PHAE_HALMT
ID PHAE_HALMT Reviewed; 182 AA.
AC I3R9Z3; B3FRM4;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Poly(3-hydroxyalkanoate) polymerase subunit PhaE;
DE Short=PHA polymerase;
DE EC=2.3.1.-;
DE AltName: Full=PHB synthase subunit PhaE;
DE AltName: Full=Poly(3-hydroxybutyrate) polymerase subunit PhaE;
DE Short=PHB polymerase;
DE AltName: Full=Polyhydroxyalkanoic acid synthase subunit PhaE;
DE Short=PHA synthase;
GN Name=phaE; OrderedLocusNames=HFX_5220; ORFNames=C439_00145;
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OG Plasmid pHM300.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RC PLASMID=pHM300;
RX PubMed=18408025; DOI=10.1128/jb.00134-08;
RA Lu Q., Han J., Zhou L., Zhou J., Xiang H.;
RT "Genetic and biochemical characterization of the poly(3-hydroxybutyrate-co-
RT 3-hydroxyvalerate) synthase in Haloferax mediterranei.";
RL J. Bacteriol. 190:4173-4180(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RC PLASMID=pHM300;
RX PubMed=22843593; DOI=10.1128/jb.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RC PLASMID=pHM300;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:18408025}.
CC -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC biosynthesis.
CC -!- SUBUNIT: Heterodimer with PhaC. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Depletion of both phaC and phaE genes leads to
CC complete loss of PHA synthase activity and PHBV production.
CC {ECO:0000269|PubMed:18408025}.
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; EU374220; ACB10369.1; -; Genomic_DNA.
DR EMBL; CP001870; AFK21053.1; -; Genomic_DNA.
DR EMBL; AOLO01000001; EMA05162.1; -; Genomic_DNA.
DR AlphaFoldDB; I3R9Z3; -.
DR EnsemblBacteria; AFK21053; AFK21053; HFX_5220.
DR EnsemblBacteria; EMA05162; EMA05162; C439_00145.
DR KEGG; hme:HFX_5220; -.
DR HOGENOM; CLU_1485849_0_0_2; -.
DR OMA; EFRDIWL; -.
DR BRENDA; 2.3.1.304; 2566.
DR UniPathway; UPA00917; -.
DR Proteomes; UP000006469; Plasmid pHM300.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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.
PE 1: Evidence at protein level;
KW Acyltransferase; PHA biosynthesis; PHB biosynthesis; Plasmid; Transferase.
FT CHAIN 1..182
FT /note="Poly(3-hydroxyalkanoate) polymerase subunit PhaE"
FT /id="PRO_0000428874"
SQ SEQUENCE 182 AA; 20452 MW; 54A71D6456B1C265 CRC64;
MSQQKGDEWT MYAAEMNETM LAALERNVEA QTQFVESWLD ALEETPEMST ETISEGLNGY
ARAYEVWMNA AEQQFERASD AFEGEDVSAN EFRDIWLNSA NEAFKEVMGT SAFAAATGQT
VEDALEMQRE VDEAAQSTLR TLGFATEGDI DEVAERLVEL ERRQHAVETK LDRLLDAMDV
EG