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Protein

Endoglucanase-6B

Gene

cel6B

Organism
Humicola insolens (Soft-rot fungus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Plays a central role in the recycling of plant biomass. 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei52SubstrateBy similarity1
Binding sitei54SubstrateBy similarity1
Active sitei92Proton donor1 PublicationPROSITE-ProRule annotation1
Active sitei139Proton donorPROSITE-ProRule annotation1 Publication1
Binding sitei183SubstrateBy similarity1
Binding sitei186SubstrateBy similarity1
Binding sitei222SubstrateBy similarity1
Binding sitei282SubstrateBy similarity1
Binding sitei310SubstrateBy similarity1
Binding sitei314SubstrateBy similarity1

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-17625.

Protein family/group databases

CAZyiGH6. Glycoside Hydrolase Family 6.
mycoCLAPiEGL6B_HUMIN.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase-6B (EC:3.2.1.4)
Alternative name(s):
Cellulase 6B
Endo-1,4-beta-glucanase 6B
Gene namesi
Name:cel6B1 Publication
OrganismiHumicola insolens (Soft-rot fungus)
Taxonomic identifieri34413 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002488421 – 348Endoglucanase-6BAdd BLAST348

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1348
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni5 – 8Combined sources4
Helixi15 – 29Combined sources15
Turni30 – 32Combined sources3
Helixi34 – 46Combined sources13
Beta strandi51 – 53Combined sources3
Helixi57 – 59Combined sources3
Helixi60 – 74Combined sources15
Beta strandi79 – 85Combined sources7
Helixi93 – 95Combined sources3
Beta strandi99 – 101Combined sources3
Helixi104 – 106Combined sources3
Helixi108 – 115Combined sources8
Helixi117 – 126Combined sources10
Beta strandi132 – 136Combined sources5
Helixi140 – 146Combined sources7
Helixi150 – 169Combined sources20
Beta strandi175 – 180Combined sources6
Helixi184 – 187Combined sources4
Helixi190 – 192Combined sources3
Helixi193 – 207Combined sources15
Beta strandi215 – 218Combined sources4
Helixi233 – 235Combined sources3
Helixi243 – 255Combined sources13
Turni256 – 258Combined sources3
Beta strandi262 – 266Combined sources5
Beta strandi268 – 271Combined sources4
Beta strandi286 – 289Combined sources4
Beta strandi294 – 296Combined sources3
Beta strandi303 – 307Combined sources5
Beta strandi316 – 318Combined sources3
Helixi332 – 340Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DYSX-ray1.60A/B1-348[»]
ProteinModelPortaliQ7SIG5.
SMRiQ7SIG5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIG5.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 6 (cellulase B) family.Sequence analysis

Family and domain databases

Gene3Di3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
SUPFAMiSSF51989. SSF51989. 1 hit.
PROSITEiPS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7SIG5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QSGNPFSGRT LLVNSDYSSK LDQTRQAFLS RGDQTNAAKV KYVQEKVGTF
60 70 80 90 100
YWISNIFLLR DIDVAIQNAR AAKARGENPI VGLVLYNLPD RDCSAGESSG
110 120 130 140 150
ELKLSQNGLN RYKNEYVNPF AQKLKAASDV QFAVILEPDA IGNMVTGTSA
160 170 180 190 200
FCRNARGPQQ EAIGYAISQL QASHIHLYLD VANGGWLGWA DKLEPTAQEV
210 220 230 240 250
ATILQKAGNN AKIRGFSSNV SNYNPYSTSN PPPYTSGSPS PDESRYATNI
260 270 280 290 300
ANAMRQRGLP TQFIIDQSRV ALSGARSEWG QWCNVNPAGF GQPFTTNTNN
310 320 330 340
PNVDAIVWVK PGGESDGQCG MGGAPAAGMW FDAYAQMLTQ NAHDEIAR
Length:348
Mass (Da):37,753
Last modified:December 15, 2003 - v1
Checksum:i5F1E4A4367402E54
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DYSX-ray1.60A/B1-348[»]
ProteinModelPortaliQ7SIG5.
SMRiQ7SIG5.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH6. Glycoside Hydrolase Family 6.
mycoCLAPiEGL6B_HUMIN.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17625.

Miscellaneous databases

EvolutionaryTraceiQ7SIG5.

Family and domain databases

Gene3Di3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
SUPFAMiSSF51989. SSF51989. 1 hit.
PROSITEiPS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUN6_HUMIN
AccessioniPrimary (citable) accession number: Q7SIG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: December 15, 2003
Last modified: November 30, 2016
This is version 53 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.