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P17901

- GUNA_CLOCE

UniProt

P17901 - GUNA_CLOCE

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Protein

Endoglucanase A

Gene

celCCA

Organism
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Status
Reviewed - Annotation score: 5 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 sitei147 – 1471Curated
Active sitei195 – 1951Proton donor
Active sitei332 – 3321Nucleophile

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC

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

BioCyciCCEL394503:GJET-1124-MONOMER.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase A (EC:3.2.1.4)
Alternative name(s):
Cellulase A
EGCCA
Endo-1,4-beta-glucanase A
Gene namesi
Name:celCCA
Ordered Locus Names:Ccel_1099
OrganismiClostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Taxonomic identifieri394503 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000001349: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi104 – 1041R → K: Small loss of activity. 1 Publication
Mutagenesisi104 – 1041R → S or V: Large decrease of activity. 1 Publication
Mutagenesisi147 – 1471H → S, E, G or F: Total loss of activity. 1 Publication
Mutagenesisi148 – 1481H → V: Large decrease of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 475449Endoglucanase APRO_0000007845Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi394503.Ccel_1099.

Structurei

Secondary structure

1
475
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 313Combined sources
Helixi46 – 549Combined sources
Beta strandi56 – 594Combined sources
Helixi75 – 773Combined sources
Helixi78 – 814Combined sources
Helixi89 – 9810Combined sources
Beta strandi102 – 1054Combined sources
Helixi110 – 1123Combined sources
Turni115 – 1184Combined sources
Helixi122 – 13615Combined sources
Turni137 – 1393Combined sources
Beta strandi141 – 1455Combined sources
Turni152 – 1543Combined sources
Helixi160 – 1623Combined sources
Helixi163 – 18018Combined sources
Turni181 – 1833Combined sources
Beta strandi188 – 1914Combined sources
Turni202 – 2054Combined sources
Helixi212 – 23423Combined sources
Helixi237 – 2404Combined sources
Beta strandi244 – 2474Combined sources
Helixi249 – 2513Combined sources
Helixi253 – 2575Combined sources
Beta strandi274 – 2796Combined sources
Helixi284 – 2874Combined sources
Helixi291 – 2933Combined sources
Helixi304 – 32017Combined sources
Helixi322 – 3243Combined sources
Beta strandi328 – 3336Combined sources
Helixi341 – 35717Combined sources
Beta strandi361 – 3644Combined sources
Beta strandi371 – 3744Combined sources
Turni382 – 3854Combined sources
Beta strandi386 – 3894Combined sources
Helixi390 – 39910Combined sources
Beta strandi418 – 4203Combined sources
Helixi424 – 43512Combined sources
Helixi443 – 4453Combined sources
Helixi455 – 46511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EDGX-ray1.60A27-401[»]
2VN5X-ray1.90B/D410-475[»]
2VN6X-ray1.49B410-472[»]
ProteinModelPortaliP17901.
SMRiP17901. Positions 27-401, 410-472.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17901.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati415 – 438241Add
BLAST
Repeati446 – 469242Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni415 – 469552 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.
HOGENOMiHOG000027405.
KOiK01179.
OMAiTWGEEAT.
OrthoDBiEOG6KHFWF.

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.
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. 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.

P17901-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKTTAFLLC FLMIFTALLP MQNANAYDAS LIPNLQIPQK NIPNNDGMNF
60 70 80 90 100
VKGLRLGWNL GNTFDAFNGT NITNELDYET SWSGIKTTKQ MIDAIKQKGF
110 120 130 140 150
NTVRIPVSWH PHVSGSDYKI SDVWMNRVQE VVNYCIDNKM YVILNTHHDV
160 170 180 190 200
DKVKGYFPSS QYMASSKKYI TSVWAQIAAR FANYDEHLIF EGMNEPRLVG
210 220 230 240 250
HANEWWPELT NSDVVDSINC INQLNQDFVN TVRATGGKNA SRYLMCPGYV
260 270 280 290 300
ASPDGATNDY FRMPNDISGN NNKIIVSVHA YCPWNFAGLA MADGGTNAWN
310 320 330 340 350
INDSKDQSEV TWFMDNIYNK YTSRGIPVII GECGAVDKNN LKTRVEYMSY
360 370 380 390 400
YVAQAKARGI LCILWDNNNF SGTGELFGFF DRRSCQFKFP EIIDGMVKYA
410 420 430 440 450
FEAKTDPDPV IVYGDYNNDG NVDALDFAGL KKYIMAADHA YVKNLDVNLD
460 470
NEVNAFDLAI LKKYLLGMVS KLPSN
Length:475
Mass (Da):53,625
Last modified:November 1, 1990 - v1
Checksum:i1AF20EA2C0A132F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93096 Genomic DNA. Translation: AAA51444.1.
M32362 Genomic DNA. Translation: AAA23221.1.
CP001348 Genomic DNA. Translation: ACL75458.1.
RefSeqiWP_015924614.1. NC_011898.1.
YP_002505438.1. NC_011898.1.

Genome annotation databases

EnsemblBacteriaiACL75458; ACL75458; Ccel_1099.
GeneIDi7309912.
KEGGicce:Ccel_1099.
PATRICi19433019. VBICloCel57783_1132.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93096 Genomic DNA. Translation: AAA51444.1 .
M32362 Genomic DNA. Translation: AAA23221.1 .
CP001348 Genomic DNA. Translation: ACL75458.1 .
RefSeqi WP_015924614.1. NC_011898.1.
YP_002505438.1. NC_011898.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EDG X-ray 1.60 A 27-401 [» ]
2VN5 X-ray 1.90 B/D 410-475 [» ]
2VN6 X-ray 1.49 B 410-472 [» ]
ProteinModelPortali P17901.
SMRi P17901. Positions 27-401, 410-472.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 394503.Ccel_1099.

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL75458 ; ACL75458 ; Ccel_1099 .
GeneIDi 7309912.
KEGGi cce:Ccel_1099.
PATRICi 19433019. VBICloCel57783_1132.

Phylogenomic databases

eggNOGi COG2730.
HOGENOMi HOG000027405.
KOi K01179.
OMAi TWGEEAT.
OrthoDBi EOG6KHFWF.

Enzyme and pathway databases

BioCyci CCEL394503:GJET-1124-MONOMER.

Miscellaneous databases

EvolutionaryTracei P17901.

Family and domain databases

Gene3Di 1.10.1330.10. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00150. Cellulase. 1 hit.
PF00404. Dockerin_1. 2 hits.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the Clostridium cellulolyticum endoglucanase-A-encoding gene, celCCA."
    Faure E., Belaich A., Bagnara C., Gaudin C., Belaich J.-P.
    Gene 84:39-46(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-39.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.
  3. "Characterization of endoglucanase A from Clostridium cellulolyticum."
    Fierobe H.-P., Gaudin C., Belaich A., Loufti M., Faure E., Bagnara C., Baty D., Belaich J.-P.
    J. Bacteriol. 173:7956-7962(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "The catalytic domain of endoglucanase A from Clostridium cellulolyticum: effects of arginine 79 and histidine 122 mutations on catalysis."
    Belaich A., Fierobe H.-P., Baty D., Busetta B., Bagnara-Tardif C., Gaudin C., Belaich J.-P.
    J. Bacteriol. 174:4677-4682(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-104; HIS-147 AND HIS-148.
  5. "Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5."
    Ducros V., Czjzek M., Belaich A., Gaudin C., Fierobe H.P., Belaich J.-P., Davies G.J., Haser R.
    Structure 3:939-949(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 27-406.

Entry informationi

Entry nameiGUNA_CLOCE
AccessioniPrimary (citable) accession number: P17901
Secondary accession number(s): B8HZV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 26, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The C-terminus (AA 411-475) may play a role in organizing the cellulosome complex.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3