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O00100

- PHYA2_ASPTE

UniProt

O00100 - PHYA2_ASPTE

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Protein
3-phytase A
Gene
phyA
Organism
Aspergillus terreus
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of inorganic orthophosphate from phytate. Releases 5 of the 6 phosphate groups to yield the end product myo-inositol 2-monophosphate. Specific for phytate.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=23.2 µM for phytate1 Publication

pH dependencei

Optimum pH is 5.5. Active from 4 to 6.5.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei82 – 821Nucleophile By similarity
Active sitei362 – 3621Proton donor By similarity

GO - Molecular functioni

  1. 3-phytase activity Source: UniProtKB-EC
  2. acid phosphatase activity Source: InterPro
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
OrganismiAspergillus terreus
Taxonomic identifieri33178 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

Secreted By similarity

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 – 19191 Publication
Add
BLAST
Chaini20 – 4664473-phytase A
PRO_0000283712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi27 – 271N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi31 ↔ 40 By similarity
Disulfide bondi71 ↔ 414 By similarity
Glycosylationi105 – 1051N-linked (GlcNAc...) Reviewed prediction
Glycosylationi120 – 1201N-linked (GlcNAc...) Reviewed prediction
Glycosylationi207 – 2071N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi215 ↔ 465 By similarity
Glycosylationi230 – 2301N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi264 ↔ 282 By similarity
Glycosylationi339 – 3391N-linked (GlcNAc...) Reviewed prediction
Glycosylationi352 – 3521N-linked (GlcNAc...) Reviewed prediction
Glycosylationi376 – 3761N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi436 ↔ 444 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi33178.CADATEAP00004553.

Structurei

3D structure databases

ProteinModelPortaliO00100.
SMRiO00100. Positions 31-466.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG319987.
HOGENOMiHOG000189493.

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.

O00100-1 [UniParc]FASTAAdd to Basket

« Hide

MGVFVVLLSI ATLFGSTSGT ALGPRGNHSD CTSVDRGYQC FPELSHKWGL    50
YAPYFSLQDE SPFPLDVPDD CHITFVQVLA RHGARSPTDS KTKAYAATIA 100
AIQKNATALP GKYAFLKSYN YSMGSENLNP FGRNQLQDLG AQFYRRYDTL 150
TRHINPFVRA ADSSRVHESA EKFVEGFQNA RQGDPHANPH QPSPRVDVVI 200
PEGTAYNNTL EHSICTAFEA STVGDAAADN FTAVFAPAIA KRLEADLPGV 250
QLSADDVVNL MAMCPFETVS LTDDAHTLSP FCDLFTAAEW TQYNYLLSLD 300
KYYGYGGGNP LGPVQGVGWA NELIARLTRS PVHDHTCVNN TLDANPATFP 350
LNATLYADFS HDSNLVSIFW ALGLYNGTKP LSQTTVEDIT RTDGYAAAWT 400
VPFAARAYIE MMQCRAEKQP LVRVLVNDRV MPLHGCAVDN LGRCKRDDFV 450
EGLSFARAGG NWAECF 466
Length:466
Mass (Da):51,055
Last modified:July 1, 1997 - v1
Checksum:iF2AECEC1AF7C22C4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U60412 Genomic DNA. Translation: AAB58465.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U60412 Genomic DNA. Translation: AAB58465.1 .

3D structure databases

ProteinModelPortali O00100.
SMRi O00100. Positions 31-466.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 33178.CADATEAP00004553.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG319987.
HOGENOMi HOG000189493.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
InterProi IPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view ]
Pfami PF00328. His_Phos_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMi SSF53254. SSF53254. 1 hit.
PROSITEi PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning of the phytases of Aspergillus nidulans and Talaromyces thermophilus and their evolutionary relation to other histidine acid phosphatases."
    Pasamontes L., Haiker M., Henriquez Huecas M., Hug D., Mitchell D.B., Broger C., van Loon A.P.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 10020 / NRRL 1960 / CBS 116.46 / IFO 6123 / DSM 826 / IMI 44243.
  2. "Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): molecular size, glycosylation pattern, and engineering of proteolytic resistance."
    Wyss M., Pasamontes L., Friedlein A., Remy R., Tessier M., Kronenberger A., Middendorf A., Lehmann M., Schnoebelen L., Roethlisberger U., Kusznir E., Wahl G., Mueller F., Lahm H.-W., Vogel K., van Loon A.P.G.M.
    Appl. Environ. Microbiol. 65:359-366(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-35, SUBUNIT.
    Strain: ATCC 10020 / NRRL 1960 / CBS 116.46 / IFO 6123 / DSM 826 / IMI 44243.
  3. "Biochemical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): catalytic properties."
    Wyss M., Brugger R., Kronenberger A., Remy R., Fimbel R., Oesterhelt G., Lehmann M., van Loon A.P.G.M.
    Appl. Environ. Microbiol. 65:367-373(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiPHYA2_ASPTE
AccessioniPrimary (citable) accession number: O00100
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: July 1, 1997
Last modified: June 11, 2014
This is version 60 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

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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