PHYA_ASPNG
ID PHYA_ASPNG Reviewed; 467 AA.
AC P34752;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=3-phytase A;
DE EC=3.1.3.8;
DE AltName: Full=3 phytase A;
DE AltName: Full=Myo-inositol hexakisphosphate phosphohydrolase A;
DE AltName: Full=Myo-inositol-hexaphosphate 3-phosphohydrolase A;
DE Flags: Precursor;
GN Name=phyA;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=NRRL 3135 / Van Tieghem / Ficuum;
RX PubMed=8387447; DOI=10.1016/0378-1119(93)90620-i;
RA van Hartingsveldt W., van Zeijl C.M.J., Harteveld G.M., Gouka R.J.,
RA Suykerbuyk M.E.G., Luiten R.G.M., van Paridon P.A., Selten G.C.M.,
RA Veenstra A.E., van Gorcom R.F.M., van den Hondel C.A.M.J.J.;
RT "Cloning, characterization and overexpression of the phytase-encoding gene
RT (phyA) of Aspergillus niger.";
RL Gene 127:87-94(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mullaney E.J.;
RT "Sequence of the Aspergillus niger (ficuum) phytase gene.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 24-464.
RC STRAIN=NRRL 3135 / Van Tieghem / Ficuum;
RX PubMed=8387289; DOI=10.1006/bbrc.1993.1477;
RA Ullah A.H.J., Dischinger H.C. Jr.;
RT "Aspergillus ficuum phytase: complete primary structure elucidation by
RT chemical sequencing.";
RL Biochem. Biophys. Res. Commun. 192:747-753(1993).
RN [4]
RP PROTEIN SEQUENCE OF 71-93.
RC STRAIN=NRRL 3135 / Van Tieghem / Ficuum;
RX PubMed=1648914; DOI=10.1016/0006-291x(91)91777-a;
RA Ullah A.H.J., Cummins B.J., Dischinger H.C. Jr.;
RT "Cyclohexanedione modification of arginine at the active site of
RT Aspergillus ficuum phytase.";
RL Biochem. Biophys. Res. Commun. 178:45-53(1991).
RN [5]
RP CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=NRRL 3135 / Van Tieghem / Ficuum;
RX PubMed=2852807; DOI=10.1080/00327488808062544;
RA Ullah A.H.J.;
RT "Aspergillus ficuum phytase: partial primary structure, substrate
RT selectivity, and kinetic characterization.";
RL Prep. Biochem. 18:459-471(1988).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC STRAIN=NRRL 3135 / Van Tieghem / Ficuum;
RX PubMed=9164457; DOI=10.1038/nsb0397-185;
RA Kostrewa D., Gruninger-Leitch F., D'Arcy A., Broger C., Mitchell D.,
RA van Loon A.P.G.M.;
RT "Crystal structure of phytase from Aspergillus ficuum at 2.5-A
RT resolution.";
RL Nat. Struct. Biol. 4:185-190(1997).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- BIOTECHNOLOGY: Is used as a food and feed additive. It can facilitate
CC the degradation of phytin in soybean and other seeds used as food for
CC monogastric animals. Sold by Novo Nordisk under the name Phytase Novo.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; Z16414; CAA78904.1; -; Genomic_DNA.
DR EMBL; M94550; AAA32705.1; -; Genomic_DNA.
DR PIR; JN0482; JN0482.
DR PIR; JN0656; JN0656.
DR PDB; 1IHP; X-ray; 2.50 A; A=30-467.
DR PDB; 3K4P; X-ray; 2.40 A; A/B=24-467.
DR PDB; 3K4Q; X-ray; 2.20 A; A/B=24-467.
DR PDBsum; 1IHP; -.
DR PDBsum; 3K4P; -.
DR PDBsum; 3K4Q; -.
DR AlphaFoldDB; P34752; -.
DR SMR; P34752; -.
DR STRING; 5061.CADANGAP00003968; -.
DR VEuPathDB; FungiDB:An04g03460; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1126241; -.
DR VEuPathDB; FungiDB:ATCC64974_79310; -.
DR VEuPathDB; FungiDB:M747DRAFT_260190; -.
DR eggNOG; KOG1382; Eukaryota.
DR BRENDA; 3.1.3.26; 518.
DR BRENDA; 3.1.3.8; 518.
DR EvolutionaryTrace; P34752; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016158; F:3-phytase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:8387289"
FT CHAIN 24..467
FT /note="3-phytase A"
FT /id="PRO_0000023970"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 362
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 31..40
FT DISULFID 71..414
FT DISULFID 215..465
FT DISULFID 264..282
FT DISULFID 436..444
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3K4Q"
FT STRAND 71..81
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 89..105
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:3K4Q"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 130..146
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:3K4Q"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 164..182
FT /evidence="ECO:0007829|PDB:3K4Q"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:3K4Q"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 254..268
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 287..304
FT /evidence="ECO:0007829|PDB:3K4Q"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 317..328
FT /evidence="ECO:0007829|PDB:3K4Q"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:3K4Q"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:3K4Q"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 362..371
FT /evidence="ECO:0007829|PDB:3K4Q"
FT TURN 372..377
FT /evidence="ECO:0007829|PDB:3K4Q"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:3K4Q"
FT TURN 389..394
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:3K4Q"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:3K4Q"
FT STRAND 406..414
FT /evidence="ECO:0007829|PDB:3K4Q"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:3K4Q"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 446..452
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 454..457
FT /evidence="ECO:0007829|PDB:3K4Q"
FT TURN 458..461
FT /evidence="ECO:0007829|PDB:3K4Q"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:3K4Q"
SQ SEQUENCE 467 AA; 51086 MW; 88FE8F3584341D6D CRC64;
MGVSAVLLPL YLLSGVTSGL AVPASRNQSS CDTVDQGYQC FSETSHLWGQ YAPFFSLANE
SVISPEVPAG CRVTFAQVLS RHGARYPTDS KGKKYSALIE EIQQNATTFD GKYAFLKTYN
YSLGADDLTP FGEQELVNSG IKFYQRYESL TRNIVPFIRS SGSSRVIASG KKFIEGFQST
KLKDPRAQPG QSSPKIDVVI SEASSSNNTL DPGTCTVFED SELADTVEAN FTATFVPSIR
QRLENDLSGV TLTDTEVTYL MDMCSFDTIS TSTVDTKLSP FCDLFTHDEW INYDYLQSLK
KYYGHGAGNP LGPTQGVGYA NELIARLTHS PVHDDTSSNH TLDSSPATFP LNSTLYADFS
HDNGIISILF ALGLYNGTKP LSTTTVENIT QTDGFSSAWT VPFASRLYVE MMQCQAEQEP
LVRVLVNDRV VPLHGCPVDA LGRCTRDSFV RGLSFARSGG DWAECFA
