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NAGD_STAAB
ID   NAGD_STAAB              Reviewed;         259 AA.
AC   Q2YWR1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-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=SAB0795;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI80483.1; -; Genomic_DNA.
DR   RefSeq; WP_000816179.1; NC_007622.1.
DR   AlphaFoldDB; Q2YWR1; -.
DR   SMR; Q2YWR1; -.
DR   KEGG; sab:SAB0795; -.
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_0000271481"
SQ   SEQUENCE   259 AA;  27980 MW;  B881119E1208C3BC CRC64;
     MKQYKAYLID LDGTMYMGTD EIDGAKQFID YLNVKGIPHL YVTNNSTKTP EQVTEKLREM
     HIDAKPEEVV TSALATADYI SEQSPGASVY MLGGSGLNTA LTEAGLVIKN DEHVDYVVIG
     LDEQVTYEKI AIATLGVRNG ATFISTNPDV SIPKERGFLP GNGAITSVVS VSTGVSPQFI
     GKPEPIIMVK ALEILGLDKS EVAMVGDLYD TDIMSGINVG MDTIHVQTGV STLEDVQNKN
     VPPTYSFKDL NEAIAELEK
 
 
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