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P34755

- PHYB_ASPAW

UniProt

P34755 - PHYB_ASPAW

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Protein

3-phytase B

Gene

phyB

Organism
Aspergillus awamori (Black koji mold)
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 – 821Nucleophile
Active sitei338 – 3381Proton donor

GO - Molecular functioni

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

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
3-phytase B (EC:3.1.3.8)
Alternative name(s):
Myo-inositol-hexaphosphate 3-phosphohydrolase B
pH 2.5 optimum acid phosphatase
Gene namesi
Name:phyB
Synonyms:aph
OrganismiAspergillus awamori (Black koji mold)
Taxonomic identifieri105351 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 4794603-phytase BPRO_0000023975Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi71 ↔ 387
Disulfide bondi128 ↔ 472
Glycosylationi191 – 1911N-linked (GlcNAc...)
Disulfide bondi216 ↔ 441
Disulfide bondi225 ↔ 298
Glycosylationi315 – 3151N-linked (GlcNAc...)
Disulfide bondi413 ↔ 421
Glycosylationi458 – 4581N-linked (GlcNAc...)

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
479
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi41 – 433
Helixi45 – 473
Beta strandi71 – 8111
Helixi89 – 10315
Helixi112 – 1198
Helixi127 – 1293
Helixi141 – 15616
Helixi157 – 1593
Beta strandi162 – 1643
Beta strandi166 – 1738
Helixi174 – 18815
Helixi189 – 1913
Helixi192 – 1954
Beta strandi196 – 2016
Helixi205 – 2073
Beta strandi210 – 2134
Turni224 – 2274
Helixi234 – 24512
Helixi253 – 26614
Turni267 – 2693
Helixi276 – 2783
Helixi281 – 29818
Helixi306 – 32318
Helixi325 – 3284
Beta strandi330 – 3367
Helixi338 – 34811
Beta strandi359 – 3613
Helixi370 – 3723
Beta strandi379 – 3879
Beta strandi395 – 4039
Beta strandi406 – 4083
Helixi417 – 4193
Helixi423 – 43311
Helixi437 – 4404
Turni453 – 4553

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QFXX-ray2.40A/B20-479[»]
ProteinModelPortaliP34755.
SMRiP34755. Positions 33-479.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34755.

Family & Domainsi

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1240. 3 hits.
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.

P34755-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPRTSLLTLA CALATGASAF SYGAAIPQST QEKQFSQEFR DGYSILKHYG
60 70 80 90 100
GNGPYSERVS YGIARDPPTS CEVDQVIMVK RHGERYPSPS AGKDIEEALA
110 120 130 140 150
KVYSINTTEY KGDLAFLNDW TYYVPNECYY NAETTSGPYA GLLDAYNHGN
160 170 180 190 200
DYKARYGHLW NGETVVPFFS SGYGRVIETA RKFGEGFFGY NYSTNAALNI
210 220 230 240 250
ISESEVMGAD SLTPTCDTDN DQTTCDNLTY QLPQFKVAAA RLNSQNPGMN
260 270 280 290 300
LTASDVYNLM VMASFELNAR PFSNWINAFT QDEWVSFGYV EDLNYYYCAG
310 320 330 340 350
PGDKNMAAVG AVYANASLTL LNQGPKEAGS LFFNFAHDTN ITPILAALGV
360 370 380 390 400
LIPNEDLPLD RVAFGNPYSI GNIVPMGGHL TIERLSCQAT ALSDEGTYVR
410 420 430 440 450
LVLNEAVLPF NDCTSGPGYS CPLANYTSIL NKNLPDYTTT CNVSASYPQY
460 470
LSFWWNYNTT TELNYRSSPI ACQEGDAMD
Length:479
Mass (Da):52,678
Last modified:February 1, 1994 - v1
Checksum:i4F8E0F3778CC3B08
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L02420 Unassigned DNA. Translation: AAA16897.1.
PIRiJN0890.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L02420 Unassigned DNA. Translation: AAA16897.1 .
PIRi JN0890.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QFX X-ray 2.40 A/B 20-479 [» ]
ProteinModelPortali P34755.
SMRi P34755. Positions 33-479.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P34755.

Family and domain databases

Gene3Di 3.40.50.1240. 3 hits.
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. "The cloning and sequencing of the genes encoding phytase (phy) and pH 2.5-optimum acid phosphatase (aph) from Aspergillus niger var. awamori."
    Piddington C.S., Houston C.S., Paloheimo M.T., Cantrell M.A., Miettinen-Oinonen A., Nevalainen H., Rambosek J.A.
    Gene 133:55-62(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ALK0243.
  2. "Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2.4-A resolution."
    Kostrewa D., Wyss M., D'Arcy A., van Loon A.P.G.M.
    J. Mol. Biol. 288:965-974(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Entry informationi

Entry nameiPHYB_ASPAW
AccessioniPrimary (citable) accession number: P34755
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 1, 2014
This is version 74 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

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