3-phytase B precursor - Emericella nidulans

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Reviewed, UniProtKB/Swiss-Prot O00093 (PHYB_EMENI)

Last modified March 24, 2009. Version 54. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
    3-phytase B
    EC=3.1.3.8
Alternative name(s):
    3 phytase B
    Myo-inositol-hexaphosphate 3-phosphohydrolase B
    Myo-inositol hexakisphosphate phosphohydrolase B

Gene names

Name:	phyB
ORF Names:	AN1685

Organism

Emericella nidulans (Aspergillus nidulans)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	463 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	Catalyzes the hydrolysis of inorganic orthophosphate from phytate.
Catalytic activity	Myo-inositol hexakisphosphate + H₂O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate.
Sequence similarities	Belongs to the histidine acid phosphatase family.

Ontologies

Keywords
Domain	Signal
Molecular function	Hydrolase
PTM	Glycoprotein
Gene Ontology (GO)
Molecular function	3-phytase activity Inferred from electronic annotation. Source: EC acid phosphatase activity 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

19

Potential

Chain

444

3-phytase B

PRO_0000023976

Sites

Active site

1

Nucleophile By similarity

Active site

1

Proton donor By similarity

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

Experimental info

Sequence conflict

1

T → A in AAB96871. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O00093-1 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 1D6BC0B0DA14F0D9
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463

51,816

        10         20         30         40         50         60 
MAFFTVALSL YYLLSRVSTQ APVVQNHSCN TADGGYQCFP NVSHVWGQYS PYFSIEQESA 

        70         80         90        100        110        120 
ISEDVPHGCE VTFVQVLSRH GARYPTESKS KAYSGLIEAI QKNATSFWGQ YAFLESYNYT 

       130        140        150        160        170        180 
LGADDLTIFG ENQMVDSGAK FYRRYKNLAR KNTPFIRASG SDRVVASAEK FINGFRKAQL 

       190        200        210        220        230        240 
HDHGSKRATP VVNVIIPEID GFNNTLDHST CVSFENDERA DEIEANFTAI MGPPIRKRLE 

       250        260        270        280        290        300 
NDLPGIKLTN ENVIYLMDMC SFDTMARTAH GTELSPFCAI FTEKEWLQYD YLQSLSKYYG 

       310        320        330        340        350        360 
YGAGSPLGPA QGIGFTNELI ARLTQSPVQD NTSTNHTLDS NPATFPLDRK LYADFSHDNS 

       370        380        390        400        410        420 
MISIFFAMGL YNGTQPLSMD SVESIQEMDG YAASWTVPFG ARAYFELMQC EKKEPLVRVL 

       430        440        450        460 
VNDRVVPLHG CAVDKFGRCT LDDWVEGLNF ARSGGNWKTC FTL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the phytases from Emericella nidulans and the thermophilic fungus Talaromyces thermophilus." Pasamontes L., Haiker M., Henriquez-Huecas M., Mitchell D.B., van Loon A.P.G.M. Biochim. Biophys. Acta 1353:217-223(1997) [PubMed: 9349716] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
	U59803 Genomic DNA. Translation: AAB96871.1. AACD01000026 Genomic DNA. Translation: EAA64805.1.
RefSeq	XP_659289.1.
3D structure databases
HSSP	HSSP built from PDB template 1IHP based on UniProtKB P34752.
SMR	O00093. Positions 29-461.
ModBase	Search...
Genome annotation databases
GeneID	2874708.
KEGG	ani:AN1685.2.
Enzyme and pathway databases
BRENDA	3.1.3.26. 3859. 3.1.3.8. 3859.
Family and domain databases
InterPro	IPR000560. Histidine_acid_Pase. IPR016274. Histidine_acid_Pase_euk. [Graphical view]
Pfam	PF00328. Acid_phosphat_A. 1 hit. [Graphical view]
PIRSF	PIRSF000894. Acid_phosphatase. 1 hit.
PROSITE	PS00616. HIS_ACID_PHOSPHAT_1. 1 hit. PS00778. HIS_ACID_PHOSPHAT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHYB_EMENI

Accession

Primary (citable) accession number: O00093
Secondary accession number(s): Q5BCP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	May 1, 2007
Last modified:	March 24, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents