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Protein

Endoglucanase A

Gene

celA

Organism
Clostridium longisporum
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes barley beta-glucan, lichenan, carboxymethylcellulose and xylan. It shows preferential activity against the larger cellooligosaccharides (cellohexaose and cellopentaose); cellotetraose is the smallest substrate degraded completely.

Catalytic activityi

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

pH dependencei

Optimum pH is 4.8.

Temperature dependencei

Optimum temperature is 43 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei185 – 1851Proton donorBy similarity
Active sitei309 – 3091NucleophileBy similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. polysaccharide binding Source: InterPro

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

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase A (EC:3.2.1.4)
Alternative name(s):
Cellulase A
Endo-1,4-beta-glucanase A
Gene namesi
Name:celA
OrganismiClostridium longisporum
Taxonomic identifieri1523 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 517492Endoglucanase APRO_0000007849Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP54937.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini416 – 517102CBM2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – ?CatalyticBy similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P54937-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRSLLKTCS IIAGATIIFS SLSISRNPLE VQAASMRSAS EIVQEMGVGW
60 70 80 90 100
NLGNTLDAKI TNLSYNTSPI SFETGWGNPV TTKAMIDKIK NAGFKTIRIP
110 120 130 140 150
TTWGEHLDGN NKLNEEWVKR VKEVVDYCIA DDLYVILNTH HEGNWVIPTY
160 170 180 190 200
AKESSVTPKL KTLWTQISEA FKDYDDHLIF ETLNEPRLEG TPYEWTGGTS
210 220 230 240 250
ESRDVVNKYN AAALESIRKT GGNNLSRAVM MPTYAASGSS TTMNDFKVPD
260 270 280 290 300
DKNVIASVHA YSPYFFAMDT SSNSVNTWGS SYDKYSLDVE LDSYLNTFKS
310 320 330 340 350
KGVPVVIGEF GSINKNNTSS RAELAEYYVT AAQKRGIPCV WWDNNYAETN
360 370 380 390 400
KGETFGLLNR STLNWYFSDI KDALIRGYKN VHPEATEDDK PSTDVTNPDS
410 420 430 440 450
GNTKPDSGNT NPGTETTTPT DNEKISITSK INDWGGAYQA DFTLKNNTSS
460 470 480 490 500
DINNWSFKIK KNDIVFTNYW DVKITEENGY YVVTPQAWKT TILANSSIVI
510
SIQGTGKVIS NFEYKFD
Length:517
Mass (Da):57,660
Last modified:September 30, 1996 - v1
Checksum:iA1D1570302FFBA30
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02868 Unassigned DNA. Translation: AAC37035.1.
PIRiI40798.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02868 Unassigned DNA. Translation: AAC37035.1.
PIRiI40798.

3D structure databases

ProteinModelPortaliP54937.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning of an endo-(1-->4)-beta-glucanase gene, celA, from the rumen bacterium Clostridium sp. ('C. longisporum') and characterization of its product, CelA, in Escherichia coli."
    Mittendorf V., Thomson J.A.
    J. Gen. Microbiol. 139:3233-3242(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 49440 / B6405.

Entry informationi

Entry nameiGUNA_CLOLO
AccessioniPrimary (citable) accession number: P54937
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1996
Last sequence update: September 30, 1996
Last modified: September 30, 2014
This is version 77 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

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

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.