ID   PHAC_THIVI              Reviewed;         355 AA.
AC   P45366;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Poly(3-hydroxyalkanoate) polymerase subunit PhaC {ECO:0000303|PubMed:7763384};
DE            Short=PHA polymerase;
DE            EC=2.3.1.-;
DE   AltName: Full=PHB synthase subunit PhaC;
DE   AltName: Full=Poly(3-hydroxyalkanoate) synthase subunit PhaC {ECO:0000303|PubMed:7763384};
DE            Short=PHA synthase {ECO:0000303|PubMed:7763384};
DE            Short=Polyhydroxyalkanoic acid synthase;
DE   AltName: Full=Poly(3-hydroxybutyrate) polymerase subunit PhaC;
DE            Short=PHB polymerase;
DE            Short=Poly-beta-hydroxybutyrate polymerase;
GN   Name=phaC {ECO:0000303|PubMed:1476773};
GN   Synonyms=phbC {ECO:0000303|PubMed:7763384};
OS   Thiocystis violacea.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiocystis.
OX   NCBI_TaxID=13725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2311 / DSM 208;
RX   PubMed=7763384; DOI=10.1007/bf00242944;
RA   Liebergesell M., Steinbuechel A.;
RT   "Cloning and molecular analysis of the poly(3-hydroxybutyric acid)
RT   biosynthetic genes of Thiocystis violacea.";
RL   Appl. Microbiol. Biotechnol. 38:493-501(1993).
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: Polymerizes D(-)-3-hydroxybutyryl-CoA to create PHB which
CC       consists of thousands of hydroxybutyrate molecules linked end to end.
CC       PHB serves as an intracellular energy reserve material when cells grow
CC       under conditions of nutrient limitation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-3-hydroxybutanoyl-CoA + [(3R)-hydroxybutanoate](n) =
CC         [(3R)-hydroxybutanoate](n+1) + CoA; Xref=Rhea:RHEA:15405, Rhea:RHEA-
CC         COMP:14464, Rhea:RHEA-COMP:14465, ChEBI:CHEBI:8298,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57315;
CC         Evidence={ECO:0000250|UniProtKB:P45370};
CC   -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC       biosynthesis.
CC   -!- SUBUNIT: Forms a heterodimer with PhaE, which may multimerize in the
CC       presence of 3-hydroxybutyryl-CoA. {ECO:0000250|UniProtKB:P45370}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: Poly(3-hydroxyalkanoic acids) (PHA), of which PHB is
CC       among the most common compounds, are prokaryotic intracellular storage
CC       compounds with potential uses as a renewable, biodegradable
CC       thermoplastic. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PHA/PHB synthase family. Type III PhaC
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L01113; AAB02862.1; -; Genomic_DNA.
DR   EMBL; S54369; AAC60430.1; -; Genomic_DNA.
DR   PIR; D48376; D48376.
DR   AlphaFoldDB; P45366; -.
DR   SMR; P45366; -.
DR   ESTHER; thivi-phbc; PHA_synth_III_C.
DR   UniPathway; UPA00917; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; 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; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR010125; PHA_synth_III_C.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01836; PHA_synth_III_C; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; PHB biosynthesis; Transferase.
FT   CHAIN           1..355
FT                   /note="Poly(3-hydroxyalkanoate) polymerase subunit PhaC"
FT                   /id="PRO_0000215473"
FT   DOMAIN          68..333
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   355 AA;  39595 MW;  04BCC52E83CCD37E CRC64;
     MRPIDIRPDK LAQEMLDYTS KLGQGMENLL NADAIDTGVS PKEAVYSEDK LVLYRYDTPA
     GVTPQKTPLL IVYALVNRPY MTDIQEDRST IKGLLATGQD VYLIDWGYPD QADSALTLDD
     YINGYIDSCV DYLCETHEVD QVNILGICQG GAFSLMYASL HPDKVKNLVT MVTPVDFKTP
     GNLLSAWVQN VDIDLAVDTM GNIPGELLNW TFLSLKPFSL TGQKYVNMVD MLDDPDKVKN
     FLRMEKWIFD SPDQAGETFR QFTKDFYQKN GFINGGVKLG GKEIDLKNVD CPVLNIYALQ
     DHLVPPDASK ALNPWSAART YTELAFPGGH IGIYVSGKAQ KEVTPAIGKW LNERS