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Protein

Endoglucanase G

Gene

celG

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: 4 out of 5-Protein inferred from homologyi

Functioni

This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei226 – 2261Proton donorBy similarity
Active sitei381 – 3811NucleophileBy similarity

GO - Molecular functioni

  1. cellulase activity Source: MENGO

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

Enzyme and pathway databases

BioCyciCTHE203119:GIW8-2979-MONOMER.
MetaCyc:MONOMER-16420.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase G (EC:3.2.1.4)
Alternative name(s):
Cellulase G
Endo-1,4-beta-glucanase G
Short name:
EgG
Gene namesi
Name:celG
Ordered Locus Names:Cthe_2872
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. cellulosome Source: MENGO
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Add
BLAST
Chaini31 – 566536Endoglucanase GPRO_0000007853Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiQ05332. 1 interaction.
STRINGi203119.Cthe_2872.

Structurei

3D structure databases

ProteinModelPortaliQ05332.
SMRiQ05332. Positions 498-565.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati503 – 526241Add
BLAST
Repeati536 – 549142Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni503 – 549472 X 24 AA approximate repeatsAdd
BLAST

Domaini

A 24 residue 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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000225207.
OMAiKYKNDDT.
OrthoDBiEOG6PS5R7.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
PF00404. Dockerin_1. 2 hits.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q05332-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKAKAIFSL VVALMVLAIF CFAQNTGSTA TTAAAAVDSN NDDWLHCKGN
60 70 80 90 100
KIYDMYGNEV WLTGANWFGF NCSENCFHGA WYDVKTILTS IADRGINLLR
110 120 130 140 150
IPISTELLYS WMIGKPNPVS SVTASNNPPY HVVNPDFYDP ETDDVKNSME
160 170 180 190 200
IFDIIMGYCK ELGIKVMIDI HSPDANNSGH NYELWYGKET STCGVVTTKM
210 220 230 240 250
WIDTLVWLAD KYKNDDTIIA FDLKNEPHGK RGYTAEVPKL LAKWDNSTDE
260 270 280 290 300
NNWKYAAETC AKAILEVNPK VLIVIEGVEQ YPKTEKGYTY DTPDIWGATG
310 320 330 340 350
DASPWYSAWW GGNLRGVKDY PIDLGPLNSQ IVYSPHDYGP SVYAQPWFEK
360 370 380 390 400
DFTMQTLLDD YWYDTWAYIH DQGIAPILIG EWGGHMDGGK NQKWMTLLRD
410 420 430 440 450
YIVQNRIHHT FWCINPNSGD TGGLLGNDWS TWDEAKYALL KPALWQTKDG
460 470 480 490 500
KFIGLDHKIP LGSKGISLGE YYGTPQASDP PATPTATPTK PAASSTPSFI
510 520 530 540 550
YGDINSDGNV NSTDLGILKR IIVKNPPASA NMDAADVNAD GKVNSTDYTV
560
LKRYLLRSID KLPHTT
Length:566
Mass (Da):63,199
Last modified:February 1, 1994 - v1
Checksum:i2CC9DE1AD87C3178
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69390 Genomic DNA. Translation: CAA49187.1.
CP000568 Genomic DNA. Translation: ABN54070.1.
PIRiA40589.
RefSeqiWP_003514548.1. NC_009012.1.
YP_001039263.1. NC_009012.1.

Genome annotation databases

EnsemblBacteriaiABN54070; ABN54070; Cthe_2872.
GeneIDi4809152.
KEGGicth:Cthe_2872.
PATRICi19519842. VBICloThe47081_3073.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69390 Genomic DNA. Translation: CAA49187.1.
CP000568 Genomic DNA. Translation: ABN54070.1.
PIRiA40589.
RefSeqiWP_003514548.1. NC_009012.1.
YP_001039263.1. NC_009012.1.

3D structure databases

ProteinModelPortaliQ05332.
SMRiQ05332. Positions 498-565.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ05332. 1 interaction.
STRINGi203119.Cthe_2872.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN54070; ABN54070; Cthe_2872.
GeneIDi4809152.
KEGGicth:Cthe_2872.
PATRICi19519842. VBICloThe47081_3073.

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000225207.
OMAiKYKNDDT.
OrthoDBiEOG6PS5R7.

Enzyme and pathway databases

BioCyciCTHE203119:GIW8-2979-MONOMER.
MetaCyc:MONOMER-16420.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
PF00404. Dockerin_1. 2 hits.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the celG gene of Clostridium thermocellum and characterization of its product, endoglucanase CelG."
    Lemaire M., Beguin P.
    J. Bacteriol. 175:3353-3360(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. 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 nameiGUNG_CLOTH
AccessioniPrimary (citable) accession number: Q05332
Secondary accession number(s): A3DJE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: January 7, 2015
This is version 95 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, 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

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 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.