ID   NAGD_STAS1              Reviewed;         259 AA.
AC   Q49W68;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Acid sugar phosphatase {ECO:0000250|UniProtKB:Q99VE8};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:Q99VE8};
GN   Name=nagD; OrderedLocusNames=SSP1846;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of 2-6 carbon acid sugars in
CC       vitro. {ECO:0000250|UniProtKB:Q99VE8}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q99VE8};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NagD family.
CC       {ECO:0000305}.
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DR   EMBL; AP008934; BAE18991.1; -; Genomic_DNA.
DR   RefSeq; WP_002483823.1; NZ_MTGA01000039.1.
DR   AlphaFoldDB; Q49W68; -.
DR   SMR; Q49W68; -.
DR   STRING; 342451.SSP1846; -.
DR   EnsemblBacteria; BAE18991; BAE18991; SSP1846.
DR   KEGG; ssp:SSP1846; -.
DR   PATRIC; fig|342451.11.peg.1842; -.
DR   eggNOG; COG0647; Bacteria.
DR   HOGENOM; CLU_043473_1_1_9; -.
DR   OMA; PPMHRET; -.
DR   OrthoDB; 1308416at2; -.
DR   Proteomes; UP000006371; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 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   Pfam; PF13344; Hydrolase_6; 1.
DR   PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR   TIGRFAMs; TIGR01457; HAD-SF-IIA-hyp2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..259
FT                   /note="Acid sugar phosphatase"
FT                   /id="PRO_0000271492"
SQ   SEQUENCE   259 AA;  28052 MW;  1A2BB7D52CD69B96 CRC64;
     MKNYKAYLID LDGTMYKGNE EIDGAAQFIS YLNNQNIPHL YVTNNSTKEP EEVASKLNTM
     GIVAQADEVV TSALATAEFI AEESPGATVY MLGGSGLSNA LTAQGLVLKD DEFVDYVVVG
     LDEQVTYEKL STATLGVRNG AKFISTNQDV SIPKERGFLP GNGAITSVVS VSTGVQPVFI
     GKPEPIIMNK ALEILDLDRS DVAMVGDLYD TDIMSGINVD IDTIHVQTGV TTKEEIEKKS
     VPPTYTFKDL NEVIKELEK