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UniProtKB - Q9H227 (GBA3_HUMAN)

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Protein

Cytosolic beta-glucosidase

Gene

GBA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Glycosidase probably involved in the intestinal absorption and metabolism of dietary flavonoid glycosides. Able to hydrolyze a broad variety of glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens. Possesses beta-glycosylceramidase activity and may be involved in a nonlysosomal catabolic pathway of glycosylceramide.3 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited by 2,4-dinitrophenyl-2-fluoro-2-deoxy-beta-D-glucopyranoside and sodium taurocholate.2 Publications

Kineticsi

  1. KM=40 µM for 4-methylumbelliferyl-beta-D-glucopyranoside2 Publications
  2. KM=50 µM for 4-methylumbelliferyl-beta-D-galactopyranoside2 Publications
  3. KM=370 µM for 4-nitrophenyl-beta-D-fucopyranoside2 Publications
  4. KM=570 µM for 4-nitrophenyl-alpha-D-arabinopyranoside2 Publications
  5. KM=1.76 mM for 4-nitrophenyl-beta-D-glucopyranoside2 Publications
  6. KM=3.14 mM for 4-nitrophenyl-beta-D-galactopyranoside2 Publications
  7. KM=1.58 mM for 4-nitrophenyl-beta-D-xylopyranoside2 Publications
  8. KM=52.6 mM for 4-nitrophenyl-beta-L-arabinopyranoside2 Publications
  9. KM=35 µM for genistein-7-glucoside2 Publications
  10. KM=118 µM for daidzein-7-glucoside2 Publications
  11. KM=31.8 µM for quercetin-4'-glucoside2 Publications
  12. KM=42.2 µM for quercetin-7-glucoside2 Publications
  13. KM=21.5 µM for apigenin-7-glucoside2 Publications
  14. KM=10 µM for luteolin-4'-glucoside2 Publications
  15. KM=50 µM for luteolin-7-glucoside2 Publications
  16. KM=432 µM for naringenin-7-glucoside2 Publications
  17. KM=253 µM for eriodictyol-7-glucoside2 Publications
  1. Vmax=10 µmol/min/mg enzyme toward 4-nitrophenyl-beta-D-glucopyranoside2 Publications
  2. Vmax=1.73 µmol/min/mg enzyme toward genistein-7-glucoside2 Publications
  3. Vmax=2.75 µmol/min/mg enzyme toward daidzein-7-glucoside2 Publications
  4. Vmax=1.19 µmol/min/mg enzyme toward quercetin-4'-glucoside2 Publications
  5. Vmax=0.77 µmol/min/mg enzyme toward quercetin-7-glucoside2 Publications
  6. Vmax=1.30 µmol/min/mg enzyme toward apigenin-7-glucoside2 Publications
  7. Vmax=1.30 µmol/min/mg enzyme toward luteolin-4'-glucoside2 Publications
  8. Vmax=2.85 µmol/min/mg enzyme toward luteolin-7-glucoside2 Publications
  9. Vmax=0.93 µmol/min/mg enzyme toward naringenin-7-glucoside2 Publications
  10. Vmax=0.90 µmol/min/mg enzyme toward eriodictyol-7-glucoside2 Publications

pH dependencei

Optimum pH is 6.5. Active from pH 5 to 7.5. Activity decreases sharply with increasing acidity and is less than 4% at pH 4.2 Publications

Temperature dependencei

Optimum temperature is 50 degrees Celsius. Stable more than 24 hours at 37 degrees Celsius. Loses activity at 58 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei17Substrate1
Binding sitei120Substrate1
Binding sitei164Substrate1
Active sitei165Proton donorSequence analysis1
Binding sitei309Substrate1
Active sitei373NucleophileSequence analysis1
Binding sitei417Substrate1

GO - Molecular functioni

  • beta-galactosidase activity Source: UniProtKB
  • beta-glucosidase activity Source: UniProtKB
  • glucosylceramidase activity Source: Reactome
  • glycosylceramidase activity Source: UniProtKB
  • scopolin beta-glucosidase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  • cellular oligosaccharide catabolic process Source: CAFA
  • glycoside catabolic process Source: UniProtKB
  • glycosphingolipid metabolic process Source: Reactome
  • glycosylceramide catabolic process Source: UniProtKB
  • positive regulation of exo-alpha-sialidase activity Source: CAFA
  • protein stabilization Source: CAFA
Complete GO annotation...

Keywordsi

Molecular functionGlycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.21. 2681.
ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
SABIO-RKiQ9H227.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic beta-glucosidase (EC:3.2.1.21)
Alternative name(s):
Cytosolic beta-glucosidase-like protein 1
Gene namesi
Name:GBA3
Synonyms:CBG, CBGL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:19069. GBA3.

Subcellular locationi

GO - Cellular componenti

  • catalytic complex Source: CAFA
  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi165E → D: Reduces catalytic activity 2-fold. 2 Publications1
Mutagenesisi165E → Q: Loss of catalytic activity. 2 Publications1
Mutagenesisi168V → Y: No change in temperature or pH dependence. Decrease in specific activity. 1 Publication1
Mutagenesisi225F → S: Decrease in specific activity. 1 Publication1
Mutagenesisi308Y → F or A: Decrease in specific activity. 1 Publication1
Mutagenesisi373E → D: Reduces catalytic activity 2-fold. 1 Publication1
Mutagenesisi373E → Q: Loss of catalytic activity. 1 Publication1

Organism-specific databases

DisGeNETi57733.
PharmGKBiPA134861643.

Chemistry databases

ChEMBLiCHEMBL3865.

Polymorphism and mutation databases

DMDMi77416427.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000639081 – 469Cytosolic beta-glucosidaseAdd BLAST469

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

EPDiQ9H227.
PaxDbiQ9H227.
PeptideAtlasiQ9H227.
PRIDEiQ9H227.

PTM databases

iPTMnetiQ9H227.
PhosphoSitePlusiQ9H227.

Expressioni

Tissue specificityi

Present in small intestine (at protein level). Expressed in liver, small intestine, colon, spleen and kidney. Down-regulated in renal cell carcinomas and hepatocellular carcinomas.2 Publications

Gene expression databases

CleanExiHS_GBA3.

Interactioni

Protein-protein interaction databases

BioGridi121753. 2 interactors.
IntActiQ9H227. 2 interactors.
STRINGi9606.ENSP00000471397.

Chemistry databases

BindingDBiQ9H227.

Structurei

Secondary structure

1469
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 12Combined sources5
Helixi15 – 18Combined sources4
Helixi24 – 26Combined sources3
Helixi31 – 38Combined sources8
Beta strandi40 – 43Combined sources4
Helixi44 – 46Combined sources3
Beta strandi49 – 51Combined sources3
Turni55 – 57Combined sources3
Helixi59 – 69Combined sources11
Beta strandi72 – 77Combined sources6
Helixi80 – 83Combined sources4
Helixi94 – 109Combined sources16
Beta strandi113 – 121Combined sources9
Helixi125 – 129Combined sources5
Helixi132 – 134Combined sources3
Helixi138 – 153Combined sources16
Turni154 – 156Combined sources3
Beta strandi159 – 164Combined sources6
Helixi166 – 174Combined sources9
Turni186 – 188Combined sources3
Helixi189 – 211Combined sources23
Helixi213 – 216Combined sources4
Beta strandi219 – 221Combined sources3
Beta strandi223 – 233Combined sources11
Helixi237 – 250Combined sources14
Helixi252 – 259Combined sources8
Helixi266 – 278Combined sources13
Helixi291 – 297Combined sources7
Beta strandi302 – 316Combined sources15
Helixi326 – 330Combined sources5
Beta strandi332 – 335Combined sources4
Helixi351 – 363Combined sources13
Beta strandi369 – 374Combined sources6
Beta strandi378 – 381Combined sources4
Helixi387 – 405Combined sources19
Beta strandi411 – 417Combined sources7
Helixi425 – 430Combined sources6
Beta strandi435 – 438Combined sources4
Beta strandi442 – 444Combined sources3
Beta strandi447 – 449Combined sources3
Helixi451 – 462Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E9LX-ray1.60A1-469[»]
2E9MX-ray1.80A1-469[»]
2JFEX-ray2.70X1-469[»]
2ZOXX-ray1.90A1-469[»]
3VKKX-ray2.00A1-469[»]
ProteinModelPortaliQ9H227.
SMRiQ9H227.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H227.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni424 – 425Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family. Klotho subfamily.Curated

Phylogenomic databases

eggNOGiKOG0626. Eukaryota.
COG2723. LUCA.
HOVERGENiHBG053101.
InParanoidiQ9H227.
KOiK05350.
PhylomeDBiQ9H227.

Family and domain databases

InterProiView protein in InterPro
IPR001360. Glyco_hydro_1.
IPR033132. Glyco_hydro_1_N_CS.
IPR017853. Glycoside_hydrolase_SF.
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiView protein in Pfam
PF00232. Glyco_hydro_1. 1 hit.
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiView protein in PROSITE
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H227-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAFPAGFGWA AATAAYQVEG GWDADGKGPC VWDTFTHQGG ERVFKNQTGD 
        60         70         80         90        100
VACGSYTLWE EDLKCIKQLG LTHYRFSLSW SRLLPDGTTG FINQKGIDYY 
       110        120        130        140        150
NKIIDDLLKN GVTPIVTLYH FDLPQTLEDQ GGWLSEAIIE SFDKYAQFCF 
       160        170        180        190        200
STFGDRVKQW ITINEANVLS VMSYDLGMFP PGIPHFGTGG YQAAHNLIKA 
       210        220        230        240        250
HARSWHSYDS LFRKKQKGMV SLSLFAVWLE PADPNSVSDQ EAAKRAITFH 
       260        270        280        290        300
LDLFAKPIFI DGDYPEVVKS QIASMSQKQG YPSSRLPEFT EEEKKMIKGT 
       310        320        330        340        350
ADFFAVQYYT TRLIKYQENK KGELGILQDA EIEFFPDPSW KNVDWIYVVP 
       360        370        380        390        400
WGVCKLLKYI KDTYNNPVIY ITENGFPQSD PAPLDDTQRW EYFRQTFQEL 
       410        420        430        440        450
FKAIQLDKVN LQVYCAWSLL DNFEWNQGYS SRFGLFHVDF EDPARPRVPY 
       460 
TSAKEYAKII RNNGLEAHL
Length:469
Mass (Da):53,696
Last modified:October 11, 2005 - v2
Checksum:i9036455485CE2E2F
GO
Isoform 2 (identifier: Q9H227-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     95-401: Missing.

Show »
Length:162
Mass (Da):18,265
Checksum:iAC2A05DB957E6997
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti29P → L in AAH70188 (PubMed:15489334).Curated1
Sequence conflicti134L → W in AAG39217 (PubMed:11784319).Curated1
Sequence conflicti309Y → C in BAD96683 (Ref. 5) Curated1
Sequence conflicti321K → R in BAD96683 (Ref. 5) Curated1
Sequence conflicti326I → T in CAC08178 (PubMed:11389701).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023587106D → N Rare polymorphism. 1 Publication1
Natural variantiVAR_049298172M → I. Corresponds to variant dbSNP:rs36090352Ensembl.1
Natural variantiVAR_023588213R → P. Corresponds to variant dbSNP:rs17612341Ensembl.1
Natural variantiVAR_023589354C → R. Corresponds to variant dbSNP:rs16873108Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01583595 – 401Missing in isoform 2. 1 PublicationAdd BLAST307

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017913 mRNA. Translation: BAB18741.1.
AJ278964 mRNA. Translation: CAC08178.1.
AF317840 mRNA. Translation: AAG39217.1.
AF323990 mRNA. Translation: AAL37305.1.
AK222963 mRNA. Translation: BAD96683.1.
BC029362 mRNA. Translation: AAH29362.1.
BC070188 mRNA. Translation: AAH70188.1.
BC101829 mRNA. Translation: AAI01830.1.
BC109377 mRNA. Translation: AAI09378.1.
RefSeqiNP_001121904.1. NM_001128432.2. [Q9H227-2]
NP_001264154.1. NM_001277225.1.
NP_066024.1. NM_020973.4. [Q9H227-1]
UniGeneiHs.653107.

Genome annotation databases

GeneIDi57733.
KEGGihsa:57733.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017913 mRNA. Translation: BAB18741.1.
AJ278964 mRNA. Translation: CAC08178.1.
AF317840 mRNA. Translation: AAG39217.1.
AF323990 mRNA. Translation: AAL37305.1.
AK222963 mRNA. Translation: BAD96683.1.
BC029362 mRNA. Translation: AAH29362.1.
BC070188 mRNA. Translation: AAH70188.1.
BC101829 mRNA. Translation: AAI01830.1.
BC109377 mRNA. Translation: AAI09378.1.
RefSeqiNP_001121904.1. NM_001128432.2. [Q9H227-2]
NP_001264154.1. NM_001277225.1.
NP_066024.1. NM_020973.4. [Q9H227-1]
UniGeneiHs.653107.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E9LX-ray1.60A1-469[»]
2E9MX-ray1.80A1-469[»]
2JFEX-ray2.70X1-469[»]
2ZOXX-ray1.90A1-469[»]
3VKKX-ray2.00A1-469[»]
ProteinModelPortaliQ9H227.
SMRiQ9H227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121753. 2 interactors.
IntActiQ9H227. 2 interactors.
STRINGi9606.ENSP00000471397.

Chemistry databases

BindingDBiQ9H227.
ChEMBLiCHEMBL3865.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

PTM databases

iPTMnetiQ9H227.
PhosphoSitePlusiQ9H227.

Polymorphism and mutation databases

DMDMi77416427.

Proteomic databases

EPDiQ9H227.
PaxDbiQ9H227.
PeptideAtlasiQ9H227.
PRIDEiQ9H227.

Protocols and materials databases

DNASUi57733.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi57733.
KEGGihsa:57733.

Organism-specific databases

CTDi57733.
DisGeNETi57733.
GeneCardsiGBA3.
HGNCiHGNC:19069. GBA3.
MIMi606619. gene.
neXtProtiNX_Q9H227.
PharmGKBiPA134861643.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0626. Eukaryota.
COG2723. LUCA.
HOVERGENiHBG053101.
InParanoidiQ9H227.
KOiK05350.
PhylomeDBiQ9H227.

Enzyme and pathway databases

BRENDAi3.2.1.21. 2681.
ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
SABIO-RKiQ9H227.

Miscellaneous databases

EvolutionaryTraceiQ9H227.
GeneWikiiGBA3.
GenomeRNAii57733.
PROiPR:Q9H227.
SOURCEiSearch...

Gene expression databases

CleanExiHS_GBA3.

Family and domain databases

InterProiView protein in InterPro
IPR001360. Glyco_hydro_1.
IPR033132. Glyco_hydro_1_N_CS.
IPR017853. Glycoside_hydrolase_SF.
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiView protein in Pfam
PF00232. Glyco_hydro_1. 1 hit.
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiView protein in PROSITE
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGBA3_HUMAN
AccessioniPrimary (citable) accession number: Q9H227
Secondary accession number(s): Q32LY7
, Q3MIH4, Q53GG8, Q6NSF4, Q8NHT8, Q9H3T4, Q9H4C6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 11, 2005
Last modified: May 10, 2017
This is version 139 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.