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O59843

- CBHB_ASPAC

UniProt

O59843 - CBHB_ASPAC

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Protein

1,4-beta-D-glucan cellobiohydrolase B

Gene

cbhB

Organism
Aspergillus aculeatus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei234 – 2341NucleophileBy similarity
Active sitei239 – 2391Proton donorBy similarity

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.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPiCBH7A_ASPAC.

Names & Taxonomyi

Protein namesi
Recommended name:
1,4-beta-D-glucan cellobiohydrolase B (EC:3.2.1.91)
Alternative name(s):
1,4-beta-D-glucan cellobiohydrolase I
Beta-glucancellobiohydrolase B
Exocellobiohydrolase B
Exoglucanase B
Gene namesi
Name:cbhB
Synonyms:cbhI
OrganismiAspergillus aculeatus
Taxonomic identifieri5053 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

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 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 5405181,4-beta-D-glucan cellobiohydrolase BPRO_0000007918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi434 – 4341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi513 ↔ 529By similarity
Disulfide bondi524 ↔ 539By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiO59843.

Structurei

3D structure databases

ProteinModelPortaliO59843.
SMRiO59843. Positions 23-462, 507-540.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini505 – 54036CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 459437CatalyticAdd
BLAST
Regioni460 – 50546Ser/Thr-rich linkerAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

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.

O59843-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVDSFSIYKT ALLLSMLATS NAQQVGTYTA ETHPSLTWQT CSGSGSCTTT
60 70 80 90 100
SGSVVIDANW RWVHEVGGYT NCYSGNTWDS SICSTDTTCA SECALEGATY
110 120 130 140 150
ESTYGVTTSG SSLRLNFVTT ASQKNIGSRL YLLADDSTYE TFKLFNREFT
160 170 180 190 200
FDVDVSNLPC GLNGALYFVS MDADGGVSRF PTNKAGAKYG TGYCDSQCPR
210 220 230 240 250
DLKFIDGQAN IEGWEPSSTD VNAGTGNHGS CCPEMDIWEA NSISSAFTAH
260 270 280 290 300
PCDSVQQTMC TGDTCGGTYS DTTDRYSGTC DPDGCDFNPY RFGNTNFYGP
310 320 330 340 350
GKTVDNSKPF TVVTQFITHD GTDTGTLTEI RRLYVQNGVV IGNGPSTYTA
360 370 380 390 400
ASGNSITESF CKAEKTLFGD TNVFETHGGL SAMGDALGDG MVLVLSLWDD
410 420 430 440 450
HAADMLWLDS DYPTTSCASS PGVARGTCPT TTGNATYVEA NYPNSYVTYS
460 470 480 490 500
NIKFGTLNST YSGTSSGGSS SSSTTLTTKA STSTTSSKTT TTTSKTSTTS
510 520 530 540
SSSTNVAQLY GQCGGQGWTG PTTCASGTCT KQNDYYSQCL
Length:540
Mass (Da):57,099
Last modified:August 1, 1998 - v1
Checksum:i002D7FD28DF194D0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB002821 mRNA. Translation: BAA25183.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB002821 mRNA. Translation: BAA25183.1 .

3D structure databases

ProteinModelPortali O59843.
SMRi O59843. Positions 23-462, 507-540.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPi CBH7A_ASPAC.

Proteomic databases

PRIDEi O59843.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.70.100.10. 1 hit.
InterProi IPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view ]
Pfami PF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view ]
PRINTSi PR00734. GLHYDRLASE7.
ProDomi PD001821. CBD_fun. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00236. fCBD. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEi PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning, nucleotide sequence, and transcriptional analysis of Aspergillus aculeatus No.F-50 cellobiohydrolase I (cbhI) gene."
    Takada G., Kawaguchi T., Sumitani J., Arai M.
    J. Ferment. Bioeng. 85:1-9(1998)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: F-50.
  2. "Overexpression of Aspergillus aculeatus cellobiohydrolase I in Aspergillus oryzae."
    Kanamasa S., Mochizuki M., Takada G., Kawaguchi T., Sumitani J., Araii M.
    J. Biosci. Bioeng. 95:627-629(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCBHB_ASPAC
AccessioniPrimary (citable) accession number: O59843
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: October 29, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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