Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

Gene

cbhB

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
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 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.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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei235 – 2351NucleophileBy similarity
Active sitei240 – 2401Proton donorBy similarity

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:ATEG_05002
OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
Taxonomic identifieri341663 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000007963 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:ATEG_05002.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 541518Probable 1,4-beta-D-glucan cellobiohydrolase BPRO_0000393549Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi513 ↔ 530By similarity
Disulfide bondi524 ↔ 540By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ0CMT2.
SMRiQ0CMT2. Positions 24-461, 507-541.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini505 – 54137CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 458435CatalyticAdd
BLAST
Regioni459 – 50547Ser/Thr-rich linkerAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000182210.
OMAiRGSCDIS.
OrthoDBiEOG7ZGXCF.

Family and domain databases

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.

Q0CMT2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSTYDIYKK LLLLASFLSA SQAQQVGTSK AEVHPSLTWQ TCTSGGSCTT
60 70 80 90 100
VNGKVVVDAN WRWVHNVDGY NNCYTGNTWD TTLCPDDETC ASNCALEGAD
110 120 130 140 150
YSGTYGVTTS GNSLRLNFVT QASQKNIGSR LYLMEDDSTY KMFKLLNQEF
160 170 180 190 200
TFDVDVSNLP CGLNGAVYFV SMDADGGMAK YPANKAGAKY GTGYCDSQCP
210 220 230 240 250
RDLKFINGMA NVEGWEPSAN DANAGTGNHG SCCAEMDIWE ANSISTAYTP
260 270 280 290 300
HPCDTPGQVM CTGDSCGGTY SSDRYGGTCD PDGCDFNSYR QGNKTFYGPG
310 320 330 340 350
MTVDTKSKIT VVTQFLTNDG TASGTLSEIK RFYVQNGKVI PNSESTWSGV
360 370 380 390 400
SGNSITTAYC NAQKTLFGDT DVFTKHGGME GMGAALAEGM VLVLSLWDDH
410 420 430 440 450
NSNMLWLDSN YPTDKPSTTP GVARGSCDIS SGDPKDVEAN DANAYVVYSN
460 470 480 490 500
IKVGPIGSTF SGSTGGGSSS STTATSKTTT TSATKTTTTT TKTTTTTSAS
510 520 530 540
STSTGGAQHW AQCGGIGWTG PTTCVAPYTC QKQNDYYSQC L
Length:541
Mass (Da):57,294
Last modified:October 17, 2006 - v1
Checksum:iB72B0BA4C5C9C263
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476600 Genomic DNA. Translation: EAU34071.1.
RefSeqiXP_001214180.1. XM_001214180.1.

Genome annotation databases

EnsemblFungiiCADATEAT00005220; CADATEAP00005220; CADATEAG00005220.
GeneIDi4321099.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476600 Genomic DNA. Translation: EAU34071.1.
RefSeqiXP_001214180.1. XM_001214180.1.

3D structure databases

ProteinModelPortaliQ0CMT2.
SMRiQ0CMT2. Positions 24-461, 507-541.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADATEAT00005220; CADATEAP00005220; CADATEAG00005220.
GeneIDi4321099.

Organism-specific databases

EuPathDBiFungiDB:ATEG_05002.

Phylogenomic databases

HOGENOMiHOG000182210.
OMAiRGSCDIS.
OrthoDBiEOG7ZGXCF.

Family and domain databases

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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NIH 2624 / FGSC A1156.

Entry informationi

Entry nameiCBHB_ASPTN
AccessioniPrimary (citable) accession number: Q0CMT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: October 17, 2006
Last modified: June 24, 2015
This is version 38 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

External Data

Dasty 3

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 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.