Probable 1,4-beta-D-glucan cellobiohydrolase A precursor - Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)

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Q2UBM3 (CBHA_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 45. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Probable 1,4-beta-D-glucan cellobiohydrolase A
EC=3.2.1.91

Alternative name(s):
Beta-glucancellobiohydrolase A
Cellobiohydrolase D
Exocellobiohydrolase A
Exoglucanase A

Gene names

Name:	cbhA
Synonyms:	celD
ORF Names:	AO090012000941

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length	455 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 activity	Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Subcellular location	Secreted Probable.
Sequence similarities	Belongs to the glycosyl hydrolase 7 (cellulase C) family.
Sequence caution	The sequence BAC07256.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cellulose 1,4-beta-cellobiosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

Potential

Chain

18 – 455

438

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

PRO_0000393542

Sites

Active site

227

Nucleophile By similarity

Active site

232

Proton donor By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

285

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

227

E → Q in BAC07256. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q2UBM3 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: BE240033EABD0ADB
Show »

FASTA

455

48,135

        10         20         30         40         50         60 
MHQRALLFSA FWTAVQAQQA GTLTAETHPS LTWQKCAAGG TCTEQKGSVV LDSNWRWLHS 

        70         80         90        100        110        120 
VDGSTNCYTG NTWDATLCPD NESCASNCAL DGADYEGTYG VTTSGDALTL QFVTGANIGS 

       130        140        150        160        170        180 
RLYLMADDDE SYQTFNLLNN EFTFDVDASK LPCGLNGAVY FVSMDADGGV AKYSTNKAGA 

       190        200        210        220        230        240 
KYGTGYCDSQ CPRDLKFING QANVEGWEPS DSDKNAGVGG HGSCCPEMDI WEANSISTAY 

       250        260        270        280        290        300 
TPHPCDDTAQ TMCEGDTCGG TYSSERYAGT CDPDGCDFNA YRMGNESFYG PSKLVDSSSP 

       310        320        330        340        350        360 
VTVVTQFITA DGTDSGALSE IKRFYVQGGK VIANAASNVD GVTGNSITAD FCTAQKKAFG 

       370        380        390        400        410        420 
DDDIFAQHGG LQGMGNALSS MVLTLSIWDD HHSSMMWLDS SYPEDADATA PGVARGTCEP 

       430        440        450 
HAGDPEKVES QSGSATVTYS NIKYGPIGST FDAPA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of two cellobiohydrolases from Aspergillus oryzae KBN616." Kitamoto N., Yoshino-Yasuda S. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. Kikuchi H. Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB089437 Genomic DNA. Translation: BAC07256.1. Sequence problems. AP007161 Genomic DNA. Translation: BAE61042.1.
3D structure databases
HSSP	HSSP built from PDB template 1GPI based on UniProtKB Q09431.
ProteinModelPortal	Q2UBM3.
SMR	Q2UBM3. Positions 18-451.
ModBase	Search...
Protein-protein interaction databases
STRING	5062.CADAORAP00006332.
Protein family/group databases
CAZy	GH7. Glycoside Hydrolase Family 7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00006462; CADAORAP00006332; CADAORAG00006462.
KEGG	aor:AOR_1_1654194.
Phylogenomic databases
eggNOG	NOG85664.
HOGENOM	HOG000182210.
OrthoDB	EOG4K3Q4P.
Family and domain databases
Gene3D	2.70.100.10. 1 hit.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR001722. Glyco_hydro_7. [Graphical view]
Pfam	PF00840. Glyco_hydro_7. 1 hit. [Graphical view]
PRINTS	PR00734. GLHYDRLASE7.
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CBHA_ASPOR

Accession

Primary (citable) accession number: Q2UBM3
Secondary accession number(s): Q8NK81

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 20, 2010
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents