(data stored in ACNUC10821 zone)

SWISSPROT: C8U288_ECO10

ID   C8U288_ECO10            Unreviewed;       193 AA.
AC   C8U288;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 48.
DE   RecName: Full=Acyl carrier protein phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_01950};
DE            Short=ACP phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_01950};
DE            EC=3.1.4.14 {ECO:0000256|HAMAP-Rule:MF_01950};
GN   Name=yajB {ECO:0000313|EMBL:BAI29246.1};
GN   Synonyms=acpH {ECO:0000256|HAMAP-Rule:MF_01950};
GN   OrderedLocusNames=ECO103_0378 {ECO:0000313|EMBL:BAI29246.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29246.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29246.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Converts holo-ACP to apo-ACP by hydrolytic cleavage of
CC       the phosphopantetheine prosthetic group from ACP.
CC       {ECO:0000256|HAMAP-Rule:MF_01950}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + holo-[ACP] = apo-[ACP] + D-pantetheine 4'-phosphate
CC         + H(+); Xref=Rhea:RHEA:20537, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:9690, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:61723, ChEBI:CHEBI:64479;
CC         EC=3.1.4.14; Evidence={ECO:0000256|HAMAP-Rule:MF_01950};
CC   -!- SIMILARITY: Belongs to the AcpH family. {ECO:0000256|HAMAP-
CC       Rule:MF_01950}.
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DR   EMBL; AP010958; BAI29246.1; -; Genomic_DNA.
DR   RefSeq; WP_001009884.1; NC_013353.1.
DR   EnsemblBacteria; BAI29246; BAI29246; ECO103_0378.
DR   KEGG; eoh:ECO103_0378; -.
DR   HOGENOM; HOG000275880; -.
DR   KO; K08682; -.
DR   OMA; MNFLAHI; -.
DR   BioCyc; ECOL585395:ECO103_RS01980-MONOMER; -.
DR   Proteomes; UP000000959; 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;
DR   PRODOM; C8U288.
DR   SWISS-2DPAGE; C8U288.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01950};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01950};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01950};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01950};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01950}.
SQ   SEQUENCE   193 AA;  22942 MW;  0DE6F0DBE1D6C523 CRC64;
     MNFLAHLHLA HLAESSLSGN LLADFVRGNP EESFPPDVVA GIHMHRRIDV LTDNLPEVRE
     AREWFRSETR RVAPITLDVM WDHFLSRHWS QLSPDFPLQE FVCYAREQVM TILPDSPPRF
     INLNNYLWSE QWLVRYRDMD FIQNVLNGMA SRRPRLDALR DSWYDLDAHY DALETRFWQF
     YPRMMAQASH KAL
//

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