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O00093 (PHYB_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-phytase B

EC=3.1.3.8
Alternative name(s):
3 phytase B
Myo-inositol hexakisphosphate phosphohydrolase B
Myo-inositol-hexaphosphate 3-phosphohydrolase B
Gene names
Name:phyB
ORF Names:AN1685
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the hydrolysis of inorganic orthophosphate from phytate.

Catalytic activity

Myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate.

Sequence similarities

Belongs to the histidine acid phosphatase family.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from direct assay PubMed 22835028. Source: ASPGD

   Molecular_function3-phytase activity

Inferred from electronic annotation. Source: UniProtKB-EC

acid phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 4634443-phytase B
PRO_0000023976

Sites

Active site801Nucleophile By similarity
Active site3581Proton donor By similarity

Amino acid modifications

Glycosylation261N-linked (GlcNAc...) Potential
Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation2031N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict191T → A in AAB96871. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O00093 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 1D6BC0B0DA14F0D9

FASTA46351,816
        10         20         30         40         50         60 
MAFFTVALSL YYLLSRVSTQ APVVQNHSCN TADGGYQCFP NVSHVWGQYS PYFSIEQESA 

        70         80         90        100        110        120 
ISEDVPHGCE VTFVQVLSRH GARYPTESKS KAYSGLIEAI QKNATSFWGQ YAFLESYNYT 

       130        140        150        160        170        180 
LGADDLTIFG ENQMVDSGAK FYRRYKNLAR KNTPFIRASG SDRVVASAEK FINGFRKAQL 

       190        200        210        220        230        240 
HDHGSKRATP VVNVIIPEID GFNNTLDHST CVSFENDERA DEIEANFTAI MGPPIRKRLE 

       250        260        270        280        290        300 
NDLPGIKLTN ENVIYLMDMC SFDTMARTAH GTELSPFCAI FTEKEWLQYD YLQSLSKYYG 

       310        320        330        340        350        360 
YGAGSPLGPA QGIGFTNELI ARLTQSPVQD NTSTNHTLDS NPATFPLDRK LYADFSHDNS 

       370        380        390        400        410        420 
MISIFFAMGL YNGTQPLSMD SVESIQEMDG YAASWTVPFG ARAYFELMQC EKKEPLVRVL 

       430        440        450        460 
VNDRVVPLHG CAVDKFGRCT LDDWVEGLNF ARSGGNWKTC FTL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the phytases from Emericella nidulans and the thermophilic fungus Talaromyces thermophilus."
Pasamontes L., Haiker M., Henriquez-Huecas M., Mitchell D.B., van Loon A.P.G.M.
Biochim. Biophys. Acta 1353:217-223(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U59803 Genomic DNA. Translation: AAB96871.1.
AACD01000026 Genomic DNA. Translation: EAA64805.1.
BN001307 Genomic DNA. Translation: CBF85365.1.
RefSeqXP_659289.1. XM_654197.1.

3D structure databases

ProteinModelPortalO00093.
SMRO00093. Positions 29-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00008327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00008327; CADANIAP00008327; CADANIAG00008327.
GeneID2874708.
KEGGani:AN1685.2.

Phylogenomic databases

eggNOGNOG260296.
HOGENOMHOG000189493.
OMAWAQYSPY.
OrthoDBEOG7QC85C.

Enzyme and pathway databases

BRENDA3.1.3.8. 2065.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
InterProIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFPIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMSSF53254. SSF53254. 1 hit.
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHYB_EMENI
AccessionPrimary (citable) accession number: O00093
Secondary accession number(s): C8VNT4, Q5BCP5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 2007
Last modified: June 11, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families