PHYB_ASPAW
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 25-MAY-2022, entry version 94.
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}.
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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 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; -; 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 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 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
