Reviewed, UniProtKB/Swiss-Prot O00100 (PHYA2_ASPTE)

Names and origin

Protein names

Recommended name:
    3-phytase A
    EC=3.1.3.8
Alternative name(s):
    3 phytase A
    Myo-inositol-hexaphosphate 3-phosphohydrolase A
    Myo-inositol hexakisphosphate phosphohydrolase A

Gene names

Name:

phyA

Organism

Aspergillus terreus

Taxonomic identifier

33178 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	466 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. Releases 5 of the 6 phosphate groups to yield the end product myo-inositol 2-monophosphate. Specific for phytate. Ref.3
Catalytic activity	Myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate.
Subunit structure	Monomer. Ref.2
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the histidine acid phosphatase family.
Biophysicochemical properties	Kinetic parameters: KM=23.2 µM for phytate pH dependence: Optimum pH is 5.5. Active from 4 to 6.5.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
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	Ref.2
	Chain	20 – 466	447	3-phytase A		PRO_0000283712
Sites
	Active site	82	1	Nucleophile By similarity
	Active site	362	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	27	1	N-linked (GlcNAc...) Potential
	Glycosylation	105	1	N-linked (GlcNAc...) Potential
	Glycosylation	120	1	N-linked (GlcNAc...) Potential
	Glycosylation	207	1	N-linked (GlcNAc...) Potential
	Glycosylation	230	1	N-linked (GlcNAc...) Potential
	Glycosylation	339	1	N-linked (GlcNAc...) Potential
	Glycosylation	352	1	N-linked (GlcNAc...) Potential
	Glycosylation	376	1	N-linked (GlcNAc...) Potential
	Disulfide bond	31 ↔ 40		By similarity
	Disulfide bond	71 ↔ 414		By similarity
	Disulfide bond	215 ↔ 465		By similarity
	Disulfide bond	264 ↔ 282		By similarity
	Disulfide bond	436 ↔ 444		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O00100-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: F2AECEC1AF7C22C4	FASTA	466	51,055
	10 20 30 40 50 60 MGVFVVLLSI ATLFGSTSGT ALGPRGNHSD CTSVDRGYQC FPELSHKWGL YAPYFSLQDE 70 80 90 100 110 120 SPFPLDVPDD CHITFVQVLA RHGARSPTDS KTKAYAATIA AIQKNATALP GKYAFLKSYN 130 140 150 160 170 180 YSMGSENLNP FGRNQLQDLG AQFYRRYDTL TRHINPFVRA ADSSRVHESA EKFVEGFQNA 190 200 210 220 230 240 RQGDPHANPH QPSPRVDVVI PEGTAYNNTL EHSICTAFEA STVGDAAADN FTAVFAPAIA 250 260 270 280 290 300 KRLEADLPGV QLSADDVVNL MAMCPFETVS LTDDAHTLSP FCDLFTAAEW TQYNYLLSLD 310 320 330 340 350 360 KYYGYGGGNP LGPVQGVGWA NELIARLTRS PVHDHTCVNN TLDANPATFP LNATLYADFS 370 380 390 400 410 420 HDSNLVSIFW ALGLYNGTKP LSQTTVEDIT RTDGYAAAWT VPFAARAYIE MMQCRAEKQP 430 440 450 460 LVRVLVNDRV MPLHGCAVDN LGRCKRDDFV EGLSFARAGG NWAECF

References

[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: 9925554] [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: 9925555] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U60412 Genomic DNA. Translation: AAB58465.1.
3D structure databases
HSSP	HSSP built from PDB template 1IHP based on UniProtKB P34752.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.3.8. 2241.
Family and domain databases
InterPro	IPR000560. Histidine_acid_Pase. IPR016274. Histidine_acid_Pase_euk. [Graphical view]
Pfam	PF00328. Acid_phosphat_A. 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

PHYA2_ASPTE

Accession

Primary (citable) accession number: O00100

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 17, 2007
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)