ID Q74KS9_LACJO Unreviewed; 260 AA.
AC Q74KS9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Acid sugar phosphatase {ECO:0000256|PIRNR:PIRNR000915};
DE EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR000915};
GN OrderedLocusNames=LJ_0498 {ECO:0000313|EMBL:AAS08490.1};
OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=257314 {ECO:0000313|EMBL:AAS08490.1, ECO:0000313|Proteomes:UP000000581};
RN [1] {ECO:0000313|EMBL:AAS08490.1, ECO:0000313|Proteomes:UP000000581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533
RC {ECO:0000313|Proteomes:UP000000581};
RX PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT johnsonii NCC 533.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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|ARBA:ARBA00006696, ECO:0000256|PIRNR:PIRNR000915}.
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DR EMBL; AE017198; AAS08490.1; -; Genomic_DNA.
DR RefSeq; WP_004896827.1; NC_005362.1.
DR AlphaFoldDB; Q74KS9; -.
DR GeneID; 83569925; -.
DR KEGG; ljo:LJ_0498; -.
DR eggNOG; COG0647; Bacteria.
DR HOGENOM; CLU_043473_1_1_9; -.
DR Proteomes; UP000000581; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07530; HAD_Pase_UmpH-like; 1.
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; IPR006354; HAD-SF_hydro_IIA_hyp1.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR NCBIfam; TIGR01457; HAD-SF-IIA-hyp2; 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; 2.
DR SFLD; SFLDG01139; C2.A:_Pyridoxal_Phosphate_Phos; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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}.
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 14
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 260 AA; 29021 MW; 782CE0A167ECE391 CRC64;
MEHKDYKCYL IDLDGTIYRG SDTIESGVRF IHRLQEKNIP HLFLTNNSTR TPQMVVDKLR
GHGVNTDIYH VYTPVLATES YLLSQNPDAT KIPIYIIGQI GLVQGLLKNE RFYYDDRNPK
YVVVGMDTDL TYHKIRVATR AIRNGATFIG TNADKNLPSG DELLPGNGAL CTMIEVATGV
KPTYIGKPSP IIVASALKML NAQGQDAILV GDNYDTDIMA GINCNIDSLL TLTGVTNKEQ
LKEKDKKPTY IVENLDEWKL
//
