PHAC_AZOC5
ID PHAC_AZOC5 Reviewed; 583 AA.
AC O66392; A8I2B4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 102.
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 Short=Poly-beta-hydroxybutyrate polymerase;
DE AltName: Full=Polyhydroxyalkanoic acid synthase subunit PhaC;
DE Short=PHA synthase;
GN Name=phaC {ECO:0000303|PubMed:1476773}; Synonyms=phbC;
GN OrderedLocusNames=AZC_1845;
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9748438; DOI=10.1128/jb.180.19.5070-5076.1998;
RA Mandon K., Michel-Reydellet N., Encarnacion S., Kaminski P.A., Leija A.,
RA Cevallos M.A., Elmerich C., Mora J.;
RT "Poly-beta-hydroxybutyrate turnover in Azorhizobium caulinodans is required
RT for growth and affects nifA expression.";
RL J. Bacteriol. 180:5070-5076(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC 13405 / ORS 571;
RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT caulinodans ORS571.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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).
CC -!- FUNCTION: Polymerizes D(-)-3-hydroxybutyryl-CoA to create PHB which
CC consists of thousands of hydroxybutyrate molecules linked end to end.
CC PHB serves as an intracellular energy reserve material when cells grow
CC under conditions of nutrient limitation.
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:0000250|UniProtKB:P45370};
CC -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PHA/PHB synthase family. Type I PhaC
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ006237; CAA06928.1; -; Genomic_DNA.
DR EMBL; AP009384; BAF87843.1; -; Genomic_DNA.
DR AlphaFoldDB; O66392; -.
DR SMR; O66392; -.
DR STRING; 438753.AZC_1845; -.
DR ESTHER; azoc5-phbc; PHA_synth_I.
DR EnsemblBacteria; BAF87843; BAF87843; AZC_1845.
DR KEGG; azc:AZC_1845; -.
DR eggNOG; COG3243; Bacteria.
DR HOGENOM; CLU_017387_1_0_5; -.
DR OMA; YIYGSRE; -.
DR OrthoDB; 891360at2; -.
DR UniPathway; UPA00917; -.
DR Proteomes; UP000000270; 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; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR010963; PHA_synth_I.
DR InterPro; IPR010941; PhaC_N.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF07167; PhaC_N; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01838; PHA_synth_I; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; PHB biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..583
FT /note="Poly(3-hydroxyalkanoate) polymerase subunit PhaC"
FT /id="PRO_0000215469"
FT DOMAIN 300..508
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 560..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 320
FT /evidence="ECO:0000255"
SQ SEQUENCE 583 AA; 64740 MW; C205763D60DD1A18 CRC64;
MEAFAQNLAK MVEEGGKAVA AYMRPREEGK PDDMTDDIAD ALKTIGEVAN YWMSDPKRSF
EAQSRLMMGY MGVWAGALQK LSGEKAEPIA KADPKDGRFK DPEWESPFFD ALKQTYLVTS
NWAESMVKEA EGLDPHTKHK AEFLVRQLSN AVAPSNFLMT NPELIRETLS SSGENLVRGM
KNLAEDLVEG KGDLKIRQTD MSAFEVGRNL ALSPGKVIFE TELMQLIQYA PSTPSVKKTP
VLIVPPWINK FYILDLTPEK SLIKWMVDQG LTVFVISWVN PDARLADKGF DDYMRDGIFA
ALDAVEKATG EHQAHTIGYC VGGTLLAVTL AYMAATGDDR VASSTFLTTQ IDFTHAGDLK
VFVDEAQLSV IERRMKEMGY LEGRKMADAF NMLRSNDLIW PYVVNNYLKG KQPFPFDLLF
WNADSTRMPA ANHSYYLRNC YLQNNIAKGL AEIAGVKIDM GKVTIPVYSL ATREDHIAPP
NSAYIGAGLL GGPVRFVLAG SGHIAGVVNP PVKHKYQYWT GGPTGGDYDV WLKGAQEHKG
SWWPDWAQWF SALHPDEVPA REPGGSAFNP IEDAPGRYVR EKS
