Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P23659

- GUNZ_CLOSR

UniProt

P23659 - GUNZ_CLOSR

Protein

Endoglucanase Z

Gene

celZ

Organism
Clostridium stercorarium
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei400 – 4001By similarity
    Active sitei438 – 4381By similarity
    Active sitei447 – 4471By similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. cellulose 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

    Protein family/group databases

    CAZyiCBM3. Carbohydrate-Binding Module Family 3.
    GH9. Glycoside Hydrolase Family 9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase Z (EC:3.2.1.4)
    Alternative name(s):
    Avicelase I
    Endo-1,4-beta-glucanase
    Thermoactive cellulase
    Gene namesi
    Name:celZ
    OrganismiClostridium stercorarium
    Taxonomic identifieri1510 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 25251 PublicationAdd
    BLAST
    Chaini26 – 986961Endoglucanase ZPRO_0000007948Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP23659.
    SMRiP23659. Positions 30-641.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini481 – 642162CBM3 1PROSITE-ProRule annotationAdd
    BLAST
    Repeati651 – 73888Domain BAdd
    BLAST
    Repeati744 – 83188Domain B'Add
    BLAST
    Domaini836 – 986151CBM3 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 CBM3 (carbohydrate binding type-3) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    2.60.40.10. 2 hits.
    2.60.40.710. 2 hits.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR008965. Carb-bd_dom.
    IPR005102. Carbo-bd_X2.
    IPR001956. CBD_3.
    IPR001701. Glyco_hydro_9.
    IPR018221. Glyco_hydro_9_AS.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    [Graphical view]
    PfamiPF00942. CBM_3. 2 hits.
    PF03442. CBM_X2. 2 hits.
    PF00759. Glyco_hydro_9. 1 hit.
    [Graphical view]
    SMARTiSM01067. CBM_3. 2 hits.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.
    SSF49384. SSF49384. 2 hits.
    SSF81296. SSF81296. 2 hits.
    PROSITEiPS51172. CBM3. 2 hits.
    PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
    PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P23659-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRKFYSFAII ISLLVTGLFI HTPKAEAAGY NYGEALQKAI MFYEFQRSGK    50
    LPENKRDNWR GDSGLNDGAD VGLDLTGGWY DAGDHVKFNL PMAYSQTMLA 100
    WAAYEAEEAL ERSGQMGYLL DAIKWVSDYL IKCHPSPNVF YYQVGDGHLD 150
    HSWWGPAEVM QMDRPAYKVD LANPGSTVVA EAAAALASAA VVFADRDPAY 200
    AATCIQHAKE LYNFAEITKS DSGYTAASGF YDSHSGFYDE LSWAGVWLYL 250
    ATGDETYLNK AEQYVAYWGT EPQTNIISYK WAHCWDDVHY GACLLLAKIT 300
    GKQIYKEAIE RHLDYWSVGY NGERVHYTPK GLAWLDSWGS LRYATTTAFL 350
    ASVYADWEGC SREKAAIYND FAKQQIDYAL GSSGRSYVVG FGVNPPKRPH 400
    HRTAHSSWAD SMSVPDYHRH VLIGALVGGP GKDDSYTDDI NNYINNEVAC 450
    DYNAGFVGAL AKMYEDYGGS PIPDLNAFEE ITNDEFFVMA GINASGQNFI 500
    EIKALLHNQS GWPARVADKL SFRYFVDLTE LIEAGYSASD VTITTNYNAG 550
    AKVTGLHPWN EAENIYYVNV DFTGTKIYPG GQSAYRKEVQ FRIAAPQNTN 600
    FWNNDNDYSF RDIKGVTSGN TVKTVYIPVY DDGVLVFGVE PEGGSGENNS 650
    SISITNATFD KNPAKQENIQ VVMNLNGNTL NGIKYGNTYL REGTDYTVSG 700
    DTVTILKSFL NSFDTSTVQL IFDFSAGRDP VLTVNIIDTT TSASIVPTTA 750
    DFDKNPDASR DVKVKLVPNG NTLLAVKKDG EALVLGRDYS IDGDEVTIFR 800
    EYLADQPVGR VTLTFDFDRG TDPVLTINIT DSRQVETGVI QIQMFNGNTS 850
    DKTNGIMPRY RLTNTGTTPI RLSDVKIRYY YTIDGEKDQN FWCDWSSVGS 900
    NNITGTFVKM AEPKEGADYY LETGFTDGAG YLQPNQSIEV QNRFSKADWT 950
    DYIQTNDYSF STNTSYGSND RITVYISGVL VSGIEP 986
    Length:986
    Mass (Da):109,512
    Last modified:November 1, 1991 - v1
    Checksum:i1802E09B22923690
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55299 Genomic DNA. Translation: CAA39010.1. Sequence problems.
    PIRiS12021.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55299 Genomic DNA. Translation: CAA39010.1 . Sequence problems.
    PIRi S12021.

    3D structure databases

    ProteinModelPortali P23659.
    SMRi P23659. Positions 30-641.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM3. Carbohydrate-Binding Module Family 3.
    GH9. Glycoside Hydrolase Family 9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.50.10.10. 1 hit.
    2.60.40.10. 2 hits.
    2.60.40.710. 2 hits.
    InterProi IPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR008965. Carb-bd_dom.
    IPR005102. Carbo-bd_X2.
    IPR001956. CBD_3.
    IPR001701. Glyco_hydro_9.
    IPR018221. Glyco_hydro_9_AS.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    [Graphical view ]
    Pfami PF00942. CBM_3. 2 hits.
    PF03442. CBM_X2. 2 hits.
    PF00759. Glyco_hydro_9. 1 hit.
    [Graphical view ]
    SMARTi SM01067. CBM_3. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48208. SSF48208. 1 hit.
    SSF49384. SSF49384. 2 hits.
    SSF81296. SSF81296. 2 hits.
    PROSITEi PS51172. CBM3. 2 hits.
    PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
    PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of the Clostridium stercorarium celZ gene encoding a thermoactive cellulase (Avicelase I): identification of catalytic and cellulose-binding domains."
      Jauris S., Ruecknagel K.P., Schwarz W.H., Kratzsch P., Bronnenmeier K., Staudenbauer W.L.
      Mol. Gen. Genet. 223:258-267(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-36 AND 475-486.
      Strain: NCIB 11745.

    Entry informationi

    Entry nameiGUNZ_CLOSR
    AccessioniPrimary (citable) accession number: P23659
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 88 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

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3