ID A0A139IS08_9PEZI Unreviewed; 502 AA.
AC A0A139IS08;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=AC579_5699 {ECO:0000313|EMBL:KXT17475.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT17475.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT17475.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT17475.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT17475.1}.
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DR EMBL; LFZO01000020; KXT17475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139IS08; -.
DR STRING; 113226.A0A139IS08; -.
DR Proteomes; UP000073492; Unassembled WGS sequence.
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 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000073492}.
SQ SEQUENCE 502 AA; 55782 MW; 4E45BF7395500A57 CRC64;
MTTLQPRPPY DDDELKKLYP SNLELQQVQI ILRHGERTPV SARFKNAGLH ATWPYCRAAY
QLKAAILAAD GSWDSLAWKR RLETFGSNDA PKLAAGSRGE IDGVCLPGEL TDRGRETTLA
LGQRLRTLYV TQLGFLPKFL DEQSKSQVSL RATPIQRALE SVQQTFTGLY PSASRSPGML
SPSIVQRSMQ DETLFPNEGG CARFAELSHQ FADRAAKLWN DSPEMMYINK KVGKWMPKDS
PMAKVDSHPR LSGLMDTINA TLAHGPATRL PSEFYDETVR ANIDRICVEE WFAGYQETNE
YRRLGIGGLV GDLTQRMVEH TTGQAKEGQD EPLKMGLSGC HDTTIAATLA ALGAFHHEKD
KWPNFTSSIA FELFKSKDAP ASSAGAVWPS KEKSWWYSLF SSSQASADVA AREPIVSMPQ
SMRQKLEGHY VRLRYNDTPV TLPFCKAQGR HLEGDESFCT LAAFKEAADM ITPKDWKTEC
KSNLGTSAFP EKVQPPPGIS AR
//
