ID A0A1Z5KF48_FISSO Unreviewed; 587 AA.
AC A0A1Z5KF48;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acid phosphatase {ECO:0000313|EMBL:GAX24869.1};
DE EC=3.1.3.2 {ECO:0000313|EMBL:GAX24869.1};
GN ORFNames=FisN_6Hh182 {ECO:0000313|EMBL:GAX24869.1};
OS Fistulifera solaris (Oleaginous diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC Fistulifera.
OX NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX24869.1, ECO:0000313|Proteomes:UP000198406};
RN [1] {ECO:0000313|EMBL:GAX24869.1, ECO:0000313|Proteomes:UP000198406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX24869.1,
RC ECO:0000313|Proteomes:UP000198406};
RX PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT by the genome and transcriptome.";
RL Plant Cell 27:162-176(2015).
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:GAX24869.1}.
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DR EMBL; BDSP01000217; GAX24869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5KF48; -.
DR InParanoid; A0A1Z5KF48; -.
DR OrthoDB; 5486499at2759; -.
DR Proteomes; UP000198406; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003993; F:acid phosphatase 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.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:GAX24869.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198406};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..587
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013097310"
FT TRANSMEM 493..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 587 AA; 66381 MW; 337C51E5176BF131 CRC64;
MQWNSGNRRI TVLLLLLFLH TPSHAQVVFS ANAESWYQRY SHYPPQCSTT AQMQNRTIPP
LTTVGHGESR LQHVTVILRH GARTPVHNQT CGVPLEPWTC PPSTYLAADR ATDDEWLTFP
QIYDALQFPQ YNLSNILPGT CQIGQLLEQG MQQQLTNGLH LRRAYIHSDD EDGPSHKNLH
LPLGGSLDKA VYFRSDDEQR TLQSGQLLLQ AMLGKELEQS GGLTIHTADY TRDIVGDHEA
LCPRLAEFRE RFYRTRDFRI FNESDDAKEL RQFQQEVLGS TGDISDCLLT TICSDRELHP
KINDYDGDQN SETSMFSRLL RFYVQQRTML ATFDFAEYSK LVSGPLRAEI MKNIQTFVES
GGETYVPPFA LFSGHDSTIM AILASMDMFD EQWPTYASML IIEIHEINLD GRKDPALYTS
DFGFRMIYDG KVITDQMKGC PSGQEICDST KLLEAMYYDV KTRNCERLYA IPVEFTPAVT
QATAILVSSR SAFGGFLLLV FFGMTLGGLF TYLYFAHWVP LNLQRKMGAP GRAEMDGIMV
EEPVCYGGDA DDGKRRSGHT ALPTDDSENF TIDDEDDDFV ITNTQLT
//
