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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: 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)DescriptionActionsGraphical viewLength
Binding sitei76SubstrateBy similarity1
Active sitei87Proton donorBy similarity1
Binding sitei140SubstrateBy similarity1
Binding sitei204SubstrateBy similarity1
Binding sitei241SubstrateBy similarity1
Binding sitei247SubstrateBy similarity1
Active sitei255NucleophileBy similarity1
Binding sitei421SubstrateBy similarity1
Binding sitei520SubstrateBy similarity1
Metal bindingi679Calcium 1By similarity1
Metal bindingi681Calcium 1By similarity1
Metal bindingi683Calcium 1By similarity1
Metal bindingi684Calcium 1; via amide nitrogenBy similarity1
Metal bindingi685Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi690Calcium 1By similarity1
Metal bindingi711Calcium 2By similarity1
Metal bindingi711Calcium 3By similarity1
Metal bindingi712Calcium 2; via amide nitrogenBy similarity1
Metal bindingi713Calcium 3By similarity1
Metal bindingi715Calcium 3By similarity1
Metal bindingi717Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi717Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi722Calcium 2By similarity1
Metal bindingi722Calcium 3By similarity1

GO - Molecular functioni

GO - Biological processi

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

BioCyciMetaCyc:MONOMER-16423.
BRENDAi3.2.1.176. 1530.

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
Proteomesi
  • UP000002145 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
ChainiPRO_000028472328 – 741Cellulose 1,4-beta-cellobiosidase (reducing end) CelSAdd BLAST714

Interactioni

Protein-protein interaction databases

STRINGi203119.Cthe_2089.

Structurei

3D structure databases

ProteinModelPortaliA3DH67.
SMRiA3DH67.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini673 – 739DockerinPROSITE-ProRule annotationAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni251 – 252Substrate bindingBy similarity2
Regioni301 – 302Substrate bindingBy similarity2
Regioni326 – 327Substrate bindingBy similarity2
Regioni645 – 646Substrate bindingBy similarity2

Sequence similaritiesi

Contains 1 dockerin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CYP. Bacteria.
ENOG410XPC9. LUCA.
HOGENOMiHOG000020369.
KOiK20829.
OMAiKYTNAPD.
OrthoDBiPOG091H0EGP.

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.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
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.
PS51766. DOCKERIN. 1 hit.
[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.

Genome annotation databases

EnsemblBacteriaiABN53296; ABN53296; Cthe_2089.
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.
PIRiA47063.

3D structure databases

ProteinModelPortaliA3DH67.
SMRiA3DH67.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi203119.Cthe_2089.

Protein family/group databases

CAZyiGH48. Glycoside Hydrolase Family 48.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105CYP. Bacteria.
ENOG410XPC9. LUCA.
HOGENOMiHOG000020369.
KOiK20829.
OMAiKYTNAPD.
OrthoDBiPOG091H0EGP.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16423.
BRENDAi3.2.1.176. 1530.

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.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
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.
PS51766. DOCKERIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 59 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.