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P26225

- GUNB_CELFI

UniProt

P26225 - GUNB_CELFI

Protein

Endoglucanase B

Gene

cenB

Organism
Cellulomonas fimi
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    • Comment

    Functioni

    The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

    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 sitei410 – 4101By similarity
    Active sitei449 – 4491By similarity
    Active sitei458 – 4581By 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

    CAZyiCBM2. Carbohydrate-Binding Module Family 2.
    CBM3. Carbohydrate-Binding Module Family 3.
    GH9. Glycoside Hydrolase Family 9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase B (EC:3.2.1.4)
    Alternative name(s):
    Cellulase B
    Endo-1,4-beta-glucanase B
    Gene namesi
    Name:cenB
    OrganismiCellulomonas fimi
    Taxonomic identifieri1708 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 10451012Endoglucanase BPRO_0000007945Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi946 ↔ 1044By similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliP26225.
    SMRiP26225. Positions 35-641.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini493 – 642150CBM3PROSITE-ProRule annotationAdd
    BLAST
    Domaini653 – 74391Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini751 – 84090Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini849 – 94092Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini939 – 1045107CBM2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni34 – 492459CatalyticAdd
    BLAST
    Regioni644 – 6507Linker ("hinge") (Pro-Thr box)
    Regioni734 – 74815Linker ("hinge") (Pro-Thr box)Add
    BLAST
    Regioni831 – 84616Linker ("hinge") (Pro-Thr box)Add
    BLAST
    Regioni931 – 94414Linker ("hinge") (Pro-Thr box)Add
    BLAST

    Domaini

    The linker region (also termed "hinge") may be a potential site for proteolysis.1 Publication

    Sequence similaritiesi

    Contains 1 CBM3 (carbohydrate binding type-3) domain.PROSITE-ProRule annotation
    Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    2.60.40.10. 3 hits.
    2.60.40.290. 1 hit.
    2.60.40.710. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR012291. CBD_carb-bd_dom.
    IPR018366. CBM2_CS.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR003961. Fibronectin_type3.
    IPR001701. Glyco_hydro_9.
    IPR018221. Glyco_hydro_9_AS.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PfamiPF00553. CBM_2. 1 hit.
    PF00942. CBM_3. 1 hit.
    PF00041. fn3. 3 hits.
    PF00759. Glyco_hydro_9. 1 hit.
    [Graphical view]
    SMARTiSM00637. CBD_II. 1 hit.
    SM01067. CBM_3. 1 hit.
    SM00060. FN3. 3 hits.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.
    SSF49265. SSF49265. 2 hits.
    SSF49384. SSF49384. 2 hits.
    PROSITEiPS51173. CBM2. 1 hit.
    PS00561. CBM2_A. 1 hit.
    PS51172. CBM3. 1 hit.
    PS50853. FN3. 3 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.

    P26225-1 [UniParc]FASTAAdd to Basket

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    MLRQVPRTLV AGGSALAVAV GVLVAPLATG AAAAPTYNYA EALQKSMFFY     50
    QAQRSGDLPA DFPVSWRGDS GLTDGADVGK DLTGGWYDAG DHVKFGFPMA 100
    FSATMLAWGA IESPTGYSKA GSLDELKDNL RFVSDYFVKA HTAPNELYVQ 150
    VGDGEADHKW WGPAEVMTMA RPSHKISASC PGSDVAAETA AALASSAIVL 200
    KGDDPAYAAT LVSHAKQLYT FADTYRGAYS DCVTAASAYY KSWSGYQDEL 250
    VWGAYWLYKA TGDATYLAKA EAEYDKLGTE NQSTTRSYKW TIAWDNKQFG 300
    TYALLAMETG KQKYVDDANR WLDYWTVGVN GQKVPYSPGG QAVLDSWGAL 350
    RYAANTSFVA LVYSDWMTDA TRKARYHDFG VRQINYALGD NPRSSSYVVG 400
    FGANPPTAPH HRTAHGSWLD SITTPAQSRH VLYGALVGGP GSPNDAYTDS 450
    RQDYVANEVA TDYNAGFTSA LARLVEEYGG TPLASFPTPE QPDGDQLFVE 500
    AMLNQPPSGT FTEVKAMIRN QSAFPARSLK NAKVRYWFTT DGFAASDVTL 550
    SANYSECGAQ SGKGVSAGGT LGYVELSCVG QDIHPGGQSQ HRREIQFRLT 600
    GPAGWNPAND PSYTGLTQTA LAKASAITLY DGSTLVWGKE PTGTTTDTTP 650
    PTTPGTPVAT GVTTVGASLS WAASTDAGSG VAGYELYRVQ GTTQTLVGTT 700
    TAAAYILRDL TPGTAYSYVV KAKDVAGNVS AASAAVTFTT DTTGETEPPT 750
    TPGTPVASAV TSTGATLAWA PSTGDPAVSG YDVLRVQGTT TTVVAQTTVP 800
    TVTLSGLTPS TAYTYAVRAK NVAGDVSALS APVTFTTAAP PVDTVAPTVP 850
    GTPVASNVAT TGATLTWTAS TDSGGSGLAG YEVLRVSGTT QTLVASPTTA 900
    TVALAGLTPA TAYSYVVRAK DGAGNVSAVS SPVTFTTLPV TSTPSCTVVY 950
    STNSWNVGFT GSVKITNTGT TPLTWTLGFA FPSGQQVTQG WSATWSQTGT 1000
    TVTATGLSWN ATLQPGQSTD IGFNGSHPGT NTNPASFTVN GEVCG 1045
    Length:1,045
    Mass (Da):108,991
    Last modified:May 1, 1992 - v1
    Checksum:iAC2F7B84E4E3C4F0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64644 Genomic DNA. Translation: AAA23086.1.
    PIRiA39199.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64644 Genomic DNA. Translation: AAA23086.1 .
    PIRi A39199.

    3D structure databases

    ProteinModelPortali P26225.
    SMRi P26225. Positions 35-641.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM2. Carbohydrate-Binding Module Family 2.
    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. 3 hits.
    2.60.40.290. 1 hit.
    2.60.40.710. 1 hit.
    InterProi IPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR012291. CBD_carb-bd_dom.
    IPR018366. CBM2_CS.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR003961. Fibronectin_type3.
    IPR001701. Glyco_hydro_9.
    IPR018221. Glyco_hydro_9_AS.
    IPR013783. Ig-like_fold.
    [Graphical view ]
    Pfami PF00553. CBM_2. 1 hit.
    PF00942. CBM_3. 1 hit.
    PF00041. fn3. 3 hits.
    PF00759. Glyco_hydro_9. 1 hit.
    [Graphical view ]
    SMARTi SM00637. CBD_II. 1 hit.
    SM01067. CBM_3. 1 hit.
    SM00060. FN3. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48208. SSF48208. 1 hit.
    SSF49265. SSF49265. 2 hits.
    SSF49384. SSF49384. 2 hits.
    PROSITEi PS51173. CBM2. 1 hit.
    PS00561. CBM2_A. 1 hit.
    PS51172. CBM3. 1 hit.
    PS50853. FN3. 3 hits.
    PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
    PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Unusual sequence organization in CenB, an inverting endoglucanase from Cellulomonas fimi."
      Meinke A., Braun C., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
      J. Bacteriol. 173:308-314(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Multiple domains in endoglucanase B (CenB) from Cellulomonas fimi: functions and relatedness to domains in other polypeptides."
      Meinke A., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
      J. Bacteriol. 173:7126-7135(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS.

    Entry informationi

    Entry nameiGUNB_CELFI
    AccessioniPrimary (citable) accession number: P26225
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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