ID   PHAC_HALMT              Reviewed;         492 AA.
AC   I3R9Z4; B3FRM5;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Poly(3-hydroxyalkanoate) polymerase subunit PhaC;
DE            Short=PHA polymerase;
DE            EC=2.3.1.-;
DE   AltName: Full=PHB synthase subunit PhaC;
DE   AltName: Full=Poly(3-hydroxybutyrate) polymerase subunit PhaC;
DE            Short=PHB polymerase;
DE   AltName: Full=Polyhydroxyalkanoic acid synthase subunit PhaC;
DE            Short=PHA synthase;
GN   Name=phaC; OrderedLocusNames=HFX_5221; ORFNames=C439_00140;
OS   Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS   14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OG   Plasmid pHM300.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=523841;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RC   PLASMID=pHM300;
RX   PubMed=18408025; DOI=10.1128/jb.00134-08;
RA   Lu Q., Han J., Zhou L., Zhou J., Xiang H.;
RT   "Genetic and biochemical characterization of the poly(3-hydroxybutyrate-co-
RT   3-hydroxyvalerate) synthase in Haloferax mediterranei.";
RL   J. Bacteriol. 190:4173-4180(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RC   PLASMID=pHM300;
RX   PubMed=22843593; DOI=10.1128/jb.00880-12;
RA   Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA   Zhou J., Hu S., Xiang H.;
RT   "Complete genome sequence of the metabolically versatile halophilic
RT   archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT   hydroxyvalerate) producer.";
RL   J. Bacteriol. 194:4463-4464(2012).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RC   PLASMID=pHM300;
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- FUNCTION: Involved in the production of polyhydroxyalkonic acids
CC       (PHAs), which are water-insoluble biopolymers used as intracellular
CC       energy reserve material when cells grow under conditions of nutrient
CC       limitation. PHAs are composed primarily of 3-hydroxybutyric acid (3HB)
CC       and 3-hydroxyvaleric acid (3HV). Required for the production of poly-
CC       beta-hydroxybutyrate (PHB) and poly(beta-hydroxybutyrate-co-beta-
CC       hydroxyvalerate) (PHBV). {ECO:0000269|PubMed:18408025}.
CC   -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC       biosynthesis.
CC   -!- SUBUNIT: Heterodimer with PhaE. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Depletion of both phaC and phaE genes leads to
CC       complete loss of PHA synthase activity and PHBV production.
CC       {ECO:0000269|PubMed:18408025}.
CC   -!- BIOTECHNOLOGY: PHB and PHBV are desirable bioplastic due to their
CC       biodegradability, biocompatibility, and mechanical properties. However,
CC       PHBV has better mechanical properties than PHB.
CC   -!- SIMILARITY: Belongs to the PHA/PHB synthase family. {ECO:0000305}.
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DR   EMBL; EU374220; ACB10370.1; -; Genomic_DNA.
DR   EMBL; CP001870; AFK21054.1; -; Genomic_DNA.
DR   EMBL; AOLO01000001; EMA05161.1; -; Genomic_DNA.
DR   RefSeq; WP_004056138.1; NZ_CP039141.1.
DR   AlphaFoldDB; I3R9Z4; -.
DR   SMR; I3R9Z4; -.
DR   ESTHER; halme-b3frm5; PHA_synth_III_C.
DR   EnsemblBacteria; AFK21054; AFK21054; HFX_5221.
DR   EnsemblBacteria; EMA05161; EMA05161; C439_00140.
DR   GeneID; 40158350; -.
DR   KEGG; hme:HFX_5221; -.
DR   HOGENOM; CLU_035017_2_0_2; -.
DR   OMA; YLIDWGY; -.
DR   OrthoDB; 22660at2157; -.
DR   BRENDA; 2.3.1.304; 2566.
DR   UniPathway; UPA00917; -.
DR   Proteomes; UP000006469; Plasmid pHM300.
DR   Proteomes; UP000011603; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR   InterPro; IPR010125; PHA_synth_III_C.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF47794; SSF47794; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01836; PHA_synth_III_C; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; PHA biosynthesis; PHB biosynthesis; Plasmid; Transferase.
FT   CHAIN           1..492
FT                   /note="Poly(3-hydroxyalkanoate) polymerase subunit PhaC"
FT                   /id="PRO_0000428871"
FT   DOMAIN          70..336
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   REGION          359..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..376
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..425
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        150
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        305
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        334
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   492 AA;  54765 MW;  AB5EB91BA93D49C6 CRC64;
     MTPVTFALDL QRRQWEQAAE LVDRTSAASD RAETVSEVSV GKTPNEVVYK ENKLRLLHYE
     SKTETQYDVP ILIVYALINR PYILDLQPDR SVVQTLLEQG FDVYLIDWGE PSRLDTHLTL
     DDYVTRYIDN CVDIVRDRSG QDSINLLGYC MGGTMSVMYA ALFPEKVRNL GLMAAGLVFD
     DTGGVLERWG DEQYYSPKAV TDAFGNVPSE FLDVGFALMD PVENFVTKYV RLFENVENES
     FVENFSRMEQ WLSDGIDVAG ETYKQFLEDV YQQNKLAQNE LMLDGKQVDL ERLEMPILQI
     VGEYDHLIPP EASKPFNDLV PSEDTEVIEG ATGHIGLSVS SRSHGDLWPA VSDWFAERSE
     TGTDETPDSE TEETRPDSQA EETDETPDEG LKPQAAASNE TVAEEPEPQV VESNETTEEE
     LEPQAVEANE TAPEELESID GIGPTYAERL ASVGITSVSG LAAADPSEIA ATIDVPVSRV
     TAWVEQASDR TD