Probable alpha-glucuronidase A precursor - Aspergillus niger

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Q96WX9 (AGUA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 39. 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

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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 alpha-glucuronidase A
EC=3.2.1.139

Alternative name(s):
Alpha-glucosiduronase A

Gene names

Name:

aguA

Organism

Aspergillus niger

Taxonomic identifier

Taxonomic lineage

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

Protein attributes

Sequence length	841 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Alpha-glucuronidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases 4-O-methylglucuronic acid from xylan By similarity.
Catalytic activity	An alpha-D-glucuronoside + H₂O = an alcohol + D-glucuronate.
Subcellular location	Secreted By similarity.
Induction	Expressed in the presence of D-xylose and L-arabinose and at very low level in the presence of D-glucuronic acid. Expression is under the control of the xylanolytic transcriptional activator xlnR and the carbon catabolite repressor creA. Ref.1
Sequence similarities	Belongs to the glycosyl hydrolase 67 family.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha-glucuronidase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

20

Potential

Chain

821

Probable alpha-glucuronidase A

PRO_5000066287

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q96WX9 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: BAA43615A2B89B73
Show »

841

93,950

        10         20         30         40         50         60 
MRGLNLFQLI LALLLSMVAA EDGYDGWLRY APVSCDLRCR QALPSHVVLL NSTKGSPIET 

        70         80         90        100        110        120 
AGRELKAGFQ SILSTNLTSR PFQCNSSTSI LVATLDEYRQ RCRDINVPEL DPDGFWLQSE 

       130        140        150        160        170        180 
GDTVRILGKD ARGALYGAYE YLAMVAQRNF SRVAYATSPH APIRWVNQWD NMDGSIERGY 

       190        200        210        220        230        240 
GGASIFFKDG TVVEDMAPVE QYARLLASIR INAIVVNNVN ANATLLLPEN MKGLGRIADA 

       250        260        270        280        290        300 
CRPYGVQIGI SLNFASPEDL GGLNTYDPLD PGVIAWWQNI TDSLYTYVPD MAGYLVKADS 

       310        320        330        340        350        360 
EGQPGPDTYN RTLSQGANLF ARALQPYGGV LMYRAFVYDD NLNESDWKAD RAKAAVEYFK 

       370        380        390        400        410        420 
DLDGQFEENV VIQIKYGPID FQVREPTSPL FANLYHTNTA IELEVSQEYL GQQCHLVYLP 

       430        440        450        460        470        480 
PLWKTVLDFD LRVDHKPSMV RDIISGQRFN RTLGGWAAVV NVGTNRTWLG SHLAMSNLYA 

       490        500        510        520        530        540 
YGRLAWSPTD ESEQILEDWT RLTFGQNHHV INTISDMSMT SWPAYENYTG NLGIQTLTDI 

       550        560        570        580        590        600 
LYTHYGPNPA TQDNNGWGQW TRADHDSVGM DRTIRNGTGY TGQYPEEVAR VYESLESTPD 

       610        620        630        640        650        660 
DLVLWFHHVP WTHRLHSGVT VIQHFYNAHY AGAEAAHGFV RQWESLEGLI DRERYEAMRS 

       670        680        690        700        710        720 
RLVYQAGHSI VWRDAINNFY YNMTGIPDVA GRVGHHPWRI EAESMRLDGY QTYTVSPFEA 

       730        740        750        760        770        780 
ASNTTAIITT SNSTTGTART SIKAPSGVYD IGVNYYDLYG GQSKWTLSVG DKVVGQWLGD 

       790        800        810        820        830        840 
MEHNSLGHTP SIYLDGHSAT RITFHGVGIR QGDQLKIVGE ANGVEPAPLD YIVLLPPGLV 


D

References

[1]	"Regulation of the a-glucuronidase encoding gene (aguA) from Aspergillus niger." de Vries R.P., van de Vondervoort P.J.I., Hendriks L., van de Belt M., Visser J.V. Mol. Genet. Genomics 268:96-102(2002) [PubMed: 12242504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION. Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ290451 Genomic DNA. Translation: CAC38119.1.
3D structure databases
HSSP	HSSP built from PDB template 1K9D based on UniProtKB Q8VVD2.
ProteinModelPortal	Q96WX9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q96WX9.
Protein family/group databases
CAZy	GH67. Glycoside Hydrolase Family 67.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR011395. Glyco_hydro_67_aGlcAse. IPR005154. Glyco_hydro_67_aGlcAse_N. IPR011099. Glyco_hydro_67_C. IPR011100. Glyco_hydro_67_M. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:3.90.1330.10. Glyco_hydro_67_C. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF07477. Glyco_hydro_67C. 1 hit. PF07488. Glyco_hydro_67M. 1 hit. PF03648. Glyco_hydro_67N. 1 hit. [Graphical view]
PIRSF	PIRSF029900. Alpha-glucuronds. 1 hit.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AGUA_ASPNG

Accession

Primary (citable) accession number: Q96WX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 20, 2010
Last sequence update:	December 1, 2001
Last modified:	September 21, 2011
This is version 39 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

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