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Protein

3-phytase A

Gene

phyA

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 5 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

Highly active from pH 3 to 5 with 4-nitrophenyl phosphate as substrate, and from 2.5 to 7.5 with phytic acid.

Temperature dependencei

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei81NucleophileBy similarity1
Active sitei360Proton donorBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.1.3.26. 508.
3.1.3.8. 508.

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
Synonyms:phyA3
ORF Names:AFUA_4G08630
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiFungiDB:Afu4g08630.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000002396927 – 4653-phytase AAdd BLAST439

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 391 Publication
Disulfide bondi70 ↔ 4121 Publication
Glycosylationi104N-linked (GlcNAc...)1
Glycosylationi119N-linked (GlcNAc...)Sequence analysis1
Glycosylationi205N-linked (GlcNAc...)1
Disulfide bondi213 ↔ 4631 Publication
Glycosylationi228N-linked (GlcNAc...)1
Disulfide bondi262 ↔ 2801 Publication
Glycosylationi337N-linked (GlcNAc...)1
Glycosylationi350N-linked (GlcNAc...)1
Glycosylationi374N-linked (GlcNAc...)1
Disulfide bondi434 ↔ 4421 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

1465
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni33 – 35Combined sources3
Helixi41 – 44Combined sources4
Helixi48 – 50Combined sources3
Turni57 – 60Combined sources4
Beta strandi70 – 80Combined sources11
Helixi88 – 104Combined sources17
Helixi110 – 116Combined sources7
Beta strandi124 – 127Combined sources4
Helixi129 – 145Combined sources17
Helixi147 – 150Combined sources4
Beta strandi156 – 161Combined sources6
Helixi163 – 181Combined sources19
Beta strandi194 – 198Combined sources5
Beta strandi201 – 204Combined sources4
Helixi214 – 217Combined sources4
Helixi221 – 244Combined sources24
Helixi252 – 269Combined sources18
Helixi280 – 282Combined sources3
Helixi285 – 302Combined sources18
Turni308 – 310Combined sources3
Helixi311 – 314Combined sources4
Helixi315 – 326Combined sources12
Beta strandi333 – 335Combined sources3
Helixi338 – 342Combined sources5
Turni344 – 346Combined sources3
Beta strandi352 – 358Combined sources7
Helixi360 – 369Combined sources10
Turni370 – 375Combined sources6
Beta strandi381 – 383Combined sources3
Helixi387 – 390Combined sources4
Helixi395 – 398Combined sources4
Beta strandi404 – 412Combined sources9
Beta strandi419 – 424Combined sources6
Beta strandi432 – 434Combined sources3
Helixi444 – 450Combined sources7
Helixi452 – 456Combined sources5
Turni457 – 459Combined sources3
Helixi460 – 463Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QWOX-ray1.50A24-465[»]
1SK8X-ray1.65A27-464[»]
1SK9X-ray1.64A27-464[»]
1SKAX-ray1.69A27-464[»]
1SKBX-ray1.58A27-464[»]
ProteinModelPortaliO00092.
SMRiO00092.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00092.

Family & Domainsi

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000189493.
InParanoidiO00092.
KOiK01083.
OrthoDBiEOG092C1SWD.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
InterProiIPR033379. Acid_Pase_AS.
IPR000560. His_Pase_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.

O00092-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTLTFLLSA AYLLSGRVSA APSSAGSKSC DTVDLGYQCS PATSHLWGQY
60 70 80 90 100
SPFFSLEDEL SVSSKLPKDC RITLVQVLSR HGARYPTSSK SKKYKKLVTA
110 120 130 140 150
IQANATDFKG KFAFLKTYNY TLGADDLTPF GEQQLVNSGI KFYQRYKALA
160 170 180 190 200
RSVVPFIRAS GSDRVIASGE KFIEGFQQAK LADPGATNRA APAISVIIPE
210 220 230 240 250
SETFNNTLDH GVCTKFEASQ LGDEVAANFT ALFAPDIRAR AEKHLPGVTL
260 270 280 290 300
TDEDVVSLMD MCSFDTVART SDASQLSPFC QLFTHNEWKK YNYLQSLGKY
310 320 330 340 350
YGYGAGNPLG PAQGIGFTNE LIARLTRSPV QDHTSTNSTL VSNPATFPLN
360 370 380 390 400
ATMYVDFSHD NSMVSIFFAL GLYNGTEPLS RTSVESAKEL DGYSASWVVP
410 420 430 440 450
FGARAYFETM QCKSEKEPLV RALINDRVVP LHGCDVDKLG RCKLNDFVKG
460
LSWARSGGNW GECFS
Length:465
Mass (Da):50,836
Last modified:July 1, 1997 - v1
Checksum:i86FC1D9058C9B2C9
GO

Sequence cautioni

The sequence EAL89926 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59804 Genomic DNA. Translation: AAB96872.1.
AAHF01000005 Genomic DNA. Translation: EAL89926.2. Different initiation.
AJ419776 Genomic DNA. Translation: CAD12029.1.
RefSeqiXP_751964.2. XM_746871.2.

Genome annotation databases

GeneIDi3509324.
KEGGiafm:AFUA_4G08630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59804 Genomic DNA. Translation: AAB96872.1.
AAHF01000005 Genomic DNA. Translation: EAL89926.2. Different initiation.
AJ419776 Genomic DNA. Translation: CAD12029.1.
RefSeqiXP_751964.2. XM_746871.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QWOX-ray1.50A24-465[»]
1SK8X-ray1.65A27-464[»]
1SK9X-ray1.64A27-464[»]
1SKAX-ray1.69A27-464[»]
1SKBX-ray1.58A27-464[»]
ProteinModelPortaliO00092.
SMRiO00092.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3509324.
KEGGiafm:AFUA_4G08630.

Organism-specific databases

EuPathDBiFungiDB:Afu4g08630.

Phylogenomic databases

HOGENOMiHOG000189493.
InParanoidiO00092.
KOiK01083.
OrthoDBiEOG092C1SWD.

Enzyme and pathway databases

BRENDAi3.1.3.26. 508.
3.1.3.8. 508.

Miscellaneous databases

EvolutionaryTraceiO00092.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
InterProiIPR033379. Acid_Pase_AS.
IPR000560. His_Pase_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]
ProtoNetiSearch...

Entry informationi

Entry nameiPHYA_ASPFU
AccessioniPrimary (citable) accession number: O00092
Secondary accession number(s): Q4WPA8, Q8WZJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: July 1, 1997
Last modified: November 2, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.