ID ACPH_ECO7I Reviewed; 193 AA. AC B7NJ98; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, 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}; GN OrderedLocusNames=ECIAI39_0277; OS Escherichia coli O7:K1 (strain IAI39 / ExPEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IAI39 / 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU928164; CAR16417.1; -; Genomic_DNA. DR RefSeq; WP_001009885.1; NC_011750.1. DR RefSeq; YP_002406320.1; NC_011750.1. DR AlphaFoldDB; B7NJ98; -. DR SMR; B7NJ98; -. DR STRING; 585057.ECIAI39_0277; -. DR KEGG; ect:ECIAI39_0277; -. DR PATRIC; fig|585057.6.peg.299; -. DR HOGENOM; CLU_099370_1_0_6; -. DR Proteomes; UP000000749; 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_1000188801" SQ SEQUENCE 193 AA; 22961 MW; 0DE6F0CE01D6C523 CRC64; MNFLAHLHLA HLAESSLSGN LLADFVRGNP EESFPPDVVA GIHMHRRIDV LTDNLPEVRE AREWFRSETR RVAPITLDVM WDHFLSRHWS QLSPDFPLQE FVCYAREQVM TILPDSPPRF INLNNYLWSE QWLVRYRDMD FIQNVLNGMA SRRPRLDALR DSWYDLDAHY DALETRFWQF YPRMMAQASR KAL //