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Protein

4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase, chloroplastic

Gene
N/A
Organism
Secale cereale (Rye)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in defense of young plant parts against pests via the production of benzoxazolinones (hydroxamic acids) from hydroxamic acid glucosides. The preferred substrate is DIBOA-beta-D-glucoside. Can also use esculin and genistein glucoside as substrates, but no activity with salicin, p-nitrophenyl-alpha-glucoside or substrates related to cell wall components.2 Publications

Catalytic activityi

(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.
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

Enzyme regulationi

Inhibited by castanospermine, Ag+ and Cu2+. 34% inhibition by Zn2+ and not affected by EDTA.1 Publication

Kineticsi

kcat is 172 sec(-1) with DIBOA-beta-D-glucoside as substrate. kcat is 118 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 119 sec(-1) with DIMBOA-beta-D-glucoside as substrate. kcat is 158 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 159 sec(-1) with o-nitrophenyl beta-D-glucopyranoside as substrate. kcat is 66 sec(-1) with p-nitrophenyl beta-D-fucoside as substrate. kcat is 52 sec(-1) with p-nitrophenyl beta-D-glucopyranoside as substrate. kcat is 3.5 sec(-1) with p-nitrophenyl beta-D-galactopyranoside as substrate. kcat is 22.2 sec(-1) with p-nitrophenyl beta-D-glucopyranoside as substrate (with recombinant enzyme).

  1. KM=1.19 mM for DIBOA-beta-D-glucoside1 Publication
  2. KM=3.3 mM for DIBOA-beta-D-glucoside1 Publication
  3. KM=0.8 mM for DIBOA-beta-D-glucoside (with recombinant enzyme)1 Publication
  4. KM=0.617 mM for DIMBOA-beta-D-glucoside1 Publication
  5. KM=2.1 mM for DIMBOA-beta-D-glucoside1 Publication
  6. KM=1.3 mM for DIMBOA-beta-D-glucoside (with recombinant enzyme)1 Publication
  7. KM=2.0 mM for HBOA-beta-D-glucoside1 Publication
  8. KM=0.893 mM for HMBOA-beta-D-glucoside1 Publication
  9. KM=1.4 mM for o-nitrophenyl beta-D-glucopyranoside1 Publication
  10. KM=0.9 mM for p-nitrophenyl beta-D-glucopyranoside1 Publication
  11. KM=2.4 mM for p-nitrophenyl beta-D-glucopyranoside1 Publication
  12. KM=1.78 mM for p-nitrophenyl beta-D-glucopyranoside (with recombinant enzyme)1 Publication
  13. KM=1.3 mM for p-nitrophenyl beta-D-galactopyranoside1 Publication
  14. KM=3.17 mM for p-nitrophenyl beta-D-xyloside1 Publication
  15. KM=0.616 mM for p-nitrophenyl beta-D-fucoside1 Publication
  16. KM=0.8 mM for p-nitrophenyl beta-D-fucoside1 Publication
  17. KM=0.151 mM for esculin1 Publication
  1. Vmax=5870 nmol/sec/mg enzyme with DIBOA-beta-D-glucoside as substrate1 Publication
  2. Vmax=2567 nmol/sec/mg enzyme with DIBOA-beta-D-glucoside as substrate1 Publication
  3. Vmax=4952 nmol/sec/mg enzyme with DIMBOA-beta-D-glucoside as substrate1 Publication
  4. Vmax=1786 nmol/sec/mg enzyme with DIMBOA-beta-D-glucoside as substrate1 Publication
  5. Vmax=2375 nmol/sec/mg enzyme with o-nitrophenyl beta-D-glucopyranoside as substrate1 Publication
  6. Vmax=1420 nmol/sec/mg enzyme with HBOA-beta-D-glucoside as substrate1 Publication
  7. Vmax=1005 nmol/sec/mg enzyme with HMBOA-beta-D-glucoside as substrate1 Publication
  8. Vmax=828 nmol/sec/mg enzyme with p-nitrophenyl beta-D-glucopyranoside as substrate1 Publication
  9. Vmax=779 nmol/sec/mg enzyme with p-nitrophenyl beta-D-glucopyranoside as substrate1 Publication
  10. Vmax=78.2 nmol/sec/mg enzyme with p-nitrophenyl beta-D-xyloside as substrate1 Publication
  11. Vmax=1671 nmol/sec/mg enzyme with p-nitrophenyl beta-D-fucoside as substrate1 Publication
  12. Vmax=997 nmol/sec/mg enzyme with p-nitrophenyl beta-D-fucoside as substrate1 Publication
  13. Vmax=51 nmol/sec/mg enzyme with p-nitrophenyl beta-D-galactopyranoside as substrate1 Publication
  14. Vmax=974 nmol/sec/mg enzyme with esculin as substrate1 Publication

pH dependencei

Optimum pH is 5.5.3 Publications

Temperature dependencei

Optimum temperature is 25-30 degrees Celsius.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei92Substrate1
Binding sitei194Substrate1
Binding sitei239Substrate1
Active sitei240Proton donorBy similarity1
Active sitei456NucleophilePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.182. 5654.
3.2.1.21. 5654.

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, chloroplastic (EC:3.2.1.182)
Alternative name(s):
Beta-glucosidase (EC:3.2.1.21)
Short name:
ScGlu
OrganismiSecale cereale (Rye)
Taxonomic identifieri4550 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeSecale

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi240E → A: Total loss of activity. 1 Publication1
Mutagenesisi247F → A: 96% loss of activity with DIBOA-Glc and DIMBOA-Glc. 1 Publication1
Mutagenesisi427Y → A: 7% loss of activity with DIBOA-Glc and 4.8 fold increased activity with DIMBOA-Glc. 1 Publication1
Mutagenesisi427Y → F: 87% loss of activity with DIBOA-Glc and 1.5 fold increased activity with DIMBOA-Glc. 1 Publication1
Mutagenesisi456E → A: Total loss of activity. 1 Publication1
Mutagenesisi513G → F: 77% loss of activity with DIBOA-Glc and 81% with DIMBOA-Glc. 1 Publication1
Mutagenesisi513G → S: 42% loss of activity with DIBOA-Glc and 2 fold increased activity with DIMBOA-Glc. 42% loss of activity with DIBOA-Glc and 4 fold increased activity with DIMBOA-Glc; when associated with L-514. 1 Publication1
Mutagenesisi514S → L: 62% loss of activity with DIBOA-Glc and 2.4 fold increased activity with DIMBOA-Glc. 42% loss of activity with DIBOA-Glc and 4 fold increased activity with DIMBOA-Glc; when associated with S-513. 1 Publication1
Mutagenesisi520F → Y: 19% loss of activity with DIBOA-Glc and 2.5 fold increased activity with DIMBOA-Glc. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 50Chloroplast1 PublicationAdd BLAST50
ChainiPRO_000042409651 – 5684-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase, chloroplasticAdd BLAST518

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi259 ↔ 265By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed in seedlings, mesocotyl, coleoptile, leaf sheath, and roots.1 Publication

Interactioni

Subunit structurei

Homohexamer.2 Publications

Structurei

Secondary structure

1568
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
Helixi106 – 113Combined sources8
Helixi115 – 117Combined sources3
Beta strandi124 – 126Combined sources3
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
Helixi212 – 228Combined sources17
Turni229 – 231Combined sources3
Beta strandi234 – 239Combined sources6
Helixi241 – 249Combined sources9
Beta strandi265 – 267Combined sources3
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
Helixi527 – 529Combined sources3
Beta strandi533 – 535Combined sources3
Helixi537 – 545Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AIUX-ray2.20A50-568[»]
3AIVX-ray2.50A50-568[»]
3AIWX-ray2.40A50-568[»]
ProteinModelPortaliQ9FYS3.
SMRiQ9FYS3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9FYS3.

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.

Q9FYS3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLVGGTLN PTTHLSLRSR AGRNSENVWL RSAASSQTSK GRFCNLTVRA
60 70 80 90 100
GTPSKPSEPI GPVFTKLKPW QIPKRDWFSK DFLFGASTSA YQIEGAWNED
110 120 130 140 150
GKGPSTWDHF CHTYPERISD GTNGDVAANS YHMYEEDVKA LKDMGMKVYR
160 170 180 190 200
FSISWSRILP NGTGKPNQKG IDYYNNLINS LIRHGIVPYV TIWHWDTPQA
210 220 230 240 250
LEDKYGGFLD KQIVNDYKYF AELCFQSFGD RVKNWFTFNE PHTYCCFSYG
260 270 280 290 300
EGIHAPGRCS PGLDCAVPEG DSLREPYTAG HHILLAHAEA VELFKAHYNK
310 320 330 340 350
HGDSKIGMAF DVMGYEPYQD SFLDDQARER SIDYNMGWFL EPVVRGDYPF
360 370 380 390 400
SMRSLIGDRL PMFTKEEQEK LGSLCDIMGL NYYTSRFSKH VDISSDYTPT
410 420 430 440 450
LNTDDAYASS ETTGSDGNEI GPITGTYWIY MYPKGLTDLL LIMKEKYGNP
460 470 480 490 500
PIFITENGIA DVEGDPEMPD PLDDWKRLDY LQRHISAVKD AIDQGADVRG
510 520 530 540 550
HFTWGLIDNF EWGSGYSSRF GLVYIDKEDG NKRKLKKSAK WFAKFNSVPK
560
TLLKTTNNNA TVTASVSV
Length:568
Mass (Da):64,212
Last modified:March 1, 2001 - v1
Checksum:i11F7E87C0CB81DF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293849 mRNA. Translation: AAG00614.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293849 mRNA. Translation: AAG00614.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AIUX-ray2.20A50-568[»]
3AIVX-ray2.50A50-568[»]
3AIWX-ray2.40A50-568[»]
ProteinModelPortaliQ9FYS3.
SMRiQ9FYS3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.182. 5654.
3.2.1.21. 5654.

Miscellaneous databases

EvolutionaryTraceiQ9FYS3.

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 nameiHGGL_SECCE
AccessioniPrimary (citable) accession number: Q9FYS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 68 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, 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

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.