PHAC_RHIME
ID PHAC_RHIME Reviewed; 611 AA.
AC P50176; O87321;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 113.
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:7582015};
GN Synonyms=phbC {ECO:0000303|PubMed:9734305}; OrderedLocusNames=R01725;
GN ORFNames=SMc00296;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=41;
RX PubMed=7582015; DOI=10.1099/13500872-141-10-2553;
RA Tombolini R., Povolo S., Buson A., Squartini A., Nuti M.P.;
RT "Poly-beta-hydroxybutyrate (PHB) biosynthetic genes in Rhizobium meliloti
RT 41.";
RL Microbiology 141:2553-2559(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=9734305; DOI=10.1139/w98-033;
RA Willis L.B., Walker G.C.;
RT "The phbC (poly-beta-hydroxybutyrate synthase) gene of Rhizobium
RT (Sinorhizobium) meliloti and characterization of phbC mutants.";
RL Can. J. Microbiol. 44:554-564(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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 -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the PHA/PHB synthase family. Type I PhaC
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA90984.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U17227; AAA90984.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF031938; AAC61899.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC46304.1; -; Genomic_DNA.
DR RefSeq; NP_385831.1; NC_003047.1.
DR RefSeq; WP_010969425.1; NC_003047.1.
DR AlphaFoldDB; P50176; -.
DR SMR; P50176; -.
DR STRING; 266834.SMc00296; -.
DR ESTHER; rhime-phbc; PHA_synth_I.
DR EnsemblBacteria; CAC46304; CAC46304; SMc00296.
DR GeneID; 61603198; -.
DR KEGG; sme:SMc00296; -.
DR PATRIC; fig|266834.11.peg.3163; -.
DR eggNOG; COG3243; Bacteria.
DR HOGENOM; CLU_017387_1_0_5; -.
DR OMA; YIYGSRE; -.
DR UniPathway; UPA00917; -.
DR Proteomes; UP000001976; 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; 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 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; PHB biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..611
FT /note="Poly(3-hydroxyalkanoate) polymerase subunit PhaC"
FT /id="PRO_0000215472"
FT ACT_SITE 349
FT /evidence="ECO:0000255"
FT CONFLICT 111
FT /note="G -> A (in Ref. 1; AAA90984)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="R -> H (in Ref. 1; AAA90984)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="R -> K (in Ref. 1; AAA90984)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="K -> R (in Ref. 1; AAA90984)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="V -> M (in Ref. 1; AAA90984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 68040 MW; ABE8A9B17F87D7A9 CRC64;
MTAEKAEGAT GFAGFDPKSV EPYIVKDPES LAINMARAAE QLGKAASAWL APREAGEKTD
SFAEPVSDMV KTLSKVSEYW LSDPRRTLEA QTHLLGSFFD MWSRTLQRMA GDAVEDPANL
QRNDKRFADE DWVKNPFFDF IRQAYFVTSD WAERMVRDAE GLDDHTRHKA AFYVRQIASA
LSPTNFITTN PQLYRETVAS SGANLVKGMQ MLAEDIAAGR GELRLRQTDT SKFAIGENIA
ITPGKVIAQN DVCQVLQYEA STETVLKRPL LICPPWINKF YVLDLNPEKS FIKWAVDQGQ
TVFVISWVNP DERHASKDWE AYAREGIGFA LDIIEQATGE REVNSIGYCV GGTLLAATLA
LHAAEGDERI RSATLFTTQV DFTHAGDLKV FVDDDQIRHL EANMSATGYL EGSKMASAFN
MLRASELIWP YFVNNYLKGQ DPLPFDLLYW NSDSTRMPAA NHSFYLRNCY LENRLSKGEM
VLAGRRVSLG DVKIPIYNLA TKEDHIAPAK SVFLGSSSFG GKVTFVLSGS GHIAGVVNPP
ARSKYQYWTG GAPKGDIETW MGKAKETAGS WWPHWQGWVE RLDKRRVPAR KAGGPLNSIE
EAPGSYVRVR A
