PHAE_ALLVD
ID PHAE_ALLVD Reviewed; 357 AA.
AC P45372; D3RUY5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Poly(3-hydroxyalkanoate) polymerase subunit PhaE;
DE Short=PHA polymerase;
DE AltName: Full=ORF2 {ECO:0000303|PubMed:1396692};
DE AltName: Full=PHB synthase subunit PhaE;
DE AltName: Full=Poly(hydroxyalkanoic acid) synthase subunit PhaE {ECO:0000303|PubMed:7957260};
DE Short=PHA synthase {ECO:0000303|PubMed:7957260};
DE Short=Polyhydroxyalkanoic acid synthase {ECO:0000303|PubMed:7957260};
DE AltName: Full=Poly-beta-hydroxybutyrate polymerase subunit PhaE {ECO:0000303|PubMed:7957260};
DE Short=PHB polymerase;
DE Short=Poly(3-hydroxybutyrate) polymerase;
GN Name=phaE {ECO:0000303|PubMed:7957260}; OrderedLocusNames=Alvin_0062;
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, AND SUBUNIT.
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 no catalytic activity but enhances the activity of PhaC,
CC the catalytic subunit, 100-fold (PubMed:9888824).
CC {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
CC poly(3-hydroxybutyric acid) granules (PHB) when grown under 'storage'
CC 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 PhaE
CC subfamily. {ECO:0000305}.
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DR EMBL; L01112; AAA23321.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC61034.1; -; Genomic_DNA.
DR RefSeq; WP_012969310.1; NC_013851.1.
DR AlphaFoldDB; P45372; -.
DR STRING; 572477.Alvin_0062; -.
DR EnsemblBacteria; ADC61034; ADC61034; Alvin_0062.
DR KEGG; alv:Alvin_0062; -.
DR eggNOG; ENOG502Z9Y0; Bacteria.
DR HOGENOM; CLU_056549_0_0_6; -.
DR OMA; REENAPW; -.
DR OrthoDB; 1113165at2; -.
DR UniPathway; UPA00917; -.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0070088; C:PHA granule; IDA:UniProtKB.
DR GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR010123; PHA_synth_III_E.
DR Pfam; PF09712; PHA_synth_III_E; 1.
DR TIGRFAMs; TIGR01834; PHA_synth_III_E; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; PHB biosynthesis; Reference proteome.
FT CHAIN 1..357
FT /note="Poly(3-hydroxyalkanoate) polymerase subunit PhaE"
FT /id="PRO_0000066400"
FT REGION 320..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 40
FT /note="T -> N (in Ref. 1; AAA23321)"
FT /evidence="ECO:0000305"
FT CONFLICT 313..314
FT /note="HS -> RD (in Ref. 1; AAA23321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 40524 MW; D87B83E54F085AD1 CRC64;
MSNTNFFNDD WLELQRKYWD NWTDMSRKAM GLDSASSSAT TPWEAAIDQW WKAMAPAAPD
LSRSFMEKMM EQGKNFFRLA DTFAKRADEG NAGNGLELWT KTLEDMQKRF SGSLDDGGNT
MQRLMSFWEL PLDNWQRMMS SMSPMPGDML RNMPHEQFKD SLDRALSAPG LGYTREEQSQ
YQELMRSAME YQAALQEYTN VYTKLGMKSV EHMGSYIQGV IDSGKTIDSA RALYDNWVAC
CEGAYADEVA TPEYARIHGR LVNAQMALKK RMSILVDENL GALNMPTRSE LRTLQDRLQE
TRRENKALRH SLHSLERRVA ALAGEEPATK PATALRSPAP AAKAPARRRT TKTNPAD
