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P07984

- GUNA_CELFI

UniProt

P07984 - GUNA_CELFI

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Protein
Endoglucanase A
Gene
cenA
Organism
Cellulomonas fimi
Status
Reviewed - 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 dissaccharide 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei247 – 2471 By similarity
Active sitei283 – 2831Proton donor By similarity
Active sitei423 – 4231Nucleophile By 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

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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Tat-type signal Reviewed prediction
Add
BLAST
Chaini32 – 449418Endoglucanase A
PRO_0000007903Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

Structurei

3D structure databases

ProteinModelPortaliP07984.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 137106CBM2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni139 – 16830Linker ("hinge") (Pro-Thr box)
Add
BLAST
Regioni438 – 44912Catalytic
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
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

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MSTRRTAAAL LAAAAVAVGG LTALTTTAAQ AAPGCRVDYA VTNQWPGGFG    50
ANVTITNLGD PVSSWKLDWT YTAGQRIQQL WNGTASTNGG QVSVTSLPWN 100
GSIPTGGTAS FGFNGSWAGS NPTPASFSLN GTTCTGTVPT TSPTPTPTPT 150
TPTPTPTPTP TPTPTVTPQP TSGFYVDPTT QGYRAWQAAS GTDKALLEKI 200
ALTPQAYWVG NWADASHAQA EVADYTGRAV AAGKTPMLVV YAIPGRDCGS 250
HSGGGVSESE YARWVDTVAQ GIKGNPIVIL EPDALAQLGD CSGQGDRVGF 300
LKYAAKSLTL KGARVYIDAG HAKWLSVDTP VNRLNQVGFE YAVGFALNTS 350
NYQTTADSKA YGQQISQRLG GKKFVIDTSR NGNGSNGEWC NPRGRALGER 400
PVAVNDGSGL DALLWVKLPG ESDGACNGGP AAGQWWQEIA LEMARNARW 449
Length:449
Mass (Da):46,731
Last modified:August 1, 1988 - v1
Checksum:i67FF887814B3348D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15823 Genomic DNA. Translation: AAA23084.1.
PIRiA24993.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15823 Genomic DNA. Translation: AAA23084.1 .
PIRi A24993.

3D structure databases

ProteinModelPortali P07984.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P07984.

Family and domain databases

Gene3Di 2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProi IPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001524. Glyco_hydro_6_CS.
IPR006311. TAT_signal.
[Graphical view ]
Pfami PF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view ]
PIRSFi PIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSi PR00733. GLHYDRLASE6.
SMARTi SM00637. CBD_II. 1 hit.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEi PS51173. 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 ]
ProtoNeti Search...

Publicationsi

  1. "Characterization and structure of an endoglucanase gene cenA of Cellulomonas fimi."
    Wong W.K.R., Gerhard B., Guo Z.M., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.
    Gene 44:315-324(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Structural and functional analysis of a bacterial cellulase by proteolysis."
    Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
    J. Biol. Chem. 264:17802-17808(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS.
  3. Cited for: DISULFIDE BONDS.

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: October 16, 2013
This is version 93 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

External Data

Dasty 3

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