ACPH_SALTI
ID ACPH_SALTI Reviewed; 193 AA.
AC Q8XEZ8; Q7ANH4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Acyl carrier protein phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_01950};
DE Short=ACP phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_01950};
DE EC=3.1.4.14 {ECO:0000255|HAMAP-Rule:MF_01950};
GN Name=acpH {ECO:0000255|HAMAP-Rule:MF_01950};
GN OrderedLocusNames=STY0441, t2460;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Converts holo-ACP to apo-ACP by hydrolytic cleavage of the
CC phosphopantetheine prosthetic group from ACP. {ECO:0000255|HAMAP-
CC Rule:MF_01950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + holo-[ACP] = (R)-4'-phosphopantetheine + apo-[ACP] +
CC H(+); Xref=Rhea:RHEA:20537, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9690,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:61723, ChEBI:CHEBI:64479; EC=3.1.4.14;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01950};
CC -!- SIMILARITY: Belongs to the AcpH family. {ECO:0000255|HAMAP-
CC Rule:MF_01950}.
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DR EMBL; AL513382; CAD08859.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70050.1; -; Genomic_DNA.
DR RefSeq; NP_454998.1; NC_003198.1.
DR RefSeq; WP_001009858.1; NZ_WSUR01000026.1.
DR AlphaFoldDB; Q8XEZ8; -.
DR SMR; Q8XEZ8; -.
DR STRING; 220341.16501672; -.
DR EnsemblBacteria; AAO70050; AAO70050; t2460.
DR KEGG; stt:t2460; -.
DR KEGG; sty:STY0441; -.
DR PATRIC; fig|220341.7.peg.439; -.
DR eggNOG; COG3124; Bacteria.
DR HOGENOM; CLU_099370_1_0_6; -.
DR OMA; MNFLAHI; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0008770; F:[acyl-carrier-protein] phosphodiesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01950; AcpH; 1.
DR InterPro; IPR007431; ACP_PD.
DR InterPro; IPR023491; ACP_phosphodiesterase_gpbac.
DR PANTHER; PTHR38764; PTHR38764; 1.
DR Pfam; PF04336; ACP_PD; 1.
DR PIRSF; PIRSF011489; DUF479; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase;
KW Lipid biosynthesis; Lipid metabolism.
FT CHAIN 1..193
FT /note="Acyl carrier protein phosphodiesterase"
FT /id="PRO_0000226272"
SQ SEQUENCE 193 AA; 22917 MW; DAC36DC0FA32B84B CRC64;
MNFLAHLHLA HLADSSLSGN LLADFVRGNP ATHYPPDVVE GIYMHRRIDV MTDNLPEVRE
AREWFRHETR RVAPITLDVM WDHFLSRHWT QISPDFPLQA FVGYAHAQVA TILPDSPPRF
VNLNDYLWSE KWLERYRDMD FIQNVLNGMA NRRPRLDALR DSWYDLDAHY DALEERFWHF
YPRMMAQAAR KAL