ID   ACPH_ESCF3              Reviewed;         193 AA.
AC   B7LMI3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=EFER_2621;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ90116.1; -; Genomic_DNA.
DR   RefSeq; WP_001009863.1; NC_011740.1.
DR   AlphaFoldDB; B7LMI3; -.
DR   SMR; B7LMI3; -.
DR   EnsemblBacteria; CAQ90116; CAQ90116; EFER_2621.
DR   KEGG; efe:EFER_2621; -.
DR   HOGENOM; CLU_099370_1_0_6; -.
DR   OMA; MNFLAHI; -.
DR   OrthoDB; 1398998at2; -.
DR   BioCyc; EFER585054:EFER_RS13205-MON; -.
DR   Proteomes; UP000000745; 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_1000188808"
SQ   SEQUENCE   193 AA;  23059 MW;  0CDEA66B2C94F55F CRC64;
     MNFLAHLHLA HLAESSLSGN LLADFVRGNP EENFPPDVVA GIHMHRRIDV LTDNLPEVRE
     AREWFRRETR RVAPITLDVM WDHFLSRHWS QLSPDFPLQE FTCYAREQVM TILPDSPPRF
     INLNNYLWSE QWLVRYRDMD FIQNVLNGMA SRRPRLDALR DSWYDLDAHY DALETRFWQF
     YPRMMAQASR KAL