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P37699

- GUNC_CLOCE

UniProt

P37699 - GUNC_CLOCE

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Protein
Endoglucanase C
Gene
celCCC, Ccel_0730
Organism
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Status
Reviewed - Annotation score: 5 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei99 – 991Proton donor By similarity
Active sitei155 – 1551Nucleophile Reviewed prediction

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-UniPathway
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 lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000001349: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 32321 Publication
Add
BLAST
Chaini33 – 460428Endoglucanase C
PRO_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.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni406 – 460552 X 24 AA approximate repeats
Add
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

MIKGSSLKRF KSLVMAAIFS VSIISTAIAS SAADQIPFPY DAKYPNGAYS    50
CLADSQSIGN NLVRSEWEQW KSAHITSNGA RGYKRVQRDA STNYDTVSEG 100
LGYGLLLSVY FGEQQLFDDL YRYVKVFLNS NGLMSWRIDS SGNIMGKDSI 150
GAATDADEDI AVSLVFAHKK WGTSGGFNYQ TEAKNYINNI YNKMVEPGTY 200
VIKAGDTWGG SNVTNPSYFA PAWYRIFADF TGNSGWINVA NKCYEIADKA 250
RNSNTGLVPD WCTANGTPAS GQGFDFYYDA IRYQWRAAID YSWYGTAKAK 300
THCDAISNFF KNIGYANIKD GYTISGSQIS SNHTATFVSC AAAAAMTGTD 350
TTYAKNIYNE CVKVKDSGNY TYFGNTLRMM VLLYTTGNFP NLYTYNSQPK 400
PDLKGDVNND GAIDALDIAA LKKAILTQTT SNISLTNADM NNDGNIDAID 450
FAQLKVKLLN 460
Length:460
Mass (Da):50,483
Last modified:May 26, 2009 - v2
Checksum:i2F31E1F6CB41504F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911S → T in AAA73867. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi7309584.
KEGGicce:Ccel_0730.
PATRICi19432257. VBICloCel57783_0755.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87018 Genomic DNA. Translation: AAA73867.1 .
CP001348 Genomic DNA. Translation: ACL75109.1 .
PIRi JC1299.
RefSeqi WP_015924276.1. NC_011898.1.
YP_002505089.1. NC_011898.1.

3D structure databases

ProteinModelPortali P37699.
SMRi P37699. Positions 39-391.
ModBasei Search...

Protein-protein interaction databases

STRINGi 394503.Ccel_0730.

Protein family/group databases

CAZyi GH8. Glycoside Hydrolase Family 8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL75109 ; ACL75109 ; Ccel_0730 .
GeneIDi 7309584.
KEGGi cce:Ccel_0730.
PATRICi 19432257. VBICloCel57783_0755.

Phylogenomic databases

eggNOGi COG3405.
HOGENOMi HOG000069581.
OMAi GNFPNLY.
OrthoDBi EOG67Q9BX.

Enzyme and pathway databases

UniPathwayi UPA00696 .
BioCyci CCEL394503:GJET-751-MONOMER.

Family and domain databases

Gene3Di 1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
InterProi IPR008928. 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 ]
Pfami PF00404. Dockerin_1. 2 hits.
PF01270. Glyco_hydro_8. 1 hit.
[Graphical view ]
PRINTSi PR00735. GLHYDRLASE8.
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS00812. GLYCOSYL_HYDROL_F8. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 96 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

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

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