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P34752

- PHYA_ASPNG

UniProt

P34752 - PHYA_ASPNG

Protein

3-phytase A

Gene

phyA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    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

    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-SubCell

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

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    MGVSAVLLPL YLLSGVTSGL AVPASRNQSS CDTVDQGYQC FSETSHLWGQ    50
    YAPFFSLANE SVISPEVPAG CRVTFAQVLS RHGARYPTDS KGKKYSALIE 100
    EIQQNATTFD GKYAFLKTYN YSLGADDLTP FGEQELVNSG IKFYQRYESL 150
    TRNIVPFIRS SGSSRVIASG KKFIEGFQST KLKDPRAQPG QSSPKIDVVI 200
    SEASSSNNTL DPGTCTVFED SELADTVEAN FTATFVPSIR QRLENDLSGV 250
    TLTDTEVTYL MDMCSFDTIS TSTVDTKLSP FCDLFTHDEW INYDYLQSLK 300
    KYYGHGAGNP LGPTQGVGYA NELIARLTHS PVHDDTSSNH TLDSSPATFP 350
    LNSTLYADFS HDNGIISILF ALGLYNGTKP LSTTTVENIT QTDGFSSAWT 400
    VPFASRLYVE MMQCQAEQEP LVRVLVNDRV VPLHGCPVDA LGRCTRDSFV 450
    RGLSFARSGG DWAECFA 467
    Length:467
    Mass (Da):51,086
    Last modified:February 1, 1994 - v1
    Checksum:i88FE8F3584341D6D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z16414 Genomic DNA. Translation: CAA78904.1.
    M94550 Genomic DNA. Translation: AAA32705.1.
    PIRiJN0482.
    JN0656.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z16414 Genomic DNA. Translation: CAA78904.1 .
    M94550 Genomic DNA. Translation: AAA32705.1 .
    PIRi JN0482.
    JN0656.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 87 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