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Protein

1,4-beta-D-glucan glucohydrolase

Gene

gghA

Organism
Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NS-E)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Broad substrate specificity glycosidase. Releases glucose from soluble glucooligomers, with a preference for longer oligomers; acts more readily on cellotetraose than on cellobiose. Displays similar activities towards the disaccharides lactose and cellobiose. Is also able to hydrolyze various aryl-beta-glycosides in vitro.1 Publication

Catalytic activityi

Hydrolysis of (1->4)-linkages in (1->4)-beta-D-glucans, to remove successive glucose units.1 Publication
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.1 Publication

Enzyme regulationi

Activated by glucose up to 200 mM when p-nitrophenyl-beta-glucoside is used as the substrate. This activation by end product concentrations may be due to a transglycosylation activity of the enzyme.1 Publication

Kineticsi

kcat is 285.0, 345.7 and 333.7 sec(-1) for the hydrolysis of cellobiose, cellotriose and cellotetraose, respectively.

  1. KM=28.6 mM for cellobiose1 Publication
  2. KM=4.55 mM for cellotriose1 Publication
  3. KM=2.15 mM for cellotetraose1 Publication

pH dependencei

Optimum pH is 6.5.1 Publication

Temperature dependencei

Optimum temperature is 95 degrees Celsius. Is highly thermostable, retaining 85% activity after incubation for 9 hours at 90 degrees Celsius and 88% activity after 1 hour at 95 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei164 – 1641Proton donorSequence Analysis
Active sitei349 – 3491NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. glucan 1,4-beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciTNEA309803:GJFG-809-MONOMER.
UniPathwayiUPA00350.
UPA00696.

Names & Taxonomyi

Protein namesi
Recommended name:
1,4-beta-D-glucan glucohydrolase1 Publication (EC:3.2.1.741 Publication)
Short name:
Glucan glucohydrolase1 Publication
Alternative name(s):
Beta-D-glucoside glucohydrolase
Beta-glucosidase (EC:3.2.1.211 Publication)
Glucan 1,4-beta-glucosidase
Gene namesi
Name:gghA1 Publication
Ordered Locus Names:CTN_0782
OrganismiThermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NS-E)
Taxonomic identifieri309803 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000000445: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4444441,4-beta-D-glucan glucohydrolasePRO_0000372089Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi309803.CTN_0782.

Structurei

3D structure databases

ProteinModelPortaliB9K7M5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088630.
KOiK05350.
OrthoDBiEOG60658J.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR017736. Glyco_hydro_1_beta-glucosidase.
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.
TIGRFAMsiTIGR03356. BGL. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B9K7M5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKFPEGFLW GVATASYQIE GSPLADGAGM SIWHTFSHTP GNVKNGDTGD
60 70 80 90 100
VACDHYNRWK EDIEIIEKIG AKAYRFSISW PRILPEGTGK VNQKGLDFYN
110 120 130 140 150
RIIDTLLEKN ITPFITIYHW DLPFSLQLKG GWANRDIADW FAEYSRVLFE
160 170 180 190 200
NFGDRVKHWI TLNEPWVVAI VGHLYGVHAP GMKDIYVAFH TVHNLLRAHA
210 220 230 240 250
KSVKVFRETV KDGKIGIVFN NGYFEPASER EEDIRAARFM HQFNNYPLFL
260 270 280 290 300
NPIYRGEYPD LVLEFAREYL PRNYEDDMEE IKQEIDFVGL NYYSGHMVKY
310 320 330 340 350
DPNSPARVSF VERNLPKTAM GWEIVPEGIY WILKGVKEEY NPQEVYITEN
360 370 380 390 400
GAAFDDVVSE GGKVHDQNRI DYLRAHIEQV WRAIQDGVPL KGYFVWSLLD
410 420 430 440
NFEWAEGYSK RFGIVYVDYN TQKRIIKDSG YWYSNVIKNN GLTD
Length:444
Mass (Da):51,535
Last modified:May 5, 2009 - v2
Checksum:i56A2D49A20A8CE01
GO

Sequence cautioni

The sequence ACM22958.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti436 – 4361V → G in AAB95492 (PubMed:10960102).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039487 Genomic DNA. Translation: AAB95492.2.
CP000916 Genomic DNA. Translation: ACM22958.1. Different initiation.
RefSeqiYP_002534324.1. NC_011978.1.

Genome annotation databases

EnsemblBacteriaiACM22958; ACM22958; CTN_0782.
GeneIDi7378641.
KEGGitna:CTN_0782.
PATRICi23940329. VBITheNea118396_0765.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039487 Genomic DNA. Translation: AAB95492.2.
CP000916 Genomic DNA. Translation: ACM22958.1. Different initiation.
RefSeqiYP_002534324.1. NC_011978.1.

3D structure databases

ProteinModelPortaliB9K7M5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi309803.CTN_0782.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACM22958; ACM22958; CTN_0782.
GeneIDi7378641.
KEGGitna:CTN_0782.
PATRICi23940329. VBITheNea118396_0765.

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088630.
KOiK05350.
OrthoDBiEOG60658J.

Enzyme and pathway databases

UniPathwayiUPA00350.
UPA00696.
BioCyciTNEA309803:GJFG-809-MONOMER.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR017736. Glyco_hydro_1_beta-glucosidase.
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.
TIGRFAMsiTIGR03356. BGL. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the glucooligosaccharide catabolic pathway beta-glucan glucohydrolase and cellobiose phosphorylase in the marine hyperthermophile Thermotoga neapolitana."
    Yernool D.A., McCarthy J.K., Eveleigh D.E., Bok J.-D.
    J. Bacteriol. 182:5172-5179(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 49049 / DSM 4359 / NS-E.
  2. "The genome sequence of the hyperthermophilic bacterium Thermotoga neapolitana."
    Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J., Kim J.J., Park K.J., Lee S.Y.
    Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49049 / DSM 4359 / NS-E.

Entry informationi

Entry nameiBGLA_THENN
AccessioniPrimary (citable) accession number: B9K7M5
Secondary accession number(s): O33843, O52505
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: February 4, 2015
This is version 39 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.