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Protein

Endoglucanase A

Gene

cenA

Organism
Cellulomonas fimi
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei247PROSITE-ProRule annotation1
Active sitei283Proton donorPROSITE-ProRule annotation1
Active sitei423NucleophilePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

SABIO-RKP07984.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

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:cenA
OrganismiCellulomonas fimi
Taxonomic identifieri1708 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesCellulomonadaceaeCellulomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Tat-type signalPROSITE-ProRule annotationAdd BLAST31
ChainiPRO_000000790332 – 449Endoglucanase AAdd BLAST418

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi35 ↔ 1341 Publication
Disulfide bondi248 ↔ 2911 Publication
Disulfide bondi390 ↔ 4261 Publication

Post-translational modificationi

The linker region (also termed "hinge") may be a potential site for proteolysis.
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi590998.Celf_3184.

Structurei

3D structure databases

ProteinModelPortaliP07984.
SMRiP07984.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 137CBM2PROSITE-ProRule annotationAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni139 – 168Linker ("hinge") (Pro-Thr box)Add BLAST30
Regioni438 – 449CatalyticAdd BLAST12

Sequence similaritiesi

Contains 1 CBM2 (carbohydrate binding type-2) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108W9Q. Bacteria.
COG5297. LUCA.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001524. Glyco_hydro_6_CS.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07984-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTRRTAAAL LAAAAVAVGG LTALTTTAAQ AAPGCRVDYA VTNQWPGGFG
60 70 80 90 100
ANVTITNLGD PVSSWKLDWT YTAGQRIQQL WNGTASTNGG QVSVTSLPWN
110 120 130 140 150
GSIPTGGTAS FGFNGSWAGS NPTPASFSLN GTTCTGTVPT TSPTPTPTPT
160 170 180 190 200
TPTPTPTPTP TPTPTVTPQP TSGFYVDPTT QGYRAWQAAS GTDKALLEKI
210 220 230 240 250
ALTPQAYWVG NWADASHAQA EVADYTGRAV AAGKTPMLVV YAIPGRDCGS
260 270 280 290 300
HSGGGVSESE YARWVDTVAQ GIKGNPIVIL EPDALAQLGD CSGQGDRVGF
310 320 330 340 350
LKYAAKSLTL KGARVYIDAG HAKWLSVDTP VNRLNQVGFE YAVGFALNTS
360 370 380 390 400
NYQTTADSKA YGQQISQRLG GKKFVIDTSR NGNGSNGEWC NPRGRALGER
410 420 430 440
PVAVNDGSGL DALLWVKLPG ESDGACNGGP AAGQWWQEIA LEMARNARW
Length:449
Mass (Da):46,731
Last modified:August 1, 1988 - v1
Checksum:i67FF887814B3348D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15823 Genomic DNA. Translation: AAA23084.1.
PIRiA24993.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15823 Genomic DNA. Translation: AAA23084.1.
PIRiA24993.

3D structure databases

ProteinModelPortaliP07984.
SMRiP07984.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi590998.Celf_3184.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108W9Q. Bacteria.
COG5297. LUCA.

Enzyme and pathway databases

SABIO-RKP07984.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001524. Glyco_hydro_6_CS.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUNA_CELFI
AccessioniPrimary (citable) accession number: P07984
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: November 30, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.