ID ACPH_ECO57 Reviewed; 193 AA.
AC Q8XE96; Q7AH16;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-NOV-2024, entry version 110.
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=Z0503, ECs0455;
OS Escherichia coli O157:H7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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=holo-[ACP] + H2O = apo-[ACP] + (R)-4'-phosphopantetheine +
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; AE005174; AAG54751.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33878.1; -; Genomic_DNA.
DR PIR; C85536; C85536.
DR PIR; G90685; G90685.
DR RefSeq; NP_308482.1; NC_002695.1.
DR RefSeq; WP_001009882.1; NZ_VOAI01000005.1.
DR AlphaFoldDB; Q8XE96; -.
DR SMR; Q8XE96; -.
DR STRING; 155864.Z0503; -.
DR GeneID; 75170421; -.
DR GeneID; 914557; -.
DR KEGG; ece:Z0503; -.
DR KEGG; ecs:ECs_0455; -.
DR PATRIC; fig|386585.9.peg.555; -.
DR eggNOG; COG3124; Bacteria.
DR HOGENOM; CLU_099370_1_0_6; -.
DR OMA; MNFLAHI; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_0000226266"
SQ SEQUENCE 193 AA; 22917 MW; F8E6F0CE01D6C395 CRC64;
MNFLAHLHLA HLAESSLSGN LLADFVRGNP EESFPPDVVA GIHMHRRIDV LTDNLPEVRE
AREWFRSETR RVAPITLDVM WDHFLSRHWS QLSPDFPLQE FVCYAREQVM TILPDSPPRF
INLNNYLWSE QWLVRYRDMD FIQNVLNGMA SRRPRLDALR DSWYDLDAHY AALETRFWQF
YPRMMAQASR KAL
//