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Acetyl-CoA acetyltransferase (EC 2.3.1.9) (Acetoacetyl-CoA thiolase) (Beta-ketothiolase)

 THIL_CUPNH              Reviewed;         393 AA.
P14611; Q0KBP8;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
18-JUL-2018, entry version 125.
RecName: Full=Acetyl-CoA acetyltransferase;
EC=2.3.1.9 {ECO:0000269|PubMed:4198758};
AltName: Full=Acetoacetyl-CoA thiolase;
AltName: Full=Beta-ketothiolase {ECO:0000303|PubMed:2670935};
Name=phaA {ECO:0000303|PubMed:1476773};
Synonyms=phbA {ECO:0000303|PubMed:2670935};
OrderedLocusNames=H16_A1438;
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
(Ralstonia eutropha).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Burkholderiaceae; Cupriavidus.
NCBI_TaxID=381666;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND FUNCTION.
STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337;
PubMed=2670935;
Peoples O.P., Sinskey A.J.;
"Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16.
Characterization of the genes encoding beta-ketothiolase and
acetoacetyl-CoA reductase.";
J. Biol. Chem. 264:15293-15297(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337;
PubMed=16964242; DOI=10.1038/nbt1244;
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H.,
Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E.,
Strittmatter A., Voss I., Gottschalk G., Steinbuechel A.,
Friedrich B., Bowien B.;
"Genome sequence of the bioplastic-producing 'Knallgas' bacterium
Ralstonia eutropha H16.";
Nat. Biotechnol. 24:1257-1262(2006).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24, FUNCTION IN PHB SYNTHESIS,
AND PATHWAY.
STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337;
PubMed=2670936;
Peoples O.P., Sinskey A.J.;
"Poly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus
H16. Identification and characterization of the PHB polymerase gene
(phbC).";
J. Biol. Chem. 264:15298-15303(1989).
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, SUBUNIT, AND PATHWAY.
STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337;
PubMed=4198758; DOI=10.1042/bj1340239;
Oeding V., Schlegel H.G.;
"Beta-ketothiolase from Hydrogenomonas eutropha H16 and its
significance in the regulation of poly-beta-hydroxybutyrate
metabolism.";
Biochem. J. 134:239-248(1973).
[5]
GENE NAME.
PubMed=1476773; DOI=10.1111/j.1574-6968.1992.tb05841.x;
Steinbuechel A., Hustede E., Liebergesell M., Pieper U., Timm A.,
Valentin H.;
"Molecular basis for biosynthesis and accumulation of
polyhydroxyalkanoic acids in bacteria.";
FEMS Microbiol. Rev. 9:217-230(1992).
[6] {ECO:0000244|PDB:4O99, ECO:0000244|PDB:4O9A, ECO:0000244|PDB:4O9C}
X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 2-393 APOPROTEIN AND IN
COMPLEX WITH COA, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT,
AND MUTAGENESIS OF CYS-88; HIS-156; PHE-219; SER-248; HIS-349 AND
CYS-379.
PubMed=25152395; DOI=10.1016/j.bbrc.2014.08.074;
Kim E.J., Kim K.J.;
"Crystal structure and biochemical characterization of PhaA from
Ralstonia eutropha, a polyhydroxyalkanoate-producing bacterium.";
Biochem. Biophys. Res. Commun. 452:124-129(2014).
-!- FUNCTION: Catalyzes the condensation of two acetyl-coA units to
form acetoacetyl-CoA (PubMed:4198758). Is involved in the
biosynthesis of polyhydroxybutyrate (PHB), which is accumulated as
an intracellular energy reserve material when cells grow under
conditions of nutrient limitation (PubMed:2670936,
PubMed:4198758). Also catalyzes the reverse reaction, i.e. the
cleavage of acetoacetyl-CoA, and is therefore also involved in the
reutilization of PHB (PubMed:4198758, PubMed:25152395).
{ECO:0000269|PubMed:25152395, ECO:0000269|PubMed:2670935,
ECO:0000269|PubMed:2670936, ECO:0000269|PubMed:4198758}.
-!- CATALYTIC ACTIVITY: 2 acetyl-CoA = CoA + acetoacetyl-CoA.
{ECO:0000255|PROSITE-ProRule:PRU10020,
ECO:0000269|PubMed:25152395, ECO:0000269|PubMed:4198758}.
-!- ENZYME REGULATION: The condensation reaction is inhibited by free
CoA. The cleavage reaction is characterized by substrate
inhibition by acetoacetyl-CoA, which is partially relieved by free
CoA. {ECO:0000269|PubMed:4198758}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=390 uM for acetyl-CoA {ECO:0000269|PubMed:4198758};
pH dependence:
Optimum pH is 7.8 for the condensation reaction and 8.1 for the
reverse cleavage reaction. {ECO:0000269|PubMed:4198758};
-!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
biosynthesis. {ECO:0000269|PubMed:2670936,
ECO:0000269|PubMed:4198758}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:25152395,
ECO:0000269|PubMed:4198758}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the thiolase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J04987; AAA21972.1; -; Genomic_DNA.
EMBL; AM260479; CAJ92573.1; -; Genomic_DNA.
EMBL; J05003; AAA21976.1; -; Genomic_DNA.
PIR; A34340; XXALAE.
RefSeq; WP_010810132.1; NC_008313.1.
PDB; 4O99; X-ray; 1.96 A; A/B/C/D=2-393.
PDB; 4O9A; X-ray; 1.52 A; A/B/C/D=2-393.
PDB; 4O9C; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-393.
PDBsum; 4O99; -.
PDBsum; 4O9A; -.
PDBsum; 4O9C; -.
ProteinModelPortal; P14611; -.
SMR; P14611; -.
STRING; 381666.H16_A1438; -.
EnsemblBacteria; CAJ92573; CAJ92573; H16_A1438.
KEGG; reh:H16_A1438; -.
eggNOG; ENOG4105CHU; Bacteria.
eggNOG; COG0183; LUCA.
HOGENOM; HOG000012238; -.
KO; K00626; -.
OMA; ICPSIAI; -.
BioCyc; MetaCyc:MONOMER-13086; -.
UniPathway; UPA00917; -.
Proteomes; UP000008210; Chromosome 1.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:UniProtKB-KW.
CDD; cd00751; thiolase; 1.
Gene3D; 3.40.47.10; -; 4.
InterPro; IPR002155; Thiolase.
InterPro; IPR016039; Thiolase-like.
InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
InterPro; IPR020610; Thiolase_AS.
InterPro; IPR020617; Thiolase_C.
InterPro; IPR020613; Thiolase_CS.
InterPro; IPR020616; Thiolase_N.
Pfam; PF02803; Thiolase_C; 1.
Pfam; PF00108; Thiolase_N; 1.
PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
SUPFAM; SSF53901; SSF53901; 2.
TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
PROSITE; PS00098; THIOLASE_1; 1.
PROSITE; PS00737; THIOLASE_2; 1.
PROSITE; PS00099; THIOLASE_3; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Complete proteome; Cytoplasm;
PHB biosynthesis; Reference proteome; Transferase.
CHAIN 1 393 Acetyl-CoA acetyltransferase.
/FTId=PRO_0000206418.
ACT_SITE 88 88 Acyl-thioester intermediate.
{ECO:0000269|PubMed:25152395}.
ACT_SITE 349 349 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10020,
ECO:0000305|PubMed:25152395}.
ACT_SITE 379 379 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10020,
ECO:0000305|PubMed:25152395}.
MUTAGEN 88 88 C->S: Almost complete loss of
acetoacetyl-CoA thiolase activity.
{ECO:0000269|PubMed:25152395}.
MUTAGEN 156 156 H->A: Almost complete loss of
acetoacetyl-CoA thiolase activity.
{ECO:0000269|PubMed:25152395}.
MUTAGEN 219 219 F->A: About 50% loss of acetoacetyl-CoA
thiolase activity.
{ECO:0000269|PubMed:25152395}.
MUTAGEN 219 219 F->Y: 2-fold increase of acetoacetyl-CoA
thiolase activity.
{ECO:0000269|PubMed:25152395}.
MUTAGEN 221 221 R->A: Almost complete loss of
acetoacetyl-CoA thiolase activity.
{ECO:0000269|PubMed:25152395}.
MUTAGEN 248 248 S->A: About 40% loss of acetoacetyl-CoA
thiolase activity.
{ECO:0000269|PubMed:25152395}.
MUTAGEN 349 349 H->A: Almost complete loss of
acetoacetyl-CoA thiolase activity.
{ECO:0000269|PubMed:25152395}.
MUTAGEN 379 379 C->S: Almost complete loss of
acetoacetyl-CoA thiolase activity.
{ECO:0000269|PubMed:25152395}.
STRAND 4 12 {ECO:0000244|PDB:4O9A}.
TURN 20 23 {ECO:0000244|PDB:4O9A}.
HELIX 26 41 {ECO:0000244|PDB:4O9A}.
HELIX 45 47 {ECO:0000244|PDB:4O9A}.
STRAND 50 54 {ECO:0000244|PDB:4O9A}.
HELIX 65 72 {ECO:0000244|PDB:4O9A}.
STRAND 81 85 {ECO:0000244|PDB:4O9A}.
HELIX 87 89 {ECO:0000244|PDB:4O9A}.
HELIX 90 103 {ECO:0000244|PDB:4O9A}.
STRAND 108 118 {ECO:0000244|PDB:4O9A}.
STRAND 123 125 {ECO:0000244|PDB:4O9A}.
TURN 126 130 {ECO:0000244|PDB:4O9A}.
STRAND 133 135 {ECO:0000244|PDB:4O9C}.
STRAND 137 141 {ECO:0000244|PDB:4O9A}.
HELIX 142 147 {ECO:0000244|PDB:4O9A}.
TURN 151 154 {ECO:0000244|PDB:4O9A}.
HELIX 157 168 {ECO:0000244|PDB:4O9A}.
HELIX 172 191 {ECO:0000244|PDB:4O9A}.
TURN 192 198 {ECO:0000244|PDB:4O9A}.
STRAND 202 204 {ECO:0000244|PDB:4O9A}.
STRAND 207 210 {ECO:0000244|PDB:4O9A}.
STRAND 212 214 {ECO:0000244|PDB:4O9A}.
HELIX 226 230 {ECO:0000244|PDB:4O9A}.
HELIX 244 246 {ECO:0000244|PDB:4O99}.
STRAND 251 261 {ECO:0000244|PDB:4O9A}.
HELIX 262 268 {ECO:0000244|PDB:4O9A}.
STRAND 273 283 {ECO:0000244|PDB:4O9A}.
HELIX 286 291 {ECO:0000244|PDB:4O9A}.
HELIX 293 304 {ECO:0000244|PDB:4O9A}.
HELIX 308 310 {ECO:0000244|PDB:4O9A}.
STRAND 312 316 {ECO:0000244|PDB:4O9A}.
HELIX 321 331 {ECO:0000244|PDB:4O9A}.
HELIX 335 337 {ECO:0000244|PDB:4O9A}.
HELIX 344 347 {ECO:0000244|PDB:4O9A}.
TURN 351 353 {ECO:0000244|PDB:4O9A}.
HELIX 354 369 {ECO:0000244|PDB:4O9A}.
STRAND 373 380 {ECO:0000244|PDB:4O9A}.
TURN 381 383 {ECO:0000244|PDB:4O9A}.
STRAND 384 391 {ECO:0000244|PDB:4O9A}.
SEQUENCE 393 AA; 40549 MW; 232C1127E20B3961 CRC64;
MTDVVIVSAA RTAVGKFGGS LAKIPAPELG AVVIKAALER AGVKPEQVSE VIMGQVLTAG
SGQNPARQAA IKAGLPAMVP AMTINKVCGS GLKAVMLAAN AIMAGDAEIV VAGGQENMSA
APHVLPGSRD GFRMGDAKLV DTMIVDGLWD VYNQYHMGIT AENVAKEYGI TREAQDEFAV
GSQNKAEAAQ KAGKFDEEIV PVLIPQRKGD PVAFKTDEFV RQGATLDSMS GLKPAFDKAG
TVTAANASGL NDGAAAVVVM SAAKAKELGL TPLATIKSYA NAGVDPKVMG MGPVPASKRA
LSRAEWTPQD LDLMEINEAF AAQALAVHQQ MGWDTSKVNV NGGAIAIGHP IGASGCRILV
TLLHEMKRRD AKKGLASLCI GGGMGVALAV ERK


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