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P50400 (GUND_CELFI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Endoglucanase D

EC=3.2.1.4
Alternative name(s):
Cellulase D
Endo-1,4-beta-glucanase D
Gene names
Name:cenD
OrganismCellulomonas fimi
Taxonomic identifier1708 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

Protein attributes

Sequence length747 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Pathway

Glycan metabolism; cellulose degradation.

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Contains 1 CBM2 (carbohydrate binding type-2) domain.

Contains 2 fibronectin type-III domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939 Potential
Chain40 – 747708Endoglucanase D
PRO_0000007843

Regions

Domain454 – 54087Fibronectin type-III 1
Domain550 – 63586Fibronectin type-III 2
Domain638 – 747110CBM2

Sites

Active site2081Proton donor By similarity
Active site3491Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
P50400 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: BD15473C9D8B42BD

FASTA74778,937
        10         20         30         40         50         60 
MHSASRTRAR TRVRTAVSGL LAATVLAAPL TLVAAPAQAA TGDDWLHVEG NTIVDSTGKE 

        70         80         90        100        110        120 
AILSGVNWFG FNASERVFHG LWSGNITQIT QQMAQRGINV VRVPVSTQLL LEWKAGTFLK 

       130        140        150        160        170        180 
PNVNTYANPE LEGKNSLQIF EYWLTLCQKY GIKVFLDVHS AEADNSGHVY NMWWKGDITT 

       190        200        210        220        230        240 
EDVYEGWEWA ATRWKDDDTI VGADIKNEPH GTQGSTERAK WDGTTDKDNF KHFAETASKK 

       250        260        270        280        290        300 
ILAINPNWLV FVEGVEIYPK PGVPWTSTGL TDYYGTWWGG NLRGVRDHPI DLGAHQDQLV 

       310        320        330        340        350        360 
YSPHDYGPLV FDQKWFQKDF DKASLTADVW GPNWLFIHDE DIAPLLIGEW GGRLGQDPRQ 

       370        380        390        400        410        420 
DKWMAALRDL VAERRLSQTF WVLNPNSGDT GGLLLDDWKT WDEVKYSTML EPTLWKHGGK 

       430        440        450        460        470        480 
YVGLDHQVPL GGVGSTTGTS ISQVGGGTPD TTAPTAPTGL RAGTPTASTV PLTWSASTDT 

       490        500        510        520        530        540 
GGSGVAGYEV YRGTTLVGTT TATSYTVTGL AADSAYTFSV RAKDGAGNTS AASAAVTART 

       550        560        570        580        590        600 
AAGGGDVTAP SVPTGLTAGT PTATSVPLTW TASTDTGGSG VTGYEVYRGS TLVARPTGTS 

       610        620        630        640        650        660 
HTVTGLSAAT AYTFTVRAVD AAGNVSAASA PVGVTTAPDP TTGSCAVTYT ANGWSGGFTA 

       670        680        690        700        710        720 
AVTLTNTGTT ALSGWTLGFA FPSGQTLTQG WSARWAQSGS SVTATNEAWN AVLAPGASVE 

       730        740 
IGFSGTHTGT NTAPATFTVG GATCTTR 

« Hide

References

[1]"Cellulose-binding polypeptides from Cellulomonas fimi: endoglucanase D (CenD), a family A beta-1,4-glucanase."
Meinke A., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
J. Bacteriol. 175:1910-1918(1993) [PubMed: 8458833] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02544 Genomic DNA. Translation: AAA23089.1.
PIRB47093.

3D structure databases

ProteinModelPortalP50400.
ModBaseSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR003961. Fibronectin_type3.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
Gene3DG3DSA:2.60.40.290. CBD_carb_bd. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 2 hits.
PfamPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
PF00041. fn3. 2 hits.
[Graphical view]
SMARTSM00637. CBD_II. 1 hit.
SM00060. FN3. 2 hits.
[Graphical view]
SUPFAMSSF49384. Cellul_bind. 1 hit.
SSF49265. FN_III-like. 2 hits.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS50853. FN3. 2 hits.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUND_CELFI
AccessionPrimary (citable) accession number: P50400
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families