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Protein

Endoglucanase 5A

Gene

cel5A

Organism
Bacillus agaradhaerens (Bacillus agaradherans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 sitei165Proton donor1
Active sitei254Nucleophile1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiCBM5. Carbohydrate-Binding Module Family 5.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase 5A (EC:3.2.1.4)
Alternative name(s):
Alkaline cellulase
Endo-1,4-beta-glucanase 5A
Gene namesi
Name:cel5A
OrganismiBacillus agaradhaerens (Bacillus agaradherans)
Taxonomic identifieri76935 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesSporolactobacillaceaeunclassified Sporolactobacillaceae

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001840431 – 400Endoglucanase 5AAdd BLAST400

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1400
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi31 – 35Combined sources5
Beta strandi39 – 41Combined sources3
Beta strandi44 – 46Combined sources3
Beta strandi56 – 61Combined sources6
Helixi63 – 66Combined sources4
Helixi67 – 69Combined sources3
Helixi72 – 80Combined sources9
Beta strandi86 – 94Combined sources9
Turni98 – 100Combined sources3
Helixi104 – 118Combined sources15
Beta strandi121 – 127Combined sources7
Beta strandi129 – 131Combined sources3
Turni134 – 137Combined sources4
Helixi138 – 152Combined sources15
Beta strandi158 – 161Combined sources4
Turni173 – 176Combined sources4
Helixi177 – 189Combined sources13
Beta strandi193 – 195Combined sources3
Beta strandi197 – 199Combined sources3
Helixi202 – 205Combined sources4
Helixi208 – 212Combined sources5
Beta strandi221 – 228Combined sources8
Turni229 – 231Combined sources3
Helixi234 – 245Combined sources12
Beta strandi250 – 258Combined sources9
Beta strandi264 – 266Combined sources3
Helixi268 – 280Combined sources13
Beta strandi285 – 291Combined sources7
Helixi312 – 314Combined sources3
Helixi317 – 328Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A3HX-ray1.57A30-329[»]
1E5JX-ray1.85A27-331[»]
1H11X-ray1.08A27-329[»]
1H2JX-ray1.15A27-329[»]
1H5VX-ray1.10A27-330[»]
1HF6X-ray1.15A27-329[»]
1OCQX-ray1.08A27-329[»]
1QHZX-ray1.95A27-331[»]
1QI0X-ray2.10A27-331[»]
1QI2X-ray1.75A27-331[»]
1W3KX-ray1.20A27-329[»]
1W3LX-ray1.04A27-329[»]
2A3HX-ray2.00A30-329[»]
2V38X-ray1.50A27-331[»]
3A3HX-ray1.64A30-329[»]
4A3HX-ray1.65A27-329[»]
5A3HX-ray1.82A27-329[»]
6A3HX-ray1.68A27-329[»]
7A3HX-ray0.95A27-329[»]
8A3HX-ray0.97A27-329[»]
ProteinModelPortaliO85465.
SMRiO85465.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO85465.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.10.10.20. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR003610. CBM_fam5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02839. CBM_5_12. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00495. ChtBD3. 1 hit.
[Graphical view]
SUPFAMiSSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O85465-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKITTIFVV LLMTVALFSI GNTTAADNDS VVEEHGQLSI SNGELVNERG
60 70 80 90 100
EQVQLKGMSS HGLQWYGQFV NYESMKWLRD DWGINVFRAA MYTSSGGYID
110 120 130 140 150
DPSVKEKVKE AVEAAIDLDI YVIIDWHILS DNDPNIYKEE AKDFFDEMSE
160 170 180 190 200
LYGDYPNVIY EIANEPNGSD VTWGNQIKPY AEEVIPIIRN NDPNNIIIVG
210 220 230 240 250
TGTWSQDVHH AADNQLADPN VMYAFHFYAG THGQNLRDQV DYALDQGAAI
260 270 280 290 300
FVSEWGTSAA TGDGGVFLDE AQVWIDFMDE RNLSWANWSL THKDESSAAL
310 320 330 340 350
MPGANPTGGW TEAELSPSGT FVREKIRESA SIPPSDPTPP SDPGEPDPTP
360 370 380 390 400
PSDPGEYPAW DPNQIYTNEI VYHNGQLWQA KWWTQNQEPG DPYGPWEPLN
Length:400
Mass (Da):44,702
Last modified:November 1, 1998 - v1
Checksum:i3F9C66FB9BC36FFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067428 Genomic DNA. Translation: AAC19169.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067428 Genomic DNA. Translation: AAC19169.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A3HX-ray1.57A30-329[»]
1E5JX-ray1.85A27-331[»]
1H11X-ray1.08A27-329[»]
1H2JX-ray1.15A27-329[»]
1H5VX-ray1.10A27-330[»]
1HF6X-ray1.15A27-329[»]
1OCQX-ray1.08A27-329[»]
1QHZX-ray1.95A27-331[»]
1QI0X-ray2.10A27-331[»]
1QI2X-ray1.75A27-331[»]
1W3KX-ray1.20A27-329[»]
1W3LX-ray1.04A27-329[»]
2A3HX-ray2.00A30-329[»]
2V38X-ray1.50A27-331[»]
3A3HX-ray1.64A30-329[»]
4A3HX-ray1.65A27-329[»]
5A3HX-ray1.82A27-329[»]
6A3HX-ray1.68A27-329[»]
7A3HX-ray0.95A27-329[»]
8A3HX-ray0.97A27-329[»]
ProteinModelPortaliO85465.
SMRiO85465.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM5. Carbohydrate-Binding Module Family 5.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO85465.

Family and domain databases

Gene3Di2.10.10.20. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR003610. CBM_fam5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02839. CBM_5_12. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00495. ChtBD3. 1 hit.
[Graphical view]
SUPFAMiSSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUN5_BACAG
AccessioniPrimary (citable) accession number: O85465
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: November 2, 2016
This is version 87 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

3D-structure

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

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.