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P34752

- PHYA_ASPNG

UniProt

P34752 - PHYA_ASPNG

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Protein

3-phytase A

Gene

phyA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 4 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei82 – 821NucleophileBy similarity
Active sitei362 – 3621Proton donorBy similarity

GO - Molecular functioni

  1. 3-phytase activity Source: UniProtKB-EC
  2. acid phosphatase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.1.3.8. 518.

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
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Biotechnological usei

Is used as a food and feed additive. It can facilitate the degradation of phytin in soybean and other seeds used as food for monogastric animals. Sold by Novo Nordisk under the name Phytase Novo.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 4674443-phytase APRO_0000023970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi27 – 271N-linked (GlcNAc...)
Disulfide bondi31 ↔ 40
Glycosylationi59 – 591N-linked (GlcNAc...)
Disulfide bondi71 ↔ 414
Glycosylationi105 – 1051N-linked (GlcNAc...)
Glycosylationi120 – 1201N-linked (GlcNAc...)
Glycosylationi207 – 2071N-linked (GlcNAc...)
Disulfide bondi215 ↔ 465
Glycosylationi230 – 2301N-linked (GlcNAc...)
Disulfide bondi264 ↔ 282
Glycosylationi339 – 3391N-linked (GlcNAc...)
Glycosylationi352 – 3521N-linked (GlcNAc...)
Glycosylationi376 – 3761N-linked (GlcNAc...)
Glycosylationi388 – 3881N-linked (GlcNAc...)
Disulfide bondi436 ↔ 444

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

1
467
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni34 – 363Combined sources
Helixi42 – 454Combined sources
Helixi49 – 513Combined sources
Helixi58 – 603Combined sources
Beta strandi71 – 8111Combined sources
Helixi89 – 10517Combined sources
Helixi111 – 1177Combined sources
Beta strandi126 – 1283Combined sources
Helixi130 – 14617Combined sources
Helixi148 – 1514Combined sources
Beta strandi157 – 1637Combined sources
Helixi164 – 18219Combined sources
Beta strandi198 – 2014Combined sources
Helixi216 – 2205Combined sources
Helixi223 – 23210Combined sources
Turni233 – 2353Combined sources
Helixi236 – 24611Combined sources
Helixi254 – 26815Combined sources
Helixi272 – 2754Combined sources
Helixi280 – 2845Combined sources
Helixi287 – 30418Combined sources
Turni310 – 3123Combined sources
Helixi313 – 3164Combined sources
Helixi317 – 32812Combined sources
Beta strandi335 – 3373Combined sources
Helixi340 – 3434Combined sources
Turni346 – 3483Combined sources
Beta strandi354 – 3607Combined sources
Helixi362 – 37110Combined sources
Turni372 – 3776Combined sources
Beta strandi383 – 3853Combined sources
Turni389 – 3946Combined sources
Helixi397 – 4004Combined sources
Beta strandi401 – 4033Combined sources
Beta strandi406 – 4149Combined sources
Beta strandi421 – 4266Combined sources
Beta strandi434 – 4363Combined sources
Helixi446 – 4527Combined sources
Helixi454 – 4574Combined sources
Turni458 – 4614Combined sources
Helixi462 – 4654Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IHPX-ray2.50A30-467[»]
3K4PX-ray2.40A/B24-467[»]
3K4QX-ray2.20A/B24-467[»]
ProteinModelPortaliP34752.
SMRiP34752. Positions 30-467.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34752.

Family & Domainsi

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG260296.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR000560. His_Pase_superF_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.

P34752-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVSAVLLPL YLLSGVTSGL AVPASRNQSS CDTVDQGYQC FSETSHLWGQ
60 70 80 90 100
YAPFFSLANE SVISPEVPAG CRVTFAQVLS RHGARYPTDS KGKKYSALIE
110 120 130 140 150
EIQQNATTFD GKYAFLKTYN YSLGADDLTP FGEQELVNSG IKFYQRYESL
160 170 180 190 200
TRNIVPFIRS SGSSRVIASG KKFIEGFQST KLKDPRAQPG QSSPKIDVVI
210 220 230 240 250
SEASSSNNTL DPGTCTVFED SELADTVEAN FTATFVPSIR QRLENDLSGV
260 270 280 290 300
TLTDTEVTYL MDMCSFDTIS TSTVDTKLSP FCDLFTHDEW INYDYLQSLK
310 320 330 340 350
KYYGHGAGNP LGPTQGVGYA NELIARLTHS PVHDDTSSNH TLDSSPATFP
360 370 380 390 400
LNSTLYADFS HDNGIISILF ALGLYNGTKP LSTTTVENIT QTDGFSSAWT
410 420 430 440 450
VPFASRLYVE MMQCQAEQEP LVRVLVNDRV VPLHGCPVDA LGRCTRDSFV
460
RGLSFARSGG DWAECFA
Length:467
Mass (Da):51,086
Last modified:February 1, 1994 - v1
Checksum:i88FE8F3584341D6D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z16414 Genomic DNA. Translation: CAA78904.1.
M94550 Genomic DNA. Translation: AAA32705.1.
PIRiJN0482.
JN0656.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z16414 Genomic DNA. Translation: CAA78904.1 .
M94550 Genomic DNA. Translation: AAA32705.1 .
PIRi JN0482.
JN0656.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IHP X-ray 2.50 A 30-467 [» ]
3K4P X-ray 2.40 A/B 24-467 [» ]
3K4Q X-ray 2.20 A/B 24-467 [» ]
ProteinModelPortali P34752.
SMRi P34752. Positions 30-467.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG260296.

Enzyme and pathway databases

BRENDAi 3.1.3.8. 518.

Miscellaneous databases

EvolutionaryTracei P34752.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
InterProi IPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view ]
Pfami PF00328. His_Phos_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMi SSF53254. SSF53254. 1 hit.
PROSITEi PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: NRRL 3135 / Van Tieghem / Ficuum.
  2. "Sequence of the Aspergillus niger (ficuum) phytase gene."
    Mullaney E.J.
    Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Aspergillus ficuum phytase: complete primary structure elucidation by chemical sequencing."
    Ullah A.H.J., Dischinger H.C. Jr.
    Biochem. Biophys. Res. Commun. 192:747-753(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-464.
    Strain: NRRL 3135 / Van Tieghem / Ficuum.
  4. "Cyclohexanedione modification of arginine at the active site of Aspergillus ficuum phytase."
    Ullah A.H.J., Cummins B.J., Dischinger H.C. Jr.
    Biochem. Biophys. Res. Commun. 178:45-53(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 71-93.
    Strain: NRRL 3135 / Van Tieghem / Ficuum.
  5. "Aspergillus ficuum phytase: partial primary structure, substrate selectivity, and kinetic characterization."
    Ullah A.H.J.
    Prep. Biochem. 18:459-471(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE.
    Strain: NRRL 3135 / Van Tieghem / Ficuum.
  6. "Crystal structure of phytase from Aspergillus ficuum at 2.5-A resolution."
    Kostrewa D., Gruninger-Leitch F., D'Arcy A., Broger C., Mitchell D., van Loon A.P.G.M.
    Nat. Struct. Biol. 4:185-190(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    Strain: NRRL 3135 / Van Tieghem / Ficuum.

Entry informationi

Entry nameiPHYA_ASPNG
AccessioniPrimary (citable) accession number: P34752
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 26, 2014
This is version 89 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, Direct protein sequencing

Documents

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

External Data

Dasty 3