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O00107

- PHYA_THIHE

UniProt

O00107 - PHYA_THIHE

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Protein

3-phytase A

Gene

PHYA

Organism
Thielavia heterothallica (Myceliophthora thermophila)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein 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.

pH dependencei

Optimum pH is 5.5-6.0. Active from 3.5 to 8.5 with phytic acid as substrate. The optimum pH is shifted to more acidic values with 4-nitrophenyl phosphate as substrate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei75 – 751NucleophileBy similarity
Active sitei369 – 3691Proton 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
OrganismiThielavia heterothallica (Myceliophthora thermophila)
Taxonomic identifieri78579 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeMyceliophthora

Subcellular locationi

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 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 4874683-phytase APRO_0000023973Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 35By similarity
Disulfide bondi64 ↔ 421By similarity
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi200 – 2001N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi208 ↔ 485By similarity
Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi260 ↔ 289By similarity
Glycosylationi346 – 3461N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi456 ↔ 464By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliO00107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi423 – 43311Poly-GlyAdd
BLAST

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

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.

O00107-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTGLGVMVVM VGFLAIASLQ SESRPCDTPD LGFQCGTAIS HFWGQYSPYF
60 70 80 90 100
SVPSELDASI PDDCEVTFAQ VLSRHGARAP TLKRAASYVD LIDRIHHGAI
110 120 130 140 150
SYGPGYEFLR TYDYTLGADE LTRTGQQQMV NSGIKFYRRY RALARKSIPF
160 170 180 190 200
VRTAGQDRVV HSAENFTQGF HSALLADRGS TVRPTLPYDM VVIPETAGAN
210 220 230 240 250
NTLHNDLCTA FEEGPYSTIG DDAQDTYLST FAGPITARVN ANLPGANLTD
260 270 280 290 300
ADTVALMDLC PFETVASSSS DPATADAGGG NGRPLSPFCR LFSESEWRAY
310 320 330 340 350
DYLQSVGKWY GYGPGNPLGP TQGVGFVNEL LARLAGVPVR DGTSTNRTLD
360 370 380 390 400
GDPRTFPLGR PLYADFSHDN DMMGVLGALG AYDGVPPLDK TARRDPEELG
410 420 430 440 450
GYAASWAVPF AARIYVEKMR CSGGGGGGGG GEGRQEKDEE MVRVLVNDRV
460 470 480
MTLKGCGADE RGMCTLERFI ESMAFARGNG KWDLCFA
Length:487
Mass (Da):52,538
Last modified:July 1, 1997 - v1
Checksum:i97D10EDC83D051DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59806 Genomic DNA. Translation: AAB52508.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59806 Genomic DNA. Translation: AAB52508.1 .

3D structure databases

ProteinModelPortali O00107.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila."
    Mitchell D.B., Vogel K., Weimann B.J., Pasamontes L., van Loon A.P.G.M.
    Microbiology 143:245-252(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.

Entry informationi

Entry nameiPHYA_THIHE
AccessioniPrimary (citable) accession number: O00107
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: July 1, 1997
Last modified: October 29, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3