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P25472

- GUND_CLOCE

UniProt

P25472 - GUND_CLOCE

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Protein
Endoglucanase D
Gene
celCCD, Ccel_0840
Organism
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

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 sitei159 – 1591Proton donor By similarity
Active sitei264 – 2641Nucleophile By similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC

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-865-MONOMER.
UniPathwayiUPA00696.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase D (EC:3.2.1.4)
Alternative name(s):
Cellulase D
EGCCD
Endo-1,4-beta-glucanase D
Gene namesi
Name:celCCD
Ordered Locus Names:Ccel_0840
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 – 2424 Reviewed prediction
Add
BLAST
Chaini25 – 584560Endoglucanase D
PRO_0000007846Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi394503.Ccel_0840.

Structurei

3D structure databases

ProteinModelPortaliP25472.
SMRiP25472. Positions 354-523.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini354 – 584231CBM11
Add
BLAST
Repeati530 – 552231
Add
BLAST
Repeati562 – 584232
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 328304Catalytic By similarity
Add
BLAST
Regioni530 – 584552 X 24 AA approximate repeats
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi329 – 35325Pro/Thr-rich (linker)
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

eggNOGiCOG2730.
KOiK01179.
OMAiDATASCK.
OrthoDBiEOG66F040.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR005087. CBM_fam11.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF03425. CBM_11. 1 hit.
PF00150. Cellulase. 1 hit.
PF00404. Dockerin_1. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P25472-1 [UniParc]FASTAAdd to Basket

« Hide

MKKILALIIS CSIIMSFLPM SVYGAINSQD MVKKMGIGMN LGNTFDAPTE    50
GSWSKAAQEY YFDDFKQAGF KHVRIPIRWD QHTLANSPYT VDSNFLNRIE 100
TVIDWSLSRG FVTVINSHHD TWLMDNYSQN IGRFEKIWEQ IAQRFKGKSE 150
NLVFEILNEP HGNITDSQIN DMNKRILNII RKTNPTRNVI IGAGYWNSYN 200
SLSQLEIPND PNLIATFHYY DPYSFTHQWQ GTWGTKNDMD AIAMVFNHVK 250
KWSDKNNIPV YLGEYGVMGH SDRTSAVKWF DFVSDQAISH GFSCGAWDNG 300
VFGSVDNDMA FYNRDTRQFD KEILNAILTT GTTYDWTPPT ETNPDPPRTP 350
ATPAYGEQLI EDFEGAMQWA AYSGVDATAS CKISSGKSNN GLEITYAGSS 400
NGYWGVVDNE HRNQDWEKWQ KISFDIKSSN TNEVRLLIAE QSKIEGEDGE 450
HWTYVIKPST SWTTIEIPFS SFTKRMDYQP PAQDGSETFD LYKVGSLHFM 500
YSNSNSGTLN IDNIKLIGLP EEQIGGKIGD VNEDGNIDAI DFALLKKYLL 550
DSSISINKVN ADINLDGDIN AIDFAKLKMM LLGD 584
Length:584
Mass (Da):66,062
Last modified:May 1, 1992 - v1
Checksum:i0FC41257E81322C3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90341 Genomic DNA. Translation: BAA14354.1.
CP001348 Genomic DNA. Translation: ACL75216.1.
RefSeqiWP_015924376.1. NC_011898.1.
YP_002505196.1. NC_011898.1.

Genome annotation databases

EnsemblBacteriaiACL75216; ACL75216; Ccel_0840.
GeneIDi7309687.
KEGGicce:Ccel_0840.
PATRICi19432493. VBICloCel57783_0870.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90341 Genomic DNA. Translation: BAA14354.1 .
CP001348 Genomic DNA. Translation: ACL75216.1 .
RefSeqi WP_015924376.1. NC_011898.1.
YP_002505196.1. NC_011898.1.

3D structure databases

ProteinModelPortali P25472.
SMRi P25472. Positions 354-523.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 394503.Ccel_0840.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL75216 ; ACL75216 ; Ccel_0840 .
GeneIDi 7309687.
KEGGi cce:Ccel_0840.
PATRICi 19432493. VBICloCel57783_0870.

Phylogenomic databases

eggNOGi COG2730.
KOi K01179.
OMAi DATASCK.
OrthoDBi EOG66F040.

Enzyme and pathway databases

UniPathwayi UPA00696 .
BioCyci CCEL394503:GJET-865-MONOMER.

Family and domain databases

Gene3Di 1.10.1330.10. 1 hit.
2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR005087. CBM_fam11.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF03425. CBM_11. 1 hit.
PF00150. Cellulase. 1 hit.
PF00404. Dockerin_1. 1 hit.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence analysis of the endoglucanase-encoding gene, celCCD, of Clostridium cellulolyticum."
    Shima S., Igarashi Y., Kodama T.
    Gene 104:33-38(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.

Entry informationi

Entry nameiGUND_CLOCE
AccessioniPrimary (citable) accession number: P25472
Secondary accession number(s): B8I8I3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: September 3, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete 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

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