ID PHYB_ASPAW Reviewed; 479 AA. AC P34755; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 22-FEB-2023, entry version 96. DE RecName: Full=3-phytase B; DE EC=3.1.3.8; DE AltName: Full=Myo-inositol-hexaphosphate 3-phosphohydrolase B; DE AltName: Full=pH 2.5 optimum acid phosphatase; DE Flags: Precursor; GN Name=phyB; Synonyms=aph; OS Aspergillus awamori (Black koji mold). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=105351; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ALK0243; RX PubMed=8224894; DOI=10.1016/0378-1119(93)90224-q; RA Piddington C.S., Houston C.S., Paloheimo M.T., Cantrell M.A., RA Miettinen-Oinonen A., Nevalainen H., Rambosek J.A.; RT "The cloning and sequencing of the genes encoding phytase (phy) and pH 2.5- RT optimum acid phosphatase (aph) from Aspergillus niger var. awamori."; RL Gene 133:55-62(1993). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=10329192; DOI=10.1006/jmbi.1999.2736; RA Kostrewa D., Wyss M., D'Arcy A., van Loon A.P.G.M.; RT "Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2.4-A RT resolution."; RL J. Mol. Biol. 288:965-974(1999). 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 -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L02420; AAA16897.1; -; Unassigned_DNA. DR PIR; JN0890; JN0890. DR PDB; 1QFX; X-ray; 2.40 A; A/B=20-479. DR PDBsum; 1QFX; -. DR AlphaFoldDB; P34755; -. DR SMR; P34755; -. DR GlyCosmos; P34755; 3 sites, No reported glycans. DR EvolutionaryTrace; P34755; -. DR GO; GO:0016158; F:3-phytase activity; IEA:UniProtKB-EC. DR CDD; cd07061; HP_HAP_like; 1. DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 3. 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 PANTHER; PTHR20963:SF18; ACID PHOSPHATASE PHO11-RELATED; 1. DR PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1. DR Pfam; PF00328; His_Phos_2; 1. DR PIRSF; PIRSF000894; Acid_phosphatase; 1. DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1. DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1. DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000250" FT CHAIN 20..479 FT /note="3-phytase B" FT /id="PRO_0000023975" FT ACT_SITE 82 FT /note="Nucleophile" FT ACT_SITE 338 FT /note="Proton donor" FT CARBOHYD 191 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 315 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 458 FT /note="N-linked (GlcNAc...) asparagine" FT DISULFID 71..387 FT DISULFID 128..472 FT DISULFID 216..441 FT DISULFID 225..298 FT DISULFID 413..421 FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:1QFX" FT STRAND 71..81 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 89..103 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 112..119 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 141..156 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:1QFX" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:1QFX" FT STRAND 166..173 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 174..188 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 192..195 FT /evidence="ECO:0007829|PDB:1QFX" FT STRAND 196..201 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:1QFX" FT STRAND 210..213 FT /evidence="ECO:0007829|PDB:1QFX" FT TURN 224..227 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 234..245 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 253..266 FT /evidence="ECO:0007829|PDB:1QFX" FT TURN 267..269 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 276..278 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 281..298 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 306..323 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 325..328 FT /evidence="ECO:0007829|PDB:1QFX" FT STRAND 330..336 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 338..348 FT /evidence="ECO:0007829|PDB:1QFX" FT STRAND 359..361 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 370..372 FT /evidence="ECO:0007829|PDB:1QFX" FT STRAND 379..387 FT /evidence="ECO:0007829|PDB:1QFX" FT STRAND 395..403 FT /evidence="ECO:0007829|PDB:1QFX" FT STRAND 406..408 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 417..419 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 423..433 FT /evidence="ECO:0007829|PDB:1QFX" FT HELIX 437..440 FT /evidence="ECO:0007829|PDB:1QFX" FT TURN 453..455 FT /evidence="ECO:0007829|PDB:1QFX" SQ SEQUENCE 479 AA; 52678 MW; 4F8E0F3778CC3B08 CRC64; MPRTSLLTLA CALATGASAF SYGAAIPQST QEKQFSQEFR DGYSILKHYG GNGPYSERVS YGIARDPPTS CEVDQVIMVK RHGERYPSPS AGKDIEEALA KVYSINTTEY KGDLAFLNDW TYYVPNECYY NAETTSGPYA GLLDAYNHGN DYKARYGHLW NGETVVPFFS SGYGRVIETA RKFGEGFFGY NYSTNAALNI ISESEVMGAD SLTPTCDTDN DQTTCDNLTY QLPQFKVAAA RLNSQNPGMN LTASDVYNLM VMASFELNAR PFSNWINAFT QDEWVSFGYV EDLNYYYCAG PGDKNMAAVG AVYANASLTL LNQGPKEAGS LFFNFAHDTN ITPILAALGV LIPNEDLPLD RVAFGNPYSI GNIVPMGGHL TIERLSCQAT ALSDEGTYVR LVLNEAVLPF NDCTSGPGYS CPLANYTSIL NKNLPDYTTT CNVSASYPQY LSFWWNYNTT TELNYRSSPI ACQEGDAMD //