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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: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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 Componenti: 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 – 443Combined sources
Beta strandi49 – 524Combined sources
Beta strandi62 – 687Combined sources
Beta strandi76 – 849Combined sources
Beta strandi91 – 10212Combined sources
Beta strandi107 – 1148Combined sources
Beta strandi119 – 1235Combined sources
Beta strandi132 – 1398Combined sources
Beta strandi155 – 1606Combined sources
Beta strandi169 – 18012Combined sources
Beta strandi184 – 1863Combined sources
Turni190 – 1923Combined sources
Beta strandi198 – 2036Combined sources
Beta strandi212 – 2154Combined sources
Beta strandi226 – 2305Combined sources
Beta strandi239 – 25113Combined sources
Beta strandi253 – 2608Combined sources
Beta strandi262 – 2654Combined sources
Beta strandi272 – 2776Combined sources
Beta strandi282 – 2898Combined sources
Beta strandi296 – 2994Combined sources
Beta strandi303 – 3075Combined sources
Beta strandi315 – 32410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

OMAiNYFYLAR.

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

        10         20         30         40         50
MVSRRSSQAR GALTAVVATL ALALAGSGTA LAASPIGEGT FDDGPEGWVA
60 70 80 90 100
YGTDGPLDTS TGALCVAVPA GSAQYGVGVV LNGVAIEEGT TYTLRYTATA
110 120 130 140 150
STDVTVRALV GQNGAPYGTV LDTSPALTSE PRQVTETFTA SATYPATPAA
160 170 180 190 200
DDPEGQIAFQ LGGFSADAWT FCLDDVALDS EVELLPHTSF AESLGPWSLY
210 220 230 240 250
GTSEPVFADG RMCVDLPGGQ GNPWDAGLVY NGVPVGEGES YVLSFTASAT
260 270 280 290 300
PDMPVRVLVG EGGGAYRTAF EQGSAPLTGE PATREYAFTS NLTFPPDGDA
310 320 330 340 350
PGQVAFHLGK AGAYEFCISQ VSLTTSATPP PGYEPDTGPR VRVNQVGYLP
360 370 380 390 400
FGPKRATLVT DAAEPVAWEL RDADGVVVAD GTSEPRGVEP SAAQAVHVLD
410 420 430 440 450
FSDVTTQGAG YTLVADGETS RPFDIDGDLY QQLRYDALNY FYLARSGTEI
460 470 480 490 500
EADVVGEEYA REAGHVGVAP NQGDTDVPCI GPRDYYDGWT CDYRLDVSGG
510 520 530 540 550
WYDAGDHGKY VVNGGIAVGQ LLQTYERALH AGTADALADG TLDVPEHGND
560 570 580 590 600
VPDVLDEARW ELEWMLSMIV PEGEYAGMVH HKVHDEGWTG LPLLPADDPQ
610 620 630 640 650
ARSLHRPSTA ATLNLSAVAA QGARLLEPYD PQLAQTLLEA ARTTWAAAQE
660 670 680 690 700
HPALYAPGEA GADGGGAYND SQVADEFYWA AAELYLTTGE DAFATAVTTS
710 720 730 740 750
PLHTADVFTA DGFGWGSVAA LGRLDLATVP NELPGLDAVQ SSVVEGAQEY
760 770 780 790 800
LAAQAGQGFG SLYSPPGGEY VWGSSSQVAN NLVVVATAYD LTGDERFRAA
810 820 830 840 850
TLEGLDYLFG RNALNQSYVT GWGEVASHQQ HSRWFAHQLD PSLPSPPPGS
860 870 880 890 900
LAGGPNSQAA TWDPTTKAAF PDGCAPSACY VDEIQAWSTN ELTVNWNSAL
910 920 930 940 950
SWVASWVADQ GSAEPVPTAP VVTRQPVDAT VALGADATFT AEASGVPAPT
960 970 980 990 1000
VRWQVRAGRG WKDVAGATGT TLTVRATART DGTRYRAVFT NAAGSVESAV
1010 1020 1030 1040 1050
VRLTVERAAP VVTQHPADVR ARVGTRAVFR AAADGYPTPC VVWQVRWGGG
1060 1070 1080 1090 1100
SWRPIPWATS TTLSVPVTVL AAGTEYRAVF TNAVGTAATE PAELAVQRPR

S
Length:1,101
Mass (Da):115,216
Last modified:March 1, 1992 - v2
Checksum:i1FBAD189CC5F8B5D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
KEGGicfi:Celf_1537.
PATRICi54613973. VBICelFim18861_1533.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

OMAiNYFYLAR.

Enzyme and pathway databases

BioCyciCFIM590998:GJFK-1554-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP14090.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 1, 2015
This is version 120 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.