ID   ACPH_ECO45              Reviewed;         193 AA.
AC   B7MD62;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=ECS88_0399;
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC;
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; CU928161; CAR01747.1; -; Genomic_DNA.
DR   RefSeq; WP_001009870.1; NC_011742.1.
DR   AlphaFoldDB; B7MD62; -.
DR   SMR; B7MD62; -.
DR   KEGG; ecz:ECS88_0399; -.
DR   HOGENOM; CLU_099370_1_0_6; -.
DR   Proteomes; UP000000747; 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; Reference proteome.
FT   CHAIN           1..193
FT                   /note="Acyl carrier protein phosphodiesterase"
FT                   /id="PRO_1000188798"
SQ   SEQUENCE   193 AA;  23021 MW;  AB5716174B14E9F7 CRC64;
     MNFLAHLHLA HLAESSLSGN LLADFVRGNP EESFPPDVVA GIHMHRRIDV LTDNLPEVRE
     AREWFRNETR RVAPITLDVM WDHFLSRHWS QLSPDFPLQE FTCYAREQVM TILPDSPPRF
     INLNNYLWSE QWLVRYRDMD FIQSVLNGMA SRRPRLDALR DSWYDLDAHY DALETRFWQF
     YPRMMEQASR KAL
//