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Reviewed, UniProtKB/Swiss-Prot P50899 (GUXB_CELFI)

Last modified May 5, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Exoglucanase B
    EC=3.2.1.91
Alternative name(s):
    Exocellobiohydrolase B
    1,4-beta-cellobiohydrolase B
    CBP120
Gene names
Name: cbhB
Synonyms: cenE
OrganismCellulomonas fimi
Taxonomic identifier1708 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

Protein attributes

Sequence length1090 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Hydrolyzes cellohexaose to a mixture of cellotetraose, cellotriose and cellobiose, with only a trace of glucose. It hydrolyzed cellopentaose to cellotriose and cellobiose, and cellotetraose to cellobiose, but it did not hydrolyze cellotriose. Has also weak endoglucanase activity. Hydrolyzes glucosidic bonds with inversion of anomeric configuration.

Catalytic activity

Hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.

Sequence similarities

Belongs to the glycosyl hydrolase 48 (cellulase L) family.

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

Contains 3 fibronectin type-III domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Propeptide34 – 5320 Ref.2 Ref.3
PRO_0000008028
Chain54 – 10901037Exoglucanase B
PRO_0000008029

Regions

Domain704 – 78784Fibronectin type-III 1
Domain794 – 88390Fibronectin type-III 2
Domain895 – 98187Fibronectin type-III 3
Domain983 – 1090108CBM2
Region54 – 699646Catalytic By similarity

Sites

Active site5131Nucleophile By similarity

Amino acid modifications

Disulfide bond990 ↔ 1089 By similarity

Sequences

Sequence LengthMass (Da)Tools
P50899-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 046BB9D956F2F399

FASTA1,090114,829
        10         20         30         40         50         60 
MSSTTRRRSA WVAAATVGVS SFLAVAGITP AIAAAGAGQP ATVTVPAASP VRAAVDGEYA 

        70         80         90        100        110        120 
QRFLAQYDKI KDPANGYFSA QGIPYHAVET LMVEAPDYGH ETTSEAYSYW LWLEALYGQV 

       130        140        150        160        170        180 
TQDWAPLNHA WDTMEKYMIP QSVDQPTNSF YNPNSPATYA PEFNHPSSYP SQLNSGISGG 

       190        200        210        220        230        240 
TDPIGAELKA TYGNADVYQM HWLADVDNIY GFGATPGAGC TLGPTATGTS FINTFQRGPQ 

       250        260        270        280        290        300 
ESVWETVPQP SCEEFKYGGK NGYLDLFTKD ASYAKQWKYT SASDADARAV EAVYWANQWA 

       310        320        330        340        350        360 
TEQGKAADVA ATVAKAAKMG DYLRYTLFDK YFKKIGCTSP TCAAGQGREA AHYLLSWYMA 

       370        380        390        400        410        420 
WGGATDTSSG WAWRIGSSHA HFGYQNPLAA WALSTDPKLT PKSPTAKADW AASMQRQLEF 

       430        440        450        460        470        480 
YTWLQASNGG IAGGATNSWD GAYAQPPAGT PTFYGMGYTE APVYVDPPSN RWFGMQAWGV 

       490        500        510        520        530        540 
QRVAELYYAS GNAQAKKILD KWVPWVVANI STDGASWKVP SELKWTGKPD TWNAAAPTGN 

       550        560        570        580        590        600 
PGLTVEVTSY GQDVGVAADT ARALLFYAAK SGDTASRDKA KALLDAIWAN NQDPLGVSAV 

       610        620        630        640        650        660 
ETRGDYKRFD DTYVANGDGI YIPSGWTGTM PNGDVIKPGV SFLDIRSFYK KDPNWSKVQT 

       670        680        690        700        710        720 
FLDGGAEPQF RYHRFWAQTA VAGALADYAR LFDDGTTTPD TTAPTVPTGL QAGVVTSTEA 

       730        740        750        760        770        780 
TISWTASTDD TRVTGYDVYR GATKVGTATT TSFTDTGLTA STAYAYTVRA FDAAGNVSAP 

       790        800        810        820        830        840 
SAALTVTTKA TPSDTTAPSV PAITSSSSTA NSVTIGWSAS TDNAGGSGLA GYDVYRGATR 

       850        860        870        880        890        900 
VAQTTALTFT DTGLTASTAY EYTVRARDVA GNVSAPSTAV SVTTKSDTTP DTTAPSVPAG 

       910        920        930        940        950        960 
LAAMTVTETS VALTWNASTD TGGSGLKGYD VYRGATRVGS TTTASYTDTG LTAATAYQYT 

       970        980        990       1000       1010       1020 
VRATDNAGNV SAASAALSVT TKTPQTGGSC SVAYNASSWN SGFTASVRIT NTGTTTINGW 

      1030       1040       1050       1060       1070       1080 
SLGFDLTAGQ KVQQGWSATW TQSGSTVTAT NAPWNGTLAP GQTVDVGFNG SHTGQNPNPA 

      1090 
SFTLNGASCT 

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References

[1]"Cellobiohydrolase B, a second exo-cellobiohydrolase from the cellulolytic bacterium Cellulomonas fimi."
Shen H., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
Biochem. J. 311:67-74(1995) [PubMed: 7575482] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 456-461.
Strain: ATCC 484 / DSM 20113 / IFO 15513 / JCM 1341 / NCTC 7547.
[2]"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: PROTEIN SEQUENCE OF 54-75.
[3]"Stereochemical course of hydrolysis catalysed by Cellulomonas fimi CenE, a member of a new family of beta-1,4-glucanases."
Shen H., Tomme P., Meinke A., Gilkes N.R., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.
Biochem. Biophys. Res. Commun. 199:1223-1228(1994) [PubMed: 8147863] [Abstract]
Cited for: PROTEIN SEQUENCE OF 54-78.

Cross-references

Sequence databases

L38827 Genomic DNA. Translation: AAB00822.1.
PIRS59077.

3D structure databases

HSSPHSSP built from PDB template 1FAE based on UniProtKB P37698.
ModBaseSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
GH48. Glycoside Hydrolase Family 48.

Enzyme and pathway databases

BRENDA3.2.1.91. 97800.

Family and domain databases

InterProIPR012341. 6hp_glycosidase.
IPR001919. CBD_bac.
IPR012291. CBD_carb_bd.
IPR018366. CBM2_CS.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR000556. Glyco_hydro_48F.
[Graphical view]
Gene3DG3DSA:2.60.40.290. CBD_carb_bd. 1 hit.
G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.
G3DSA:2.60.40.30. FN_III-like. 3 hits.
PfamPF00553. CBM_2. 1 hit.
PF00041. fn3. 3 hits.
PF02011. Glyco_hydro_48. 1 hit.
[Graphical view]
PRINTSPR00844. GLHYDRLASE48.
ProDomPD011903. Glyco_hydro_48. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00637. CBD_II. 1 hit.
SM00060. FN3. 3 hits.
[Graphical view]
PROSITEPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS50853. FN3. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUXB_CELFI
AccessionPrimary (citable) accession number: P50899
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 5, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents