ID R4XFC4_TAPDE Unreviewed; 421 AA.
AC R4XFC4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=3-phytase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TAPDE_005013 {ECO:0000313|EMBL:CCG84574.1};
OS Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC Taphrinales; Taphrinaceae; Taphrina.
OX NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG84574.1, ECO:0000313|Proteomes:UP000013776};
RN [1] {ECO:0000313|EMBL:CCG84574.1, ECO:0000313|Proteomes:UP000013776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA Overmyer K., Hauser P.M., Pagni M.;
RT "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT agent of peach leaf curl.";
RL MBio 4:e00055-e00013(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000032};
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCG84574.1}.
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DR EMBL; CAHR02000266; CCG84574.1; -; Genomic_DNA.
DR AlphaFoldDB; R4XFC4; -.
DR STRING; 1097556.R4XFC4; -.
DR VEuPathDB; FungiDB:TAPDE_005013; -.
DR eggNOG; KOG3720; Eukaryota.
DR Proteomes; UP000013776; Unassembled WGS sequence.
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 PANTHER; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000013776}.
SQ SEQUENCE 421 AA; 47386 MW; 19A1AACF29637781 CRC64;
MASLLPSDIH RYSDAELSEL YPADLKLLLV QSIFRHGERA PVRVRLENAG IPRHFDLCNH
VSLFQAAVKL VNDAGNTTWG RLPYTRLIEE TDDTGKARLA SPGSAKGTCL LGELTDKGRA
STVHLGERLR ELYVTRLGFA REINVSKELY LRSSPMPRAL ESLQQVYSGL FPVDTLNRLT
EPIHIRQRNF TEENLFPNEG MCPKLRQLSV EYAKKAADEW NPILAGHVTD VLGRYVDAPV
RVDGHPRLSG LMDTINATRG NDLELPAELL DAEMLDTMHK AVVSEWFGGY LADNTYRRLG
AGRILGDFKD QIVAVTKGSP LKFALYGAHD TTLGAILASV GGFDHEWPRF TSHIALETFE
RKSSSFLGLF EARQHLVRMR YNDRIINIPS CRNPQMCTLK EFVDLVDKLT PDDWQEECKI
N
//
