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Protein

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

Gene

cbhB

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

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:ACLA_085260
OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Taxonomic identifieri344612 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006701 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:ACLA_085260.

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_000039354627 – 539Probable 1,4-beta-D-glucan cellobiohydrolase BAdd BLAST513

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi90N-linked (GlcNAc...)Sequence analysis1
Glycosylationi296N-linked (GlcNAc...)Sequence analysis1
Glycosylationi495N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi511 ↔ 528By similarity
Disulfide bondi522 ↔ 538By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiA1CU44.

Structurei

3D structure databases

ProteinModelPortaliA1CU44.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini503 – 539CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni27 – 461CatalyticAdd BLAST435
Regioni462 – 503Thr-rich linkerAdd BLAST42

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000182210.
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.

A1CU44-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPSTISYRI YKNALFFAAL FGAVQAQKVG TSKAEVHPSM AWQTCAADGT
60 70 80 90 100
CTTKNGKVVI DANWRWVHDV KGYTNCYTGN TWNAELCPDN ESCAENCALE
110 120 130 140 150
GADYAATYGA TTSGNALSLK FVTQSQQKNI GSRLYMMKDD NTYETFKLLN
160 170 180 190 200
QEFTFDVDVS NLPCGLNGAL YFVSMDADGG LSRYTGNEAG AKYGTGYCDS
210 220 230 240 250
QCPRDLKFIN GLANVEGWTP SSSDANAGNG GHGSCCAEMD IWEANSISTA
260 270 280 290 300
YTPHPCDTPG QAMCNGDSCG GTYSSDRYGG TCDPDGCDFN SYRQGNKSFY
310 320 330 340 350
GPGMTVDTKK KMTVVTQFLT NDGTATGTLS EIKRFYVQDG KVIANSESTW
360 370 380 390 400
PNLGGNSLTN DFCKAQKTVF GDMDTFSKHG GMEGMGAALA EGMVLVMSLW
410 420 430 440 450
DDHNSNMLWL DSNSPTTGTS TTPGVARGSC DISSGDPKDL EANHPDASVV
460 470 480 490 500
YSNIKVGPIG STFNSGGSNP GGSTTTTKPA TSTTTTKATT TATTNTTGPT
510 520 530
GTGVAQPWAQ CGGIGYSGPT QCAAPYTCTK QNDYYSQCL
Length:539
Mass (Da):57,042
Last modified:January 23, 2007 - v1
Checksum:i27D7BD8E58C17687
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027060 Genomic DNA. Translation: EAW06831.1.
RefSeqiXP_001268257.1. XM_001268256.1.

Genome annotation databases

EnsemblFungiiCADACLAT00007517; CADACLAP00007326; CADACLAG00007517.
GeneIDi4699868.
KEGGiact:ACLA_085260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027060 Genomic DNA. Translation: EAW06831.1.
RefSeqiXP_001268257.1. XM_001268256.1.

3D structure databases

ProteinModelPortaliA1CU44.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiA1CU44.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADACLAT00007517; CADACLAP00007326; CADACLAG00007517.
GeneIDi4699868.
KEGGiact:ACLA_085260.

Organism-specific databases

EuPathDBiFungiDB:ACLA_085260.

Phylogenomic databases

HOGENOMiHOG000182210.
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_ASPCL
AccessioniPrimary (citable) accession number: A1CU44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 46 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

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.