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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: 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
  1. Vmax=1060 nmol/sec/mg enzyme with DIBOA-beta-D-glucoside as substrate (with native hexamer)1 Publication
  2. Vmax=4100 nmol/sec/mg enzyme with DIMBOA-beta-D-glucoside as substrate (with native hexamer)1 Publication
  3. Vmax=220 nmol/sec/mg enzyme with HBOA-beta-D-glucoside as substrate (with native hexamer)1 Publication
  4. Vmax=540 nmol/sec/mg enzyme with HMBOA-beta-D-glucoside as substrate (with native hexamer)1 Publication
  5. Vmax=520 nmol/sec/mg enzyme with p-nitrophenyl beta-D-glucopyranoside as substrate (with native hexamer)1 Publication
  6. Vmax=47 nmol/sec/mg enzyme with p-nitrophenyl beta-D-galactopyranoside as substrate (with native hexamer)1 Publication
  7. Vmax=35 nmol/sec/mg enzyme with p-nitrophenyl beta-D-xyloside as substrate (with native hexamer)1 Publication
  8. Vmax=1080 nmol/sec/mg enzyme with p-nitrophenyl beta-D-fucoside as substrate (with native hexamer)1 Publication
  9. 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)DescriptionActionsGraphical viewLength
Binding sitei92Substrate1
Binding sitei239Substrate1
Active sitei240Proton donorBy similarity1
Binding sitei243Substrate1
Active sitei456NucleophilePROSITE-ProRule annotation1
Binding sitei504Substrate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.182. 6500.
3.2.1.21. 6500.

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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeTriticinaeTriticum
Proteomesi
  • UP000019116 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 50Chloroplast1 PublicationAdd BLAST50
ChainiPRO_000042409851 – 5694-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1b, chloroplasticAdd BLAST519

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1569
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
Turni124 – 128Combined sources5
Helixi130 – 144Combined sources15
Beta strandi147 – 152Combined sources6
Helixi155 – 158Combined sources4
Beta strandi162 – 165Combined sources4
Helixi168 – 183Combined sources16
Beta strandi187 – 195Combined sources9
Helixi199 – 205Combined sources7
Helixi207 – 209Combined sources3
Helixi213 – 228Combined sources16
Turni229 – 231Combined sources3
Beta strandi234 – 239Combined sources6
Helixi241 – 249Combined sources9
Beta strandi263 – 267Combined sources5
Turni272 – 274Combined sources3
Helixi275 – 297Combined sources23
Beta strandi305 – 321Combined sources17
Helixi322 – 335Combined sources14
Helixi337 – 345Combined sources9
Helixi350 – 356Combined sources7
Helixi357 – 359Combined sources3
Helixi365 – 371Combined sources7
Beta strandi376 – 390Combined sources15
Helixi402 – 406Combined sources5
Beta strandi408 – 413Combined sources6
Beta strandi419 – 421Combined sources3
Helixi433 – 445Combined sources13
Beta strandi452 – 456Combined sources5
Helixi475 – 493Combined sources19
Beta strandi498 – 504Combined sources7
Helixi512 – 517Combined sources6
Beta strandi522 – 525Combined sources4
Turni527 – 531Combined sources5
Beta strandi533 – 535Combined sources3
Helixi537 – 545Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DGAX-ray1.80A50-569[»]
3AIQX-ray1.90A50-569[»]
3AIRX-ray2.00A50-569[»]
3AISX-ray2.20A50-569[»]
ProteinModelPortaliQ1XH05.
SMRiQ1XH05.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ1XH05.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni511 – 512Substrate binding2

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.
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.

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.

Genome annotation databases

EnsemblPlantsiTRIAE_CS42_2BL_TGACv1_129397_AA0381780.1; TRIAE_CS42_2BL_TGACv1_129397_AA0381780.1; TRIAE_CS42_2BL_TGACv1_129397_AA0381780.
GrameneiTRIAE_CS42_2BL_TGACv1_129397_AA0381780.1; TRIAE_CS42_2BL_TGACv1_129397_AA0381780.1; TRIAE_CS42_2BL_TGACv1_129397_AA0381780.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DGAX-ray1.80A50-569[»]
3AIQX-ray1.90A50-569[»]
3AIRX-ray2.00A50-569[»]
3AISX-ray2.20A50-569[»]
ProteinModelPortaliQ1XH05.
SMRiQ1XH05.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiTRIAE_CS42_2BL_TGACv1_129397_AA0381780.1; TRIAE_CS42_2BL_TGACv1_129397_AA0381780.1; TRIAE_CS42_2BL_TGACv1_129397_AA0381780.
GrameneiTRIAE_CS42_2BL_TGACv1_129397_AA0381780.1; TRIAE_CS42_2BL_TGACv1_129397_AA0381780.1; TRIAE_CS42_2BL_TGACv1_129397_AA0381780.

Enzyme and pathway databases

BRENDAi3.2.1.182. 6500.
3.2.1.21. 6500.

Miscellaneous databases

EvolutionaryTraceiQ1XH05.

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 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 30, 2016
This is version 61 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

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.