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)

P14090

- GUNC_CELFA

UniProt

P14090 - GUNC_CELFA

Protein

Endoglucanase C

Gene

cenC

Organism
Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (01 Mar 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • 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 sitei831 – 8311PROSITE-ProRule annotation
    Active sitei882 – 8821PROSITE-ProRule annotation
    Active sitei891 – 8911PROSITE-ProRule annotation

    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

    Enzyme and pathway databases

    BioCyciCFIM590998:GJFK-1554-MONOMER.

    Protein family/group databases

    CAZyiCBM4. Carbohydrate-Binding Module Family 4.
    GH9. Glycoside Hydrolase Family 9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase C (EC:3.2.1.4)
    Alternative name(s):
    Cellulase C
    Endo-1,4-beta-glucanase C
    Gene namesi
    Name:cenC
    Ordered Locus Names:Celf_1537
    OrganismiCellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547)
    Taxonomic identifieri590998 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas
    ProteomesiUP000008460: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 32321 PublicationAdd
    BLAST
    Chaini33 – 11011069Endoglucanase CPRO_0000007946Add
    BLAST

    Structurei

    Secondary structure

    1
    1101
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi42 – 443
    Beta strandi49 – 524
    Beta strandi62 – 687
    Beta strandi76 – 849
    Beta strandi91 – 10212
    Beta strandi107 – 1148
    Beta strandi119 – 1235
    Beta strandi132 – 1398
    Beta strandi155 – 1606
    Beta strandi169 – 18012
    Beta strandi184 – 1863
    Turni190 – 1923
    Beta strandi198 – 2036
    Beta strandi212 – 2154
    Beta strandi226 – 2305
    Beta strandi239 – 25113
    Beta strandi253 – 2608
    Beta strandi262 – 2654
    Beta strandi272 – 2776
    Beta strandi282 – 2898
    Beta strandi296 – 2994
    Beta strandi303 – 3075
    Beta strandi315 – 32410

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CX1NMR-A178-328[»]
    1GU3X-ray2.30A33-181[»]
    1ULONMR-A33-184[»]
    1ULPNMR-A33-184[»]
    ProteinModelPortaliP14090.
    SMRiP14090. Positions 33-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14090.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini64 – 173110CBM-cenC 1Add
    BLAST
    Domaini212 – 318107CBM-cenC 2Add
    BLAST
    Domaini918 – 100689Ig-like 1Add
    BLAST
    Domaini1008 – 109790Ig-like 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni329 – 880552CatalyticAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal

    Phylogenomic databases

    OMAiWTFCLDD.

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    2.60.120.260. 2 hits.
    2.60.40.10. 3 hits.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR003305. CenC_carb-bd.
    IPR008979. Galactose-bd-like.
    IPR001701. Glyco_hydro_9.
    IPR018221. Glyco_hydro_9_AS.
    IPR004197. Glyco_hydro_9_Ig-like.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    [Graphical view]
    PfamiPF02018. CBM_4_9. 2 hits.
    PF02927. CelD_N. 1 hit.
    PF00759. Glyco_hydro_9. 1 hit.
    PF07679. I-set. 1 hit.
    [Graphical view]
    SMARTiSM00409. IG. 1 hit.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.
    SSF49785. SSF49785. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
    PS50835. IG_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P14090-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVSRRSSQAR GALTAVVATL ALALAGSGTA LAASPIGEGT FDDGPEGWVA     50
    YGTDGPLDTS TGALCVAVPA GSAQYGVGVV LNGVAIEEGT TYTLRYTATA 100
    STDVTVRALV GQNGAPYGTV LDTSPALTSE PRQVTETFTA SATYPATPAA 150
    DDPEGQIAFQ LGGFSADAWT FCLDDVALDS EVELLPHTSF AESLGPWSLY 200
    GTSEPVFADG RMCVDLPGGQ GNPWDAGLVY NGVPVGEGES YVLSFTASAT 250
    PDMPVRVLVG EGGGAYRTAF EQGSAPLTGE PATREYAFTS NLTFPPDGDA 300
    PGQVAFHLGK AGAYEFCISQ VSLTTSATPP PGYEPDTGPR VRVNQVGYLP 350
    FGPKRATLVT DAAEPVAWEL RDADGVVVAD GTSEPRGVEP SAAQAVHVLD 400
    FSDVTTQGAG YTLVADGETS RPFDIDGDLY QQLRYDALNY FYLARSGTEI 450
    EADVVGEEYA REAGHVGVAP NQGDTDVPCI GPRDYYDGWT CDYRLDVSGG 500
    WYDAGDHGKY VVNGGIAVGQ LLQTYERALH AGTADALADG TLDVPEHGND 550
    VPDVLDEARW ELEWMLSMIV PEGEYAGMVH HKVHDEGWTG LPLLPADDPQ 600
    ARSLHRPSTA ATLNLSAVAA QGARLLEPYD PQLAQTLLEA ARTTWAAAQE 650
    HPALYAPGEA GADGGGAYND SQVADEFYWA AAELYLTTGE DAFATAVTTS 700
    PLHTADVFTA DGFGWGSVAA LGRLDLATVP NELPGLDAVQ SSVVEGAQEY 750
    LAAQAGQGFG SLYSPPGGEY VWGSSSQVAN NLVVVATAYD LTGDERFRAA 800
    TLEGLDYLFG RNALNQSYVT GWGEVASHQQ HSRWFAHQLD PSLPSPPPGS 850
    LAGGPNSQAA TWDPTTKAAF PDGCAPSACY VDEIQAWSTN ELTVNWNSAL 900
    SWVASWVADQ GSAEPVPTAP VVTRQPVDAT VALGADATFT AEASGVPAPT 950
    VRWQVRAGRG WKDVAGATGT TLTVRATART DGTRYRAVFT NAAGSVESAV 1000
    VRLTVERAAP VVTQHPADVR ARVGTRAVFR AAADGYPTPC VVWQVRWGGG 1050
    SWRPIPWATS TTLSVPVTVL AAGTEYRAVF TNAVGTAATE PAELAVQRPR 1100
    S 1101
    Length:1,101
    Mass (Da):115,216
    Last modified:March 1, 1992 - v2
    Checksum:i1FBAD189CC5F8B5D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57858 Genomic DNA. Translation: CAA40993.1.
    CP002666 Genomic DNA. Translation: AEE45671.1.
    M29707 Genomic DNA. Translation: AAA23087.1. Different termination.
    M29708 Genomic DNA. Translation: AAA23088.1. Sequence problems.
    PIRiS15271.
    RefSeqiWP_013770697.1. NC_015514.1.
    YP_004453058.1. NC_015514.1.

    Genome annotation databases

    EnsemblBacteriaiAEE45671; AEE45671; Celf_1537.
    GeneIDi10592314.
    KEGGicfi:Celf_1537.
    PATRICi54613973. VBICelFim18861_1533.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57858 Genomic DNA. Translation: CAA40993.1 .
    CP002666 Genomic DNA. Translation: AEE45671.1 .
    M29707 Genomic DNA. Translation: AAA23087.1 . Different termination.
    M29708 Genomic DNA. Translation: AAA23088.1 . Sequence problems.
    PIRi S15271.
    RefSeqi WP_013770697.1. NC_015514.1.
    YP_004453058.1. NC_015514.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CX1 NMR - A 178-328 [» ]
    1GU3 X-ray 2.30 A 33-181 [» ]
    1ULO NMR - A 33-184 [» ]
    1ULP NMR - A 33-184 [» ]
    ProteinModelPortali P14090.
    SMRi P14090. Positions 33-328.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM4. Carbohydrate-Binding Module Family 4.
    GH9. Glycoside Hydrolase Family 9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AEE45671 ; AEE45671 ; Celf_1537 .
    GeneIDi 10592314.
    KEGGi cfi:Celf_1537.
    PATRICi 54613973. VBICelFim18861_1533.

    Phylogenomic databases

    OMAi WTFCLDD.

    Enzyme and pathway databases

    BioCyci CFIM590998:GJFK-1554-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P14090.

    Family and domain databases

    Gene3Di 1.50.10.10. 1 hit.
    2.60.120.260. 2 hits.
    2.60.40.10. 3 hits.
    InterProi IPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR003305. CenC_carb-bd.
    IPR008979. Galactose-bd-like.
    IPR001701. Glyco_hydro_9.
    IPR018221. Glyco_hydro_9_AS.
    IPR004197. Glyco_hydro_9_Ig-like.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    [Graphical view ]
    Pfami PF02018. CBM_4_9. 2 hits.
    PF02927. CelD_N. 1 hit.
    PF00759. Glyco_hydro_9. 1 hit.
    PF07679. I-set. 1 hit.
    [Graphical view ]
    SMARTi SM00409. IG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48208. SSF48208. 1 hit.
    SSF49785. SSF49785. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
    PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the endoglucanase C gene (cenC) of Cellulomonas fimi, its high-level expression in Escherichia coli, and characterization of its products."
      Coutinho J.B., Moser B., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.
      Mol. Microbiol. 5:1221-1233(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-42.
      Strain: ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547.
    2. "Complete sequence of Cellulomonas fimi ATCC 484."
      US DOE Joint Genome Institute
      Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P., Woyke T.
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547.
    3. "Purification and characterization of endoglucanase C of Cellulomonas fimi, cloning of the gene, and analysis of in vivo transcripts of the gene."
      Moser B., Gilkes N.R., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.
      Appl. Environ. Microbiol. 55:2480-2487(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64, PROTEIN SEQUENCE OF 625-641.
      Strain: ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547.
    4. "The binding of Cellulomonas fimi endoglucanase C (CenC) to cellulose and Sephadex is mediated by the N-terminal repeats."
      Coutinho J.B., Gilkes N.R., Warren R.A.J., Kilburn D.G., Miller R.C. Jr.
      Mol. Microbiol. 6:1243-1252(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS CELLULOSE BINDING.
    5. "Members of the immunoglobulin superfamily in bacteria."
      Bateman A., Eddy S.R., Chothia C.
      Protein Sci. 5:1939-1942(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS IG-LIKE.
    6. "Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy."
      Johnson P.E., Joshi M.D., Tomme P., Kilburn D.G., McIntosh L.P.
      Biochemistry 35:14381-14394(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 33-184.

    Entry informationi

    Entry nameiGUNC_CELFA
    AccessioniPrimary (citable) accession number: P14090
    Secondary accession number(s): F4H737
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 117 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

    3D-structure, Complete proteome, Direct protein sequencing, 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