ID   NAGD_STAAS              Reviewed;         259 AA.
AC   Q6GAZ7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Acid sugar phosphatase {ECO:0000250|UniProtKB:Q99VE8};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:Q99VE8};
GN   Name=nagD; OrderedLocusNames=SAS0799;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX571857; CAG42574.1; -; Genomic_DNA.
DR   RefSeq; WP_000816184.1; NC_002953.3.
DR   AlphaFoldDB; Q6GAZ7; -.
DR   SMR; Q6GAZ7; -.
DR   KEGG; sas:SAS0799; -.
DR   HOGENOM; CLU_043473_1_1_9; -.
DR   OMA; PPMHRET; -.
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.
FT   CHAIN           1..259
FT                   /note="Acid sugar phosphatase"
FT                   /id="PRO_0000271484"
SQ   SEQUENCE   259 AA;  27946 MW;  F120BAB9E006C355 CRC64;
     MKQYKAYLID LDGTMYMGTD EIDGAKQFID YLNVKGIPHL YVTNNSTKTP EQVTEKLREM
     HIDAKPEEVV TSALATADYI SEQSPGASVY MLGGSGLNTA LTEAGLVIKN DEHVDYVVIG
     LDEQVTYEKL AIATLGVRNG ATFISTNPDV SIPKERGLLP GNGAITSVVS VSTGVSPQFI
     GKPEPIIMVK ALEILGLDKS EVAMVGDLYD TDIMSGINVG MDTIHVQTGV STLEDVQNKN
     VPPTYSFKDL NEAIAELEK