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P14090 (GUNC_CELFA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoglucanase C

EC=3.2.1.4
Alternative name(s):
Cellulase C
Endo-1,4-beta-glucanase C
Gene names
Name:cenC
Ordered Locus Names:Celf_1537
OrganismCellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547) [Complete proteome] [HAMAP]
Taxonomic identifier590998 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

Protein attributes

Sequence length1101 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 9 (cellulase E) family.

Contains 2 CBM-cenC (cenC-type cellulose-binding) domains.

Contains 2 Ig-like (immunoglobulin-like) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Ref.1
Chain33 – 11011069Endoglucanase C
PRO_0000007946

Regions

Domain64 – 173110CBM-cenC 1
Domain212 – 318107CBM-cenC 2
Domain918 – 100689Ig-like 1
Domain1008 – 109790Ig-like 2
Region329 – 880552Catalytic

Sites

Active site8311 By similarity
Active site8821 By similarity
Active site8911 By similarity

Secondary structure

............................................... 1101
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14090 [UniParc].

Last modified March 1, 1992. Version 2.
Checksum: 1FBAD189CC5F8B5D

FASTA1,101115,216
        10         20         30         40         50         60 
MVSRRSSQAR GALTAVVATL ALALAGSGTA LAASPIGEGT FDDGPEGWVA YGTDGPLDTS 

        70         80         90        100        110        120 
TGALCVAVPA GSAQYGVGVV LNGVAIEEGT TYTLRYTATA STDVTVRALV GQNGAPYGTV 

       130        140        150        160        170        180 
LDTSPALTSE PRQVTETFTA SATYPATPAA DDPEGQIAFQ LGGFSADAWT FCLDDVALDS 

       190        200        210        220        230        240 
EVELLPHTSF AESLGPWSLY GTSEPVFADG RMCVDLPGGQ GNPWDAGLVY NGVPVGEGES 

       250        260        270        280        290        300 
YVLSFTASAT PDMPVRVLVG EGGGAYRTAF EQGSAPLTGE PATREYAFTS NLTFPPDGDA 

       310        320        330        340        350        360 
PGQVAFHLGK AGAYEFCISQ VSLTTSATPP PGYEPDTGPR VRVNQVGYLP FGPKRATLVT 

       370        380        390        400        410        420 
DAAEPVAWEL RDADGVVVAD GTSEPRGVEP SAAQAVHVLD FSDVTTQGAG YTLVADGETS 

       430        440        450        460        470        480 
RPFDIDGDLY QQLRYDALNY FYLARSGTEI EADVVGEEYA REAGHVGVAP NQGDTDVPCI 

       490        500        510        520        530        540 
GPRDYYDGWT CDYRLDVSGG WYDAGDHGKY VVNGGIAVGQ LLQTYERALH AGTADALADG 

       550        560        570        580        590        600 
TLDVPEHGND VPDVLDEARW ELEWMLSMIV PEGEYAGMVH HKVHDEGWTG LPLLPADDPQ 

       610        620        630        640        650        660 
ARSLHRPSTA ATLNLSAVAA QGARLLEPYD PQLAQTLLEA ARTTWAAAQE HPALYAPGEA 

       670        680        690        700        710        720 
GADGGGAYND SQVADEFYWA AAELYLTTGE DAFATAVTTS PLHTADVFTA DGFGWGSVAA 

       730        740        750        760        770        780 
LGRLDLATVP NELPGLDAVQ SSVVEGAQEY LAAQAGQGFG SLYSPPGGEY VWGSSSQVAN 

       790        800        810        820        830        840 
NLVVVATAYD LTGDERFRAA TLEGLDYLFG RNALNQSYVT GWGEVASHQQ HSRWFAHQLD 

       850        860        870        880        890        900 
PSLPSPPPGS LAGGPNSQAA TWDPTTKAAF PDGCAPSACY VDEIQAWSTN ELTVNWNSAL 

       910        920        930        940        950        960 
SWVASWVADQ GSAEPVPTAP VVTRQPVDAT VALGADATFT AEASGVPAPT VRWQVRAGRG 

       970        980        990       1000       1010       1020 
WKDVAGATGT TLTVRATART DGTRYRAVFT NAAGSVESAV VRLTVERAAP VVTQHPADVR 

      1030       1040       1050       1060       1070       1080 
ARVGTRAVFR AAADGYPTPC VVWQVRWGGG SWRPIPWATS TTLSVPVTVL AAGTEYRAVF 

      1090       1100 
TNAVGTAATE PAELAVQRPR S 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS15271.
RefSeqYP_004453058.1. NC_015514.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CX1NMR-A178-328[»]
1GU3X-ray2.30A33-181[»]
1ULONMR-A33-184[»]
1ULPNMR-A33-184[»]
ProteinModelPortalP14090.
SMRP14090. Positions 33-328.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM4. Carbohydrate-Binding Module Family 4.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEE45671; AEE45671; Celf_1537.
GeneID10592314.
KEGGcfi:Celf_1537.
PATRIC54613973. VBICelFim18861_1533.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAWTFCLDD.

Enzyme and pathway databases

BioCycCFIM590998:GJFK-1554-MONOMER.

Family and domain databases

Gene3D1.50.10.10. 1 hit.
2.60.120.260. 2 hits.
2.60.40.10. 3 hits.
InterProIPR008928. 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]
PfamPF02018. CBM_4_9. 2 hits.
PF02927. CelD_N. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
PF07679. I-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
SSF49785. SSF49785. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEPS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14090.

Entry information

Entry nameGUNC_CELFA
AccessionPrimary (citable) accession number: P14090
Secondary accession number(s): F4H737
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: March 1, 1992
Last modified: July 9, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries