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Protein

3-phytase B

Gene

phyB

Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei82Nucleophile1
Active sitei338Proton donor1

GO - Molecular functioni

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
ChainiPRO_000002397520 – 4793-phytase BAdd BLAST460

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi71 ↔ 387
Disulfide bondi128 ↔ 472
Glycosylationi191N-linked (GlcNAc...)1
Disulfide bondi216 ↔ 441
Disulfide bondi225 ↔ 298
Glycosylationi315N-linked (GlcNAc...)1
Disulfide bondi413 ↔ 421
Glycosylationi458N-linked (GlcNAc...)1

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1479
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi41 – 43Combined sources3
Helixi45 – 47Combined sources3
Beta strandi71 – 81Combined sources11
Helixi89 – 103Combined sources15
Helixi112 – 119Combined sources8
Helixi127 – 129Combined sources3
Helixi141 – 156Combined sources16
Helixi157 – 159Combined sources3
Beta strandi162 – 164Combined sources3
Beta strandi166 – 173Combined sources8
Helixi174 – 188Combined sources15
Helixi189 – 191Combined sources3
Helixi192 – 195Combined sources4
Beta strandi196 – 201Combined sources6
Helixi205 – 207Combined sources3
Beta strandi210 – 213Combined sources4
Turni224 – 227Combined sources4
Helixi234 – 245Combined sources12
Helixi253 – 266Combined sources14
Turni267 – 269Combined sources3
Helixi276 – 278Combined sources3
Helixi281 – 298Combined sources18
Helixi306 – 323Combined sources18
Helixi325 – 328Combined sources4
Beta strandi330 – 336Combined sources7
Helixi338 – 348Combined sources11
Beta strandi359 – 361Combined sources3
Helixi370 – 372Combined sources3
Beta strandi379 – 387Combined sources9
Beta strandi395 – 403Combined sources9
Beta strandi406 – 408Combined sources3
Helixi417 – 419Combined sources3
Helixi423 – 433Combined sources11
Helixi437 – 440Combined sources4
Turni453 – 455Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QFXX-ray2.40A/B20-479[»]
ProteinModelPortaliP34755.
SMRiP34755.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34755.

Family & Domainsi

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 3 hits.
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.

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:
EMBLi
GenBanki
DDBJi
Links Updated
L02420 Unassigned DNA. Translation: AAA16897.1.
PIRiJN0890.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02420 Unassigned DNA. Translation: AAA16897.1.
PIRiJN0890.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QFXX-ray2.40A/B20-479[»]
ProteinModelPortaliP34755.
SMRiP34755.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP34755.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 3 hits.
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 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: November 2, 2016
This is version 83 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

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.