ID   NAGD_STAAC              Reviewed;         259 AA.
AC   Q5HHF6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Acid sugar phosphatase {ECO:0000250|UniProtKB:Q99VE8};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:Q99VE8};
GN   Name=nagD; OrderedLocusNames=SACOL0931;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000046; AAW37900.1; -; Genomic_DNA.
DR   RefSeq; WP_000816184.1; NC_002951.2.
DR   AlphaFoldDB; Q5HHF6; -.
DR   SMR; Q5HHF6; -.
DR   EnsemblBacteria; AAW37900; AAW37900; SACOL0931.
DR   KEGG; sac:SACOL0931; -.
DR   HOGENOM; CLU_043473_1_1_9; -.
DR   OMA; PPMHRET; -.
DR   Proteomes; UP000000530; 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.
FT   CHAIN           1..259
FT                   /note="Acid sugar phosphatase"
FT                   /id="PRO_0000271482"
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