ID   ACPH_SALPA              Reviewed;         193 AA.
AC   Q5PFT4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=SPA2320;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV78205.1; -; Genomic_DNA.
DR   RefSeq; WP_001009851.1; NC_006511.1.
DR   AlphaFoldDB; Q5PFT4; -.
DR   KEGG; spt:SPA2320; -.
DR   HOGENOM; CLU_099370_1_0_6; -.
DR   Proteomes; UP000008185; 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; ACYL CARRIER PROTEIN PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR38764:SF1; ACYL CARRIER PROTEIN PHOSPHODIESTERASE; 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_0000226271"
SQ   SEQUENCE   193 AA;  22976 MW;  3D865EF628D2D43E CRC64;
     MNFLAHLHLA HLADNSLSGN LLADFVRGNP ATHYPPDVVE GIYMHRRIDV MTDNLPEARE
     AREWFRHETR RVAPITLDVM WDHFLSRHWT QISPDFPLQA FVGYAHAQVA TILPDFPPRF
     VNLNDYLWSE KWLERYRDMD FIQNVLNGMA NRRPRLDALR DSWYDLDAHY DALEERFWHF
     YPRMMAQAAR KAL
//