ID   PHAE_THIVI              Reviewed;         364 AA.
AC   P45367;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Poly(3-hydroxyalkanoate) polymerase subunit PhaE {ECO:0000303|PubMed:7763384};
DE            Short=PHA polymerase;
DE   AltName: Full=ORF2 {ECO:0000303|PubMed:7763384};
DE   AltName: Full=PHB synthase subunit PhaE;
DE   AltName: Full=Poly(3-hydroxyalkanoate) synthase subunit PhaE;
DE            Short=PHA synthase {ECO:0000303|PubMed:7763384};
DE            Short=Polyhydroxyalkanoic acid synthase;
DE   AltName: Full=Poly(3-hydroxybutyrate) polymerase subunit PhaE;
DE            Short=PHB polymerase;
DE            Short=Poly-beta-hydroxybutyrate polymerase;
GN   Name=phaE {ECO:0000303|PubMed:1476773};
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
CC       polyhydroxybutyrate (PHB) which consists of thousands of
CC       hydroxybutyrate molecules linked end to end. This subunit has no
CC       catalytic activity but enhances the activity of PhaC, the catalytic
CC       subunit. {ECO:0000250|UniProtKB:P45372}.
CC   -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC       biosynthesis.
CC   -!- SUBUNIT: Forms a heterodimer with PhaC, which may multimerize in the
CC       presence of 3-hydroxybutyryl-CoA. {ECO:0000250|UniProtKB:P73389}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P45372}.
CC   -!- MISCELLANEOUS: Poly(3-hydroxyalkanoic acids) (PHA), of which PHB is
CC       among the most common compounds, has potential uses as a renewable,
CC       biodegradable thermoplastic. PHB serves as an intracellular energy
CC       reserve material when cells grow under conditions of nutrient
CC       limitation. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PHA/PHB synthase family. Type III PhaE
CC       subfamily. {ECO:0000305}.
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; L01113; AAB02861.1; -; Genomic_DNA.
DR   EMBL; S54369; AAC60429.2; -; Genomic_DNA.
DR   PIR; C48376; C48376.
DR   AlphaFoldDB; P45367; -.
DR   SMR; P45367; -.
DR   UniPathway; UPA00917; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR010123; PHA_synth_III_E.
DR   Pfam; PF09712; PHA_synth_III_E; 1.
DR   TIGRFAMs; TIGR01834; PHA_synth_III_E; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; PHB biosynthesis.
FT   CHAIN           1..364
FT                   /note="Poly(3-hydroxyalkanoate) polymerase subunit PhaE"
FT                   /id="PRO_0000066401"
FT   REGION          322..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        161..162
FT                   /note="SG -> FD (in Ref. 1; AAC60429)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        181..182
FT                   /note="HQ -> QE (in Ref. 1; AAC60429)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   364 AA;  41387 MW;  1F099324A2BACD4B CRC64;
     MSNDSFFNND WLELQRKYWD SWSEMGRKAM GLENQQTLTT PWEGALDHWW KAMSPATPDF
     SKTFMEKMME QGKNFFRMAE TFANTPEDTT ATNGLTWWTK ALEDMQKQFS GSLDDGGNSM
     QRMMSFWELP IDNWQRMMSS MSPMPGDMLR NMPHEQLKDR SGRALSAPGL GYTREEQSQY
     HQLTRTAMDY QAALQEYTGF YSQLGMKSVE RMGDFIQGVI DSGKSIDSAR TLYDNWISCC
     ETVYAAEVAT PEYAQIHGRL VNAQMALKRR MAIMVDENLG AMNMPTRSEL RTLQDRLQET
     RRDNKQLHRA LHALEKQVAA LSGKTPTTAL KAPAPATKAT EKPATRATTR RKTAAKPTGG
     TADD