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Database: UniProt
Entry: Q1G964_LACDA
LinkDB: Q1G964_LACDA
Original site: Q1G964_LACDA 
ID   Q1G964_LACDA            Unreviewed;       256 AA.
AC   Q1G964;
DT   27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   27-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Acid sugar phosphatase {ECO:0000256|PIRNR:PIRNR000915};
DE            EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR000915};
GN   OrderedLocusNames=Ldb1589 {ECO:0000313|EMBL:CAI98378.1};
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS   / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS   00102 / Lb 14).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=390333 {ECO:0000313|EMBL:CAI98378.1, ECO:0000313|Proteomes:UP000001259};
RN   [1] {ECO:0000313|EMBL:CAI98378.1, ECO:0000313|Proteomes:UP000001259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 /
RC   NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14
RC   {ECO:0000313|Proteomes:UP000001259};
RX   PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA   van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA   Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA   Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA   Weissenbach J., Ehrlich S.D., Maguin E.;
RT   "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT   and ongoing reductive evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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; CR954253; CAI98378.1; -; Genomic_DNA.
DR   RefSeq; WP_003623771.1; NZ_JQAV01000002.1.
DR   AlphaFoldDB; Q1G964; -.
DR   STRING; 390333.Ldb1589; -.
DR   KEGG; ldb:Ldb1589; -.
DR   PATRIC; fig|390333.13.peg.1036; -.
DR   eggNOG; COG0647; Bacteria.
DR   HOGENOM; CLU_043473_1_1_9; -.
DR   BioCyc; LDEL390333:LDB_RS06850-MONOMER; -.
DR   Proteomes; UP000001259; 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   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:UP000001259}.
FT   ACT_SITE        10
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   ACT_SITE        12
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         209
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   256 AA;  28094 MW;  36FB5046948214C3 CRC64;
     MKDYRLFLID LDGTIYRGKD TIESGVRFVK RLDEAGLDYL FLTNNTTRTP QMVADKLAGH
     GVKTDVSKIY TPSMATASYI LEKEAKRPIG VYIIGQIGLW KEILDRPEFY YDEENPDYVI
     VGMDTDLTYH KLMVATRCIH RGAVFIGTNS DQNLPVGKEL RPGNGSICAA LEVASGQKPL
     FIGKPEAIIV NRALDLAGVK AEEALIVGDN YPTDIMAGIN SGVDTLLTLT GVTQKADLAG
     LTPPTYLVND LDEFSL
//
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