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ACYP_SALTY
ID   ACYP_SALTY              Reviewed;          93 AA.
AC   Q7CQS9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Acylphosphatase {ECO:0000255|HAMAP-Rule:MF_01450};
DE            EC=3.6.1.7 {ECO:0000255|HAMAP-Rule:MF_01450};
DE   AltName: Full=Acylphosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01450};
GN   Name=yccX {ECO:0000255|HAMAP-Rule:MF_01450}; OrderedLocusNames=STM1083;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01450};
CC   -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01450}.
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DR   EMBL; AE006468; AAL20016.1; -; Genomic_DNA.
DR   RefSeq; NP_460057.1; NC_003197.2.
DR   RefSeq; WP_000072884.1; NC_003197.2.
DR   AlphaFoldDB; Q7CQS9; -.
DR   SMR; Q7CQS9; -.
DR   STRING; 99287.STM1083; -.
DR   PaxDb; Q7CQS9; -.
DR   EnsemblBacteria; AAL20016; AAL20016; STM1083.
DR   GeneID; 1252601; -.
DR   KEGG; stm:STM1083; -.
DR   PATRIC; fig|99287.12.peg.1148; -.
DR   HOGENOM; CLU_141932_1_2_6; -.
DR   OMA; VGFRWSM; -.
DR   PhylomeDB; Q7CQS9; -.
DR   BioCyc; SENT99287:STM1083-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0003998; F:acylphosphatase activity; IBA:GO_Central.
DR   HAMAP; MF_01450; Acylphosphatase_entero; 1.
DR   InterPro; IPR020456; Acylphosphatase.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR028627; Acylphosphatase_bac.
DR   InterPro; IPR017968; Acylphosphatase_CS.
DR   PANTHER; PTHR47268; PTHR47268; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   PRINTS; PR00112; ACYLPHPHTASE.
DR   SUPFAM; SSF54975; SSF54975; 1.
DR   PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR   PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Reference proteome.
FT   CHAIN           1..93
FT                   /note="Acylphosphatase"
FT                   /id="PRO_0000285206"
FT   DOMAIN          5..93
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT   ACT_SITE        20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT   DISULFID        5..49
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
SQ   SEQUENCE   93 AA;  10329 MW;  1FB3C26E4E065D77 CRC64;
     MSNVCIIAWV YGRVQGVGFR YTTQHEAQRL GLTGYAKNMD DGSVEVVACG DAAQVEKLIK
     WLKEGGPRSA RVDKILTEPH SPRETLTGFS IRY
 
 
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