ID   NAGD_STAEQ              Reviewed;         259 AA.
AC   Q5HQN3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Acid sugar phosphatase {ECO:0000250|UniProtKB:Q99VE8};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:Q99VE8};
GN   Name=nagD; OrderedLocusNames=SERP0515;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
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; CP000029; AAW53898.1; -; Genomic_DNA.
DR   RefSeq; WP_002475052.1; NC_002976.3.
DR   AlphaFoldDB; Q5HQN3; -.
DR   SMR; Q5HQN3; -.
DR   STRING; 176279.SERP0515; -.
DR   EnsemblBacteria; AAW53898; AAW53898; SERP0515.
DR   KEGG; ser:SERP0515; -.
DR   eggNOG; COG0647; Bacteria.
DR   HOGENOM; CLU_043473_1_1_9; -.
DR   OMA; PPMHRET; -.
DR   OrthoDB; 1308416at2; -.
DR   Proteomes; UP000000531; 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_0000271490"
SQ   SEQUENCE   259 AA;  28297 MW;  3E49BE26772B88B7 CRC64;
     MKHYQAYLID LDGTMYKGTE EIDGAAQFID YLNNNRIPHL YVTNNSTKTP VQVTEKLREM
     HIDAKPDEVV TSALATADYI SEQHPNATVY MIGGHGLKTA LTDAGLSIKN DEHVDYVVIG
     LDEKVTYEKL SIATLAVRNG AKFISTNPDV SIPKERGFLP GNGAITSVVS VSTGIQPEFI
     GKPETIIMSK SLDILGLEKS EVAMVGDLYD TDIMSGINVG IDTIHVQTGV STYEDIQSKE
     IPPTYSFKDL NVAIAELEK