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Q9C1S9

- GUX6_HUMIN

UniProt

Q9C1S9 - GUX6_HUMIN

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Protein

Exoglucanase-6A

Gene

cel6A

Organism
Humicola insolens (Soft-rot fungus)
Status
Reviewed - 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 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.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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei163 – 1631Substrate3 Publications
Binding sitei165 – 1651Substrate3 Publications
Active sitei252 – 2521Proton donor2 PublicationsPROSITE-ProRule annotation
Binding sitei297 – 2971Substrate3 Publications
Binding sitei300 – 3001Substrate3 Publications
Binding sitei336 – 3361Substrate3 Publications
Binding sitei397 – 3971Substrate3 Publications
Binding sitei425 – 4251Substrate3 Publications
Binding sitei429 – 4291Substrate3 Publications
Active sitei431 – 4311Proton acceptor3 PublicationsPROSITE-ProRule annotation

GO - Molecular functioni

  1. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro

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.
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

  1. extracellular region Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 476460Exoglucanase-6APRO_0000248843Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 50Sequence Analysis
Disulfide bondi44 ↔ 60Sequence Analysis
Glycosylationi144 – 1441O-linked (Man...)1 Publication
Glycosylationi153 – 1531O-linked (Man...)1 Publication
Glycosylationi167 – 1671N-linked (GlcNAc...)4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.4 Publications

Structurei

Secondary structure

1
476
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni119 – 1224
Beta strandi123 – 1253
Helixi129 – 1379
Helixi140 – 1423
Helixi146 – 15510
Beta strandi162 – 1643
Helixi167 – 1693
Turni170 – 1723
Helixi173 – 18614
Beta strandi193 – 1997
Beta strandi209 – 2113
Helixi218 – 2203
Helixi222 – 23918
Turni240 – 2423
Beta strandi245 – 2495
Helixi255 – 2595
Helixi264 – 28320
Beta strandi289 – 2946
Turni298 – 3025
Helixi304 – 32017
Beta strandi327 – 3337
Helixi347 – 3493
Helixi357 – 37014
Beta strandi376 – 3805
Beta strandi385 – 3884
Beta strandi398 – 4025
Beta strandi418 – 4225
Helixi443 – 4464
Helixi462 – 4709

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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-ray1.50A117-157[»]
4I5UX-ray1.22A117-161[»]
ProteinModelPortaliQ9C1S9.
SMRiQ9C1S9. Positions 30-61, 116-476.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9C1S9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 6028CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni200 – 22223Substrate binding loop 13 PublicationsAdd
BLAST
Regioni423 – 46139Substrate binding loop 23 PublicationsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi73 – 786Poly-SerSequence Analysis

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:
EMBL
GenBank
DDBJ
Links Updated
AB048710 Genomic DNA. Translation: BAB39154.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB048710 Genomic DNA. Translation: BAB39154.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BVW X-ray 1.92 A 117-476 [» ]
1GZ1 X-ray 1.90 A 115-476 [» ]
1OC5 X-ray 1.70 A 113-476 [» ]
1OC6 X-ray 1.50 A 113-476 [» ]
1OC7 X-ray 1.11 A 113-476 [» ]
1OCB X-ray 1.75 A/B 115-476 [» ]
1OCJ X-ray 1.30 A 115-476 [» ]
1OCN X-ray 1.31 A 115-476 [» ]
2BVW X-ray 1.70 A/B 115-476 [» ]
4I5R X-ray 1.50 A 117-157 [» ]
4I5U X-ray 1.22 A 117-161 [» ]
ProteinModelPortali Q9C1S9.
SMRi Q9C1S9. Positions 30-61, 116-476.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.
mycoCLAPi CBH6A_HUMIN.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q9C1S9.

Family and domain databases

Gene3Di 3.20.20.40. 1 hit.
InterProi IPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view ]
Pfami PF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view ]
PIRSFi PIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSi PR00733. GLHYDRLASE6.
ProDomi PD001821. CBD_fun. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00236. fCBD. 1 hit.
[Graphical view ]
SUPFAMi SSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEi PS00562. 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 ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and overexpression of the avi2 gene encoding a major cellulase produced by Humicola insolens FERM BP-5977."
    Moriya T., Watanabe M., Sumida N., Okakura K., Murakami T.
    Biosci. Biotechnol. Biochem. 67:1434-1437(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: FERM BP-5977.
  2. "Enzymatic properties of cellulases from Humicola insolens."
    Schuelein M.
    J. Biotechnol. 57:71-81(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  3. "Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding."
    Varrot A., Schuelein M., Davies G.J.
    Biochemistry 38:8884-8891(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 115-476 IN COMPLEX WITH GLUCOSE AND CELLOTETRAOSE, ACTIVE SITE, GLYCOSYLATION AT ASN-167.
  4. "Structure of the Humicola insolens cellobiohydrolase Cel6A D416A mutant in complex with a non-hydrolysable substrate analogue, methyl cellobiosyl-4-thio-beta-cellobioside, at 1.9 A."
    Varrot A., Frandsen T.P., Driguez H., Davies G.J.
    Acta Crystallogr. D 58:2201-2204(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 115-476 OF MUTANT ALA-416 IN COMPLEX WITH SUBSTRATE ANALOG, GLYCOSYLATION AT ASN-167.
  5. "Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens."
    Varrot A., Frandsen T.P., von Ossowski I., Boyer V., Cottaz S., Driguez H., Schuelein M., Davies G.J.
    Structure 11:855-864(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 113-476 OF MUTANT ASN-431 IN COMPLEX WITH SUBSTRATE ANALOGS, GLYCOSYLATION AT ASN-167.
  6. "Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A resolution."
    Varrot A., Hastrup S., Schuelein M., Davies G.J.
    Biochem. J. 337:297-304(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 117-476, FUNCTION, SUBUNIT, GLYCOSYLATION AT THR-144; SER-153 AND ASN-167.

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: October 1, 2014
This is version 59 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