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Protein

Probable 1,4-beta-D-glucan cellobiohydrolase B

Gene

cbhB

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei238NucleophileBy similarity1
Active sitei243Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

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.
GH7. Glycoside Hydrolase Family 7.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 1,4-beta-D-glucan cellobiohydrolase B (EC:3.2.1.91)
Alternative name(s):
Beta-glucancellobiohydrolase B
Exocellobiohydrolase B
Exoglucanase B
Gene namesi
Name:cbhB
ORF Names:AFUA_6G11610
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiFungiDB:Afu6g11610.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000039354827 – 532Probable 1,4-beta-D-glucan cellobiohydrolase BAdd BLAST506

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi296N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi504 ↔ 521By similarity
Disulfide bondi515 ↔ 531By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Inductioni

Expressed at high levels in the presence of carboxymethylcellulose and repressed in the presence of glucose.1 Publication

Structurei

Secondary structure

1532
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi42 – 45Combined sources4
Beta strandi51 – 54Combined sources4
Beta strandi57 – 60Combined sources4
Helixi62 – 64Combined sources3
Beta strandi67 – 69Combined sources3
Beta strandi75 – 78Combined sources4
Turni84 – 86Combined sources3
Helixi90 – 96Combined sources7
Beta strandi97 – 99Combined sources3
Helixi104 – 108Combined sources5
Beta strandi110 – 113Combined sources4
Beta strandi116 – 130Combined sources15
Beta strandi132 – 139Combined sources8
Beta strandi151 – 158Combined sources8
Beta strandi166 – 173Combined sources8
Turni177 – 183Combined sources7
Helixi190 – 193Combined sources4
Beta strandi207 – 209Combined sources3
Beta strandi231 – 235Combined sources5
Beta strandi238 – 244Combined sources7
Beta strandi249 – 254Combined sources6
Beta strandi256 – 260Combined sources5
Beta strandi262 – 265Combined sources4
Helixi266 – 269Combined sources4
Beta strandi279 – 282Combined sources4
Turni291 – 295Combined sources5
Beta strandi299 – 301Combined sources3
Beta strandi304 – 307Combined sources4
Beta strandi312 – 320Combined sources9
Beta strandi329 – 338Combined sources10
Beta strandi341 – 344Combined sources4
Beta strandi356 – 358Combined sources3
Helixi360 – 370Combined sources11
Helixi375 – 378Combined sources4
Helixi381 – 391Combined sources11
Beta strandi393 – 401Combined sources9
Turni403 – 407Combined sources5
Helixi408 – 411Combined sources4
Beta strandi412 – 415Combined sources4
Turni423 – 425Combined sources3
Helixi437 – 443Combined sources7
Beta strandi448 – 458Combined sources11
Turni459 – 464Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4V1ZX-ray1.78A28-466[»]
4V20X-ray1.50A28-466[»]
ProteinModelPortaliQ4WM08.
SMRiQ4WM08.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini496 – 532CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni27 – 461CatalyticAdd BLAST435
Regioni462 – 496Thr-rich linkerAdd BLAST35

Sequence similaritiesi

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000182210.
InParanoidiQ4WM08.
KOiK01225.
OMAiRGSCDIS.
OrthoDBiEOG092C1XF1.

Family and domain databases

CDDicd07999. GH7_CBH_EG. 1 hit.
Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q4WM08-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLASTFSYRM YKTALILAAL LGSGQAQQVG TSQAEVHPSM TWQSCTAGGS
60 70 80 90 100
CTTNNGKVVI DANWRWVHKV GDYTNCYTGN TWDTTICPDD ATCASNCALE
110 120 130 140 150
GANYESTYGV TASGNSLRLN FVTTSQQKNI GSRLYMMKDD STYEMFKLLN
160 170 180 190 200
QEFTFDVDVS NLPCGLNGAL YFVAMDADGG MSKYPTNKAG AKYGTGYCDS
210 220 230 240 250
QCPRDLKFIN GQANVEGWQP SSNDANAGTG NHGSCCAEMD IWEANSISTA
260 270 280 290 300
FTPHPCDTPG QVMCTGDACG GTYSSDRYGG TCDPDGCDFN SFRQGNKTFY
310 320 330 340 350
GPGMTVDTKS KFTVVTQFIT DDGTSSGTLK EIKRFYVQNG KVIPNSESTW
360 370 380 390 400
TGVSGNSITT EYCTAQKSLF QDQNVFEKHG GLEGMGAALA QGMVLVMSLW
410 420 430 440 450
DDHSANMLWL DSNYPTTASS TTPGVARGTC DISSGVPADV EANHPDAYVV
460 470 480 490 500
YSNIKVGPIG STFNSGGSNP GGGTTTTTTT QPTTTTTTAG NPGGTGVAQH
510 520 530
YGQCGGIGWT GPTTCASPYT CQKLNDYYSQ CL
Length:532
Mass (Da):56,457
Last modified:July 5, 2005 - v1
Checksum:i03EBC7D15A5EAE78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000006 Genomic DNA. Translation: EAL89006.1.
RefSeqiXP_751044.1. XM_745951.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00002184; CADAFUAP00002184; CADAFUAG00002184.
GeneIDi3508349.
KEGGiafm:AFUA_6G11610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000006 Genomic DNA. Translation: EAL89006.1.
RefSeqiXP_751044.1. XM_745951.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4V1ZX-ray1.78A28-466[»]
4V20X-ray1.50A28-466[»]
ProteinModelPortaliQ4WM08.
SMRiQ4WM08.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00002184; CADAFUAP00002184; CADAFUAG00002184.
GeneIDi3508349.
KEGGiafm:AFUA_6G11610.

Organism-specific databases

EuPathDBiFungiDB:Afu6g11610.

Phylogenomic databases

HOGENOMiHOG000182210.
InParanoidiQ4WM08.
KOiK01225.
OMAiRGSCDIS.
OrthoDBiEOG092C1XF1.

Family and domain databases

CDDicd07999. GH7_CBH_EG. 1 hit.
Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBHB_ASPFU
AccessioniPrimary (citable) accession number: Q4WM08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: July 5, 2005
Last modified: November 30, 2016
This is version 75 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, Complete proteome, Reference proteome

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.