ID   NAGD_STAAM              Reviewed;         259 AA.
AC   Q99VE8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Acid sugar phosphatase {ECO:0000303|PubMed:25848029};
DE            EC=3.1.3.- {ECO:0000305|PubMed:25848029};
GN   Name=nagD; OrderedLocusNames=SAV0929;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   FUNCTION, AND COFACTOR.
RX   PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA   Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA   Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA   Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA   Allen K.N., Farelli J.D.;
RT   "Panoramic view of a superfamily of phosphatases through substrate
RT   profiling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of 2-6 carbon acid sugars in
CC       vitro. {ECO:0000269|PubMed:25848029}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:25848029};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NagD family.
CC       {ECO:0000305}.
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DR   EMBL; BA000017; BAB57091.1; -; Genomic_DNA.
DR   RefSeq; WP_000816184.1; NC_002758.2.
DR   AlphaFoldDB; Q99VE8; -.
DR   SMR; Q99VE8; -.
DR   World-2DPAGE; 0002:Q99VE8; -.
DR   PaxDb; Q99VE8; -.
DR   DNASU; 1120904; -.
DR   EnsemblBacteria; BAB57091; BAB57091; SAV0929.
DR   KEGG; sav:SAV0929; -.
DR   HOGENOM; CLU_043473_1_1_9; -.
DR   OMA; PPMHRET; -.
DR   PhylomeDB; Q99VE8; -.
DR   BioCyc; SAUR158878:SAV_RS05055-MON; -.
DR   Proteomes; UP000002481; 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_0000271485"
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