ID   PHAG_PSEAE              Reviewed;         300 AA.
AC   Q51553; Q9L8E1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=(R)-3-hydroxydecanoyl-ACP:CoA transacylase;
DE            EC=2.4.1.-;
DE   AltName: Full=3-hydroxyacyl-CoA-acyl carrier protein transferase;
DE   AltName: Full=Quinolone sensitivity protein;
GN   Name=phaG; Synonyms=qin; OrderedLocusNames=PA0730;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10713430; DOI=10.1111/j.1574-6968.2000.tb09023.x;
RA   Hoffmann N., Steinbuchel A., Rehm B.H.A.;
RT   "The Pseudomonas aeruginosa phaG gene product is involved in the synthesis
RT   of polyhydroxyalkanoic acid consisting of medium-chain-length constituents
RT   from non-related carbon sources.";
RL   FEMS Microbiol. Lett. 184:253-259(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-300.
RA   Tonetti D.A., Miller R.V.;
RL   Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of the acyl moiety from in vitro
CC       synthesized 3-hydroxydecanoyl-CoA to acyl carrier protein.
CC   -!- PATHWAY: Polyester biosynthesis; polyhydroxyalkanoate biosynthesis.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA25978.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF209711; AAF61903.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG04119.1; -; Genomic_DNA.
DR   EMBL; L02105; AAA25978.1; ALT_FRAME; Genomic_DNA.
DR   PIR; B83554; B83554.
DR   RefSeq; NP_249421.1; NC_002516.2.
DR   RefSeq; WP_003114157.1; NZ_QZGE01000007.1.
DR   AlphaFoldDB; Q51553; -.
DR   SMR; Q51553; -.
DR   STRING; 287.DR97_1256; -.
DR   ESTHER; pseae-phag; 6_AlphaBeta_hydrolase.
DR   PaxDb; Q51553; -.
DR   DNASU; 877678; -.
DR   EnsemblBacteria; AAG04119; AAG04119; PA0730.
DR   GeneID; 877678; -.
DR   KEGG; pae:PA0730; -.
DR   PATRIC; fig|208964.12.peg.757; -.
DR   PseudoCAP; PA0730; -.
DR   HOGENOM; CLU_062012_0_0_6; -.
DR   InParanoid; Q51553; -.
DR   OMA; FLDMEHK; -.
DR   PhylomeDB; Q51553; -.
DR   BioCyc; PAER208964:G1FZ6-742-MON; -.
DR   UniPathway; UPA00212; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   4: Predicted;
KW   Reference proteome; Transferase.
FT   CHAIN           1..300
FT                   /note="(R)-3-hydroxydecanoyl-ACP:CoA transacylase"
FT                   /id="PRO_0000058370"
FT   DOMAIN          29..253
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        63..64
FT                   /note="YA -> MP (in Ref. 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        83
FT                   /note="A -> V (in Ref. 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        99
FT                   /note="M -> L (in Ref. 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="Y -> D (in Ref. 3; AAA25978)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277
FT                   /note="T -> Q (in Ref. 3; AAA25978)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        292
FT                   /note="S -> T (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   300 AA;  34247 MW;  6D2B3037162BCECB CRC64;
     MRPETAIIEI HGQYRIHTEF YGNPAAQQTI ILVNGSLSTT ASFAQTVKYL QPHYNVVLYD
     QPYAGQSKPH NENHTPISKE CEARILLELI ERFRAEVVMS FSWGGVATLL ALAQRPGRIR
     RAVVNSFSPQ LNPAMLDYLH RGLDYLAACD RTQIGNLVNE TIGRYLPQLF KRYNFRHVSS
     LDEHEYHQMH FHIREVLRLN ADSYTESFAG IEIPMLFMNG ELDIYTTPHE ARQFGQLIRG
     AEFHTIRNAG HFIDVEHKAA WQQTQDALLA FLRPQRTQPL NPIYRPQPNG ASVPLAALAS