ID   PHAC2_PSEOL             Reviewed;         560 AA.
AC   P26496;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Poly(3-hydroxyalkanoate) polymerase 2;
DE            Short=PHA polymerase 2 {ECO:0000303|PubMed:1989978};
DE            EC=2.3.1.-;
DE   AltName: Full=ORF3 {ECO:0000303|PubMed:1989978};
DE   AltName: Full=PHA synthase 2;
DE   AltName: Full=Polyhydroxyalkanoic acid synthase 2;
GN   Name=phaC2 {ECO:0000303|PubMed:1476773};
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; AAA25934.1; -; Genomic_DNA.
DR   PIR; C38604; C38604.
DR   AlphaFoldDB; P26496; -.
DR   SMR; P26496; -.
DR   ESTHER; pseol-phac; PHA_synth_II.
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..560
FT                   /note="Poly(3-hydroxyalkanoate) polymerase 2"
FT                   /id="PRO_0000215466"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   560 AA;  62631 MW;  E2CD844FC1616B83 CRC64;
     MKDKPAKGTP TLPATSMNVQ NAILGLRGRD LISTLRNVSR QSLRHPLHTA HHLLALGGQL
     GRVILGDTPL QPNPRDPRFS DPTWSQNPFY RRGLQAYLAW QKQTRLWIEE SHLDDDDRAR
     AHFLFNLIND ALAPSNSLLN PLAVKELFNS GGQSLVRGVA HLLDDLRHND GLPRQVDERA
     FEVGGNLAAT AGAVVFRNEL LELIQYKPMS EKQHARPLLV VPPQINKFYI FDLSSTNSFV
     QYMLKNGLQV FMVSWRNPDP RHREWGLSSY VQALEEALNA CRSISGNRDP NLMGACAGGL
     TMAALQGHLQ AKHQLRRVRS ATYLVSLLDS KFESPASLFA DEQTIEAAKR RSYQRGVLDG
     AEVARIFAWM RPNDLIWNYW VNNYLLGKTP PAFDILYWNA DSTRLPAALH GDLLDFFKLN
     PLTHPAGLEV CGTPIDLQKV ELDSFTVAGS NDHITPWDAV YRSALLLGGD RRFVLANSGH
     IQSIINPPGN PKAYYLANPK LSSDPRAWLH DAKRSEGSWW PLWLEWITAR SGPLKAPRSE
     LGNATYPPLG PAPGTYVLTR