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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

Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761SubstrateBy similarity
Active sitei87 – 871Proton donorBy similarity
Binding sitei140 – 1401SubstrateBy similarity
Binding sitei204 – 2041SubstrateBy similarity
Binding sitei241 – 2411SubstrateBy similarity
Binding sitei247 – 2471SubstrateBy similarity
Active sitei255 – 2551NucleophileBy similarity
Binding sitei421 – 4211SubstrateBy similarity
Binding sitei520 – 5201SubstrateBy similarity
Metal bindingi679 – 6791Calcium 1By similarity
Metal bindingi681 – 6811Calcium 1By similarity
Metal bindingi683 – 6831Calcium 1By similarity
Metal bindingi684 – 6841Calcium 1; via amide nitrogenBy similarity
Metal bindingi685 – 6851Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi690 – 6901Calcium 1By similarity
Metal bindingi711 – 7111Calcium 2By similarity
Metal bindingi711 – 7111Calcium 3By similarity
Metal bindingi712 – 7121Calcium 2; via amide nitrogenBy similarity
Metal bindingi713 – 7131Calcium 3By similarity
Metal bindingi715 – 7151Calcium 3By similarity
Metal bindingi717 – 7171Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi717 – 7171Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi722 – 7221Calcium 2By similarity
Metal bindingi722 – 7221Calcium 3By 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 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
Taxonomic identifieri203119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
ProteomesiUP000002145: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
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.
ModBaseiSearch...
MobiDBiSearch...

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 bindingBy similarity
Regioni301 – 3022Substrate bindingBy similarity
Regioni326 – 3272Substrate bindingBy similarity
Regioni645 – 6462Substrate bindingBy 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.Curated

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

        10         20         30         40         50
MVKSRKISIL LAVAMLVSIM IPTTAFAGPT KAPTKDGTSY KDLFLELYGK
60 70 80 90 100
IKDPKNGYFS PDEGIPYHSI ETLIVEAPDY GHVTTSEAFS YYVWLEAMYG
110 120 130 140 150
NLTGNWSGVE TAWKVMEDWI IPDSTEQPGM SSYNPNSPAT YADEYEDPSY
160 170 180 190 200
YPSELKFDTV RVGSDPVHND LVSAYGPNMY LMHWLMDVDN WYGFGTGTRA
210 220 230 240 250
TFINTFQRGE QESTWETIPH PSIEEFKYGG PNGFLDLFTK DRSYAKQWRY
260 270 280 290 300
TNAPDAEGRA IQAVYWANKW AKEQGKGSAV ASVVSKAAKM GDFLRNDMFD
310 320 330 340 350
KYFMKIGAQD KTPATGYDSA HYLMAWYTAW GGGIGASWAW KIGCSHAHFG
360 370 380 390 400
YQNPFQGWVS ATQSDFAPKS SNGKRDWTTS YKRQLEFYQW LQSAEGGIAG
410 420 430 440 450
GATNSWNGRY EKYPAGTSTF YGMAYVPHPV YADPGSNQWF GFQAWSMQRV
460 470 480 490 500
MEYYLETGDS SVKNLIKKWV DWVMSEIKLY DDGTFAIPSD LEWSGQPDTW
510 520 530 540 550
TGTYTGNPNL HVRVTSYGTD LGVAGSLANA LATYAAATER WEGKLDTKAR
560 570 580 590 600
DMAAELVNRA WYNFYCSEGK GVVTEEARAD YKRFFEQEVY VPAGWSGTMP
610 620 630 640 650
NGDKIQPGIK FIDIRTKYRQ DPYYDIVYQA YLRGEAPVLN YHRFWHEVDL
660 670 680 690 700
AVAMGVLATY FPDMTYKVPG TPSTKLYGDV NDDGKVNSTD AVALKRYVLR
710 720 730 740
SGISINTDNA DLNEDGRVNS TDLGILKRYI LKEIDTLPYK N
Length:741
Mass (Da):83,558
Last modified:March 20, 2007 - v1
Checksum:i39FDF4680BDB1144
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372.

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: October 29, 2014
This is version 48 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, Reference proteome

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