ID   PHAC_HALMA              Reviewed;         475 AA.
AC   Q5UYM0;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=rrnAC2886;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=17675423; DOI=10.1128/aem.00953-07;
RA   Han J., Lu Q., Zhou L., Zhou J., Xiang H.;
RT   "Molecular characterization of the phaECHm genes, required for biosynthesis
RT   of poly(3-hydroxybutyrate) in the extremely halophilic archaeon Haloarcula
RT   marismortui.";
RL   Appl. Environ. Microbiol. 73:6058-6065(2007).
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:17675423}.
CC   -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC       biosynthesis.
CC   -!- SUBUNIT: Heterodimer with PhaE. {ECO:0000250}.
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; AY596297; AAV47633.1; -; Genomic_DNA.
DR   RefSeq; WP_011224492.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UYM0; -.
DR   SMR; Q5UYM0; -.
DR   STRING; 272569.rrnAC2886; -.
DR   ESTHER; halma-q5uym0; PHA_synth_III_C.
DR   EnsemblBacteria; AAV47633; AAV47633; rrnAC2886.
DR   GeneID; 40153729; -.
DR   KEGG; hma:rrnAC2886; -.
DR   PATRIC; fig|272569.17.peg.3454; -.
DR   eggNOG; arCOG06344; Archaea.
DR   HOGENOM; CLU_035017_2_0_2; -.
DR   OMA; YLIDWGY; -.
DR   UniPathway; UPA00917; -.
DR   Proteomes; UP000001169; Chromosome I.
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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..475
FT                   /note="Poly(3-hydroxyalkanoate) polymerase subunit PhaC"
FT                   /id="PRO_0000428870"
FT   DOMAIN          82..348
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   REGION          369..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..422
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        162
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        317
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        346
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   475 AA;  53121 MW;  C0B8B3069D0E12D0 CRC64;
     MSSNPFNPFE AALNWQRKTL ENMTDAAETS QVADERLELM ESVDVGQTPS NVVYEENKLE
     LLHYDAEAAG IEVPDEEKED VPILIVYALI NRPYILDLQE ERSVVRRLLE AGHDVYLIDW
     NEPSRLDQHL TLDDYVNRYM DNCVDVVRDR SGQDAINILG YCMGGTMSVM YTALHKEKVN
     TLGLMAAGLC FDHTGGVLEE WGSEEYYSPQ DVVDTFGNVP ADMLDIGFAL MDPVENYVTK
     YIRFAENMEN EGFVENFGRM EQWLGDGIDV AGEAYVQFLE DVYQDNKLYK NELELDGKHV
     DLDNIDMPVL QLMGEYDHLI PPEASKPFND VIASDDTRTI EFSTGHIGLS VSSSTHADLW
     PEVAEWYSER STGSEEVDIE VESPEAAEDD AVDQSELTDI DVDATDDVDA DATEDDATDE
     PADVDSVSGI GPTYAERLHD AGIHSVADLA EYDAADLADI AETTESRAQD WLDQL