PHYA_ASPFU
ID PHYA_ASPFU Reviewed; 465 AA.
AC O00092; Q4WPA8; Q8WZJ5;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 137.
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; Synonyms=phyA3; ORFNames=AFUA_4G08630;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-37, AND
RP CHARACTERIZATION.
RC STRAIN=ATCC 34625 / CS-270;
RX PubMed=9143104; DOI=10.1128/aem.63.5.1696-1700.1997;
RA Pasamontes L., Haiker M., Wyss M., Tessier M., van Loon A.P.G.M.;
RT "Gene cloning, purification, and characterization of a heat-stable phytase
RT from the fungus Aspergillus fumigatus.";
RL Appl. Environ. Microbiol. 63:1696-1700(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-465.
RC STRAIN=CCTCC AF93024;
RA Zhang G.;
RT "Cloning of phytase gene from Aspergillus fumigatus and its expression in
RT Pichia pastoris.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 27-465, AND DISULFIDE BONDS.
RX PubMed=15341723; DOI=10.1016/j.str.2004.06.015;
RA Liu Q., Huang Q., Lei X.G., Hao Q.;
RT "Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its
RT enzymatic dynamics.";
RL Structure 12:1575-1583(2004).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Highly active from pH 3 to 5 with 4-nitrophenyl phosphate as
CC substrate, and from 2.5 to 7.5 with phytic acid.;
CC Temperature dependence:
CC Able to withstand temperatures up to 100 degrees Celsius over a
CC period of 20 min, with a loss of only 10% of the initial enzymatic
CC activity.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL89926.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U59804; AAB96872.1; -; Genomic_DNA.
DR EMBL; AAHF01000005; EAL89926.2; ALT_INIT; Genomic_DNA.
DR EMBL; AJ419776; CAD12029.1; -; Genomic_DNA.
DR RefSeq; XP_751964.2; XM_746871.2.
DR PDB; 1QWO; X-ray; 1.50 A; A=24-465.
DR PDB; 1SK8; X-ray; 1.65 A; A=27-464.
DR PDB; 1SK9; X-ray; 1.64 A; A=27-464.
DR PDB; 1SKA; X-ray; 1.69 A; A=27-464.
DR PDB; 1SKB; X-ray; 1.58 A; A=27-464.
DR PDBsum; 1QWO; -.
DR PDBsum; 1SK8; -.
DR PDBsum; 1SK9; -.
DR PDBsum; 1SKA; -.
DR PDBsum; 1SKB; -.
DR AlphaFoldDB; O00092; -.
DR SMR; O00092; -.
DR STRING; 746128.CADAFUBP00006397; -.
DR GeneID; 3509324; -.
DR KEGG; afm:AFUA_4G08630; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_0_0_1; -.
DR InParanoid; O00092; -.
DR OrthoDB; 1046588at2759; -.
DR BRENDA; 3.1.3.26; 508.
DR BRENDA; 3.1.3.8; 508.
DR EvolutionaryTrace; O00092; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:9143104"
FT CHAIN 27..465
FT /note="3-phytase A"
FT /id="PRO_0000023969"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 360
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 30..39
FT /evidence="ECO:0000269|PubMed:15341723"
FT DISULFID 70..412
FT /evidence="ECO:0000269|PubMed:15341723"
FT DISULFID 213..463
FT /evidence="ECO:0000269|PubMed:15341723"
FT DISULFID 262..280
FT /evidence="ECO:0000269|PubMed:15341723"
FT DISULFID 434..442
FT /evidence="ECO:0000269|PubMed:15341723"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1QWO"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:1QWO"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 88..104
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:1QWO"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:1QWO"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 163..181
FT /evidence="ECO:0007829|PDB:1QWO"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:1QWO"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1SK8"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 221..244
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 252..269
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 285..302
FT /evidence="ECO:0007829|PDB:1QWO"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 315..326
FT /evidence="ECO:0007829|PDB:1QWO"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:1QWO"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:1QWO"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 360..369
FT /evidence="ECO:0007829|PDB:1QWO"
FT TURN 370..375
FT /evidence="ECO:0007829|PDB:1QWO"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:1QWO"
FT STRAND 404..412
FT /evidence="ECO:0007829|PDB:1QWO"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:1QWO"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 444..450
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 452..456
FT /evidence="ECO:0007829|PDB:1QWO"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:1QWO"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:1QWO"
SQ SEQUENCE 465 AA; 50836 MW; 86FC1D9058C9B2C9 CRC64;
MVTLTFLLSA AYLLSGRVSA APSSAGSKSC DTVDLGYQCS PATSHLWGQY SPFFSLEDEL
SVSSKLPKDC RITLVQVLSR HGARYPTSSK SKKYKKLVTA IQANATDFKG KFAFLKTYNY
TLGADDLTPF GEQQLVNSGI KFYQRYKALA RSVVPFIRAS GSDRVIASGE KFIEGFQQAK
LADPGATNRA APAISVIIPE SETFNNTLDH GVCTKFEASQ LGDEVAANFT ALFAPDIRAR
AEKHLPGVTL TDEDVVSLMD MCSFDTVART SDASQLSPFC QLFTHNEWKK YNYLQSLGKY
YGYGAGNPLG PAQGIGFTNE LIARLTRSPV QDHTSTNSTL VSNPATFPLN ATMYVDFSHD
NSMVSIFFAL GLYNGTEPLS RTSVESAKEL DGYSASWVVP FGARAYFETM QCKSEKEPLV
RALINDRVVP LHGCDVDKLG RCKLNDFVKG LSWARSGGNW GECFS
