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Protein

Endoglucanase 5A

Gene

cel5A

Organism
Salipaludibacillus agaradhaerens (Bacillus agaradhaerens)
Status
Reviewed-Annotation score: Annotation score: 4 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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei61SubstrateCombined sources3 Publications1
Binding sitei92SubstrateCombined sources3 Publications1
Binding sitei127SubstrateCombined sources3 Publications1
Active sitei165Proton donor4 Publications1
Binding sitei228SubstrateCombined sources2 Publications1
Active sitei254NucleophileCombined sources4 Publications1
Binding sitei288SubstrateCombined sources4 Publications1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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:3.2.1.42 Publications)
Alternative name(s):
Alkaline cellulase
Endo-1,4-beta-glucanase 5A
Gene namesi
Name:cel5A
OrganismiSalipaludibacillus agaradhaerens (Bacillus agaradhaerens)
Taxonomic identifieri76935 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceae

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

DrugBankiDB03584. 4-Thio-beta-D-glucopyranose.
DB02379. Beta-D-Glucose.
DB02061. Cellobiose.
DB01633. Deoxy-2-Fluoro-B-D-Cellotrioside.
DB02017. Imidazole-Derived Cellobiose.
DB01642. O1-Methyl-Glucose.
DB03862. Tetrahydrooxazine.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000018404327 – 400Endoglucanase 5AAdd BLAST374

Interactioni

Subunit structurei

Monomer.1 Publication

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini357 – 396Chitin-binding type-3Sequence analysisAdd BLAST40

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni65 – 66Substrate bindingCombined sources3 Publications2
Regioni260 – 261Substrate bindingCombined sources2 Publications2
Regioni293 – 295Substrate bindingCombined sources3 Publications3

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

InterProiView protein in InterPro
IPR003610. CBM_fam5/12.
IPR036573. CBM_sf_5/12.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR017853. Glycoside_hydrolase_SF.
PfamiView protein in Pfam
PF00150. Cellulase. 1 hit.
SMARTiView protein in SMART
SM00495. ChtBD3. 1 hit.
SUPFAMiSSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiView protein in PROSITE
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.

Sequencei

Sequence statusi: Complete.

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

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.

Similar proteinsi

Entry informationi

Entry nameiGUN5_SALAG
AccessioniPrimary (citable) accession number: O85465
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: October 25, 2017
This is version 92 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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