O00107 (PHYA_THIHE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

PHYA

Organism

Thielavia heterothallica (Myceliophthora thermophila)

Taxonomic identifier

78579 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Sordariales › Chaetomiaceae › mitosporic Chaetomiaceae › Myceliophthora

Protein attributes

Sequence length	487 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the histidine acid phosphatase family.
Biophysicochemical properties	pH dependence: 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.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological_process	dephosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3-phytase activity Inferred from electronic annotation. Source: EC acid phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 487	468	3-phytase A		PRO_0000023973
Regions
	Compositional bias	423 – 433	11	Poly-Gly
Sites
	Active site	75	1	Nucleophile By similarity
	Active site	369	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	165	1	N-linked (GlcNAc...) Potential
	Glycosylation	200	1	N-linked (GlcNAc...) Potential
	Glycosylation	247	1	N-linked (GlcNAc...) Potential
	Glycosylation	346	1	N-linked (GlcNAc...) Potential
	Disulfide bond	26 ↔ 35		By similarity
	Disulfide bond	64 ↔ 421		By similarity
	Disulfide bond	208 ↔ 485		By similarity
	Disulfide bond	260 ↔ 289		By similarity
	Disulfide bond	456 ↔ 464		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O00107 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 97D10EDC83D051DB	FASTA	487	52,538
	10 20 30 40 50 60 MTGLGVMVVM VGFLAIASLQ SESRPCDTPD LGFQCGTAIS HFWGQYSPYF SVPSELDASI 70 80 90 100 110 120 PDDCEVTFAQ VLSRHGARAP TLKRAASYVD LIDRIHHGAI SYGPGYEFLR TYDYTLGADE 130 140 150 160 170 180 LTRTGQQQMV NSGIKFYRRY RALARKSIPF VRTAGQDRVV HSAENFTQGF HSALLADRGS 190 200 210 220 230 240 TVRPTLPYDM VVIPETAGAN NTLHNDLCTA FEEGPYSTIG DDAQDTYLST FAGPITARVN 250 260 270 280 290 300 ANLPGANLTD ADTVALMDLC PFETVASSSS DPATADAGGG NGRPLSPFCR LFSESEWRAY 310 320 330 340 350 360 DYLQSVGKWY GYGPGNPLGP TQGVGFVNEL LARLAGVPVR DGTSTNRTLD GDPRTFPLGR 370 380 390 400 410 420 PLYADFSHDN DMMGVLGALG AYDGVPPLDK TARRDPEELG GYAASWAVPF AARIYVEKMR 430 440 450 460 470 480 CSGGGGGGGG GEGRQEKDEE MVRVLVNDRV MTLKGCGADE RGMCTLERFI ESMAFARGNG KWDLCFA

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U59806 Genomic DNA. Translation: AAB52508.1.
3D structure databases
ProteinModelPortal	O00107.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR000560. His_Pase_superF_clade-2. IPR016274. Histidine_acid_Pase_euk. [Graphical view]
Pfam	PF00328. His_Phos_2. 1 hit. [Graphical view]
PIRSF	PIRSF000894. Acid_phosphatase. 1 hit.
PROSITE	PS00616. HIS_ACID_PHOSPHAT_1. 1 hit. PS00778. HIS_ACID_PHOSPHAT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHYA_THIHE

Accession

Primary (citable) accession number: O00107

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	July 1, 1997
Last modified:	April 3, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program