ID A0A0D2FY57_9EURO Unreviewed; 564 AA.
AC A0A0D2FY57;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=Z518_01885 {ECO:0000313|EMBL:KIX07232.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX07232.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX07232.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX07232.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-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}.
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DR EMBL; KN847476; KIX07232.1; -; Genomic_DNA.
DR RefSeq; XP_013274368.1; XM_013418914.1.
DR AlphaFoldDB; A0A0D2FY57; -.
DR STRING; 1442369.A0A0D2FY57; -.
DR GeneID; 25289956; -.
DR VEuPathDB; FungiDB:Z518_01885; -.
DR HOGENOM; CLU_030431_3_1_1; -.
DR OrthoDB; 5486499at2759; -.
DR Proteomes; UP000053617; 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:UP000053617}.
FT REGION 395..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 62448 MW; 8CFAE334970E7F01 CRC64;
MTSLIPRPPY TQEELDRLYP KGLELRLVQI LLRHGERTPV SARFGNAGLP AYWPYCNAAQ
RLLSVAMTPE SVSQWNSLQW RRRLERFGED DGPVIAAGPA GEADGVCQLG ELTDRGRETT
YELGRRLRHL YVDQLKFMPA LIANADLIYL RATPLPRALE SVQQTFWGMY PLTARTAAFP
APTIVTRTPA DETLFPNDGN CRRFAQLSRA FAQRTADRWN DTDDMKYVTK LIGKWMPENS
NKQVAVDSHP RLSGIMDTIN ATLAHGPPTR LPREFYDEKS RAIIDRIGVE EWFSGYNENR
EYRMLGIGSL IGDIVERMTS KIEGAGLSIN EIGGENGRLG KGRGGEKGIR FAISGCHDTT
LAGVLTSLGA FNGEKWPPYT SHIAFELFRK SDLDTPASAE TSDTPVFSEP RAPGDSSTKQ
DFFASFLGLR SPTTSSQSSS ASSSSNPLSP SRLSAHSTFS SVVPPQDLIA RSPHNELSES
QKARLEPYYV RIRYNDGVMK IPACAKPGNN YEGDESICTF EAFKRVADGY VPKNWKVQCG
ENMDKAIAGL DSAPEMAGQI EEGF
//
