Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 disaccharide 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)DescriptionActionsGraphical viewLength
Active sitei197Nucleophile1
Active sitei202Proton donor1

GO - Molecular functioni

GO - Biological processi

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei8280. Hum in Cellulase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001840571 – 402Endoglucanase 1Add BLAST402

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Pyrrolidone carboxylic acid1
Disulfide bondi18 ↔ 24
Disulfide bondi51 ↔ 73
Disulfide bondi63 ↔ 69
Glycosylationi89N-linked (GlcNAc...)1
Disulfide bondi140 ↔ 365
Disulfide bondi172 ↔ 195
Disulfide bondi176 ↔ 194
Disulfide bondi215 ↔ 234
Disulfide bondi223 ↔ 228
Disulfide bondi239 ↔ 315
Glycosylationi247N-linked (GlcNAc...)1

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1402
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 19Combined sources8
Turni20 – 22Combined sources3
Beta strandi23 – 33Combined sources11
Helixi35 – 37Combined sources3
Beta strandi40 – 42Combined sources3
Turni60 – 62Combined sources3
Helixi66 – 72Combined sources7
Beta strandi73 – 75Combined sources3
Helixi81 – 84Combined sources4
Beta strandi86 – 89Combined sources4
Beta strandi92 – 98Combined sources7
Beta strandi108 – 112Combined sources5
Beta strandi116 – 119Combined sources4
Beta strandi127 – 134Combined sources8
Beta strandi143 – 149Combined sources7
Turni153 – 156Combined sources4
Helixi164 – 167Combined sources4
Beta strandi180 – 182Combined sources3
Beta strandi192 – 194Combined sources3
Beta strandi197 – 203Combined sources7
Beta strandi208 – 213Combined sources6
Beta strandi215 – 219Combined sources5
Beta strandi221 – 223Combined sources3
Helixi225 – 228Combined sources4
Beta strandi232 – 234Combined sources3
Helixi243 – 246Combined sources4
Beta strandi250 – 255Combined sources6
Beta strandi258 – 261Combined sources4
Beta strandi266 – 274Combined sources9
Beta strandi280 – 289Combined sources10
Beta strandi292 – 294Combined sources3
Beta strandi308 – 310Combined sources3
Helixi312 – 317Combined sources6
Helixi321 – 325Combined sources5
Helixi328 – 338Combined sources11
Beta strandi340 – 347Combined sources8
Turni350 – 354Combined sources5
Helixi355 – 358Combined sources4
Helixi360 – 362Combined sources3
Turni367 – 370Combined sources4
Helixi372 – 378Combined sources7
Beta strandi383 – 393Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56680.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

CDDicd07999. GH7_CBH_EG. 1 hit.
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
PDB 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.
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

CDDicd07999. GH7_CBH_EG. 1 hit.
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...

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: November 30, 2016
This is version 89 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

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.