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P46237 (GUNC_FUSOX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoglucanase type C
EC=3.2.1.4
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Endoglucanase I
Short name=EG I
OrganismFusarium oxysporum (Panama disease fungus)
Taxonomic identifier5507 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › mitosporic Nectriaceae › Fusarium › Fusarium oxysporum species complex

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 7 (cellulase C) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 429411Endoglucanase type C
PRO_0000007912

Sites

Active site2151Nucleophile By similarity
Active site2201Proton donor By similarity

Amino acid modifications

Modified residue191Pyrrolidone carboxylic acid
Glycosylation741N-linked (GlcNAc...)
Glycosylation2651N-linked (GlcNAc...)
Glycosylation3181N-linked (GlcNAc...)
Disulfide bond36 ↔ 42
Disulfide bond66 ↔ 88
Disulfide bond78 ↔ 84
Disulfide bond156 ↔ 383
Disulfide bond190 ↔ 213
Disulfide bond194 ↔ 212
Disulfide bond233 ↔ 252
Disulfide bond241 ↔ 246
Disulfide bond257 ↔ 333

Secondary structure

1 ............................................................................... 429
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46237 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: FAE8A880B1F880F9

FASTA42946,445
        10         20         30         40         50         60 
MKSLSLILSA LAVQVAVAQT PDKAKEQHPK LETYRCTKAS GCKKQTNYIV ADAGIHGIRQ 

        70         80         90        100        110        120 
KNGAGCGDWG QKPNATACPD EASCAKNCIL SGMDSNAYKN AGITTSGNKL RLQQLINNQL 

       130        140        150        160        170        180 
VSPRVYLLEE NKKKYEMLHL TGTEFSFDVE MEKLPCGMNG ALYLSEMPQD GGKSTSRNSK 

       190        200        210        220        230        240 
AGAYYGAGYC DAQCYVTPFI NGVGNIKGQG VCCNELDIWE ANSRATHIAP HPCSKPGLYG 

       250        260        270        280        290        300 
CTGDECGSSG ICDKAGCGWN HNRINVTDFY GRGKQYKVDS TRKFTVTSQF VANKQGDLIE 

       310        320        330        340        350        360 
LHRHYIQDNK VIESAVVNIS GPPKINFIND KYCAATGANE YMRLGGTKQM GDAMSRGMVL 

       370        380        390        400        410        420 
AMSVWWSEGD FMAWLDQGVA GPCDATEGDP KNIVKVQPNP EVTFSNIRIG EIGSTSSVKA 


PAYPGPHRL

« Hide

References

[1]"The use of conserved cellulase family-specific sequences to clone cellulase homologue cDNAs from Fusarium oxysporum."
Sheppard P.O., Grant F.J., Oort P.J., Sprecher C.A., Foster D.C., Hagen F.S., Upshall A., McKnight G.L., O'Hara P.J.
Gene 150:163-167(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group."
Sulzenbacher G., Driguez H., Henrissat B., Schuelein M., Davies G.J.
Biochemistry 35:15280-15287(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[3]"Structure of the endoglucanase I from Fusarium oxysporum: native, cellobiose, and 3,4-epoxybutyl beta-D-cellobioside-inhibited forms, at 2.3-A resolution."
Sulzenbacher G., Schuelein M., Davies G.J.
Biochemistry 36:5902-5911(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L29378 mRNA. Translation: AAA65586.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OVWX-ray2.70A/B/C/D20-416[»]
2OVWX-ray2.30A/B/C/D20-429[»]
3OVWX-ray2.30A/B20-429[»]
4OVWX-ray2.30A/B20-429[»]
ProteinModelPortalP46237.
SMRP46237. Positions 19-418.
ModBaseSearch...

Protein family/group databases

CAZyGH7. Glycoside Hydrolase Family 7.
mycoCLAPEGL7A_FUSOX.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.70.100.10. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSPR00734. GLHYDRLASE7.
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP46237.

Entry information

Entry nameGUNC_FUSOX
AccessionPrimary (citable) accession number: P46237
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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