PHAC_ALLVD
ID PHAC_ALLVD Reviewed; 355 AA.
AC P45370; D3RUY4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Poly(3-hydroxyalkanoate) polymerase subunit PhaC;
DE Short=PHA polymerase;
DE EC=2.3.1.- {ECO:0000269|PubMed:7957260};
DE AltName: Full=PHB synthase subunit PhaC;
DE AltName: Full=Poly(hydroxyalkanoic acid) synthase subunit PhaC {ECO:0000303|PubMed:7957260};
DE Short=PHA synthase subunit PhaC {ECO:0000303|PubMed:7957260};
DE Short=Polyhydroxyalkanoic acid synthase {ECO:0000303|PubMed:7957260};
DE AltName: Full=Poly-beta-hydroxybutyrate polymerase {ECO:0000303|PubMed:7957260};
DE Short=PHB polymerase;
DE Short=Poly(3-hydroxybutyrate) polymerase;
GN Name=phaC {ECO:0000303|PubMed:7957260};
GN Synonyms=phbC {ECO:0000303|PubMed:1396692}; OrderedLocusNames=Alvin_0061;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=1396692; DOI=10.1111/j.1432-1033.1992.tb17270.x;
RA Liebergesell M., Steinbuechel A.;
RT "Cloning and nucleotide sequences of genes relevant for biosynthesis of
RT poly(3-hydroxybutyric acid) in Chromatium vinosum strain D.";
RL Eur. J. Biochem. 209:135-150(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
RN [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=7957260; DOI=10.1111/j.1432-1033.1994.tb20027.x;
RA Liebergesell M., Sonomoto K., Madkour M., Mayer F., Steinbuechel A.;
RT "Purification and characterization of the poly(hydroxyalkanoic acid)
RT synthase from Chromatium vinosum and localization of the enzyme at the
RT surface of poly(hydroxyalkanoic acid) granules.";
RL Eur. J. Biochem. 226:71-80(1994).
RN [5]
RP FUNCTION, ACTIVE SITE, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF
RP CYS-130; CYS-149 AND CYS-292.
RX PubMed=9888824; DOI=10.1021/bi9818319;
RA Mueh U., Sinskey A.J., Kirby D.P., Lane W.S., Stubbe J.;
RT "PHA synthase from Chromatium vinosum: cysteine 149 is involved in covalent
RT catalysis.";
RL Biochemistry 38:826-837(1999).
CC -!- FUNCTION: Polymerizes D(-)-3-hydroxybutyryl-CoA to create
CC polyhydroxybutyrate (PHB) which consists of thousands of
CC hydroxybutyrate molecules linked end to end (PubMed:7957260). This
CC subunit has catalytic activity that is enhanced 100-fold by PhaE, the
CC non-catalytic subunit (PubMed:9888824). {ECO:0000269|PubMed:7957260,
CC ECO:0000269|PubMed:9888824}.
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:7957260, ECO:0000269|PubMed:9888824};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.063 mM for D(-)-3-hydroxybutyryl-CoA
CC {ECO:0000269|PubMed:7957260};
CC Note=Measured with the heterodimeric enzyme (PubMed:7957260). There
CC are at least 2 substrate binding sites which display positive
CC cooperativity (PubMed:7957260). {ECO:0000269|PubMed:7957260};
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:7957260};
CC -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC biosynthesis.
CC -!- SUBUNIT: A large complex of PhaC and PhaE; the ratio of the subunits
CC has been estimated to be from 1:1 to 4:1, with more PhaE than PhaC
CC (PubMed:7957260, PubMed:9888824). {ECO:0000269|PubMed:7957260,
CC ECO:0000269|PubMed:9888824}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Associates with the
CC exterior of poly(3-hydroxybutyric acid) granules (PHB) when grown under
CC 'storage' conditions. {ECO:0000269|PubMed:7957260}.
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 PhaC
CC subfamily. {ECO:0000305}.
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DR EMBL; L01112; AAA23320.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC61033.1; -; Genomic_DNA.
DR PIR; S29274; S29274.
DR RefSeq; WP_012969309.1; NC_013851.1.
DR AlphaFoldDB; P45370; -.
DR SMR; P45370; -.
DR STRING; 572477.Alvin_0061; -.
DR ESTHER; chrvi-phbc; PHA_synth_III_C.
DR EnsemblBacteria; ADC61033; ADC61033; Alvin_0061.
DR KEGG; alv:Alvin_0061; -.
DR eggNOG; COG3243; Bacteria.
DR HOGENOM; CLU_035017_0_0_6; -.
DR OMA; YLIDWGY; -.
DR OrthoDB; 891360at2; -.
DR BRENDA; 2.3.1.304; 257.
DR UniPathway; UPA00917; -.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0070088; C:PHA granule; IDA:UniProtKB.
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..355
FT /note="Poly(3-hydroxyalkanoate) polymerase subunit PhaC"
FT /id="PRO_0000215470"
FT DOMAIN 69..334
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 149
FT /evidence="ECO:0000255, ECO:0000269|PubMed:9888824"
FT MUTAGEN 130
FT /note="C->A: 400-fold decrease in PHA synthase activity."
FT /evidence="ECO:0000269|PubMed:9888824"
FT MUTAGEN 149
FT /note="C->A: No PHA synthase activity."
FT /evidence="ECO:0000269|PubMed:9888824"
FT MUTAGEN 292
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:9888824"
FT CONFLICT 113
FT /note="A -> G (in Ref. 1; AAA23320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 39775 MW; 544CE7BC44F55BBF CRC64;
MFPIDIRPDK LTQEMLDYSR KLGQGMENLL NAEAIDTGVS PKQAVYSEDK LVLYRYDRPE
GAPEAQPVPL LIVYALVNRP YMTDIQEDRS TIKGLLATGQ DVYLIDWGYP DQADRALTLD
DYINGYIDRC VDYLREAHGV DKVNLLGICQ GGAFSLMYSA LHPDKVRNLV TMVTPVDFKT
PDNLLSAWVQ NVDIDLAVDT MGNIPGELLN WTFLSLKPFS LTGQKYVNMV DLLDDPDKVK
NFLRMEKWIF DSPDQAGETF RQFIKDFYQN NGFLNGGVVL GGQEVDLKDI TCPVLNIFAL
QDHLVPPDAS RALKGLTSSP DYTELAFPGG HIGIYVSGKA QKEVTPAIGK WLNER
