PHYB_EMENI
ID PHYB_EMENI Reviewed; 463 AA.
AC O00093; C8VNT4; Q5BCP5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=3-phytase B;
DE EC=3.1.3.8;
DE AltName: Full=3 phytase B;
DE AltName: Full=Myo-inositol hexakisphosphate phosphohydrolase B;
DE AltName: Full=Myo-inositol-hexaphosphate 3-phosphohydrolase B;
DE Flags: Precursor;
GN Name=phyB; ORFNames=AN1685;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9349716; DOI=10.1016/s0167-4781(97)00107-3;
RA Pasamontes L., Haiker M., Henriquez-Huecas M., Mitchell D.B.,
RA van Loon A.P.G.M.;
RT "Cloning of the phytases from Emericella nidulans and the thermophilic
RT fungus Talaromyces thermophilus.";
RL Biochim. Biophys. Acta 1353:217-223(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of inorganic orthophosphate from
CC phytate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol
CC 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798,
CC ChEBI:CHEBI:58130; EC=3.1.3.8;
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; U59803; AAB96871.1; -; Genomic_DNA.
DR EMBL; AACD01000026; EAA64805.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF85365.1; -; Genomic_DNA.
DR RefSeq; XP_659289.1; XM_654197.1.
DR AlphaFoldDB; O00093; -.
DR SMR; O00093; -.
DR STRING; 162425.CADANIAP00008327; -.
DR EnsemblFungi; CBF85365; CBF85365; ANIA_01685.
DR EnsemblFungi; EAA64805; EAA64805; AN1685.2.
DR GeneID; 2874708; -.
DR KEGG; ani:AN1685.2; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_0_0_1; -.
DR InParanoid; O00093; -.
DR OMA; YLMDLCP; -.
DR OrthoDB; 1046588at2759; -.
DR BRENDA; 3.1.3.26; 517.
DR BRENDA; 3.1.3.8; 517.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016158; F:3-phytase activity; IEA:UniProtKB-EC.
DR GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR016274; Histidine_acid_Pase_euk.
DR Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..463
FT /note="3-phytase B"
FT /id="PRO_0000023976"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 358
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 19
FT /note="T -> A (in Ref. 1; AAB96871)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 51816 MW; 1D6BC0B0DA14F0D9 CRC64;
MAFFTVALSL YYLLSRVSTQ APVVQNHSCN TADGGYQCFP NVSHVWGQYS PYFSIEQESA
ISEDVPHGCE VTFVQVLSRH GARYPTESKS KAYSGLIEAI QKNATSFWGQ YAFLESYNYT
LGADDLTIFG ENQMVDSGAK FYRRYKNLAR KNTPFIRASG SDRVVASAEK FINGFRKAQL
HDHGSKRATP VVNVIIPEID GFNNTLDHST CVSFENDERA DEIEANFTAI MGPPIRKRLE
NDLPGIKLTN ENVIYLMDMC SFDTMARTAH GTELSPFCAI FTEKEWLQYD YLQSLSKYYG
YGAGSPLGPA QGIGFTNELI ARLTQSPVQD NTSTNHTLDS NPATFPLDRK LYADFSHDNS
MISIFFAMGL YNGTQPLSMD SVESIQEMDG YAASWTVPFG ARAYFELMQC EKKEPLVRVL
VNDRVVPLHG CAVDKFGRCT LDDWVEGLNF ARSGGNWKTC FTL
