PHAG_PSEPK
ID PHAG_PSEPK Reviewed; 295 AA.
AC O85207;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=(R)-3-hydroxydecanoyl-ACP:CoA transacylase;
DE EC=2.4.1.-;
DE AltName: Full=3-hydroxyacyl-CoA-acyl carrier protein transferase;
GN Name=phaG; OrderedLocusNames=PP_1408;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9727022; DOI=10.1074/jbc.273.37.24044;
RA Rehm B.H.A., Kruger N., Steinbuchel A.;
RT "A new metabolic link between fatty acid de novo synthesis and
RT polyhydroxyalkanoic acid synthesis. The phaG gene from Pseudomonas putida
RT KT2440 encodes a 3-hydroxyacyl-acyl carrier protein-coenzyme A
RT transferase.";
RL J. Biol. Chem. 273:24044-24051(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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 ---------------------------------------------------------------------------
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; AF052507; AAC34749.1; -; Genomic_DNA.
DR EMBL; AE015451; AAN67031.1; -; Genomic_DNA.
DR RefSeq; NP_743567.1; NC_002947.4.
DR RefSeq; WP_010952516.1; NC_002947.4.
DR AlphaFoldDB; O85207; -.
DR STRING; 160488.PP_1408; -.
DR ESTHER; psepu-PHAG; 6_AlphaBeta_hydrolase.
DR EnsemblBacteria; AAN67031; AAN67031; PP_1408.
DR KEGG; ppu:PP_1408; -.
DR PATRIC; fig|160488.4.peg.1493; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_062012_0_0_6; -.
DR OMA; FLDMEHK; -.
DR PhylomeDB; O85207; -.
DR BioCyc; MetaCyc:G1G01-1499-MON; -.
DR BioCyc; PPUT160488:G1G01-1499-MON; -.
DR UniPathway; UPA00212; -.
DR Proteomes; UP000000556; 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..295
FT /note="(R)-3-hydroxydecanoyl-ACP:CoA transacylase"
FT /id="PRO_0000058372"
FT DOMAIN 28..254
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
SQ SEQUENCE 295 AA; 33914 MW; 1B4DBEFA25C9675C CRC64;
MRPEIAVLDI QGQYRVYTEF YRADAAENTI ILINGSLATT ASFAQTVRNL HPQFNVVLFD
QPYSGKSKPH NRQERLISKE TEAHILLELI EHFQADHVMS FSWGGASTLL ALAHQPRYVK
KAVVSSFSPV INEPMRDYLD RGCQYLAACD RYQVGNLVND TIGKHLPSLF KRFNYRHVSS
LDSHEYAQMH FHINQVLEHD LERALQGARN INIPVLFING ERDEYTTVED ARQFSKHVGR
SQFSVIRDAG HFLDMENKTA CENTRNVMLG FLKPTVREPR QRYQPVQQGQ HAFAI
