PHAC_CUPNH
ID PHAC_CUPNH Reviewed; 589 AA.
AC P23608; Q0KBP9;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 126.
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 {ECO:0000303|PubMed:2670936};
DE Short=Poly-beta-hydroxybutyrate polymerase {ECO:0000303|PubMed:2670936};
DE AltName: Full=Polyhydroxyalkanoate synthase subunit PhaC;
DE Short=PHA synthase;
GN Name=phaC {ECO:0000303|PubMed:1476773};
GN Synonyms=phbC {ECO:0000303|PubMed:2670936}; OrderedLocusNames=H16_A1437;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION IN PHB
RP SYNTHESIS, SUBUNIT, AND PATHWAY.
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=2670936; DOI=10.1016/s0021-9258(19)84825-1;
RA Peoples O.P., Sinskey A.J.;
RT "Poly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16.
RT Identification and characterization of the PHB polymerase gene (phbC).";
RL J. Biol. Chem. 264:15298-15303(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND BIOTECHNOLOGY.
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-219.
RX PubMed=1987116; DOI=10.1128/jb.173.1.168-175.1991;
RA Schubert P., Krueger N., Steinbuechel A.;
RT "Molecular analysis of the Alcaligenes eutrophus poly(3-hydroxybutyrate)
RT biosynthetic operon: identification of the N-terminus of poly(3-
RT hydroxybutyrate) synthase and identification of the promoter.";
RL J. Bacteriol. 173:168-175(1991).
RN [4]
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 (R)-3-hydroxybutyryl-CoA to create
CC polyhydroxybutyrate (PHB) which consists of thousands of
CC hydroxybutyrate molecules linked end to end. PHB serves as an
CC intracellular energy reserve material when cells grow under conditions
CC of nutrient limitation. {ECO:0000269|PubMed:2670936}.
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. {ECO:0000269|PubMed:2670936}.
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:2670936}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- BIOTECHNOLOGY: Forms a biodegradable plastic that is degraded naturally
CC and completely by bacteria into carbon dioxide and water. Utilized in
CC the medical industry. Plates made from PHA-based plastics can be left
CC in place to help heal fractured bones. After the bone has healed, the
CC plastic slowly breaks down in the body. Utilized by Imperial Chemical
CC Industries (ICI) to produce a PHB-PHV (poly-B-valerate) copolymer sold
CC under the trade name 'Biopol'. Biopol is used as packaging material.
CC The PHB-PHV copolymer consists of approximately 20% PHV and 80% PHB. It
CC can be synthesized by incorporating glucose and valeric acid into the
CC medium. PHB-PHV is stronger and more flexible than regular PHB. Under
CC industrial conditions, 80% or higher of the cell dry weight of
CC A.eutrophus usually consists of the PHB-PHV copolymer.
CC {ECO:0000269|PubMed:16964242}.
CC -!- SIMILARITY: Belongs to the PHA/PHB synthase family. Type I PhaC
CC subfamily. {ECO:0000305}.
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DR EMBL; J05003; AAA21975.1; -; Genomic_DNA.
DR EMBL; AM260479; CAJ92572.1; -; Genomic_DNA.
DR EMBL; M64341; AAA21979.1; -; Genomic_DNA.
DR PIR; A34341; A34341.
DR RefSeq; WP_011615085.1; NZ_CP039287.1.
DR PDB; 5HZ2; X-ray; 1.80 A; A=202-589.
DR PDB; 5T6O; X-ray; 1.80 A; A=201-589.
DR PDBsum; 5HZ2; -.
DR PDBsum; 5T6O; -.
DR AlphaFoldDB; P23608; -.
DR SMR; P23608; -.
DR STRING; 381666.H16_A1437; -.
DR ESTHER; alceu-phbc; PHA_synth_I.
DR EnsemblBacteria; CAJ92572; CAJ92572; H16_A1437.
DR GeneID; 57643536; -.
DR KEGG; reh:H16_A1437; -.
DR PATRIC; fig|381666.6.peg.1826; -.
DR eggNOG; COG3243; Bacteria.
DR HOGENOM; CLU_017387_1_0_4; -.
DR OMA; YIYGSRE; -.
DR OrthoDB; 891360at2; -.
DR BioCyc; MetaCyc:MON-13090; -.
DR BRENDA; 2.3.1.304; 231.
DR UniPathway; UPA00917; -.
DR Proteomes; UP000008210; Chromosome 1.
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; IPR010963; PHA_synth_I.
DR InterPro; IPR010941; PhaC_N.
DR Pfam; PF07167; PhaC_N; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01838; PHA_synth_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; PHB biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..589
FT /note="Poly(3-hydroxyalkanoate) polymerase subunit PhaC"
FT /id="PRO_0000215468"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 319
FT /evidence="ECO:0000255"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 320..334
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:5HZ2"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 402..415
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 420..427
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 434..443
FT /evidence="ECO:0007829|PDB:5HZ2"
FT TURN 444..447
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:5T6O"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 485..489
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 490..493
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 499..506
FT /evidence="ECO:0007829|PDB:5HZ2"
FT TURN 508..512
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 533..538
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 541..545
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 548..558
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 567..570
FT /evidence="ECO:0007829|PDB:5HZ2"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:5HZ2"
FT HELIX 584..586
FT /evidence="ECO:0007829|PDB:5HZ2"
SQ SEQUENCE 589 AA; 64317 MW; A822F35CF70D8B68 CRC64;
MATGKGAAAS TQEGKSQPFK VTPGPFDPAT WLEWSRQWQG TEGNGHAAAS GIPGLDALAG
VKIAPAQLGD IQQRYMKDFS ALWQAMAEGK AEATGPLHDR RFAGDAWRTN LPYRFAAAFY
LLNARALTEL ADAVEADAKT RQRIRFAISQ WVDAMSPANF LATNPEAQRL LIESGGESLR
AGVRNMMEDL TRGKISQTDE SAFEVGRNVA VTEGAVVFEN EYFQLLQYKP LTDKVHARPL
LMVPPCINKY YILDLQPESS LVRHVVEQGH TVFLVSWRNP DASMAGSTWD DYIEHAAIRA
IEVARDISGQ DKINVLGFCV GGTIVSTALA VLAARGEHPA ASVTLLTTLL DFADTGILDV
FVDEGHVQLR EATLGGGAGA PCALLRGLEL ANTFSFLRPN DLVWNYVVDN YLKGNTPVPF
DLLFWNGDAT NLPGPWYCWY LRHTYLQNEL KVPGKLTVCG VPVDLASIDV PTYIYGSRED
HIVPWTAAYA STALLANKLR FVLGASGHIA GVINPPAKNK RSHWTNDALP ESPQQWLAGA
IEHHGSWWPD WTAWLAGQAG AKRAAPANYG NARYRAIEPA PGRYVKAKA
