ID C1GXU3_PARBA Unreviewed; 528 AA.
AC C1GXU3;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Phytase A {ECO:0000256|ARBA:ARBA00044106};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
DE AltName: Full=Histidine acid phosphatase phyA {ECO:0000256|ARBA:ARBA00044262};
DE AltName: Full=Myo-inositol hexakisphosphate phosphohydrolase A {ECO:0000256|ARBA:ARBA00042300};
DE AltName: Full=Myo-inositol-hexaphosphate 3-phosphohydrolase A {ECO:0000256|ARBA:ARBA00041857};
GN ORFNames=PAAG_03226 {ECO:0000313|EMBL:EEH41663.2};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH41663.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH41663.2, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-
CC inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798,
CC ChEBI:CHEBI:195535; Evidence={ECO:0000256|ARBA:ARBA00043748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116;
CC Evidence={ECO:0000256|ARBA:ARBA00043748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-
CC inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535,
CC ChEBI:CHEBI:195537; Evidence={ECO:0000256|ARBA:ARBA00043670};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120;
CC Evidence={ECO:0000256|ARBA:ARBA00043670};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol
CC 1,2-bisphosphate + phosphate; Xref=Rhea:RHEA:77131,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195537,
CC ChEBI:CHEBI:195539; Evidence={ECO:0000256|ARBA:ARBA00043721};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132;
CC Evidence={ECO:0000256|ARBA:ARBA00043721};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-
CC phosphate + phosphate; Xref=Rhea:RHEA:77135, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195539;
CC Evidence={ECO:0000256|ARBA:ARBA00043675};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136;
CC Evidence={ECO:0000256|ARBA:ARBA00043675};
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 Evidence={ECO:0000256|ARBA:ARBA00043788};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990;
CC Evidence={ECO:0000256|ARBA:ARBA00043788};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; KN293999; EEH41663.2; -; Genomic_DNA.
DR RefSeq; XP_015702095.1; XM_015844889.1.
DR AlphaFoldDB; C1GXU3; -.
DR STRING; 502779.C1GXU3; -.
DR GeneID; 9097778; -.
DR KEGG; pbl:PAAG_03226; -.
DR VEuPathDB; FungiDB:PAAG_03226; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_0_0_1; -.
DR OMA; CRVTFAQ; -.
DR OrthoDB; 2721627at2759; -.
DR Proteomes; UP000002059; Partially assembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 PANTHER; PTHR20963:SF24; 3-PHYTASE B; 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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000894-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 15..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 420
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 89..98
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 129..472
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 273..526
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 322..340
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 497..505
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 528 AA; 58963 MW; 8047D02C6C812F40 CRC64;
MEVNDRTALL AFHDADDESE REVESRASLS SPDVGDSDRR RWTRFSLKDR GSYLQDRCFA
VSAVLILMLI CGGFIVAFVY KSSGRGLVCT TVQNGYQCHQ KYSQHWGQYT PFFSLRTISE
TSPDIPVGCT VTFVQVLSRH GARYPTKNKS STYSQLIKRI QDRTKTYLSE FAVLETFNYQ
LQTDDLTPFG ESQLTDSGIK FYRRYQHLTK KSKIFIRASG SPRVIVSAEK FIEGFYQEKL
RDPTATDKDA KPSVAVILSE DPGSNNTLEH GNCDLFEETK PSHVVQKEFA KVFASPILNR
FSSHLIGSNL DVADIVHLMD LCSFHTVAFT PDARTISPLC NLFSNEEWTQ YDYYNTLGKY
YGFGAGNPLG ASQGVGFVNE LISRLTSKPV SDSTSVNHTL DSDPKTFPLG LPLYADFGHD
NTMTSIFTAL GIFNDTQPLS NSTVQGPSET KGFSASWIVP FAARAYIEKM ECDSTPVARE
PLVRVVINDR VVPLHGCKVD SLGRCRLKDF VEGLSYARAG GDWEKCSI
//
