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P10474 (GUNB_CALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Endoglucanase/exoglucanase B

Including the following 2 domains:

  1. Endoglucanase
    EC=3.2.1.4
    Alternative name(s):
    Cellobiohydrolase
    Cellulase
    Endo-1,4-beta-glucanase
  2. Exoglucanase
    EC=3.2.1.91
    Alternative name(s):
    1,4-beta-cellobiohydrolase
    Exocellobiohydrolase
Gene names
Name:celB
OrganismCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Taxonomic identifier44001 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length1039 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

This protein is made up of two domains: the N-terminal domain has exoglucanase activity while the C-terminal domain is an endoglucanase.

Catalytic activity

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

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

Sequence similarities

In the N-terminal section; belongs to the glycosyl hydrolase 10 (cellulase F) family.

In the C-terminal section; belongs to the glycosyl hydrolase 5 (cellulase A) family.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828
Chain29 – 10391011Endoglucanase/exoglucanase B
PRO_0000007983

Regions

Domain418 – 571154CBM3
Compositional bias376 – 41641Pro/Thr-rich
Compositional bias574 – 61845Pro/Thr-rich

Sites

Active site1771Proton donor Potential
Active site2851Nucleophile By similarity
Active site7921 By similarity

Sequences

Sequence LengthMass (Da)Tools
P10474 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 0E0378171594DDAE

FASTA1,039117,641
        10         20         30         40         50         60 
MKRNLFRIVS RVVLIAFIAS ISLVGAMSYF PVETQAAPDW SIPSLCESYK DDFMIGVAIP 

        70         80         90        100        110        120 
ARCLSNDTDK RMVLKHFNSI TAENEMKPES LLAGQTSTGL SYRFSTADAF VDFASTNKIG 

       130        140        150        160        170        180 
IRGHTLVWHN QTPDWFFKDS NGQRLSKDAL LARLKQYIYD VVGRYKGKVY AWDVVNEAID 

       190        200        210        220        230        240 
ENQPDSYRRS TWYEICGPEY IEKAFIWAHE ADPNAKLFYN DYNTEISKKR DFIYNMVKNL 

       250        260        270        280        290        300 
KSKGIPIHGI GMQCHINVNW PSVSEIENSI KLFSSIPGIE IHITELDMSL YNYGSSENYS 

       310        320        330        340        350        360 
TPPQDLLQKQ SQKYKEIFTM LKKYKNVVKS VTFWGLKDDY SWLRSFYGKN DWPLLFFEDY 

       370        380        390        400        410        420 
SAKPAYWAVI EASGVTTSSP TPTPTPTVTV TPTPTPTPTP TVTATPTPTP TPVSTPATGG 

       430        440        450        460        470        480 
QIKVLYANKE TNSTTNTIRP WLKVVNSGSS SIDLSRVTIR YWYTVDGERA QSAVSDWAQI 

       490        500        510        520        530        540 
GASNVTFKFV KLSSSVSGAD YYLEIGFKSG AGQLQPGKDT GEIQIRFNKS DWSNYNQGND 

       550        560        570        580        590        600 
WSWLQSMTSY GENEKVTAYI DGVLVWGQEP SGATPAPTMT VAPTATPTPT LSPTVTPTPA 

       610        620        630        640        650        660 
PTQTAIPTPT LTPNPTPTSS IPDDTNDDWL YVSGNKIVDK DGRPVWLTGI NWFGYNTGTN 

       670        680        690        700        710        720 
VFDGVWSCNL KDTLAEIANR GFNLLRVPIS AELILNWSQG IYPKPNINYY VNPELEGKNS 

       730        740        750        760        770        780 
LEVFDIVVQT CKEVGLKIML DIHSIKTDAM GHIYPVWYDE KFTPEDFYKA CEWITNRYKN 

       790        800        810        820        830        840 
DDTIIAFDLK NEPHGKPWQD TTFAKWDNST DINNWKYAAE TCAKRILNIN PNLLIVIEGI 

       850        860        870        880        890        900 
EAYPKDDVTW TSKSSSDYYS TWWGGNLRGV RKYPINLGKY QNKVVYSPHD YGPSVYQQPW 

       910        920        930        940        950        960 
FYPGFTKESL LQDCWRPNWA YIMEENIAPL LIGEWGGHLD GADNEKWMKY LRDYIIENHI 

       970        980        990       1000       1010       1020 
HHTFWCFNAN SGDTGGLVGY DFTTWDEKKY SFLKPALWQD SQGRFVGLDH KRPLGTNGKN 

      1030 
INITTYYNNN EPEPVPASK 

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References

[1]"Nucleotide sequence of a gene from Caldocellum saccharolyticum encoding for exocellulase and endocellulase activity."
Saul D.J., Williams L.C., Love D.R., Chamley L.W., Bergquist P.L.
Nucleic Acids Res. 17:439-439(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13602 Genomic DNA. Translation: CAA31936.1.
PIRS02711.

3D structure databases

ProteinModelPortalP10474.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM3. Carbohydrate-Binding Module Family 3.
GH10. Glycoside Hydrolase Family 10.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.710. 1 hit.
3.20.20.80. 2 hits.
InterProIPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR001000. Glyco_hydro_10.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00942. CBM_3. 1 hit.
PF00150. Cellulase. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM01067. CBM_3. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 2 hits.
PROSITEPS51172. CBM3. 1 hit.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNB_CALSA
AccessionPrimary (citable) accession number: P10474
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: December 11, 2013
This is version 96 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