Reviewed, UniProtKB/Swiss-Prot O00092 (PHYA_ASPFU)

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
Synonyms:	phyA3
ORF Names:	AFUA_4G08630

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	465 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: Highly active from pH 3 to 5 with 4-nitrophenyl phosphate as substrate, and from 2.5 to 7.5 with phytic acid. Temperature dependence: Able to withstand temperatures up to 100 degrees Celsius over a period of 20 min, with a loss of only 10% of the initial enzymatic activity.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome 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 – 26

26

Ref.1

Chain

27 – 465

439

3-phytase A

PRO_0000023969

Sites

Active site

81

1

Nucleophile By similarity

Active site

360

1

Proton donor By similarity

Amino acid modifications

Glycosylation

104

1

N-linked (GlcNAc...)

Glycosylation

119

1

N-linked (GlcNAc...) Potential

Glycosylation

205

1

N-linked (GlcNAc...)

Glycosylation

228

1

N-linked (GlcNAc...)

Glycosylation

337

1

N-linked (GlcNAc...)

Glycosylation

350

1

N-linked (GlcNAc...)

Glycosylation

374

1

N-linked (GlcNAc...)

Disulfide bond

30 ↔ 39

Ref.4

Disulfide bond

70 ↔ 412

Ref.4

Disulfide bond

213 ↔ 463

Ref.4

Disulfide bond

262 ↔ 280

Ref.4

Disulfide bond

434 ↔ 442

Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

465

Helix Strand Turn

Details...

Turn

33 – 35

3

Helix

41 – 44

4

Helix

48 – 50

3

Turn

57 – 60

4

Beta strand

70 – 80

11

Helix

88 – 104

17

Helix

110 – 116

7

Beta strand

124 – 127

4

Helix

129 – 145

17

Helix

147 – 150

4

Beta strand

156 – 161

6

Helix

163 – 181

19

Beta strand

194 – 198

5

Helix

214 – 217

4

Helix

221 – 244

24

Helix

252 – 269

18

Helix

280 – 282

3

Helix

285 – 302

18

Turn

308 – 310

3

Helix

311 – 314

4

Helix

315 – 326

12

Beta strand

333 – 335

3

Helix

338 – 342

5

Turn

344 – 346

3

Beta strand

352 – 358

7

Helix

360 – 369

10

Turn

370 – 375

6

Beta strand

381 – 383

3

Helix

387 – 390

4

Helix

395 – 398

4

Beta strand

404 – 412

9

Beta strand

419 – 424

6

Beta strand

432 – 434

3

Helix

444 – 450

7

Helix

452 – 456

5

Turn

457 – 459

3

Helix

460 – 463

4

Sequences

	Sequence		Length	Mass (Da)
	O00092-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 86FC1D9058C9B2C9	FASTA	465	50,836
	10 20 30 40 50 60 MVTLTFLLSA AYLLSGRVSA APSSAGSKSC DTVDLGYQCS PATSHLWGQY SPFFSLEDEL 70 80 90 100 110 120 SVSSKLPKDC RITLVQVLSR HGARYPTSSK SKKYKKLVTA IQANATDFKG KFAFLKTYNY 130 140 150 160 170 180 TLGADDLTPF GEQQLVNSGI KFYQRYKALA RSVVPFIRAS GSDRVIASGE KFIEGFQQAK 190 200 210 220 230 240 LADPGATNRA APAISVIIPE SETFNNTLDH GVCTKFEASQ LGDEVAANFT ALFAPDIRAR 250 260 270 280 290 300 AEKHLPGVTL TDEDVVSLMD MCSFDTVART SDASQLSPFC QLFTHNEWKK YNYLQSLGKY 310 320 330 340 350 360 YGYGAGNPLG PAQGIGFTNE LIARLTRSPV QDHTSTNSTL VSNPATFPLN ATMYVDFSHD 370 380 390 400 410 420 NSMVSIFFAL GLYNGTEPLS RTSVESAKEL DGYSASWVVP FGARAYFETM QCKSEKEPLV 430 440 450 460 RALINDRVVP LHGCDVDKLG RCKLNDFVKG LSWARSGGNW GECFS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene cloning, purification, and characterization of a heat-stable phytase from the fungus Aspergillus fumigatus." Pasamontes L., Haiker M., Wyss M., Tessier M., van Loon A.P.G.M. Appl. Environ. Microbiol. 63:1696-1700(1997) [PubMed: 9143104] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-37, CHARACTERIZATION. Strain: ATCC 34625 / CS-270.
[2]	"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.
[3]	"Cloning of phytase gene from Aspergillus fumigatus and its expression in Pichia pastoris." Zhang G. Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-465. Strain: CCTCC AF93024.
[4]	"Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics." Liu Q., Huang Q., Lei X.G., Hao Q. Structure 12:1575-1583(2004) [PubMed: 15341723] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 27-465, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U59804 Genomic DNA. Translation: AAB96872.1.
AAHF01000005 Genomic DNA. Translation: EAL89926.2. Different initiation.
AJ419776 Genomic DNA. Translation: CAD12029.1.

RefSeq

XP_751964.2.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QWO	X-ray	1.50	A	24-465	[»]
1SK8	X-ray	1.65	A	27-465	[»]
1SK9	X-ray	1.64	A	27-465	[»]
1SKA	X-ray	1.69	A	27-465	[»]
1SKB	X-ray	1.58	A	27-465	[»]

ModBase

Search...

Genome annotation databases

GeneID

3509324.

KEGG

afm:AFUA_4G08630.

Phylogenomic databases

HOGENOM

O00092.

OMA

O00092. VEKMTCA.

Enzyme and pathway databases

BRENDA

3.1.3.26. 18841.
3.1.3.8. 18841.

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

PHYA_ASPFU

Accession

Primary (citable) accession number: O00092
Secondary accession number(s): Q4WPA8, Q8WZJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)