PHAC_HALHT
ID PHAC_HALHT Reviewed; 474 AA.
AC G0HQZ6; A8C9M4;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 45.
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 AltName: Full=Polyhydroxyalkanoic acid synthase subunit PhaC;
DE Short=PHA synthase;
GN Name=phaC; OrderedLocusNames=HAH_0154;
OS Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182
OS / NCIMB 2187 / VKM B-1755).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=634497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM
RC B-1755;
RX PubMed=17675423; DOI=10.1128/aem.00953-07;
RA Han J., Lu Q., Zhou L., Zhou J., Xiang H.;
RT "Molecular characterization of the phaECHm genes, required for biosynthesis
RT of poly(3-hydroxybutyrate) in the extremely halophilic archaeon Haloarcula
RT marismortui.";
RL Appl. Environ. Microbiol. 73:6058-6065(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM
RC B-1755;
RX PubMed=21994921; DOI=10.1128/jb.05953-11;
RA Liu H., Wu Z., Li M., Zhang F., Zheng H., Han J., Liu J., Zhou J., Wang S.,
RA Xiang H.;
RT "Complete genome sequence of Haloarcula hispanica, a model haloarchaeon for
RT studying genetics, metabolism, and virus-host interaction.";
RL J. Bacteriol. 193:6086-6087(2011).
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:17675423}.
CC -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC biosynthesis.
CC -!- SUBUNIT: Heterodimer with PhaE. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Depletion of both phaC and phaE genes leads to
CC complete loss of the PHA synthase activity.
CC {ECO:0000269|PubMed:17675423}.
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; EU022705; ABV71394.1; -; Genomic_DNA.
DR EMBL; CP002921; AEM55787.1; -; Genomic_DNA.
DR RefSeq; WP_014039171.1; NC_015948.1.
DR AlphaFoldDB; G0HQZ6; -.
DR SMR; G0HQZ6; -.
DR STRING; 634497.HAH_0154; -.
DR EnsemblBacteria; AEM55787; AEM55787; HAH_0154.
DR GeneID; 23804483; -.
DR KEGG; hhi:HAH_0154; -.
DR eggNOG; arCOG06344; Archaea.
DR HOGENOM; CLU_035017_2_0_2; -.
DR OMA; YLIDWGY; -.
DR OrthoDB; 22660at2157; -.
DR UniPathway; UPA00917; -.
DR Proteomes; UP000005629; Chromosome I.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR010125; PHA_synth_III_C.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01836; PHA_synth_III_C; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; PHA biosynthesis; PHB biosynthesis; Transferase.
FT CHAIN 1..474
FT /note="Poly(3-hydroxyalkanoate) polymerase subunit PhaC"
FT /id="PRO_0000428869"
FT DOMAIN 82..348
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 368..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..404
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 317
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 346
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT CONFLICT 213
FT /note="V -> A (in Ref. 1; ABV71394)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="G -> S (in Ref. 1; ABV71394)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 52982 MW; 4A3F441436787BA0 CRC64;
MSSNPFNPFE AALNWQRKTL ENMTDAAETS QIADERLELM ESVEVGQTPS DVVYEENKLE
LLHYDAEATG IEVAEEDKEA VPILIVYALI NRPYILDLQE ERSVVRRLLE AGHDVYLIDW
NEPSRLDQHL TLDDYVNRYM DNCVDVVRER SGQDAINILG YCMGGTMSVM YTALHKEKVN
TLGLMAAGLC FDHTGGVLEE WGSEEYYSPQ DVVDTFGNVP SDMLDIGFAL MDPVENYVTK
YIRFAENMEN EGFVENFGRM EQWLGDGIDV AGEAYVQFLE DVYQDNKLYK NELELNGKHV
DLDNIDMPVL QLMGEYDHLI PPEASKPFND VIASDDTRTI EFSTGHIGLS VSSSTHADLW
PEVAEWYSER STGGEEVDIE VESPEDDTVD QSESTDIEVD ATDDVDADAT EDDADAADEP
ADVDSVSGIG PTYAERLHAA GIHSVADLAE YDAAELADIA ETTESRAQDW LDQL
