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Protein

Lysosomal beta glucosidase

Gene

gluA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei363By similarity1

GO - Molecular functioni

  • beta-glucosidase activity Source: dictyBase
  • scopolin beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysosomal beta glucosidase (EC:3.2.1.21)
Gene namesi
Name:gluA
ORF Names:DDB_G0292810
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 6, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0292810. gluA.

Subcellular locationi

GO - Cellular componenti

  • lysosome Source: dictyBase
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000036152325 – 691 PublicationAdd BLAST45
ChainiPRO_000036152470 – 821Lysosomal beta glucosidaseAdd BLAST752

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi113N-linked (GlcNAc...)Sequence analysis1
Glycosylationi146N-linked (GlcNAc...)Sequence analysis1
Glycosylationi266N-linked (GlcNAc...)Sequence analysis1
Glycosylationi535N-linked (GlcNAc...)Sequence analysis1
Glycosylationi555N-linked (GlcNAc...)Sequence analysis1
Glycosylationi703N-linked (GlcNAc...)Sequence analysis1
Glycosylationi721N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Glycosylated. The polyoligosaccharides are of the high-mannose type and are highly substituted with both phosphate and sulfate moieties.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ23892.

Interactioni

Protein-protein interaction databases

STRINGi44689.DDB0215373.

Structurei

3D structure databases

ProteinModelPortaliQ23892.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi461 – 466Poly-Ala6
Compositional biasi571 – 575Poly-Val5

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IGIA. Eukaryota.
COG1472. LUCA.
InParanoidiQ23892.
KOiK05349.
OMAiIKHGVAS.
PhylomeDBiQ23892.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 2 hits.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SMARTiSM01217. Fn3_like. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q23892-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTIKSLFLL SLLIVNLLIS STYGSSIRVS IVGGEEAEVI EKPRTFGNKR
60 70 80 90 100
ELKLEYSQIY PKKQLNQENI NFMSARDTFV DNLMSKMSIT EKIGQMTQLD
110 120 130 140 150
ITTLTSPNTI TINETTLAYY AKTYYIGSYL NSPVSGGLAG DIHHINSSVW
160 170 180 190 200
LDMINTIQTI VIEGSPNKIP MIYGLDSVHG ANYVHKATLF PHNTGLAATF
210 220 230 240 250
NIEHATTAAQ ITSKDTVAVG IPWVFAPVLG IGVQPLWSRI YETFGEDPYV
260 270 280 290 300
ASMMGAAAVR GFQGGNNSFD GPINAPSAVC TAKHYFGYSD PTSGKDRTAA
310 320 330 340 350
WIPERMLRRY FLPSFAEAIT GAGAGTIMIN SGEVNGVPMH TSYKYLTEVL
360 370 380 390 400
RGELQFEGVA VTDWQDIEKL VYFHHTAGSA EEAILQALDA GIDMSMVPLD
410 420 430 440 450
LSFPIILAEM VAAGTVPESR LDLSVRRILN LKYALGLFSN PYPNPNAAIV
460 470 480 490 500
DTIGQVQDRE AAAATAEESI TLLQNKNNIL PLNTNTIKNV LLTGPSADSI
510 520 530 540 550
RNLNGGWSVH WQGAYEDSEF PFGTSILTGL REITNDTADF NIQYTIGHEI
560 570 580 590 600
GVPTNQTSID EAVELAQSSD VVVVVIGELP EAETPGDIYD LSMDPNEVLL
610 620 630 640 650
LQQLVDTGKP VVLILVEARP RILPPDLVYS CAAVLMAYLP GSEGGKPIAN
660 670 680 690 700
ILMGNVNPSG RLPLTYPGTT GDIGVPYYHK YSENGVTTPL FQFGDGLSYT
710 720 730 740 750
TFNYTNLACS NCKPISGQSG NYTGVLGQSY TFTVTVTNNG NVQGKDSVLL
760 770 780 790 800
YLSDLWAQVT PEVKMLRGFQ KVDLMPAKSQ QISFTLNAYE FSFIGVDNKI
810 820
TLESGQFIIM VGNQQLGLYL Q
Length:821
Mass (Da):89,344
Last modified:January 20, 2009 - v2
Checksum:i297758E5007DD13D
GO

Sequence cautioni

The sequence AAA74233 differs from that shown. Reason: Frameshift at positions 393, 397, 399, 402 and 409.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti290D → N in AAA74233 (PubMed:8288612).Curated1
Sequence conflicti474 – 475QN → LF in AAA74233 (PubMed:8288612).Curated2
Sequence conflicti725Missing in AAA74233 (PubMed:8288612).Curated1
Sequence conflicti737T → TVT in AAA74233 (PubMed:8288612).Curated1
Sequence conflicti806Q → P in AAA74233 (PubMed:8288612).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L21014 mRNA. Translation: AAA74233.1. Frameshift.
AAFI02000197 Genomic DNA. Translation: EAL60954.1.
PIRiA49881.
RefSeqiXP_629427.1. XM_629425.1.

Genome annotation databases

EnsemblProtistsiEAL60954; EAL60954; DDB_G0292810.
GeneIDi8628946.
KEGGiddi:DDB_G0292810.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L21014 mRNA. Translation: AAA74233.1. Frameshift.
AAFI02000197 Genomic DNA. Translation: EAL60954.1.
PIRiA49881.
RefSeqiXP_629427.1. XM_629425.1.

3D structure databases

ProteinModelPortaliQ23892.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0215373.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Proteomic databases

PaxDbiQ23892.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAL60954; EAL60954; DDB_G0292810.
GeneIDi8628946.
KEGGiddi:DDB_G0292810.

Organism-specific databases

dictyBaseiDDB_G0292810. gluA.

Phylogenomic databases

eggNOGiENOG410IGIA. Eukaryota.
COG1472. LUCA.
InParanoidiQ23892.
KOiK05349.
OMAiIKHGVAS.
PhylomeDBiQ23892.

Miscellaneous databases

PROiQ23892.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 2 hits.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SMARTiSM01217. Fn3_like. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGLUA_DICDI
AccessioniPrimary (citable) accession number: Q23892
Secondary accession number(s): Q54CI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 20, 2009
Last modified: November 2, 2016
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Caution

PubMed:8288612 reports 2 different N-termini by direct protein sequencing: mature protein either starts at Ile-70 or Ser-74.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  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.