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P26225 (GUNB_CELFI) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 88. 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 B

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

Protein attributes

Sequence length1045 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

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

Domain

The linker region (also termed "hinge") may be a potential site for proteolysis. Ref.2

Sequence similarities

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

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

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

Contains 3 fibronectin type-III domains.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 10451012Endoglucanase B
PRO_0000007945

Regions

Domain493 – 642150CBM3
Domain653 – 74391Fibronectin type-III 1
Domain751 – 84090Fibronectin type-III 2
Domain849 – 94092Fibronectin type-III 3
Domain939 – 1045107CBM2
Region34 – 492459Catalytic
Region644 – 6507Linker ("hinge") (Pro-Thr box)
Region734 – 74815Linker ("hinge") (Pro-Thr box)
Region831 – 84616Linker ("hinge") (Pro-Thr box)
Region931 – 94414Linker ("hinge") (Pro-Thr box)

Sites

Active site4101 By similarity
Active site4491 By similarity
Active site4581 By similarity

Amino acid modifications

Disulfide bond946 ↔ 1044 By similarity

Sequences

Sequence LengthMass (Da)Tools
P26225 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: AC2F7B84E4E3C4F0

FASTA1,045108,991
        10         20         30         40         50         60 
MLRQVPRTLV AGGSALAVAV GVLVAPLATG AAAAPTYNYA EALQKSMFFY QAQRSGDLPA 

        70         80         90        100        110        120 
DFPVSWRGDS GLTDGADVGK DLTGGWYDAG DHVKFGFPMA FSATMLAWGA IESPTGYSKA 

       130        140        150        160        170        180 
GSLDELKDNL RFVSDYFVKA HTAPNELYVQ VGDGEADHKW WGPAEVMTMA RPSHKISASC 

       190        200        210        220        230        240 
PGSDVAAETA AALASSAIVL KGDDPAYAAT LVSHAKQLYT FADTYRGAYS DCVTAASAYY 

       250        260        270        280        290        300 
KSWSGYQDEL VWGAYWLYKA TGDATYLAKA EAEYDKLGTE NQSTTRSYKW TIAWDNKQFG 

       310        320        330        340        350        360 
TYALLAMETG KQKYVDDANR WLDYWTVGVN GQKVPYSPGG QAVLDSWGAL RYAANTSFVA 

       370        380        390        400        410        420 
LVYSDWMTDA TRKARYHDFG VRQINYALGD NPRSSSYVVG FGANPPTAPH HRTAHGSWLD 

       430        440        450        460        470        480 
SITTPAQSRH VLYGALVGGP GSPNDAYTDS RQDYVANEVA TDYNAGFTSA LARLVEEYGG 

       490        500        510        520        530        540 
TPLASFPTPE QPDGDQLFVE AMLNQPPSGT FTEVKAMIRN QSAFPARSLK NAKVRYWFTT 

       550        560        570        580        590        600 
DGFAASDVTL SANYSECGAQ SGKGVSAGGT LGYVELSCVG QDIHPGGQSQ HRREIQFRLT 

       610        620        630        640        650        660 
GPAGWNPAND PSYTGLTQTA LAKASAITLY DGSTLVWGKE PTGTTTDTTP PTTPGTPVAT 

       670        680        690        700        710        720 
GVTTVGASLS WAASTDAGSG VAGYELYRVQ GTTQTLVGTT TAAAYILRDL TPGTAYSYVV 

       730        740        750        760        770        780 
KAKDVAGNVS AASAAVTFTT DTTGETEPPT TPGTPVASAV TSTGATLAWA PSTGDPAVSG 

       790        800        810        820        830        840 
YDVLRVQGTT TTVVAQTTVP TVTLSGLTPS TAYTYAVRAK NVAGDVSALS APVTFTTAAP 

       850        860        870        880        890        900 
PVDTVAPTVP GTPVASNVAT TGATLTWTAS TDSGGSGLAG YEVLRVSGTT QTLVASPTTA 

       910        920        930        940        950        960 
TVALAGLTPA TAYSYVVRAK DGAGNVSAVS SPVTFTTLPV TSTPSCTVVY STNSWNVGFT 

       970        980        990       1000       1010       1020 
GSVKITNTGT TPLTWTLGFA FPSGQQVTQG WSATWSQTGT TVTATGLSWN ATLQPGQSTD 

      1030       1040 
IGFNGSHPGT NTNPASFTVN GEVCG 

« Hide

References

[1]"Unusual sequence organization in CenB, an inverting endoglucanase from Cellulomonas fimi."
Meinke A., Braun C., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
J. Bacteriol. 173:308-314(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Multiple domains in endoglucanase B (CenB) from Cellulomonas fimi: functions and relatedness to domains in other polypeptides."
Meinke A., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
J. Bacteriol. 173:7126-7135(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAINS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64644 Genomic DNA. Translation: AAA23086.1.
PIRA39199.

3D structure databases

ProteinModelPortalP26225.
SMRP26225. Positions 35-641.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
CBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.50.10.10. 1 hit.
2.60.40.10. 3 hits.
2.60.40.290. 1 hit.
2.60.40.710. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR003961. Fibronectin_type3.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR013783. Ig-like_fold.
[Graphical view]
PfamPF00553. CBM_2. 1 hit.
PF00942. CBM_3. 1 hit.
PF00041. fn3. 3 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SMARTSM00637. CBD_II. 1 hit.
SM01067. CBM_3. 1 hit.
SM00060. FN3. 3 hits.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
SSF49265. SSF49265. 2 hits.
SSF49384. SSF49384. 2 hits.
PROSITEPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS51172. CBM3. 1 hit.
PS50853. FN3. 3 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNB_CELFI
AccessionPrimary (citable) accession number: P26225
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: December 11, 2013
This is version 88 of the entry and version 1 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