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P43316

- GUN5_HUMIN

UniProt

P43316 - GUN5_HUMIN

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Protein

Endoglucanase-5

Gene
N/A
Organism
Humicola insolens (Soft-rot fungus)
Status
Reviewed - Annotation score: 2 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Nucleophile
Active sitei121 – 1211Proton donor

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

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH45. Glycoside Hydrolase Family 45.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase-5 (EC:3.2.1.4)
Alternative name(s):
Cellulase V
Endo-1,4-beta-glucanase V
Short name:
EG V
Endoglucanase V
OrganismiHumicola insolens (Soft-rot fungus)
Taxonomic identifieri34413 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213Endoglucanase-5PRO_0000184074Add
BLAST

Interactioni

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Helixi15 – 173Combined sources
Beta strandi21 – 266Combined sources
Beta strandi62 – 654Combined sources
Beta strandi68 – 769Combined sources
Helixi82 – 854Combined sources
Beta strandi89 – 946Combined sources
Helixi97 – 993Combined sources
Beta strandi103 – 1108Combined sources
Beta strandi119 – 1235Combined sources
Turni130 – 1323Combined sources
Helixi135 – 1395Combined sources
Beta strandi143 – 1453Combined sources
Turni146 – 1483Combined sources
Helixi153 – 1586Combined sources
Helixi161 – 1633Combined sources
Helixi164 – 1718Combined sources
Turni172 – 1765Combined sources
Beta strandi181 – 1877Combined sources
Helixi191 – 1977Combined sources
Helixi204 – 2063Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HD5X-ray1.66A5-213[»]
2ENGX-ray1.50A1-210[»]
3ENGX-ray1.90A1-213[»]
4ENGX-ray1.90A1-210[»]
ProteinModelPortaliP43316.
SMRiP43316. Positions 1-213.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43316.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.40.40.10. 1 hit.
InterProiIPR014733. Barwin-like_endoglucanase.
IPR000334. Glyco_hydro_45.
IPR009009. RlpA-like_DPBB.
[Graphical view]
PfamiPF02015. Glyco_hydro_45. 1 hit.
[Graphical view]
SUPFAMiSSF50685. SSF50685. 1 hit.
PROSITEiPS01140. GLYCOSYL_HYDROL_F45. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P43316-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
ADGRSTRYWD CCKPSCGWAK KAPVNQPVFS CNANFQRITD FDAKSGCEPG
60 70 80 90 100
GVAYSCADQT PWAVNDDFAL GFAATSIAGS NEAGWCCACY ELTFTSGPVA
110 120 130 140 150
GKKMVVQSTS TGGDLGSNHF DLNIPGGGVG IFDGCTPQFG GLPGQRYGGI
160 170 180 190 200
SSRNECDRFP DALKPGCYWR FDWFKNADNP SFSFRQVQCP AELVARTGCR
210
RNDDGNFPAV QIP
Length:213
Mass (Da):22,864
Last modified:November 1, 1995 - v1
Checksum:i24334301BA3BC804
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HD5 X-ray 1.66 A 5-213 [» ]
2ENG X-ray 1.50 A 1-210 [» ]
3ENG X-ray 1.90 A 1-213 [» ]
4ENG X-ray 1.90 A 1-210 [» ]
ProteinModelPortali P43316.
SMRi P43316. Positions 1-213.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P43316.
ChEMBLi CHEMBL1795107.

Protein family/group databases

CAZyi CBM1. Carbohydrate-Binding Module Family 1.
GH45. Glycoside Hydrolase Family 45.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P43316.

Family and domain databases

Gene3Di 2.40.40.10. 1 hit.
InterProi IPR014733. Barwin-like_endoglucanase.
IPR000334. Glyco_hydro_45.
IPR009009. RlpA-like_DPBB.
[Graphical view ]
Pfami PF02015. Glyco_hydro_45. 1 hit.
[Graphical view ]
SUPFAMi SSF50685. SSF50685. 1 hit.
PROSITEi PS01140. GLYCOSYL_HYDROL_F45. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  3. "Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9-A resolution."
    Davies G.J., Tolley S.P., Henrissat B., Hjort C., Schuelein M.
    Biochemistry 34:16210-16220(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  4. "Structure determination and refinement of the Humicola insolens endoglucanase V at 1.5-A resolution."
    Davies G.J., Dodson G.G., Moore M.H., Tolley S.P., Dauter Z., Wilson K.S., Rasmussen G., Schuelein M.
    Acta Crystallogr. D 52:7-17(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

Entry informationi

Entry nameiGUN5_HUMIN
AccessioniPrimary (citable) accession number: P43316
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

External Data

Dasty 3