ID C0Q8C2_SALPC Unreviewed; 93 AA.
AC C0Q8C2;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Acylphosphatase {ECO:0000256|ARBA:ARBA00015991, ECO:0000256|HAMAP-Rule:MF_01450};
DE EC=3.6.1.7 {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|HAMAP-Rule:MF_01450};
DE AltName: Full=Acylphosphate phosphohydrolase {ECO:0000256|HAMAP-Rule:MF_01450};
GN Name=yccX {ECO:0000256|HAMAP-Rule:MF_01450,
GN ECO:0000313|EMBL:ACN46767.1};
GN OrderedLocusNames=SPC_2666 {ECO:0000313|EMBL:ACN46767.1};
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213 {ECO:0000313|EMBL:ACN46767.1, ECO:0000313|Proteomes:UP000001599};
RN [1] {ECO:0000313|EMBL:ACN46767.1, ECO:0000313|Proteomes:UP000001599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594 {ECO:0000313|EMBL:ACN46767.1,
RC ECO:0000313|Proteomes:UP000001599};
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
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:0000256|ARBA:ARBA00000744, ECO:0000256|HAMAP-
CC Rule:MF_01450, ECO:0000256|PROSITE-ProRule:PRU00520,
CC ECO:0000256|RuleBase:RU000553};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|ARBA:ARBA00005614, ECO:0000256|HAMAP-Rule:MF_01450,
CC ECO:0000256|RuleBase:RU004168}.
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DR EMBL; CP000857; ACN46767.1; -; Genomic_DNA.
DR RefSeq; WP_000072884.1; NC_012125.1.
DR AlphaFoldDB; C0Q8C2; -.
DR SMR; C0Q8C2; -.
DR KEGG; sei:SPC_2666; -.
DR HOGENOM; CLU_141932_1_2_6; -.
DR Proteomes; UP000001599; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.100; -; 1.
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; ACYLPHOSPHATASE; 1.
DR PANTHER; PTHR47268:SF4; ACYLPHOSPHATASE; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR PRINTS; PR00112; ACYLPHPHTASE.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 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 {ECO:0000256|HAMAP-Rule:MF_01450};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01450, ECO:0000256|PROSITE-
KW ProRule:PRU00520}.
FT DOMAIN 5..93
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 20
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01450,
FT ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 38
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01450,
FT ECO:0000256|PROSITE-ProRule:PRU00520"
FT DISULFID 5..49
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01450"
SQ SEQUENCE 93 AA; 10329 MW; 1FB3C26E4E065D77 CRC64;
MSNVCIIAWV YGRVQGVGFR YTTQHEAQRL GLTGYAKNMD DGSVEVVACG DAAQVEKLIK
WLKEGGPRSA RVDKILTEPH SPRETLTGFS IRY
//
