ID   PHAC1_PSEOL             Reviewed;         559 AA.
AC   P26494;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Poly(3-hydroxyalkanoate) polymerase 1;
DE            Short=PHA polymerase 1 {ECO:0000303|PubMed:1989978};
DE            EC=2.3.1.-;
DE   AltName: Full=ORF1 {ECO:0000303|PubMed:1989978};
DE   AltName: Full=Polyhydroxyalkanoic acid synthase 1;
DE            Short=PHA synthase 1;
GN   Name=phaC1 {ECO:0000303|PubMed:1476773}; Synonyms=phaA;
OS   Pseudomonas oleovorans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas;
OC   Pseudomonas oleovorans/pseudoalcaligenes group.
OX   NCBI_TaxID=301;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=GPo1;
RX   PubMed=1989978; DOI=10.1016/s0021-9258(18)52227-4;
RA   Huisman G.W., Wonink E., Meima R., Kazemier B., Terpstra P., Witholt B.;
RT   "Metabolism of poly(3-hydroxyalkanoates) (PHAs) by Pseudomonas oleovorans.
RT   Identification and sequences of genes and function of the encoded proteins
RT   in the synthesis and degradation of PHA.";
RL   J. Biol. Chem. 266:2191-2198(1991).
RN   [2]
RP   GENE NAME.
RX   PubMed=1476773; DOI=10.1111/j.1574-6968.1992.tb05841.x;
RA   Steinbuechel A., Hustede E., Liebergesell M., Pieper U., Timm A.,
RA   Valentin H.;
RT   "Molecular basis for biosynthesis and accumulation of polyhydroxyalkanoic
RT   acids in bacteria.";
RL   FEMS Microbiol. Rev. 9:217-230(1992).
CC   -!- FUNCTION: Synthesizes poly(3-hydroxyalkanoates) (PHA), complements a
CC       mutant of P.putida that does not make PHA.
CC       {ECO:0000269|PubMed:1989978}.
CC   -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC       biosynthesis.
CC   -!- MISCELLANEOUS: P.oleovorans accumulates poly(3-hydroxyalkanoates) after
CC       growth on medium chain length hydrocarbons. Large amounts of this
CC       polyester are synthesized when cells are grown under nitrogen-limiting
CC       conditions. When nitrogen is resupplied in the medium, the accumulated
CC       PHA is degraded. {ECO:0000305|PubMed:1989978}.
CC   -!- SIMILARITY: Belongs to the PHA/PHB synthase family. Type II PhaC
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M58445; AAA25932.1; -; Genomic_DNA.
DR   PIR; A38604; A38604.
DR   AlphaFoldDB; P26494; -.
DR   SMR; P26494; -.
DR   ESTHER; pseol-phaa; PHA_synth_II.
DR   BRENDA; 2.3.1.304; 5150.
DR   UniPathway; UPA00917; -.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042621; P:poly(3-hydroxyalkanoate) biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR011287; PHA_synth_II.
DR   InterPro; IPR010941; PhaC_N.
DR   Pfam; PF07167; PhaC_N; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01839; PHA_synth_II; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; PHA biosynthesis; PHB biosynthesis; Transferase.
FT   CHAIN           1..559
FT                   /note="Poly(3-hydroxyalkanoate) polymerase 1"
FT                   /id="PRO_0000215465"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   559 AA;  62364 MW;  9B8800EE7838E723 CRC64;
     MSNKNNDELQ RQASENTLGL NPVIGIRRKD LLSSARTVLR QAVRQPLHSA KHVAHFGLEL
     KNVLLGKSSL APESDDRRFN DPAWSNNPLY RRYLQTYLAW RKELQDWIGN SDLSPQDISR
     GQFVINLMTE AMAPTNTLSN PAAVKRFFET GGKSLLDGLS NLAKDLVNNG GMPSQVNMDA
     FEVGKNLGTS EGAVVYRNDV LELIQYKPIT EQVHARPLLV VPPQINKFYV FDLSPEKSLA
     RYCLRSQQQT FIISWRNPTK AQREWGLSTY IDALKEAVDA VLAITGSKDL NMLGACSGGI
     TCTALVGHYA ALGENKVNAL TLLVSVLDTT MDNQVALFVD EQTLEAAKRH SYQAGVLEGS
     EMAKVFAWMR PNDLIWNYWV NNYLLGNEPP VFDILFWNND TTRLPAAFHG DLIEMFKSNP
     LTRPDALEVC GTPIDLKQVK CDIYSLAGTN DHITPWQSCY RSAHLFGGKI EFVLSNSGHI
     QSILNPPGNP KARFMTGADR PGDPVAWQEN ATKHADSWWL HWQSWLGERA GELEKAPTRL
     GNRAYAAGEA SPGTYVHER