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P25472

- GUND_CLOCE

UniProt

P25472 - GUND_CLOCE

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Protein

Endoglucanase D

Gene

celCCD

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 donorBy similarity
Active sitei264 – 2641NucleophileBy 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 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 584560Endoglucanase DPRO_0000007846Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi394503.Ccel_0840.

Structurei

3D structure databases

ProteinModelPortaliP25472.
SMRiP25472. Positions 354-523.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini354 – 584231CBM11Add
BLAST
Repeati530 – 552231Add
BLAST
Repeati562 – 584232Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 328304CatalyticBy similarityAdd
BLAST
Regioni530 – 584552 X 24 AA approximate repeatsAdd
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

        10         20         30         40         50
MKKILALIIS CSIIMSFLPM SVYGAINSQD MVKKMGIGMN LGNTFDAPTE
60 70 80 90 100
GSWSKAAQEY YFDDFKQAGF KHVRIPIRWD QHTLANSPYT VDSNFLNRIE
110 120 130 140 150
TVIDWSLSRG FVTVINSHHD TWLMDNYSQN IGRFEKIWEQ IAQRFKGKSE
160 170 180 190 200
NLVFEILNEP HGNITDSQIN DMNKRILNII RKTNPTRNVI IGAGYWNSYN
210 220 230 240 250
SLSQLEIPND PNLIATFHYY DPYSFTHQWQ GTWGTKNDMD AIAMVFNHVK
260 270 280 290 300
KWSDKNNIPV YLGEYGVMGH SDRTSAVKWF DFVSDQAISH GFSCGAWDNG
310 320 330 340 350
VFGSVDNDMA FYNRDTRQFD KEILNAILTT GTTYDWTPPT ETNPDPPRTP
360 370 380 390 400
ATPAYGEQLI EDFEGAMQWA AYSGVDATAS CKISSGKSNN GLEITYAGSS
410 420 430 440 450
NGYWGVVDNE HRNQDWEKWQ KISFDIKSSN TNEVRLLIAE QSKIEGEDGE
460 470 480 490 500
HWTYVIKPST SWTTIEIPFS SFTKRMDYQP PAQDGSETFD LYKVGSLHFM
510 520 530 540 550
YSNSNSGTLN IDNIKLIGLP EEQIGGKIGD VNEDGNIDAI DFALLKKYLL
560 570 580
DSSISINKVN ADINLDGDIN AIDFAKLKMM LLGD
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: October 1, 2014
This is version 104 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, 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