Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

    Pathway: cellulose degradation

    This protein is involved in the pathway cellulose degradation, which is part of Glycan metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway cellulose degradation and in Glycan metabolism.

    Pathway: beta-D-glucan degradation

    This protein is involved in the pathway beta-D-glucan degradation, which is part of Glycan metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway beta-D-glucan degradation and in Glycan metabolism.

    Sites

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

    GO - Molecular functioni

    GO - Biological processi

    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.
    SABIO-RKB9K7M5.
    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 Componenti: 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.
    RefSeqiWP_015919275.1. NC_011978.1.
    YP_002534324.1. NC_011978.1.

    Genome annotation databases

    EnsemblBacteriaiACM22958; ACM22958; CTN_0782.
    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.
    RefSeqiWP_015919275.1. NC_011978.1.
    YP_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.
    KEGGitna:CTN_0782.
    PATRICi23940329. VBITheNea118396_0765.

    Phylogenomic databases

    eggNOGiCOG2723.
    HOGENOMiHOG000088630.
    KOiK05350.
    OrthoDBiEOG60658J.

    Enzyme and pathway databases

    UniPathwayiUPA00350.
    UPA00696.
    BioCyciTNEA309803:GJFG-809-MONOMER.
    SABIO-RKB9K7M5.

    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: May 27, 2015
    This is version 41 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.