Skip Header

Contribute Send feedback
Read comments (?) or add your own

P19424 (GUN_BACS6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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
EC=3.2.1.4
Alternative name(s):
Alkaline cellulase
Endo-1,4-beta-glucanase
OrganismBacillus sp. (strain KSM-635)
Taxonomic identifier1415 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length941 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 5 (cellulase A) family.

Contains 3 SLH (S-layer homology) domains.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
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 – 2929
Chain30 – 941912Endoglucanase
PRO_0000007838

Regions

Domain37 – 9458SLH 1
Domain95 – 15864SLH 2
Domain161 – 22464SLH 3

Sites

Active site3731Proton donor
Active site4851Nucleophile

Secondary structure

1 .............................................................. 941
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19424 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: BEA2AC3B169BFADA

FASTA941104,628
        10         20         30         40         50         60 
MKIKQIKQSL SLLLIITLIM SLFVPMASAN TNESKSNAFP FSDVKKTSWS FPYIKDLYEQ 

        70         80         90        100        110        120 
EVITGTSATT FSPTDSVTRA QFTVMLTRGL GLEASSKDYP FKDRKNWAYK EIQAAYEAGI 

       130        140        150        160        170        180 
VTGKTNGEFA PNENITREQM AAMAVRAYEY LENELSLPEE QREYNDSSSI STFAQDAVQK 

       190        200        210        220        230        240 
AYVLELMEGN TDGYFQPKRN STREQSAKVI STLLWKVASH DYLYHTEAVK SPSEAGALQL 

       250        260        270        280        290        300 
VELNGQLTLA GEDGTPVQLR GMSTHGLQWF GEIVNENAFV ALSNDWGSNM IRLAMYIGEN 

       310        320        330        340        350        360 
GYATNPEVKD LVYEGIELAF EHDMYVIVDW HVHAPGDPRA DVYSGAYDFF EEIADHYKDH 

       370        380        390        400        410        420 
PKNHYIIWEL ANEPSPNNNG GPGLTNDEKG WEAVKEYAEP IVEMLREKGD NMILVGNPNW 

       430        440        450        460        470        480 
SQRPDLSADN PIDAENIMYS VHFYTGSHGA SHIGYPEGTP SSERSNVMAN VRYALDNGVA 

       490        500        510        520        530        540 
VFATEWGTSQ ANGDGGPYFD EADVWLNFLN KHNISWANWS LTNKNEISGA FTPFELGRTD 

       550        560        570        580        590        600 
ATDLDPGANQ VWAPEELSLS GEYVRARIKG IEYTPIDRTK FTKLVWDFND GTTQGFQVNG 

       610        620        630        640        650        660 
DSPNKESITL SNNNDALQIE GLNVSNDISE GNYWDNVRLS ADGWSENVDI LGATELTIDV 

       670        680        690        700        710        720 
IVEEPTTVSI AAIPQGPAAG WANPTRAIKV TEDDFESFGD GYKALVTITS EDSPSLETIA 

       730        740        750        760        770        780 
TSPEDNTMSN IILFVGTEDA DVISLDNITV SGTEIEIEVI HDEKGTATLP STFEDGTRQG 

       790        800        810        820        830        840 
WDWHTESGVK TALTIEEANG SNALSWEYAY PEVKPSDGWA TAPRLDFWKD ELVRGTSDYI 

       850        860        870        880        890        900 
SFDFYIDAVR ASEGAISINA VFQPPANGYW QEVPTTFEID LTELDSATVT SDELYHYEVK 

       910        920        930        940 
INIRDIEAIT DDTELRNLLL IFADEDSDFA GRVFVDNVRF E

« Hide

References

[1]"Molecular cloning and nucleotide sequence of a gene for alkaline cellulase from Bacillus sp. KSM-635."
Ozaki K., Shikata S., Kawai S., Ito S., Okamoto K.
J. Gen. Microbiol. 136:1327-1334(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Crystallization and preliminary X-ray analysis of a truncated family A alkaline endoglucanase isolated from Bacillus sp. KSM-635."
Shirai T., Yamane T., Hidaka T., Kuyama K., Suzuki A., Ashida T., Ozaki K., Ito S.
J. Biochem. 122:683-685(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 228-584, CRYSTALLIZATION.
[3]"Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme."
Shirai T., Ishida H., Noda J., Yamane T., Ozaki K., Hakamada Y., Ito S.
J. Mol. Biol. 310:1079-1087(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 221-584.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M27420 Genomic DNA. Translation: AAA22304.1.
PIRS29043.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G01X-ray1.90A228-584[»]
1G0CX-ray1.90A228-584[»]
ProteinModelPortalP19424.
SMRP19424. Positions 227-752, 759-941.
ModBaseSearch...

Protein family/group databases

CAZyCBM17. Carbohydrate-Binding Module Family 17.
CBM28. Carbohydrate-Binding Module Family 28.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR005086. CBM_fam_17/28.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR001119. S-layer_homology_dom.
[Graphical view]
PfamPF03424. CBM_17_28. 2 hits.
PF00150. Cellulase. 1 hit.
PF00395. SLH. 3 hits.
[Graphical view]
SUPFAMSSF49785. Gal_bind_like. 2 hits.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
PS51272. SLH. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19424.

Entry information

Entry nameGUN_BACS6
AccessionPrimary (citable) accession number: P19424
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 1, 2013
This is version 95 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents