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A3DH67

- GUNS_CLOTH

UniProt

A3DH67 - GUNS_CLOTH

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Protein

Cellulose 1,4-beta-cellobiosidase (reducing end) CelS

Gene
celS, Cthe_2089
Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

This enzyme catalyzes the exohydrolysis of 1,4-beta-glucosidic linkages in cellulose with a preference for amorphous or crystalline cellulose over carboxymethyl cellulose.1 Publication

Catalytic activityi

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

Enzyme regulationi

Inhibited by cellobiose and lactose, but not by glucose.1 Publication

pH dependencei

Optimum pH is 5-6.1 Publication

Temperature dependencei

Optimum temperature is 70 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761Substrate By similarity
Active sitei87 – 871Proton donor By similarity
Binding sitei140 – 1401Substrate By similarity
Binding sitei204 – 2041Substrate By similarity
Binding sitei241 – 2411Substrate By similarity
Binding sitei247 – 2471Substrate By similarity
Active sitei255 – 2551Nucleophile By similarity
Binding sitei421 – 4211Substrate By similarity
Binding sitei520 – 5201Substrate By similarity
Metal bindingi679 – 6791Calcium 1 By similarity
Metal bindingi681 – 6811Calcium 1 By similarity
Metal bindingi683 – 6831Calcium 1 By similarity
Metal bindingi684 – 6841Calcium 1; via amide nitrogen By similarity
Metal bindingi685 – 6851Calcium 1; via carbonyl oxygen By similarity
Metal bindingi690 – 6901Calcium 1 By similarity
Metal bindingi711 – 7111Calcium 2 By similarity
Metal bindingi711 – 7111Calcium 3 By similarity
Metal bindingi712 – 7121Calcium 2; via amide nitrogen By similarity
Metal bindingi713 – 7131Calcium 3 By similarity
Metal bindingi715 – 7151Calcium 3 By similarity
Metal bindingi717 – 7171Calcium 2; via carbonyl oxygen By similarity
Metal bindingi717 – 7171Calcium 3; via carbonyl oxygen By similarity
Metal bindingi722 – 7221Calcium 2 By similarity
Metal bindingi722 – 7221Calcium 3 By similarity

GO - Molecular functioni

  1. cellulase activity Source: InterPro
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciCTHE203119:GIW8-2150-MONOMER.
MetaCyc:MONOMER-16423.

Protein family/group databases

CAZyiGH48. Glycoside Hydrolase Family 48.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellulose 1,4-beta-cellobiosidase (reducing end) CelS (EC:3.2.1.176)
Alternative name(s):
Cellobiohydrolase CelS
Cellulase SS
Endo-1,4-beta-glucanase
Endoglucanase SS
Short name:
EGSS
Exocellulase
Gene namesi
Name:celS
Ordered Locus Names:Cthe_2089
OrganismiClostridium thermocellum (strain ATCC 27405 / DSM 1237)
Taxonomic identifieri203119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
ProteomesiUP000002145: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 741714Cellulose 1,4-beta-cellobiosidase (reducing end) CelSPRO_0000284723Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi203119.Cthe_2089.

Structurei

3D structure databases

ProteinModelPortaliA3DH67.
SMRiA3DH67. Positions 28-669, 673-741.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini679 – 69921Dockerin 1Add
BLAST
Domaini711 – 73121Dockerin 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni251 – 2522Substrate binding By similarity
Regioni301 – 3022Substrate binding By similarity
Regioni326 – 3272Substrate binding By similarity
Regioni645 – 6462Substrate binding By similarity

Domaini

The dockerin domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

Sequence similaritiesi

Contains 2 dockerin domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG10655.
HOGENOMiHOG000020369.
OMAiTYHRFWS.
OrthoDBiEOG64V28H.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
1.50.10.10. 4 hits.
4.10.870.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR027390. Endoglucanase_F_dom3.
IPR000556. Glyco_hydro_48F.
[Graphical view]
PfamiPF00404. Dockerin_1. 2 hits.
PF02011. Glyco_hydro_48. 1 hit.
[Graphical view]
PRINTSiPR00844. GLHYDRLASE48.
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A3DH67-1 [UniParc]FASTAAdd to Basket

« Hide

MVKSRKISIL LAVAMLVSIM IPTTAFAGPT KAPTKDGTSY KDLFLELYGK    50
IKDPKNGYFS PDEGIPYHSI ETLIVEAPDY GHVTTSEAFS YYVWLEAMYG 100
NLTGNWSGVE TAWKVMEDWI IPDSTEQPGM SSYNPNSPAT YADEYEDPSY 150
YPSELKFDTV RVGSDPVHND LVSAYGPNMY LMHWLMDVDN WYGFGTGTRA 200
TFINTFQRGE QESTWETIPH PSIEEFKYGG PNGFLDLFTK DRSYAKQWRY 250
TNAPDAEGRA IQAVYWANKW AKEQGKGSAV ASVVSKAAKM GDFLRNDMFD 300
KYFMKIGAQD KTPATGYDSA HYLMAWYTAW GGGIGASWAW KIGCSHAHFG 350
YQNPFQGWVS ATQSDFAPKS SNGKRDWTTS YKRQLEFYQW LQSAEGGIAG 400
GATNSWNGRY EKYPAGTSTF YGMAYVPHPV YADPGSNQWF GFQAWSMQRV 450
MEYYLETGDS SVKNLIKKWV DWVMSEIKLY DDGTFAIPSD LEWSGQPDTW 500
TGTYTGNPNL HVRVTSYGTD LGVAGSLANA LATYAAATER WEGKLDTKAR 550
DMAAELVNRA WYNFYCSEGK GVVTEEARAD YKRFFEQEVY VPAGWSGTMP 600
NGDKIQPGIK FIDIRTKYRQ DPYYDIVYQA YLRGEAPVLN YHRFWHEVDL 650
AVAMGVLATY FPDMTYKVPG TPSTKLYGDV NDDGKVNSTD AVALKRYVLR 700
SGISINTDNA DLNEDGRVNS TDLGILKRYI LKEIDTLPYK N 741
Length:741
Mass (Da):83,558
Last modified:March 20, 2007 - v1
Checksum:i39FDF4680BDB1144
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L06942 Genomic DNA. Translation: AAA23226.1.
CP000568 Genomic DNA. Translation: ABN53296.1.
PIRiA47063.
RefSeqiWP_020457708.1. NC_009012.1.
YP_001038489.1. NC_009012.1.

Genome annotation databases

EnsemblBacteriaiABN53296; ABN53296; Cthe_2089.
GeneIDi4810949.
KEGGicth:Cthe_2089.
PATRICi19518092. VBICloThe47081_2217.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L06942 Genomic DNA. Translation: AAA23226.1 .
CP000568 Genomic DNA. Translation: ABN53296.1 .
PIRi A47063.
RefSeqi WP_020457708.1. NC_009012.1.
YP_001038489.1. NC_009012.1.

3D structure databases

ProteinModelPortali A3DH67.
SMRi A3DH67. Positions 28-669, 673-741.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 203119.Cthe_2089.

Protein family/group databases

CAZyi GH48. Glycoside Hydrolase Family 48.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABN53296 ; ABN53296 ; Cthe_2089 .
GeneIDi 4810949.
KEGGi cth:Cthe_2089.
PATRICi 19518092. VBICloThe47081_2217.

Phylogenomic databases

eggNOGi NOG10655.
HOGENOMi HOG000020369.
OMAi TYHRFWS.
OrthoDBi EOG64V28H.

Enzyme and pathway databases

BioCyci CTHE203119:GIW8-2150-MONOMER.
MetaCyc:MONOMER-16423.

Family and domain databases

Gene3Di 1.10.1330.10. 1 hit.
1.50.10.10. 4 hits.
4.10.870.10. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR027390. Endoglucanase_F_dom3.
IPR000556. Glyco_hydro_48F.
[Graphical view ]
Pfami PF00404. Dockerin_1. 2 hits.
PF02011. Glyco_hydro_48. 1 hit.
[Graphical view ]
PRINTSi PR00844. GLHYDRLASE48.
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and DNA sequence of the gene coding for Clostridium thermocellum cellulase Ss (CelS), a major cellulosome component."
    Wang W.K., Kruus K., Wu J.H.D.
    J. Bacteriol. 175:1293-1302(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-37; 412-431 AND 589-605.
  2. "Product inhibition of the recombinant CelS, an exoglucanase component of the Clostridium thermocellum cellulosome."
    Kruus K., Andreacchi A., Wang W.K., Wu J.H.D.
    Appl. Microbiol. Biotechnol. 44:399-404(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME REGULATION.
  3. "Exoglucanase activities of the recombinant Clostridium thermocellum CelS, a major cellulosome component."
    Kruus K., Wang W.K., Ching J., Wu J.H.
    J. Bacteriol. 177:1641-1644(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27405 / DSM 1237.

Entry informationi

Entry nameiGUNS_CLOTH
AccessioniPrimary (citable) accession number: A3DH67
Secondary accession number(s): P38686
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: March 20, 2007
Last modified: September 3, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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