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Protein
Submitted name:

Beta-galactosidase

Gene

celB

Organism
Pyrococcus furiosus
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.21. 5243.
3.2.1.B28. 5243.
3.2.1.B31. 5243.
SABIO-RKQ51723.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Submitted name:
Beta-galactosidaseImported
Submitted name:
Beta-glucosidaseImported
Gene namesi
Name:celBImported
OrganismiPyrococcus furiosusImported
Taxonomic identifieri2261 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Interactioni

Protein-protein interaction databases

STRINGi186497.PF0073.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3APGX-ray2.35A/B/C/D2-472[»]
3WDPX-ray1.70P/Q/R/S2-472[»]
3WQ8X-ray2.81A/B/C/D/E/F/G/H/I/J/K/L2-449[»]
SMRiQ51723. Positions 1-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG05412. Archaea.
COG2723. LUCA.

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. 2 hits.
PfamiPF00232. Glyco_hydro_1. 3 hits.
[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.

Q51723-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFPKNFMFG YSWSGFQFEM GLPGSEVESD WWVWVHDKEN IASGLVSGDL
60 70 80 90 100
PENGPAYWHL YKQDHDIAEK LGMDCIRGGI EWARIFPKPT FDVKVDVEKD
110 120 130 140 150
EEGNIISVDV PESTIKELEK IANMEALEHY RKIYSDWKER GKTFILNLYH
160 170 180 190 200
WPLPLWIHDP IAVRKLGPDR APAGWLDEKT VVEFVKFAAF VAYHLDDLVD
210 220 230 240 250
MWSTMNEPNV VYNQGYINLR SGFPPGYLSF EAAEKAKFNL IQAHIGAYDA
260 270 280 290 300
IKEYSEKSVG VIYAFAWHDP LAEEYKDEVE EIRKKDYEFV TILHSKGKLD
310 320 330 340 350
WIGVNYYSRL VYGAKDGHLV PLPGYGFMSE RGGFAKSGRP ASDFGWEMYP
360 370 380 390 400
EGLENLLKYL NNAYELPMII TENGMADAAD RYRPHYLVSH LKAVYNAMKE
410 420 430 440 450
GADVRGYLHW SLTDNYEWAQ GFRMRFGLVY VDFETKKRYL RPSALVFREI
460 470
ATQKEIPEEL AHLADLKFVT RK
Length:472
Mass (Da):54,665
Last modified:November 1, 1996 - v1
Checksum:i4E6BC9E3D8B8E33A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF013169 Genomic DNA. Translation: AAC25555.1.
KF420204 Genomic DNA. Translation: AHW49177.1.

Genome annotation databases

GeneIDi1467902.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF013169 Genomic DNA. Translation: AAC25555.1.
KF420204 Genomic DNA. Translation: AHW49177.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3APGX-ray2.35A/B/C/D2-472[»]
3WDPX-ray1.70P/Q/R/S2-472[»]
3WQ8X-ray2.81A/B/C/D/E/F/G/H/I/J/K/L2-449[»]
SMRiQ51723. Positions 1-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF0073.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1467902.

Phylogenomic databases

eggNOGiarCOG05412. Archaea.
COG2723. LUCA.

Enzyme and pathway databases

BRENDAi3.2.1.21. 5243.
3.2.1.B28. 5243.
3.2.1.B31. 5243.
SABIO-RKQ51723.

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. 2 hits.
PfamiPF00232. Glyco_hydro_1. 3 hits.
[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...

Publicationsi

  1. "Characterization of the celB gene coding for beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coli."
    Voorhorst W.G., Eggen R.I., Luesink E.J., de Vos W.M.
    J. Bacteriol. 177:7105-7111(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: DSM 3638Imported.
  2. "Transcriptional regulation in the hyperthermophilic archaeon Pyrococcus furiosus: coordinated expression of divergently oriented genes in response to beta-linked glucose polymers."
    Voorhorst W.G., Gueguen Y., Geerling A.C., Schut G., Dahlke I., Thomm M., van der Oost J., de Vos W.M.
    J. Bacteriol. 181:3777-3783(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: DSM 3638Imported.
  3. van der Oost J.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: DSM 3638Imported.
  4. "Crystal structure of hyperthermophilic beta-glucosidase from pyrococcus furiosus."
    Kado Y., Inoue T., Ishikawa K.
    Submitted (OCT-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2-472.
  5. "Presep: predicting the propensity of a protein being secreted into the supernatant when expressed in Pichia pastoris."
    Tian J., Zhang Y., Liu B., Zuo D., Jiang T., Guo J., Zhang W., Wu N., Fan Y.
    PLoS ONE 8:E79749-E79749(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: B232Imported.
  6. "Monomer structure of a hyperthermophilic [beta]-glucosidase mutant forming a dodecameric structure in the crystal form."
    Nakabayashi M., Kataoka M., Watanabe M., Ishikawa K.
    Acta Crystallogr F Struct Biol Commun 70:854-859(2014)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 2-449.
  7. "Structural analysis of beta-glucosidase mutants derived from a hyperthermophilic tetrameric structure."
    Nakabayashi M., Kataoka M., Mishima Y., Maeno Y., Ishikawa K.
    Acta Crystallogr. D 70:877-888(2014)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-472.

Entry informationi

Entry nameiQ51723_9EURY
AccessioniPrimary (citable) accession number: Q51723
Secondary accession number(s): Q7LX20
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: April 13, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.