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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 6.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei82 – 821NucleophileBy similarity
Active sitei362 – 3621Proton donorBy 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-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 4664473-phytase APRO_0000283712Add
BLAST

Amino acid modifications

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

Family & Domainsi

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVFVVLLSI ATLFGSTSGT ALGPRGNHSD CTSVDRGYQC FPELSHKWGL
60 70 80 90 100
YAPYFSLQDE SPFPLDVPDD CHITFVQVLA RHGARSPTDS KTKAYAATIA
110 120 130 140 150
AIQKNATALP GKYAFLKSYN YSMGSENLNP FGRNQLQDLG AQFYRRYDTL
160 170 180 190 200
TRHINPFVRA ADSSRVHESA EKFVEGFQNA RQGDPHANPH QPSPRVDVVI
210 220 230 240 250
PEGTAYNNTL EHSICTAFEA STVGDAAADN FTAVFAPAIA KRLEADLPGV
260 270 280 290 300
QLSADDVVNL MAMCPFETVS LTDDAHTLSP FCDLFTAAEW TQYNYLLSLD
310 320 330 340 350
KYYGYGGGNP LGPVQGVGWA NELIARLTRS PVHDHTCVNN TLDANPATFP
360 370 380 390 400
LNATLYADFS HDSNLVSIFW ALGLYNGTKP LSQTTVEDIT RTDGYAAAWT
410 420 430 440 450
VPFAARAYIE MMQCRAEKQP LVRVLVNDRV MPLHGCAVDN LGRCKRDDFV
460
EGLSFARAGG NWAECF
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: October 29, 2014
This is version 62 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