Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endoglucanase C

Gene

celCCC

Organism
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
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.

Pathway: cellulose degradation

This protein is involved in the pathway cellulose degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway cellulose degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei99 – 991Proton donorBy similarity
Active sitei155 – 1551NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciCCEL394503:GJET-751-MONOMER.
UniPathwayiUPA00696.

Protein family/group databases

CAZyiGH8. Glycoside Hydrolase Family 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase C (EC:3.2.1.4)
Alternative name(s):
Cellulase C
EGCCC
Endo-1,4-beta-glucanase C
Gene namesi
Name:celCCC
Ordered Locus Names:Ccel_0730
OrganismiClostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Taxonomic identifieri394503 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
ProteomesiUP000001349 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 32321 PublicationAdd
BLAST
Chaini33 – 460428Endoglucanase CPRO_0000007936Add
BLAST

Post-translational modificationi

There are two forms of the cellulase. The shorter form lacks probably the C-terminal reiterated domains.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi394503.Ccel_0730.

Structurei

3D structure databases

ProteinModelPortaliP37699.
SMRiP37699. Positions 39-391.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati406 – 429241Add
BLAST
Repeati439 – 460222Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni406 – 460552 X 24 AA approximate repeatsAdd
BLAST

Domaini

A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG3405.
HOGENOMiHOG000069581.
OMAiGNFPNLY.
OrthoDBiEOG67Q9BX.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR002037. Glyco_hydro_8.
IPR019834. Glyco_hydro_8_CS.
[Graphical view]
PfamiPF00404. Dockerin_1. 2 hits.
PF01270. Glyco_hydro_8. 1 hit.
[Graphical view]
PRINTSiPR00735. GLHYDRLASE8.
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS00812. GLYCOSYL_HYDROL_F8. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P37699-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKGSSLKRF KSLVMAAIFS VSIISTAIAS SAADQIPFPY DAKYPNGAYS
60 70 80 90 100
CLADSQSIGN NLVRSEWEQW KSAHITSNGA RGYKRVQRDA STNYDTVSEG
110 120 130 140 150
LGYGLLLSVY FGEQQLFDDL YRYVKVFLNS NGLMSWRIDS SGNIMGKDSI
160 170 180 190 200
GAATDADEDI AVSLVFAHKK WGTSGGFNYQ TEAKNYINNI YNKMVEPGTY
210 220 230 240 250
VIKAGDTWGG SNVTNPSYFA PAWYRIFADF TGNSGWINVA NKCYEIADKA
260 270 280 290 300
RNSNTGLVPD WCTANGTPAS GQGFDFYYDA IRYQWRAAID YSWYGTAKAK
310 320 330 340 350
THCDAISNFF KNIGYANIKD GYTISGSQIS SNHTATFVSC AAAAAMTGTD
360 370 380 390 400
TTYAKNIYNE CVKVKDSGNY TYFGNTLRMM VLLYTTGNFP NLYTYNSQPK
410 420 430 440 450
PDLKGDVNND GAIDALDIAA LKKAILTQTT SNISLTNADM NNDGNIDAID
460
FAQLKVKLLN
Length:460
Mass (Da):50,483
Last modified:May 26, 2009 - v2
Checksum:i2F31E1F6CB41504F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911S → T in AAA73867 (PubMed:1398087).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87018 Genomic DNA. Translation: AAA73867.1.
CP001348 Genomic DNA. Translation: ACL75109.1.
PIRiJC1299.
RefSeqiWP_015924276.1. NC_011898.1.
YP_002505089.1. NC_011898.1.

Genome annotation databases

EnsemblBacteriaiACL75109; ACL75109; Ccel_0730.
KEGGicce:Ccel_0730.
PATRICi19432257. VBICloCel57783_0755.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87018 Genomic DNA. Translation: AAA73867.1.
CP001348 Genomic DNA. Translation: ACL75109.1.
PIRiJC1299.
RefSeqiWP_015924276.1. NC_011898.1.
YP_002505089.1. NC_011898.1.

3D structure databases

ProteinModelPortaliP37699.
SMRiP37699. Positions 39-391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi394503.Ccel_0730.

Protein family/group databases

CAZyiGH8. Glycoside Hydrolase Family 8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACL75109; ACL75109; Ccel_0730.
KEGGicce:Ccel_0730.
PATRICi19432257. VBICloCel57783_0755.

Phylogenomic databases

eggNOGiCOG3405.
HOGENOMiHOG000069581.
OMAiGNFPNLY.
OrthoDBiEOG67Q9BX.

Enzyme and pathway databases

UniPathwayiUPA00696.
BioCyciCCEL394503:GJET-751-MONOMER.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR002037. Glyco_hydro_8.
IPR019834. Glyco_hydro_8_CS.
[Graphical view]
PfamiPF00404. Dockerin_1. 2 hits.
PF01270. Glyco_hydro_8. 1 hit.
[Graphical view]
PRINTSiPR00735. GLHYDRLASE8.
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS00812. GLYCOSYL_HYDROL_F8. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a gene cluster encoding cellulases from Clostridium cellulolyticum."
    Bagnara-Tardif C., Gaudin C., Belaich A., Hoest P., Citard T., Belaich J.-P.
    Gene 119:17-28(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.
  3. "Purification and characterization of endoglucanase C from Clostridium cellulolyticum. Catalytic comparison with endoglucanase A."
    Fierobe H.-P., Bagnara-Tardif C., Gaudin C., Guerlesquin F., Sauve P., Belaich A., Belaich J.-P.
    Eur. J. Biochem. 217:557-565(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 33-37, CHARACTERIZATION.
    Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.

Entry informationi

Entry nameiGUNC_CLOCE
AccessioniPrimary (citable) accession number: P37699
Secondary accession number(s): B8I7V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 26, 2009
Last modified: June 24, 2015
This is version 103 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.