BKTB_CUPNH
ID BKTB_CUPNH Reviewed; 394 AA.
AC Q0KBP1; O68275;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Beta-ketothiolase BktB;
DE EC=2.3.1.16;
DE EC=2.3.1.9;
DE AltName: Full=Acetyl-CoA acetyltransferase;
DE AltName: Full=Acetyl-CoA acyltransferase;
GN Name=bktB; OrderedLocusNames=H16_A1445;
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], PROTEIN SEQUENCE OF 1-16, FUNCTION,
RP CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=9555876; DOI=10.1128/jb.180.8.1979-1987.1998;
RA Slater S., Houmiel K.L., Tran M., Mitsky T.A., Taylor N.B., Padgette S.R.,
RA Gruys K.J.;
RT "Multiple beta-ketothiolases mediate poly(beta-hydroxyalkanoate) copolymer
RT synthesis in Ralstonia eutropha.";
RL J. Bacteriol. 180:1979-1987(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
CC -!- FUNCTION: Required for efficient production of poly(beta-
CC hydroxybutyrate-co-beta-hydroxyvalerate) (PHBV). Catalyzes the
CC condensation of acetyl-CoA and propionyl-CoA to form beta-ketovaleryl-
CC CoA, and the condensation of two acetyl-CoA molecules to form
CC acetoacetyl-CoA. {ECO:0000269|PubMed:9555876}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC Evidence={ECO:0000269|PubMed:9555876};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10020,
CC ECO:0000269|PubMed:9555876};
CC -!- DISRUPTION PHENOTYPE: Mutants are impaired in their ability to produce
CC PHBV when grown on propionate. {ECO:0000269|PubMed:9555876}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; AF026544; AAC38322.1; -; Genomic_DNA.
DR EMBL; AM260479; CAJ92580.1; -; Genomic_DNA.
DR RefSeq; WP_011615089.1; NZ_CP039287.1.
DR PDB; 4NZS; X-ray; 2.29 A; A/B=2-394.
DR PDB; 4W61; X-ray; 2.01 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-394.
DR PDBsum; 4NZS; -.
DR PDBsum; 4W61; -.
DR AlphaFoldDB; Q0KBP1; -.
DR SMR; Q0KBP1; -.
DR STRING; 381666.H16_A1445; -.
DR EnsemblBacteria; CAJ92580; CAJ92580; H16_A1445.
DR GeneID; 57643544; -.
DR KEGG; reh:H16_A1445; -.
DR PATRIC; fig|381666.6.peg.1834; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_4; -.
DR OMA; GIWEINE; -.
DR OrthoDB; 1058688at2; -.
DR BioCyc; MetaCyc:MON-16779; -.
DR BRENDA; 2.3.1.16; 231.
DR Proteomes; UP000008210; Chromosome 1.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Direct protein sequencing;
KW Reference proteome; Transferase.
FT CHAIN 1..394
FT /note="Beta-ketothiolase BktB"
FT /id="PRO_0000413033"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:4W61"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 27..42
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 110..120
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:4W61"
FT TURN 128..132
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4NZS"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:4W61"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 173..193
FT /evidence="ECO:0007829|PDB:4W61"
FT TURN 194..199
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 252..262
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 274..284
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 322..332
FT /evidence="ECO:0007829|PDB:4W61"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:4W61"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:4W61"
FT HELIX 352..369
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 373..381
FT /evidence="ECO:0007829|PDB:4W61"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:4W61"
FT STRAND 385..392
FT /evidence="ECO:0007829|PDB:4W61"
SQ SEQUENCE 394 AA; 40904 MW; 363248C8FB46C0E7 CRC64;
MTREVVVVSG VRTAIGTFGG SLKDVAPAEL GALVVREALA RAQVSGDDVG HVVFGNVIQT
EPRDMYLGRV AAVNGGVTIN APALTVNRLC GSGLQAIVSA AQTILLGDTD VAIGGGAESM
SRAPYLAPAA RWGARMGDAG LVDMMLGALH DPFHRIHMGV TAENVAKEYD ISRAQQDEAA
LESHRRASAA IKAGYFKDQI VPVVSKGRKG DVTFDTDEHV RHDATIDDMT KLRPVFVKEN
GTVTAGNASG LNDAAAAVVM MERAEAERRG LKPLARLVSY GHAGVDPKAM GIGPVPATKI
ALERAGLQVS DLDVIEANEA FAAQACAVTK ALGLDPAKVN PNGSGISLGH PIGATGALIT
VKALHELNRV QGRYALVTMC IGGGQGIAAI FERI
