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Q9UVS9

- CBHA_ASPNG

UniProt

Q9UVS9 - CBHA_ASPNG

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Protein
1,4-beta-D-glucan cellobiohydrolase A
Gene
cbhA, celD
Organism
Aspergillus niger
Status
Reviewed - Annotation score: 3 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 sitei227 – 2271Nucleophile By similarity
Active sitei232 – 2321Proton donor By similarity

GO - Molecular functioni

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

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

CAZyiGH7. Glycoside Hydrolase Family 7.
mycoCLAPiCBH7A_ASPNG.

Names & Taxonomyi

Protein namesi
Recommended name:
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
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

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 prediction
Add
BLAST
Chaini18 – 4524351,4-beta-D-glucan cellobiohydrolase A
PRO_5000056394Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...) Reviewed prediction
Glycosylationi285 – 2851N-linked (GlcNAc...) Reviewed prediction
Glycosylationi335 – 3351N-linked (GlcNAc...) Reviewed prediction
Glycosylationi402 – 4021N-linked (GlcNAc...) Reviewed prediction
Glycosylationi445 – 4451N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Expressioni

Inductioni

Expression is under the control of the xylanolytic transcriptional activator xlnR.2 Publications

Structurei

3D structure databases

ProteinModelPortaliQ9UVS9.
SMRiQ9UVS9. Positions 18-449.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85664.

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.

Q9UVS9-1 [UniParc]FASTAAdd to Basket

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MHQRALLFSA LLTAVRAQQA GTLTEEVHPS LTWQKCTSEG SCTEQSGSVV    50
IDSNWRWTHS VNDSTNCYTG NTWDATLCPD DETCAANCAL DGADYESTYG 100
VTTDGDSLTL KFVTGSNVGS RLYLMDTSDE GYQTFNLLDA EFTFDVDVSN 150
LPCGLNGALY FTAMDADGGV SKYPANKAGA KYGTGYCDSQ CPRDLKFIDG 200
QANVDGWEPS SNNDNTGIGN HGSCCPEMDI WEANKISTAL TPHPCDSSEQ 250
TMCEGNDCGG TYSDDRYGGT CDPDGCDFNP YRMGNDSFYG PGKTIDTGSK 300
MTVVTQFITD GSGSLSEIKR YYVQNGNVIA NADSNISGVT GNSITTDFCT 350
AQKKAFGDED IFAEHNGLAG ISDAMSSMVL ILSLWDDYYA SMEWLDSDYP 400
ENATATDPGV ARGTCDSESG VPATVEGAHP DSSVTFSNIK FGPINSTFSA 450
SA 452
Length:452
Mass (Da):48,258
Last modified:May 1, 2000 - v1
Checksum:i6364A0F4BF7D254F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011V → I in ACT65727. 1 Publication
Sequence conflicti170 – 1701V → A in ACT65727. 1 Publication
Sequence conflicti359 – 3591E → D in ACT65727. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF156268 Genomic DNA. Translation: AAF04491.1.
GQ281319 Genomic DNA. Translation: ACT65727.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF156268 Genomic DNA. Translation: AAF04491.1 .
GQ281319 Genomic DNA. Translation: ACT65727.1 .

3D structure databases

ProteinModelPortali Q9UVS9.
SMRi Q9UVS9. Positions 18-449.
ModBasei Search...

Protein family/group databases

CAZyi GH7. Glycoside Hydrolase Family 7.
mycoCLAPi CBH7A_ASPNG.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG85664.

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. "Two cellobiohydrolase-encoding genes from Aspergillus niger require D-xylose and the xylanolytic transcriptional activator XlnR for their expression."
    Gielkens M.M., Dekkers E., Visser J., de Graaff L.H.
    Appl. Environ. Microbiol. 65:4340-4345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
  2. Hsing-Ren W., Trong-Rong Y.
    Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BCRC 31494.
  3. "Induction, production, repression, and de-repression of exoglucanase synthesis in Aspergillus niger."
    Hanif A., Yasmeen A., Rajoka M.I.
    Bioresour. Technol. 94:311-319(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.

Entry informationi

Entry nameiCBHA_ASPNG
AccessioniPrimary (citable) accession number: Q9UVS9
Secondary accession number(s): C7ENW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: May 1, 2000
Last modified: November 13, 2013
This is version 54 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

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