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Protein

Exoglucanase-6A

Gene

cel6A

Organism
Humicola insolens (Soft-rot fungus)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

Catalytic activityi

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei163Substrate3 Publications1
Binding sitei165Substrate3 Publications1
Active sitei252Proton donorPROSITE-ProRule annotation2 Publications1
Binding sitei297Substrate3 Publications1
Binding sitei300Substrate3 Publications1
Binding sitei336Substrate3 Publications1
Binding sitei397Substrate3 Publications1
Binding sitei425Substrate3 Publications1
Binding sitei429Substrate3 Publications1
Active sitei431Proton acceptorPROSITE-ProRule annotation3 Publications1

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

BRENDAi3.2.1.91. 2710.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.
mycoCLAPiCBH6A_HUMIN.

Names & Taxonomyi

Protein namesi
Recommended name:
Exoglucanase-6A (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase 6A
Avicelase 2
Beta-glucancellobiohydrolase 6A
Exocellobiohydrolase 6A
Gene namesi
Name:cel6A4 Publications
Synonyms:avi2Imported
OrganismiHumicola insolens (Soft-rot fungus)
Taxonomic identifieri34413 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_000024884317 – 476Exoglucanase-6AAdd BLAST460

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi33 ↔ 50Sequence analysis
Disulfide bondi44 ↔ 60Sequence analysis
Glycosylationi144O-linked (Man...)1 Publication1
Glycosylationi153O-linked (Man...)1 Publication1
Glycosylationi167N-linked (GlcNAc...)4 Publications1

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.4 Publications

Structurei

Secondary structure

1476
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni119 – 122Combined sources4
Beta strandi123 – 125Combined sources3
Helixi129 – 137Combined sources9
Helixi140 – 142Combined sources3
Helixi146 – 155Combined sources10
Beta strandi162 – 164Combined sources3
Helixi167 – 169Combined sources3
Turni170 – 172Combined sources3
Helixi173 – 186Combined sources14
Beta strandi193 – 199Combined sources7
Beta strandi209 – 211Combined sources3
Helixi218 – 220Combined sources3
Helixi222 – 239Combined sources18
Turni240 – 242Combined sources3
Beta strandi245 – 249Combined sources5
Helixi255 – 259Combined sources5
Helixi264 – 283Combined sources20
Beta strandi289 – 294Combined sources6
Turni298 – 302Combined sources5
Helixi304 – 320Combined sources17
Beta strandi327 – 333Combined sources7
Helixi347 – 349Combined sources3
Helixi357 – 370Combined sources14
Beta strandi376 – 380Combined sources5
Beta strandi385 – 388Combined sources4
Beta strandi398 – 402Combined sources5
Beta strandi418 – 422Combined sources5
Helixi443 – 446Combined sources4
Helixi462 – 470Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BVWX-ray1.92A117-476[»]
1GZ1X-ray1.90A115-476[»]
1OC5X-ray1.70A113-476[»]
1OC6X-ray1.50A113-476[»]
1OC7X-ray1.11A113-476[»]
1OCBX-ray1.75A/B115-476[»]
1OCJX-ray1.30A115-476[»]
1OCNX-ray1.31A115-476[»]
2BVWX-ray1.70A/B115-476[»]
4I5RX-ray1.50A117-161[»]
4I5UX-ray1.22A117-161[»]
ProteinModelPortaliQ9C1S9.
SMRiQ9C1S9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9C1S9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 60CBM1PROSITE-ProRule annotationAdd BLAST28

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni200 – 222Substrate binding loop 13 PublicationsAdd BLAST23
Regioni423 – 461Substrate binding loop 23 PublicationsAdd BLAST39

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi73 – 78Poly-SerSequence analysis6

Sequence similaritiesi

Belongs to the glycosyl hydrolase 6 (cellulase A) family.Sequence analysis
Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9C1S9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKFFLTAAF AAAALAAPVV EERQNCAPTW GQCGGIGFNG PTCCQSGSTC
60 70 80 90 100
VKQNDWYSQC LPGSQVTTTS TTSTSSSSTT SRATSTTRTG GVTSITTAPT
110 120 130 140 150
RTVTIPGGAT TTASYNGNPF EGVQLWANNY YRSEVHTLAI PQITDPALRA
160 170 180 190 200
AASAVAEVPS FQWLDRNVTV DTLLVETLSE IRAANQAGAN PPYAAQIVVY
210 220 230 240 250
DLPDRDCAAA ASNGEWAIAN NGANNYKGYI NRIREILISF SDVRTILVIE
260 270 280 290 300
PDSLANMVTN MNVAKCSGAA STYRELTIYA LKQLDLPHVA MYMDAGHAGW
310 320 330 340 350
LGWPANIQPA AELFAKIYED AGKPRAVRGL ATNVANYNAW SISSPPPYTS
360 370 380 390 400
PNPNYDEKHY IEAFRPLLEA RGFPAQFIVD QGRSGKQPTG QKEWGHWCNA
410 420 430 440 450
IGTGFGMRPT ANTGHQYVDA FVWVKPGGEC DGTSDTTAAR YDYHCGLEDA
460 470
LKPAPEAGQW FQAYFEQLLR NANPPF
Length:476
Mass (Da):51,276
Last modified:June 1, 2001 - v1
Checksum:iD2B0054F1381E653
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB048710 Genomic DNA. Translation: BAB39154.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB048710 Genomic DNA. Translation: BAB39154.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BVWX-ray1.92A117-476[»]
1GZ1X-ray1.90A115-476[»]
1OC5X-ray1.70A113-476[»]
1OC6X-ray1.50A113-476[»]
1OC7X-ray1.11A113-476[»]
1OCBX-ray1.75A/B115-476[»]
1OCJX-ray1.30A115-476[»]
1OCNX-ray1.31A115-476[»]
2BVWX-ray1.70A/B115-476[»]
4I5RX-ray1.50A117-161[»]
4I5UX-ray1.22A117-161[»]
ProteinModelPortaliQ9C1S9.
SMRiQ9C1S9.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.
mycoCLAPiCBH6A_HUMIN.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.91. 2710.

Miscellaneous databases

EvolutionaryTraceiQ9C1S9.
PROiQ9C1S9.

Family and domain databases

Gene3Di3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUX6_HUMIN
AccessioniPrimary (citable) accession number: Q9C1S9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 67 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.