ID   ACPH_SALG2              Reviewed;         193 AA.
AC   B5R6Q5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
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}; OrderedLocusNames=SG0415;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR36314.1; -; Genomic_DNA.
DR   RefSeq; WP_001009858.1; NC_011274.1.
DR   AlphaFoldDB; B5R6Q5; -.
DR   SMR; B5R6Q5; -.
DR   KEGG; seg:SG0415; -.
DR   HOGENOM; CLU_099370_1_0_6; -.
DR   Proteomes; UP000008321; 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_1000188813"
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
//