ID   PHAC_RHIEC              Reviewed;         636 AA.
AC   Q52728; Q2K920;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 114.
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            Short=Poly-beta-hydroxybutyrate polymerase;
DE   AltName: Full=Polyhydroxyalkanoic acid synthase subunit PhaC;
DE            Short=PHA synthase;
GN   Name=phaC {ECO:0000303|PubMed:16505379}; Synonyms=phbC;
GN   OrderedLocusNames=RHE_CH01875;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CE3;
RX   PubMed=8626293; DOI=10.1128/jb.178.6.1646-1654.1996;
RA   Cevallos M.A., Encarnacion S., Leija A., Mora Y., Mora J.;
RT   "Genetic and physiological characterization of a Rhizobium etli mutant
RT   strain unable to synthesize poly-beta-hydroxybutyrate.";
RL   J. Bacteriol. 178:1646-1654(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PHA/PHB synthase family. Type I PhaC
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC90666.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U30612; AAB05020.1; -; Genomic_DNA.
DR   EMBL; CP000133; ABC90666.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_042118340.1; NC_007761.1.
DR   AlphaFoldDB; Q52728; -.
DR   SMR; Q52728; -.
DR   STRING; 347834.RHE_CH01875; -.
DR   ESTHER; rhiet-phbc; PHA_synth_I.
DR   EnsemblBacteria; ABC90666; ABC90666; RHE_CH01875.
DR   KEGG; ret:RHE_CH01875; -.
DR   eggNOG; COG3243; Bacteria.
DR   HOGENOM; CLU_017387_1_0_5; -.
DR   UniPathway; UPA00917; -.
DR   Proteomes; UP000001936; Chromosome.
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; IPR010963; PHA_synth_I.
DR   InterPro; IPR010941; PhaC_N.
DR   Pfam; PF07167; PhaC_N; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01838; PHA_synth_I; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; PHB biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..636
FT                   /note="Poly(3-hydroxyalkanoate) polymerase subunit PhaC"
FT                   /id="PRO_0000215471"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        373
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   636 AA;  71936 MW;  DD370C10ECC89D12 CRC64;
     MYNKRIKRVL PPEEMVTDSK QESGGQKNGD KTGFDATDLK PYLLKDPETM AMNFARALEN
     LGQAASAWLA PRERGEITET AIDPMTDMVK TLSKISEYWI SDPRRTFEAQ TQLMSSFFGI
     WMRSMQRMQG TRGMQGEPLP PEPDTRKDKR FSDEDWQKNP FFDFLRQVYF VTSDWVDKLV
     SETDGLDEHT KHKAGFYVKQ ITAALSPSNF IATNPQLYRE TIASNGENLV RGMKMLAEDI
     AAGKGELRLR QTDMTKFAVG RDMALTPGKV IAQNDICQII QYEASTETVL KRPLLICPPW
     INKFYILDLN PQKSFIKWCV DQGQTVFVIS WVNPDGRHAE KDWAAYAREG IDFALETIEK
     ATGEKEVNAV GYCVGGTLLA ATLALHAKEK NKRIKTATLF TTQVDFTHAG DLKVFVDEEQ
     LAALEEHMQA AGYLDGSKMS MAFNMLRASE LIWPYFVNSY LKGQEPLPFD LLFWNADSTR
     MAAANHAFYL RNCYLRNALT QNEMILDGKR ISLKDVKIPI YNLATREDHI APAKSVFLGS
     RFFGGKVEFV VTGSGHIAGV VNPPDKRKYQ FWTGGPAKGE YETWLEQASE TPGSWWPHWQ
     AWIETHDGRR VAARKPGGDA LNAIEEAPGS YVMERT