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ACPH_SHIFL
ID   ACPH_SHIFL              Reviewed;         143 AA.
AC   Q83SG7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Putative acyl carrier protein phosphodiesterase;
DE            Short=ACP phosphodiesterase;
DE            EC=3.1.4.14;
GN   Name=acpH; OrderedLocusNames=SF0341, S0349;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Converts holo-ACP to apo-ACP by hydrolytic cleavage of the
CC       phosphopantetheine prosthetic group from ACP. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the AcpH family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. The N-terminus is
CC       shorter than in related proteins. {ECO:0000305}.
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DR   EMBL; AE005674; AAN41999.1; -; Genomic_DNA.
DR   EMBL; AE014073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q83SG7; -.
DR   SMR; Q83SG7; -.
DR   STRING; 198214.SF0341; -.
DR   EnsemblBacteria; AAN41999; AAN41999; SF0341.
DR   PATRIC; fig|623.156.peg.3490; -.
DR   HOGENOM; CLU_099370_1_0_6; -.
DR   OMA; MNFLAHI; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0008770; F:[acyl-carrier-protein] phosphodiesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR007431; ACP_PD.
DR   PANTHER; PTHR38764; PTHR38764; 1.
DR   Pfam; PF04336; ACP_PD; 1.
PE   5: Uncertain;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase;
KW   Lipid biosynthesis; Lipid metabolism; Reference proteome.
FT   CHAIN           1..143
FT                   /note="Putative acyl carrier protein phosphodiesterase"
FT                   /id="PRO_0000226276"
SQ   SEQUENCE   143 AA;  17418 MW;  A0731A290EB3F83D CRC64;
     MTDNLPEVRE AQEWFRSETR RVAPITLDVM WDHFLSRHWS QLSPDFPLQE FVCYAREQVM
     TILPDSPPRF INLNNYLWSE QWLVRYRDMD FIQNVLNGMA SRRPRLDALR DSWYDLDAHY
     DALETRFWQF YPRMMAQASH KAL
 
 
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