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Database: UniProt
Entry: R5CJ75_9FIRM
LinkDB: R5CJ75_9FIRM
Original site: R5CJ75_9FIRM 
ID   R5CJ75_9FIRM            Unreviewed;       287 AA.
AC   R5CJ75;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Acid sugar phosphatase {ECO:0000256|PIRNR:PIRNR000915};
DE            EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR000915};
GN   ORFNames=BN785_00413 {ECO:0000313|EMBL:CCX66514.1};
OS   Firmicutes bacterium CAG:791.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262993 {ECO:0000313|EMBL:CCX66514.1, ECO:0000313|Proteomes:UP000018038};
RN   [1] {ECO:0000313|EMBL:CCX66514.1, ECO:0000313|Proteomes:UP000018038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:791 {ECO:0000313|Proteomes:UP000018038};
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   -!- FUNCTION: Catalyzes the dephosphorylation of 2-6 carbon acid sugars in
CC       vitro. {ECO:0000256|PIRNR:PIRNR000915}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000915-3};
CC       Note=Divalent metal ions. Mg(2+) is the most effective.
CC       {ECO:0000256|PIRSR:PIRSR000915-3};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NagD family.
CC       {ECO:0000256|PIRNR:PIRNR000915}.
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:CCX66514.1}.
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DR   EMBL; CAWT010000211; CCX66514.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5CJ75; -.
DR   STRING; 1262993.BN785_00413; -.
DR   Proteomes; UP000018038; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR   PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR19288:SF46; HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   Pfam; PF13242; Hydrolase_like; 1.
DR   PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|PIRNR:PIRNR000915, ECO:0000256|PIRSR:PIRSR000915-3};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000915,
KW   ECO:0000256|PIRSR:PIRSR000915-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018038};
KW   Transferase {ECO:0000313|EMBL:CCX66514.1}.
FT   ACT_SITE        27
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   ACT_SITE        29
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         27
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         29
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   287 AA;  32065 MW;  30582074EAB3BB99 CRC64;
     MKNTTNSTDY FGKDADSLKS KRLFLLDMDG TIYQENTVFD GTRQMLDYIR DSGGRYVFIT
     NNSSKSVKDY MDKVHQMGLP AEAENFFTST QATILYLKEH FPDALVYCQG TKSMISELLH
     AGIRVTEEVR DGIDVVLVGF DMELTMQKLR NTCEILTCQS PAYIATNPDE CCPVSFGETA
     GFVPDCGSMC YGIEKATGKW PVFIGKPEPT MIDIVRNKFG YTREETLVIG DRLYTDIASG
     NNAGVDTVCV LSGEASEGDI RNSEEKPAYT FRDIKALWRY CDAAQGR
//
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