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P19424

- GUN_BACS6

UniProt

P19424 - GUN_BACS6

Protein

Endoglucanase

Gene
N/A
Organism
Bacillus sp. (strain KSM-635)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei373 – 3731Proton donor
    Active sitei485 – 4851Nucleophile

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiCBM17. Carbohydrate-Binding Module Family 17.
    CBM28. Carbohydrate-Binding Module Family 28.
    GH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase (EC:3.2.1.4)
    Alternative name(s):
    Alkaline cellulase
    Endo-1,4-beta-glucanase
    OrganismiBacillus sp. (strain KSM-635)
    Taxonomic identifieri1415 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Add
    BLAST
    Chaini30 – 941912EndoglucanasePRO_0000007838Add
    BLAST

    Structurei

    Secondary structure

    1
    941
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi232 – 2354
    Beta strandi239 – 2435
    Beta strandi246 – 2505
    Beta strandi254 – 2563
    Beta strandi260 – 2656
    Helixi267 – 2704
    Helixi271 – 2733
    Helixi276 – 2838
    Beta strandi289 – 30113
    Turni302 – 3043
    Helixi308 – 32114
    Beta strandi325 – 3317
    Beta strandi334 – 3363
    Helixi341 – 3433
    Helixi346 – 35712
    Helixi363 – 3653
    Beta strandi366 – 3694
    Helixi388 – 40821
    Beta strandi413 – 4153
    Helixi418 – 4214
    Helixi424 – 4296
    Beta strandi433 – 44412
    Turni445 – 4473
    Helixi461 – 4633
    Helixi467 – 47610
    Beta strandi481 – 49010
    Turni491 – 4933
    Helixi499 – 51113
    Beta strandi516 – 5216
    Beta strandi524 – 5263
    Turni536 – 5383
    Helixi554 – 5563
    Helixi559 – 56911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G01X-ray1.90A228-584[»]
    1G0CX-ray1.90A228-584[»]
    ProteinModelPortaliP19424.
    SMRiP19424. Positions 227-752, 759-941.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19424.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini37 – 9458SLH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini95 – 15864SLH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini161 – 22464SLH 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 3 SLH (S-layer homology) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.60.120.260. 2 hits.
    3.20.20.80. 1 hit.
    InterProiIPR005086. CBM_fam_17/28.
    IPR008979. Galactose-bd-like.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR001119. S-layer_homology_dom.
    [Graphical view]
    PfamiPF03424. CBM_17_28. 2 hits.
    PF00150. Cellulase. 1 hit.
    PF00395. SLH. 3 hits.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    PS51272. SLH. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P19424-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIKQIKQSL SLLLIITLIM SLFVPMASAN TNESKSNAFP FSDVKKTSWS    50
    FPYIKDLYEQ EVITGTSATT FSPTDSVTRA QFTVMLTRGL GLEASSKDYP 100
    FKDRKNWAYK EIQAAYEAGI VTGKTNGEFA PNENITREQM AAMAVRAYEY 150
    LENELSLPEE QREYNDSSSI STFAQDAVQK AYVLELMEGN TDGYFQPKRN 200
    STREQSAKVI STLLWKVASH DYLYHTEAVK SPSEAGALQL VELNGQLTLA 250
    GEDGTPVQLR GMSTHGLQWF GEIVNENAFV ALSNDWGSNM IRLAMYIGEN 300
    GYATNPEVKD LVYEGIELAF EHDMYVIVDW HVHAPGDPRA DVYSGAYDFF 350
    EEIADHYKDH PKNHYIIWEL ANEPSPNNNG GPGLTNDEKG WEAVKEYAEP 400
    IVEMLREKGD NMILVGNPNW SQRPDLSADN PIDAENIMYS VHFYTGSHGA 450
    SHIGYPEGTP SSERSNVMAN VRYALDNGVA VFATEWGTSQ ANGDGGPYFD 500
    EADVWLNFLN KHNISWANWS LTNKNEISGA FTPFELGRTD ATDLDPGANQ 550
    VWAPEELSLS GEYVRARIKG IEYTPIDRTK FTKLVWDFND GTTQGFQVNG 600
    DSPNKESITL SNNNDALQIE GLNVSNDISE GNYWDNVRLS ADGWSENVDI 650
    LGATELTIDV IVEEPTTVSI AAIPQGPAAG WANPTRAIKV TEDDFESFGD 700
    GYKALVTITS EDSPSLETIA TSPEDNTMSN IILFVGTEDA DVISLDNITV 750
    SGTEIEIEVI HDEKGTATLP STFEDGTRQG WDWHTESGVK TALTIEEANG 800
    SNALSWEYAY PEVKPSDGWA TAPRLDFWKD ELVRGTSDYI SFDFYIDAVR 850
    ASEGAISINA VFQPPANGYW QEVPTTFEID LTELDSATVT SDELYHYEVK 900
    INIRDIEAIT DDTELRNLLL IFADEDSDFA GRVFVDNVRF E 941
    Length:941
    Mass (Da):104,628
    Last modified:November 1, 1990 - v1
    Checksum:iBEA2AC3B169BFADA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27420 Genomic DNA. Translation: AAA22304.1.
    PIRiS29043.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27420 Genomic DNA. Translation: AAA22304.1 .
    PIRi S29043.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G01 X-ray 1.90 A 228-584 [» ]
    1G0C X-ray 1.90 A 228-584 [» ]
    ProteinModelPortali P19424.
    SMRi P19424. Positions 227-752, 759-941.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM17. Carbohydrate-Binding Module Family 17.
    CBM28. Carbohydrate-Binding Module Family 28.
    GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P19424.

    Family and domain databases

    Gene3Di 2.60.120.260. 2 hits.
    3.20.20.80. 1 hit.
    InterProi IPR005086. CBM_fam_17/28.
    IPR008979. Galactose-bd-like.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR001119. S-layer_homology_dom.
    [Graphical view ]
    Pfami PF03424. CBM_17_28. 2 hits.
    PF00150. Cellulase. 1 hit.
    PF00395. SLH. 3 hits.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    PS51272. SLH. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and nucleotide sequence of a gene for alkaline cellulase from Bacillus sp. KSM-635."
      Ozaki K., Shikata S., Kawai S., Ito S., Okamoto K.
      J. Gen. Microbiol. 136:1327-1334(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Crystallization and preliminary X-ray analysis of a truncated family A alkaline endoglucanase isolated from Bacillus sp. KSM-635."
      Shirai T., Yamane T., Hidaka T., Kuyama K., Suzuki A., Ashida T., Ozaki K., Ito S.
      J. Biochem. 122:683-685(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 228-584, CRYSTALLIZATION.
    3. "Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme."
      Shirai T., Ishida H., Noda J., Yamane T., Ozaki K., Hakamada Y., Ito S.
      J. Mol. Biol. 310:1079-1087(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 221-584.

    Entry informationi

    Entry nameiGUN_BACS6
    AccessioniPrimary (citable) accession number: P19424
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 99 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, Direct protein sequencing

    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