PHAC_SYNY3
ID PHAC_SYNY3 Reviewed; 378 AA.
AC P73390;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Poly(3-hydroxyalkanoate) polymerase subunit PhaC;
DE Short=PHA polymerase;
DE EC=2.3.1.- {ECO:0000269|PubMed:25629766};
DE AltName: Full=PHB synthase subunit PhaC;
DE AltName: Full=Poly(3-hydroxybutyrate) polymerase subunit PhaC;
DE Short=PHB polymerase;
DE AltName: Full=Poly(hydroxyalkanoic acid) synthase subunit PhaC;
DE Short=PHA synthase {ECO:0000303|PubMed:9683655};
DE Short=Polyhydroxyalkanoic acid synthase subunit PhaC {ECO:0000303|PubMed:9683655};
GN Name=phaC {ECO:0000303|PubMed:9683655};
GN Synonyms=phbC {ECO:0000312|EMBL:BAA17430.1}; OrderedLocusNames=slr1830;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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).
RN [3]
RP FUNCTION, PATHWAY, SUBUNIT, AND EXPRESSION IN E.COLI.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=9683655; DOI=10.1007/s002030050629;
RA Hein S., Tran H., Steinbuechel A.;
RT "Synechocystis sp. PCC6803 possesses a two-component polyhydroxyalkanoic
RT acid synthase similar to that of anoxygenic purple sulfur bacteria.";
RL Arch. Microbiol. 170:162-170(1998).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=25629766; DOI=10.1021/bi501560b;
RA Numata K., Motoda Y., Watanabe S., Osanai T., Kigawa T.;
RT "Co-expression of two polyhydroxyalkanoate synthase subunits from
RT Synechocystis sp. PCC 6803 by cell-free synthesis and their specific
RT activity for polymerization of 3-hydroxybutyryl-coenzyme A.";
RL Biochemistry 54:1401-1407(2015).
CC -!- FUNCTION: When expressed in E.coli with Synechocystis PhaE and
CC C.necator PhaA and PhaB, confers the ability to synthesize up to 13%
CC (w/w) poly(3-hydroxybutyrate) (PHB) depending on the carbon source; all
CC 4 genes are necessary for PHB production (PubMed:9683655). Cell-free in
CC vitro coexpression with PhaE gives a heterodimer able to polymerize 3-
CC hydroxybutyrate-CoA (PubMed:25629766). {ECO:0000269|PubMed:25629766,
CC ECO:0000269|PubMed:9683655}.
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:0000269|PubMed:25629766};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=478 uM for 3-hydroxybutyryl-CoA {ECO:0000269|PubMed:25629766};
CC -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC biosynthesis. {ECO:0000305|PubMed:9683655}.
CC -!- SUBUNIT: Forms a heterodimer with PhaE, which may multimerize in the
CC presence of 3-hydroxybutyryl-CoA (PubMed:25629766). Both subunits are
CC required for PHB synthesis in E.coli and in PHA-negative A.eutrophus.
CC {ECO:0000269|PubMed:25629766, ECO:0000269|PubMed:9683655}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- BIOTECHNOLOGY: 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 renewable, biodegradable
CC thermoplastics. Cyanobacterial PHB synthesis is particularly attractive
CC as cyanobacteria use CO(2) as the carbon source. {ECO:0000305}.
CC -!- MISCELLANEOUS: Nitrogen-free medium induces chlorosis in Synechocystis,
CC leading to the degradation of the photosynthetic apparatus and
CC concomitant accumulation of cytoplasmic polyhydroxyalkanoic acid (PHA)
CC granules which in this cyanobacterium are composed of PHB.
CC {ECO:0000269|PubMed:9683655}.
CC -!- SIMILARITY: Belongs to the PHA/PHB synthase family. Type III PhaC
CC subfamily. {ECO:0000305}.
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DR EMBL; BA000022; BAA17430.1; -; Genomic_DNA.
DR PIR; S77327; S77327.
DR AlphaFoldDB; P73390; -.
DR SMR; P73390; -.
DR STRING; 1148.1652509; -.
DR ESTHER; synsp-PHBC; PHA_synth_III_C.
DR PaxDb; P73390; -.
DR EnsemblBacteria; BAA17430; BAA17430; BAA17430.
DR KEGG; syn:slr1830; -.
DR eggNOG; COG3243; Bacteria.
DR InParanoid; P73390; -.
DR OMA; YLIDWGY; -.
DR PhylomeDB; P73390; -.
DR UniPathway; UPA00917; -.
DR Proteomes; UP000001425; 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; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; PHB biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..378
FT /note="Poly(3-hydroxyalkanoate) polymerase subunit PhaC"
FT /id="PRO_0000438832"
FT DOMAIN 84..356
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
SQ SEQUENCE 378 AA; 42961 MW; 75832BBDE6E06424 CRC64;
MFLLFFIVHW LKIMLPFFAQ VGLEENLHET LDFTEKFLSG LENLQGLNED DIQVGFTPKE
AVYQEDKVIL YRFQPVVENP LPIPVLIVYA LVNRPYMVDL QEGRSLVANL LKLGLDVYLI
DWGYPSRGDR WLTLEDYLSG YLNNCVDIIC QRSQQEKITL LGVCQGGTFS LCYASLFPDK
VKNLVVMVAP VDFEQPGTLL NARGGCTLGA EAVDIDLMVD AMGNIPGDYL NLEFLMLKPL
QLGYQKYLDV PDIMGDEAKL LNFLRMEKWI FDSPDQAGET YRQFLKDFYQ QNKLIKGEVM
IGDRLVDLHN LTMPILNLYA EKDHLVAPAS SLALGDYLPE NCDYTVQSFP VGHIGMYVSG
KVQRDLPPAI AHWLSERQ
