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Database: UniProt
Entry: R5PG66_9BACT
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ID   R5PG66_9BACT            Unreviewed;       322 AA.
AC   R5PG66;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=acid phosphatase {ECO:0000256|ARBA:ARBA00012646, ECO:0000256|PIRNR:PIRNR000898};
DE            EC=3.1.3.2 {ECO:0000256|ARBA:ARBA00012646, ECO:0000256|PIRNR:PIRNR000898};
GN   ORFNames=BN465_02333 {ECO:0000313|EMBL:CCZ13114.1};
OS   Prevotella sp. CAG:1092.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262919 {ECO:0000313|EMBL:CCZ13114.1, ECO:0000313|Proteomes:UP000017987};
RN   [1] {ECO:0000313|EMBL:CCZ13114.1, ECO:0000313|Proteomes:UP000017987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1092 {ECO:0000313|Proteomes:UP000017987};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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         ECO:0000256|PIRNR:PIRNR000898};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000898-1};
CC       Note=Binds 2 iron ions per subunit. {ECO:0000256|PIRSR:PIRSR000898-1};
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:CCZ13114.1}.
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DR   EMBL; CAZL010000428; CCZ13114.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5PG66; -.
DR   STRING; 1262919.BN465_02333; -.
DR   Proteomes; UP000017987; Unassembled WGS sequence.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR024927; Acid_PPase.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR10161; TARTRATE-RESISTANT ACID PHOSPHATASE TYPE 5; 1.
DR   PANTHER; PTHR10161:SF14; TARTRATE-RESISTANT ACID PHOSPHATASE TYPE 5; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF000898; Acid_Ptase_5; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000898};
KW   Iron {ECO:0000256|PIRNR:PIRNR000898, ECO:0000256|PIRSR:PIRSR000898-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000898-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017987};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..322
FT                   /note="acid phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004388739"
FT   DOMAIN          44..252
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   BINDING         49
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT   BINDING         82
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT   BINDING         82
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT   BINDING         120
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT   BINDING         211
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT   BINDING         249
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT   BINDING         251
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
SQ   SEQUENCE   322 AA;  36778 MW;  BAC6DEDA9AAA1517 CRC64;
     MKVMRVCGNS VAMMLMVAYL LLGSLQMQAQ NRAEWEKLKG DVTLYITNDM GRNGYYDQKP
     IAELMGEMAG VVDPECVLAV GDIHHFNGVA SLQDPLWMTN YELIYSHPDL MLDWFPVCGN
     HEYRGNTQAF MDYGKVSRRW MMPAKYYTKV FNHGNTTIRI VFLDTTPLID FYRENSAVYP
     DACKQDMQAQ LSWLDETLKN AKEDWVVVVG HHPIYAETGK KENERIDMQK RLLPILHKYN
     NVAIYACGHI HNFQHIQKKG DNIDYVVNSS SSLARPVKPI DGTVFCSSAD GFSVFTADKT
     QLRMSMIDKD GNIIHTISKV KK
//
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