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Q1XH05

- HGL1B_WHEAT

UniProt

Q1XH05 - HGL1B_WHEAT

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
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (02 May 2006)
      Previous versions | rss
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    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

    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-SubCell

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ1XH05.

    Family & Domainsi

    Region

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

    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: October 1, 2014
    This is version 46 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