Q9C1T1 (PHYA_ASPOR) 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
ORF Names:	AO090023000692

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus oryzae

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 transcript 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.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
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 – 466	447	3-phytase A		PRO_0000043346
Sites
	Active site	81	1	Nucleophile By similarity
	Active site	361	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	104	1	N-linked (GlcNAc...) Potential
	Glycosylation	119	1	N-linked (GlcNAc...) Potential
	Glycosylation	206	1	N-linked (GlcNAc...) Potential
	Glycosylation	219	1	N-linked (GlcNAc...) Potential
	Glycosylation	338	1	N-linked (GlcNAc...) Potential
	Glycosylation	351	1	N-linked (GlcNAc...) Potential
	Glycosylation	375	1	N-linked (GlcNAc...) Potential
	Disulfide bond	30 ↔ 39		By similarity
	Disulfide bond	70 ↔ 413		By similarity
	Disulfide bond	214 ↔ 464		By similarity
	Disulfide bond	263 ↔ 281		By similarity
	Disulfide bond	435 ↔ 443		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9C1T1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 8033BED57FBA2791	FASTA	466	51,257
	10 20 30 40 50 60 MAVLSVLLPI TFLLSSVTGT PVTSPRQQSC NTVDEGYQCF SGVSHLWGQY SPYFSVDDES 70 80 90 100 110 120 SLSEDVPDHC QVTFAQVLSR HGARYPTKSK SEKYAKLIKA VQHNATSFSG KYAFLKSYNY 130 140 150 160 170 180 SLGADDLTPF GENQLVDSGI KFYQRYEELA KNVVPFIRAS GSDRVIASGE KFIEGFQKAK 190 200 210 220 230 240 LGDSKSKRGQ PAPIVNVVIT ETEGFNNTLD HSLCTAFENS TTGDDAEDKF TAVFTPSIVE 250 260 270 280 290 300 RLEKDLPGTT LSSKEVVYLM DMCSFDTIAL TRDGSRLSPF CALFTQEEWA QYDYLQSVSK 310 320 330 340 350 360 YYGYGGGNPL GPAQGIGFAN ELIARLTKSP VKDHTTTNTT LDSNPATFPL NATLYADFSH 370 380 390 400 410 420 DNTMTSVFFA LGLYNTTEPL SQTSVQSTEE TNGYSSARTV PFGARAYVEM MQCTDEKEPL 430 440 450 460 VRVLVNDRVI PLQGCDADEY GRCKRDDFVE GLSFVTSGGN WGECFA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of Aspergillus oryzae phytase cDNA." Gomi K. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB042805 mRNA. Translation: BAB40715.1. AP007157 Genomic DNA. Translation: BAE59208.1.
RefSeq	XP_001821210.1. XM_001821158.2.
3D structure databases
ProteinModelPortal	Q9C1T1.
SMR	Q9C1T1. Positions 30-465.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00007793; CADAORAP00007634; CADAORAG00007793.
GeneID	5993212.
KEGG	aor:AOR_1_1198144.
Phylogenomic databases
HOGENOM	HOG000189493.
OrthoDB	EOG42Z7ZR.
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_ASPOR

Accession

Primary (citable) accession number: Q9C1T1
Secondary accession number(s): Q2UGV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	June 1, 2001
Last modified:	May 1, 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