NAGD_STAHJ
ID NAGD_STAHJ Reviewed; 263 AA.
AC Q4L4U2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Acid sugar phosphatase {ECO:0000250|UniProtKB:Q99VE8};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q99VE8};
GN Name=nagD; OrderedLocusNames=SH2024;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(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; AP006716; BAE05333.1; -; Genomic_DNA.
DR RefSeq; WP_011276290.1; NC_007168.1.
DR AlphaFoldDB; Q4L4U2; -.
DR SMR; Q4L4U2; -.
DR STRING; 279808.SH2024; -.
DR EnsemblBacteria; BAE05333; BAE05333; SH2024.
DR KEGG; sha:SH2024; -.
DR eggNOG; COG0647; Bacteria.
DR HOGENOM; CLU_043473_1_1_9; -.
DR OMA; PPMHRET; -.
DR OrthoDB; 1308416at2; -.
DR Proteomes; UP000000543; 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..263
FT /note="Acid sugar phosphatase"
FT /id="PRO_0000271491"
SQ SEQUENCE 263 AA; 28678 MW; BA23DA2B4209CFED CRC64;
MKNYKGYLID LDGTMYLGTD EIDGAAQFID YLNNHQIPHL YVTNNSTKTP EEVTQKLKEM
NIDAKPEEVV TSALATANYI SDEKSDATVY MLGGNGLRTA LTEAGLTVKD DENVDYVAIG
LDENVTYEKL AVATLAVRKG ARFISTNPDV SIPKERGFLP GNGAITSVVS VSTGQAPQFI
GKPEPVIMDI ALDILKLDKS DVAMVGDLYD TDIMSGINVG VDTIHVQTGV TTYEELKEKD
QQPTYSFKDL NVAISELEKN AQK