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P54583

- GUN1_ACIC1

UniProt

P54583 - GUN1_ACIC1

Protein

Endoglucanase E1

Gene

Acel_0614

Organism
Acidothermus cellulolyticus (strain ATCC 43068 / 11B)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Has a very high specific activity on carboxymethylcellulose.

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

    Temperature dependencei

    Optimum temperature is 81 degrees Celsius. Thermostable.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei203 – 2031Proton donor
    Active sitei323 – 3231Nucleophile

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. polysaccharide binding Source: InterPro

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Enzyme and pathway databases

    BioCyciACEL351607:GIXW-627-MONOMER.

    Protein family/group databases

    CAZyiCBM2. Carbohydrate-Binding Module Family 2.
    GH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase E1 (EC:3.2.1.4)
    Alternative name(s):
    Cellulase E1
    Endo-1,4-beta-glucanase E1
    Endocellulase E1
    Gene namesi
    Ordered Locus Names:Acel_0614
    OrganismiAcidothermus cellulolyticus (strain ATCC 43068 / 11B)
    Taxonomic identifieri351607 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeAcidothermaceaeAcidothermus
    ProteomesiUP000008221: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141Add
    BLAST
    Chaini42 – 562521Endoglucanase E1PRO_0000007834Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi75 ↔ 161
    Disulfide bondi209 ↔ 212

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    STRINGi351607.Acel_0614.

    Structurei

    Secondary structure

    1
    562
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi48 – 503
    Beta strandi53 – 553
    Beta strandi65 – 684
    Turni80 – 845
    Helixi87 – 9610
    Beta strandi101 – 1077
    Helixi108 – 1114
    Beta strandi123 – 1253
    Turni127 – 1315
    Helixi134 – 14714
    Beta strandi151 – 16010
    Beta strandi166 – 1683
    Beta strandi171 – 1733
    Helixi175 – 18814
    Turni189 – 1913
    Beta strandi195 – 1995
    Beta strandi209 – 2113
    Turni215 – 2173
    Helixi219 – 23315
    Beta strandi237 – 2426
    Beta strandi244 – 2474
    Turni254 – 2563
    Turni259 – 2635
    Beta strandi269 – 2724
    Beta strandi274 – 2796
    Turni283 – 2853
    Helixi289 – 2913
    Turni294 – 2996
    Helixi300 – 3078
    Helixi309 – 3135
    Beta strandi319 – 3235
    Helixi331 – 34313
    Helixi347 – 3504
    Beta strandi356 – 3605
    Turni367 – 3693
    Beta strandi377 – 3804
    Helixi382 – 3887
    Helixi389 – 3913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ECEX-ray2.40A/B42-399[»]
    1VRXX-ray2.40A/B42-399[»]
    ProteinModelPortaliP54583.
    SMRiP54583. Positions 42-399.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54583.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini458 – 562105CBM2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni42 – 400359CatalyticAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi401 – 46161Pro/Ser/Thr-rich (linker)Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000225207.
    KOiK01179.
    OMAiNSWGMRC.
    OrthoDBiEOG6FRCSN.

    Family and domain databases

    Gene3Di2.60.40.290. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00553. CBM_2. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view]
    SMARTiSM00637. CBD_II. 1 hit.
    [Graphical view]
    SUPFAMiSSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS51173. CBM2. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P54583-1 [UniParc]FASTAAdd to Basket

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    MPRALRRVPG SRVMLRVGVV VAVLALVAAL ANLAVPRPAR AAGGGYWHTS    50
    GREILDANNV PVRIAGINWF GFETCNYVVH GLWSRDYRSM LDQIKSLGYN 100
    TIRLPYSDDI LKPGTMPNSI NFYQMNQDLQ GLTSLQVMDK IVAYAGQIGL 150
    RIILDRHRPD CSGQSALWYT SSVSEATWIS DLQALAQRYK GNPTVVGFDL 200
    HNEPHDPACW GCGDPSIDWR LAAERAGNAV LSVNPNLLIF VEGVQSYNGD 250
    SYWWGGNLQG AGQYPVVLNV PNRLVYSAHD YATSVYPQTW FSDPTFPNNM 300
    PGIWNKNWGY LFNQNIAPVW LGEFGTTLQS TTDQTWLKTL VQYLRPTAQY 350
    GADSFQWTFW SWNPDSGDTG GILKDDWQTV DTVKDGYLAP IKSSIFDPVG 400
    ASASPSSQPS PSVSPSPSPS PSASRTPTPT PTPTASPTPT LTPTATPTPT 450
    ASPTPSPTAA SGARCTASYQ VNSDWGNGFT VTVAVTNSGS VATKTWTVSW 500
    TFGGNQTITN SWNAAVTQNG QSVTARNMSY NNVIQPGQNT TFGFQASYTG 550
    SNAAPTVACA AS 562
    Length:562
    Mass (Da):60,748
    Last modified:October 1, 1996 - v1
    Checksum:i84E6256406A35041
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33212 Genomic DNA. Translation: AAA75477.1.
    CP000481 Genomic DNA. Translation: ABK52387.1.
    RefSeqiWP_011719450.1. NC_008578.1.
    YP_872373.1. NC_008578.1.

    Genome annotation databases

    EnsemblBacteriaiABK52387; ABK52387; Acel_0614.
    GeneIDi4486396.
    KEGGiace:Acel_0614.
    PATRICi20671622. VBIAciCel132453_0657.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33212 Genomic DNA. Translation: AAA75477.1 .
    CP000481 Genomic DNA. Translation: ABK52387.1 .
    RefSeqi WP_011719450.1. NC_008578.1.
    YP_872373.1. NC_008578.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ECE X-ray 2.40 A/B 42-399 [» ]
    1VRX X-ray 2.40 A/B 42-399 [» ]
    ProteinModelPortali P54583.
    SMRi P54583. Positions 42-399.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 351607.Acel_0614.

    Protein family/group databases

    CAZyi CBM2. Carbohydrate-Binding Module Family 2.
    GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABK52387 ; ABK52387 ; Acel_0614 .
    GeneIDi 4486396.
    KEGGi ace:Acel_0614.
    PATRICi 20671622. VBIAciCel132453_0657.

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000225207.
    KOi K01179.
    OMAi NSWGMRC.
    OrthoDBi EOG6FRCSN.

    Enzyme and pathway databases

    BioCyci ACEL351607:GIXW-627-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P54583.

    Family and domain databases

    Gene3Di 2.60.40.290. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00553. CBM_2. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SMARTi SM00637. CBD_II. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS51173. CBM2. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Laymon R.A., Himmel M.E., Thomas S.R.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43068 / 11B.
    3. "Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose."
      Sakon J., Adney W.S., Himmel M.E., Thomas S.R., Kaplus P.A.
      Biochemistry 35:10648-10660(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 42-398.

    Entry informationi

    Entry nameiGUN1_ACIC1
    AccessioniPrimary (citable) accession number: P54583
    Secondary accession number(s): A0LSH7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3