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O00093

- PHYB_EMENI

UniProt

O00093 - PHYB_EMENI

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Protein

3-phytase B

Gene

phyB

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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 sitei80 – 801NucleophileBy similarity
Active sitei358 – 3581Proton 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. 2065.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:phyB
ORF Names:AN1685
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome VII

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: ASPGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 4634443-phytase BPRO_0000023976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi26 – 261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00008327.

Structurei

3D structure databases

ProteinModelPortaliO00093.
SMRiO00093. Positions 29-461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG260296.
HOGENOMiHOG000189493.
InParanoidiO00093.
OMAiWAQYSPY.
OrthoDBiEOG7QC85C.

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.

O00093-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFFTVALSL YYLLSRVSTQ APVVQNHSCN TADGGYQCFP NVSHVWGQYS
60 70 80 90 100
PYFSIEQESA ISEDVPHGCE VTFVQVLSRH GARYPTESKS KAYSGLIEAI
110 120 130 140 150
QKNATSFWGQ YAFLESYNYT LGADDLTIFG ENQMVDSGAK FYRRYKNLAR
160 170 180 190 200
KNTPFIRASG SDRVVASAEK FINGFRKAQL HDHGSKRATP VVNVIIPEID
210 220 230 240 250
GFNNTLDHST CVSFENDERA DEIEANFTAI MGPPIRKRLE NDLPGIKLTN
260 270 280 290 300
ENVIYLMDMC SFDTMARTAH GTELSPFCAI FTEKEWLQYD YLQSLSKYYG
310 320 330 340 350
YGAGSPLGPA QGIGFTNELI ARLTQSPVQD NTSTNHTLDS NPATFPLDRK
360 370 380 390 400
LYADFSHDNS MISIFFAMGL YNGTQPLSMD SVESIQEMDG YAASWTVPFG
410 420 430 440 450
ARAYFELMQC EKKEPLVRVL VNDRVVPLHG CAVDKFGRCT LDDWVEGLNF
460
ARSGGNWKTC FTL
Length:463
Mass (Da):51,816
Last modified:May 1, 2007 - v2
Checksum:i1D6BC0B0DA14F0D9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191T → A in AAB96871. (PubMed:9349716)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59803 Genomic DNA. Translation: AAB96871.1.
AACD01000026 Genomic DNA. Translation: EAA64805.1.
BN001307 Genomic DNA. Translation: CBF85365.1.
RefSeqiXP_659289.1. XM_654197.1.

Genome annotation databases

EnsemblFungiiCADANIAT00008327; CADANIAP00008327; CADANIAG00008327.
GeneIDi2874708.
KEGGiani:AN1685.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59803 Genomic DNA. Translation: AAB96871.1 .
AACD01000026 Genomic DNA. Translation: EAA64805.1 .
BN001307 Genomic DNA. Translation: CBF85365.1 .
RefSeqi XP_659289.1. XM_654197.1.

3D structure databases

ProteinModelPortali O00093.
SMRi O00093. Positions 29-461.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00008327.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00008327 ; CADANIAP00008327 ; CADANIAG00008327 .
GeneIDi 2874708.
KEGGi ani:AN1685.2.

Phylogenomic databases

eggNOGi NOG260296.
HOGENOMi HOG000189493.
InParanoidi O00093.
OMAi WAQYSPY.
OrthoDBi EOG7QC85C.

Enzyme and pathway databases

BRENDAi 3.1.3.8. 2065.

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

« Hide 'large scale' publications
  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. 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.
    , 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.

Entry informationi

Entry nameiPHYB_EMENI
AccessioniPrimary (citable) accession number: O00093
Secondary accession number(s): C8VNT4, Q5BCP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 2007
Last modified: October 29, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3