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A1CE97

- CBHA_ASPCL

UniProt

A1CE97 - CBHA_ASPCL

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Protein

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

Gene
cbhA, celD, ACLA_088870
Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Status
Reviewed - 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 sitei226 – 2261Nucleophile By similarity
Active sitei231 – 2311Proton donor By similarity

GO - Molecular functioni

  1. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC

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

Names & Taxonomyi

Protein namesi
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 namesi
Name:cbhA
Synonyms:celD
ORF Names:ACLA_088870
OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Taxonomic identifieri344612 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006701: Unassembled WGS sequence

Subcellular locationi

Secreted Inferred

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed predictionAdd
BLAST
Chaini18 – 453436Probable 1,4-beta-D-glucan cellobiohydrolase APRO_0000393538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi284 – 2841N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5057.CADACLAP00008198.

Structurei

3D structure databases

ProteinModelPortaliA1CE97.
SMRiA1CE97. Positions 18-450.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85664.
HOGENOMiHOG000182210.
OMAiNWSKCTS.
OrthoDBiEOG7ZGXCF.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A1CE97-1 [UniParc]FASTAAdd to Basket

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MYQRALLFSA LATAVSAQQV GTQKAEVHPA LTWQKCTAAG SCTDQKGSVV    50
IDANWRWLHS TEDTTNCYTG NEWNAELCPD NEACAKNCAL DGADYSGTYG 100
VTADGSSLKL NFVTSANVGS RLYLMEDDET YQMFNLLNNE FTFDVDVSNL 150
PCGLNGALYF VSMDADGGLS KYPGNKAGAK YGTGYCDSQC PRDLKFINGE 200
ANVEGWKPSD NDKNAGVGGY GSCCPEMDIW EANSISTAYT PHPCDGMEQT 250
RCDGNDCGGT YSSTRYAGTC DPDGCDFNSF RMGNESFYGP GGLVDTKSPI 300
TVVTQFVTAG GTDSGALKEI RRVYVQGGKV IGNSASNVAG VEGDSITSDF 350
CTAQKKAFGD EDIFSKHGGL EGMGKALNKM ALIVSIWDDH ASSMMWLDST 400
YPVDADASTP GVARGTCEHG LGDPETVESQ HPDASVTFSN IKFGPIGSTY 450
KSV 453
Length:453
Mass (Da):48,214
Last modified:January 23, 2007 - v1
Checksum:i472F3E0D782C2396
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS027052 Genomic DNA. Translation: EAW11196.1.
RefSeqiXP_001272622.1. XM_001272621.1.

Genome annotation databases

EnsemblFungiiCADACLAT00008408; CADACLAP00008198; CADACLAG00008408.
GeneIDi4704945.
KEGGiact:ACLA_088870.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS027052 Genomic DNA. Translation: EAW11196.1 .
RefSeqi XP_001272622.1. XM_001272621.1.

3D structure databases

ProteinModelPortali A1CE97.
SMRi A1CE97. Positions 18-450.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5057.CADACLAP00008198.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADACLAT00008408 ; CADACLAP00008198 ; CADACLAG00008408 .
GeneIDi 4704945.
KEGGi act:ACLA_088870.

Phylogenomic databases

eggNOGi NOG85664.
HOGENOMi HOG000182210.
OMAi NWSKCTS.
OrthoDBi EOG7ZGXCF.

Family and domain databases

Gene3Di 2.70.100.10. 1 hit.
InterProi IPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view ]
Pfami PF00840. Glyco_hydro_7. 1 hit.
[Graphical view ]
PRINTSi PR00734. GLHYDRLASE7.
SUPFAMi SSF49899. SSF49899. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Entry informationi

Entry nameiCBHA_ASPCL
AccessioniPrimary (citable) accession number: A1CE97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 32 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

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

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