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P34752 (PHYA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-phytase A
EC=3.1.3.8
Alternative name(s):
3 phytase A
Myo-inositol hexakisphosphate phosphohydrolase A
Myo-inositol-hexaphosphate 3-phosphohydrolase A
Gene names
Name:phyA
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

Subcellular location

Secreted.

Biotechnological use

Is used as a food and feed additive. It can facilitate the degradation of phytin in soybean and other seeds used as food for monogastric animals. Sold by Novo Nordisk under the name Phytase Novo.

Sequence similarities

Belongs to the histidine acid phosphatase family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processdephosphorylation

Inferred from electronic annotation. Source: GOC

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-phytase activity

Inferred from electronic annotation. Source: EC

acid phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.3
Chain24 – 4674443-phytase A
PRO_0000023970

Sites

Active site821Nucleophile By similarity
Active site3621Proton donor By similarity

Amino acid modifications

Glycosylation271N-linked (GlcNAc...)
Glycosylation591N-linked (GlcNAc...)
Glycosylation1051N-linked (GlcNAc...)
Glycosylation1201N-linked (GlcNAc...)
Glycosylation2071N-linked (GlcNAc...)
Glycosylation2301N-linked (GlcNAc...)
Glycosylation3391N-linked (GlcNAc...)
Glycosylation3521N-linked (GlcNAc...)
Glycosylation3761N-linked (GlcNAc...)
Glycosylation3881N-linked (GlcNAc...)
Disulfide bond31 ↔ 40
Disulfide bond71 ↔ 414
Disulfide bond215 ↔ 465
Disulfide bond264 ↔ 282
Disulfide bond436 ↔ 444

Secondary structure

1 .......................................................................... 467
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P34752 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 88FE8F3584341D6D

FASTA46751,086
        10         20         30         40         50         60 
MGVSAVLLPL YLLSGVTSGL AVPASRNQSS CDTVDQGYQC FSETSHLWGQ YAPFFSLANE 

        70         80         90        100        110        120 
SVISPEVPAG CRVTFAQVLS RHGARYPTDS KGKKYSALIE EIQQNATTFD GKYAFLKTYN 

       130        140        150        160        170        180 
YSLGADDLTP FGEQELVNSG IKFYQRYESL TRNIVPFIRS SGSSRVIASG KKFIEGFQST 

       190        200        210        220        230        240 
KLKDPRAQPG QSSPKIDVVI SEASSSNNTL DPGTCTVFED SELADTVEAN FTATFVPSIR 

       250        260        270        280        290        300 
QRLENDLSGV TLTDTEVTYL MDMCSFDTIS TSTVDTKLSP FCDLFTHDEW INYDYLQSLK 

       310        320        330        340        350        360 
KYYGHGAGNP LGPTQGVGYA NELIARLTHS PVHDDTSSNH TLDSSPATFP LNSTLYADFS 

       370        380        390        400        410        420 
HDNGIISILF ALGLYNGTKP LSTTTVENIT QTDGFSSAWT VPFASRLYVE MMQCQAEQEP 

       430        440        450        460 
LVRVLVNDRV VPLHGCPVDA LGRCTRDSFV RGLSFARSGG DWAECFA

« Hide

References

[1]"Cloning, characterization and overexpression of the phytase-encoding gene (phyA) of Aspergillus niger."
van Hartingsveldt W., van Zeijl C.M.J., Harteveld G.M., Gouka R.J., Suykerbuyk M.E.G., Luiten R.G.M., van Paridon P.A., Selten G.C.M., Veenstra A.E., van Gorcom R.F.M., van den Hondel C.A.M.J.J.
Gene 127:87-94(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: NRRL 3135 / Van Tieghem / Ficuum.
[2]"Sequence of the Aspergillus niger (ficuum) phytase gene."
Mullaney E.J.
Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Aspergillus ficuum phytase: complete primary structure elucidation by chemical sequencing."
Ullah A.H.J., Dischinger H.C. Jr.
Biochem. Biophys. Res. Commun. 192:747-753(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-464.
Strain: NRRL 3135 / Van Tieghem / Ficuum.
[4]"Cyclohexanedione modification of arginine at the active site of Aspergillus ficuum phytase."
Ullah A.H.J., Cummins B.J., Dischinger H.C. Jr.
Biochem. Biophys. Res. Commun. 178:45-53(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 71-93.
Strain: NRRL 3135 / Van Tieghem / Ficuum.
[5]"Aspergillus ficuum phytase: partial primary structure, substrate selectivity, and kinetic characterization."
Ullah A.H.J.
Prep. Biochem. 18:459-471(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE.
Strain: NRRL 3135 / Van Tieghem / Ficuum.
[6]"Crystal structure of phytase from Aspergillus ficuum at 2.5-A resolution."
Kostrewa D., Gruninger-Leitch F., D'Arcy A., Broger C., Mitchell D., van Loon A.P.G.M.
Nat. Struct. Biol. 4:185-190(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Strain: NRRL 3135 / Van Tieghem / Ficuum.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z16414 Genomic DNA. Translation: CAA78904.1.
M94550 Genomic DNA. Translation: AAA32705.1.
PIRJN0482.
JN0656.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IHPX-ray2.50A30-467[»]
3K4PX-ray2.40A/B24-467[»]
3K4QX-ray2.20A/B24-467[»]
ProteinModelPortalP34752.
SMRP34752. Positions 30-467.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG260296.

Enzyme and pathway databases

BRENDA3.1.3.8. 518.

Family and domain databases

InterProIPR000560. His_Pase_superF_clade-2.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFPIRSF000894. Acid_phosphatase. 1 hit.
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP34752.

Entry information

Entry namePHYA_ASPNG
AccessionPrimary (citable) accession number: P34752
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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