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Protein

Endoglucanase 1

Gene

CEL7B

Organism
Humicola insolens (Soft-rot fungus)
Status
Reviewed-Annotation score: 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 sitei197 – 1971Nucleophile
Active sitei202 – 2021Proton 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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17623.

Protein family/group databases

CAZyiGH7. Glycoside Hydrolase Family 7.
mycoCLAPiEGL7B_HUMIN.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase 1 (EC:3.2.1.4)
Alternative name(s):
Cellulase 1
Endo-1,4-beta-glucanase 1
Endoglucanase I
Gene namesi
Name:CEL7B
OrganismiHumicola insolens (Soft-rot fungus)
Taxonomic identifieri34413 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei8280. Hum in Cellulase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 402402Endoglucanase 1PRO_0000184057Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid
Disulfide bondi18 ↔ 24
Disulfide bondi51 ↔ 73
Disulfide bondi63 ↔ 69
Glycosylationi89 – 891N-linked (GlcNAc...)
Disulfide bondi140 ↔ 365
Disulfide bondi172 ↔ 195
Disulfide bondi176 ↔ 194
Disulfide bondi215 ↔ 234
Disulfide bondi223 ↔ 228
Disulfide bondi239 ↔ 315
Glycosylationi247 – 2471N-linked (GlcNAc...)

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
402
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 198Combined sources
Turni20 – 223Combined sources
Beta strandi23 – 3311Combined sources
Helixi35 – 373Combined sources
Beta strandi40 – 423Combined sources
Turni60 – 623Combined sources
Helixi66 – 727Combined sources
Beta strandi73 – 753Combined sources
Helixi81 – 844Combined sources
Beta strandi86 – 894Combined sources
Beta strandi92 – 987Combined sources
Beta strandi108 – 1125Combined sources
Beta strandi116 – 1194Combined sources
Beta strandi127 – 1348Combined sources
Beta strandi143 – 1497Combined sources
Turni153 – 1564Combined sources
Helixi164 – 1674Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi197 – 2037Combined sources
Beta strandi208 – 2136Combined sources
Beta strandi215 – 2195Combined sources
Beta strandi221 – 2233Combined sources
Helixi225 – 2284Combined sources
Beta strandi232 – 2343Combined sources
Helixi243 – 2464Combined sources
Beta strandi250 – 2556Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi266 – 2749Combined sources
Beta strandi280 – 28910Combined sources
Beta strandi292 – 2943Combined sources
Beta strandi308 – 3103Combined sources
Helixi312 – 3176Combined sources
Helixi321 – 3255Combined sources
Helixi328 – 33811Combined sources
Beta strandi340 – 3478Combined sources
Turni350 – 3545Combined sources
Helixi355 – 3584Combined sources
Helixi360 – 3623Combined sources
Turni367 – 3704Combined sources
Helixi372 – 3787Combined sources
Beta strandi383 – 39311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A39X-ray2.20A2-402[»]
1DYMX-ray1.75A2-402[»]
1OJIX-ray2.15A2-402[»]
1OJJX-ray1.40A/B2-402[»]
1OJKX-ray1.50A/B2-402[»]
2A39X-ray2.20A/B2-398[»]
ProteinModelPortaliP56680.
SMRiP56680. Positions 1-398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56680.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

P56680-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
QKPGETKEVH PQLTTFRCTK RGGCKPATNF IVLDSLSHPI HRAEGLGPGG
60 70 80 90 100
CGDWGNPPPK DVCPDVESCA KNCIMEGIPD YSQYGVTTNG TSLRLQHILP
110 120 130 140 150
DGRVPSPRVY LLDKTKRRYE MLHLTGFEFT FDVDATKLPC GMNSALYLSE
160 170 180 190 200
MHPTGAKSKY NPGGAYYGTG YCDAQCFVTP FINGLGNIEG KGSCCNEMDI
210 220 230 240 250
WEANSRASHV APHTCNKKGL YLCEGEECAF EGVCDKNGCG WNNYRVNVTD
260 270 280 290 300
YYGRGEEFKV NTLKPFTVVT QFLANRRGKL EKIHRFYVQD GKVIESFYTN
310 320 330 340 350
KEGVPYTNMI DDEFCEATGS RKYMELGATQ GMGEALTRGM VLAMSIWWDQ
360 370 380 390 400
GGNMEWLDHG EAGPCAKGEG APSNIVQVEP FPEVTYTNLR WGEIGSTYQE

LQ
Length:402
Mass (Da):44,577
Last modified:July 15, 1999 - v1
Checksum:iE0C6D31375D1635F
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A39X-ray2.20A2-402[»]
1DYMX-ray1.75A2-402[»]
1OJIX-ray2.15A2-402[»]
1OJJX-ray1.40A/B2-402[»]
1OJKX-ray1.50A/B2-402[»]
2A39X-ray2.20A/B2-398[»]
ProteinModelPortaliP56680.
SMRiP56680. Positions 1-398.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei8280. Hum in Cellulase.
CAZyiGH7. Glycoside Hydrolase Family 7.
mycoCLAPiEGL7B_HUMIN.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17623.

Miscellaneous databases

EvolutionaryTraceiP56680.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SUPFAMiSSF49899. SSF49899. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Oligosaccharide specificity of a family 7 endoglucanase: insertion of potential sugar-binding subsites."
    Davies G.J., Ducros V., Lewis R.J., Borchert T.V., Schuelein M.
    J. Biotechnol. 57:91-100(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT TRP-37/TRP-39.
  2. "Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2 A resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate."
    MacKenzie L.F., Sulzenbacher G., Divne C., Jones T.A., Woeldike H.F., Schuelein M., Withers S.G., Davies G.J.
    Biochem. J. 335:409-416(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), MUTAGENESIS.

Entry informationi

Entry nameiGUN1_HUMIN
AccessioniPrimary (citable) accession number: P56680
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: January 7, 2015
This is version 83 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

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 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.