GenomeNet

Database: UniProt
Entry: ACPH_ECOL6
LinkDB: ACPH_ECOL6
Original site: ACPH_ECOL6 
ID   ACPH_ECOL6              Reviewed;         193 AA.
AC   Q8FKC6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   27-NOV-2024, entry version 91.
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=c0514;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN78992.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AE014075; AAN78992.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001009873.1; NZ_CP051263.1.
DR   AlphaFoldDB; Q8FKC6; -.
DR   SMR; Q8FKC6; -.
DR   STRING; 199310.c0514; -.
DR   KEGG; ecc:c0514; -.
DR   eggNOG; COG3124; Bacteria.
DR   HOGENOM; CLU_099370_1_0_6; -.
DR   Proteomes; UP000001410; 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_0000226267"
SQ   SEQUENCE   193 AA;  23052 MW;  C02716160F51E8B3 CRC64;
     MNFLAHLHLA HLAESSLSGN LLADFVRGNP EESFPPDVVA GIHMHRRIDV LTDNLPEVRE
     AREWFRNETR RVAPITLDVM WDHFLSRHWS QLSPDFPLQE FTCYAREQVM TILPDSPQRF
     INLNNYLWSE QWLVRYRDMD FIQSVLNGMA SRRPRLDALR DSWYDLDAHY DALETRFWQF
     YPRMMEQASR KAL
//
DBGET integrated database retrieval system