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Protein

3-phytase A

Gene

phyA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the hydrolysis of inorganic orthophosphate from phytate.

Catalytic activityi

Myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei81 – 811NucleophileBy similarity
Active sitei361 – 3611Proton donorBy similarity

GO - Molecular functioni

  1. 3-phytase activity Source: ASPGD
  2. acid phosphatase activity Source: InterPro

GO - Biological processi

  1. myo-inositol hexakisphosphate dephosphorylation Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:phyA
ORF Names:AO090023000692
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 3

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: ASPGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 4664473-phytase APRO_0000043346Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 39By similarity
Disulfide bondi70 ↔ 413By similarity
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi214 ↔ 464By similarity
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi263 ↔ 281By similarity
Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi375 – 3751N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi435 ↔ 443By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ9C1T1.
SMRiQ9C1T1. Positions 30-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000189493.
OrthoDBiEOG7QC85C.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9C1T1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVLSVLLPI TFLLSSVTGT PVTSPRQQSC NTVDEGYQCF SGVSHLWGQY
60 70 80 90 100
SPYFSVDDES SLSEDVPDHC QVTFAQVLSR HGARYPTKSK SEKYAKLIKA
110 120 130 140 150
VQHNATSFSG KYAFLKSYNY SLGADDLTPF GENQLVDSGI KFYQRYEELA
160 170 180 190 200
KNVVPFIRAS GSDRVIASGE KFIEGFQKAK LGDSKSKRGQ PAPIVNVVIT
210 220 230 240 250
ETEGFNNTLD HSLCTAFENS TTGDDAEDKF TAVFTPSIVE RLEKDLPGTT
260 270 280 290 300
LSSKEVVYLM DMCSFDTIAL TRDGSRLSPF CALFTQEEWA QYDYLQSVSK
310 320 330 340 350
YYGYGGGNPL GPAQGIGFAN ELIARLTKSP VKDHTTTNTT LDSNPATFPL
360 370 380 390 400
NATLYADFSH DNTMTSVFFA LGLYNTTEPL SQTSVQSTEE TNGYSSARTV
410 420 430 440 450
PFGARAYVEM MQCTDEKEPL VRVLVNDRVI PLQGCDADEY GRCKRDDFVE
460
GLSFVTSGGN WGECFA
Length:466
Mass (Da):51,257
Last modified:June 1, 2001 - v1
Checksum:i8033BED57FBA2791
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB042805 mRNA. Translation: BAB40715.1.
AP007157 Genomic DNA. Translation: BAE59208.1.
RefSeqiXP_001821210.1. XM_001821158.2.

Genome annotation databases

EnsemblFungiiCADAORAT00007793; CADAORAP00007634; CADAORAG00007793.
GeneIDi5993212.
KEGGiaor:AOR_1_1198144.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB042805 mRNA. Translation: BAB40715.1.
AP007157 Genomic DNA. Translation: BAE59208.1.
RefSeqiXP_001821210.1. XM_001821158.2.

3D structure databases

ProteinModelPortaliQ9C1T1.
SMRiQ9C1T1. Positions 30-465.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00007793; CADAORAP00007634; CADAORAG00007793.
GeneIDi5993212.
KEGGiaor:AOR_1_1198144.

Phylogenomic databases

HOGENOMiHOG000189493.
OrthoDBiEOG7QC85C.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of Aspergillus oryzae phytase cDNA."
    Gomi K.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiPHYA_ASPOR
AccessioniPrimary (citable) accession number: Q9C1T1
Secondary accession number(s): Q2UGV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: June 1, 2001
Last modified: January 7, 2015
This is version 64 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.