandi376 – 39015Combined sources
Helixi402 – 4065Combined sources
Beta strandi408 – 4136Combined sources
Beta strandi419 – 4213Combined sources
Helixi433 – 44513Combined sources
Beta strandi452 – 4565Combined sources
Helixi475 – 49319Combined sources
Beta strandi498 – 5047Combined sources
Helixi512 – 5176Combined sources
Beta strandi522 – 5254Combined sources
Turni527 – 5315Combined sources
Beta strandi533 – 5353Combined sources
Helixi537 – 5459Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ1XH05.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

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

« Hide

        10         20         30         40         50
MALLAAATLN PTTHLSLRSR AGRNSENLWL RSTASSQKSK GRFCNLTIRA
60 70 80 90 100
GTPSKPAEPI GPVFTKLKPW QIPKRDWFDK DFLFGASTSA YQIEGAWNED
110 120 130 140 150
GKGPSTWDHF CHTYPERISD MTNGDVAANS YHLYEEDVKA LKDMGMKVYR
160 170 180 190 200
FSISWSRILP DGTGKVNQAG IDYYNKLINS LIDNDIVPYV TIWHWDTPQA
210 220 230 240 250
LEDKYGGFLN RQIVDDYKQF AEVCFKNFGD RVKNWFTFNE PHTYCCFSYG
260 270 280 290 300
EGIHAPGRCS PGMDCAVPEG DSLREPYTAG HHILLAHAEA VQLFKARYNM
310 320 330 340 350
HGDSKIGMAF DVMGYEPYQD SFLDDQARER SIDYNMGWFL EPVVRGDYPF
360 370 380 390 400
SMRSLIGDRL PMFTKEEQEK LASSCDIMGL NYYTSRFSKH VDMSPDFTPT
410 420 430 440 450
LNTDDAYASS ETTGSDGNDI GPITGTYWIY MYPKGLTDLL LIMKEKYGNP
460 470 480 490 500
PVFITENGIA DVEGDESMPD PLDDWKRLDY LQRHISAVKD AIDQGADVRG
510 520 530 540 550
HFTWGLIDNF EWSLGYSSRF GLVYIDKNDG NKRKLKKSAK WFSKFNSVPK
560
PLLKTTNNNA TMTAASVSV
Length:569
Mass (Da):64,482
Last modified:May 2, 2006 - v1
Checksum:i44FAB6E047F86F85
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB236422 mRNA. Translation: BAE92259.1.
UniGeneiTa.24442.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB236422 mRNA. Translation: BAE92259.1 .
UniGenei Ta.24442.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 48 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 PubMed:10750901. The hexameric structure is required for activity toward DIMBOA-beta-D-glucoside (PubMed:16751439).1 Publication

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

External Data

Dasty 3