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P28622 (GUN4_BACS5) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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 4

EC=3.2.1.4
Alternative name(s):
Cellulase 4
EG-IV
Endo-1,4-beta-glucanase 4
OrganismBacillus sp. (strain KSM-522)
Taxonomic identifier120046 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length636 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.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 9 (cellulase E) family.

Contains 1 CBM3 (carbohydrate binding type-3) domain.

Caution

Was originally (Ref.2) thought to originate from Clostridium cellulovorans and was termed endoglucanase C (engC).

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cellulose binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 636611Endoglucanase 4
PRO_0000007952

Regions

Domain478 – 635158CBM3

Sites

Active site4001 By similarity
Active site4381 By similarity
Active site4471 By similarity

Experimental info

Sequence conflict530 – 5345AKGFT → CEGIH Ref.2

Sequences

Sequence LengthMass (Da)Tools
P28622 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 76718BF57A8EF6A2

FASTA63672,245
        10         20         30         40         50         60 
MTRRWSFLVQ CFTFKKKEGV RSRYMSDYNY VEVLQKSILF YEAQRSGKLP ESNRLNWRGD 

        70         80         90        100        110        120 
SGLEDGKDVG HDLTGGWYDA GDHVKFGLPM AYSAAVLAWT VYEYREAYEE AELLDDMLDQ 

       130        140        150        160        170        180 
IKWATDYFLK AHTGPNEFWA QVGDGNADHG WWGPAEVMPM NRPAFKIDEH CPGTEVAAQT 

       190        200        210        220        230        240 
AAALAAGSII FKETDAPYAA KLLTHAKQLY AFADQYRGEY TDCVTNAQPF YNSWSGYIDE 

       250        260        270        280        290        300 
LIWGGIWLYL ATNDQTYLNK ALKAVEEWPK DWDYTFTMSW DNTFFLSQIL LARITKEKRF 

       310        320        330        340        350        360 
IESTERNLDY WSTGFVQNGK VERITYTPGG LAWLDQWGSL RYTANAAFLA FVYADWVSDQ 

       370        380        390        400        410        420 
EKKNRYQTFA IRQTHYMLGD NPQNRSYVVG FGKNPPMHPH HRTAHGSWSN QLTTPSSHRH 

       430        440        450        460        470        480 
TLYGPLVGGP NRQDQYTDDI SDYVSNEVAT DYNAAFTGNG AAVWSGQSKL PNFPPKEKVE 

       490        500        510        520        530        540 
DEFFVEAAVM SNDTTSTQIK AILYNRSGWP ARSSQSLSFR YYVNLSEIFA KGFTDKDIQV 

       550        560        570        580        590        600 
TAVYNEGASL SPLTVYDASS HIYFTEIDFT GVAIFPGGES LHKKEIQFRL SAPNGANIWD 

       610        620        630 
ASNDYSFQGL TSNMQKTARI PVFDQGDLVF GTLPNK 

« Hide

References

[1]"Amino acid sequence and stereoselective hydrolytic reaction of an endo-1,4-beta-glucanase from a Bacillus strain."
Hitomi J., Hatada Y., Kawaminami S., Kawai S., Ito S.
Biosci. Biotechnol. Biochem. 61:2004-2009(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning of Clostridium cellulovorans endo-1,4-beta-glucanase genes."
Shoseyov O., Foong F., Hamamoto T., Doi R.H.
Biochem. Biophys. Res. Commun. 169:667-672(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-534.
[3]Doi R.H.
Unpublished observations (JAN-2000)
Cited for: SHOWS THAT SEQUENCE DID NOT ORIGINATE FROM C.CELLULOVORANS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB004098 Genomic DNA. Translation: BAA24918.1.
PIRJC5874.

3D structure databases

ProteinModelPortalP28622.
SMRP28622. Positions 27-634.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Proteomic databases

PRIDEP28622.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.50.10.10. 1 hit.
2.60.40.710. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view]
PfamPF00942. CBM_3. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SMARTSM01067. CBM_3. 1 hit.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
SSF49384. SSF49384. 1 hit.
PROSITEPS51172. CBM3. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN4_BACS5
AccessionPrimary (citable) accession number: P28622
Secondary accession number(s): O50589
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: May 30, 2000
Last modified: October 16, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries