ID A0A193G7X8_9BORD Unreviewed; 394 AA.
AC A0A193G7X8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ANN76092.1};
GN ORFNames=BAU07_02215 {ECO:0000313|EMBL:ANN76092.1};
OS Bordetella flabilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463014 {ECO:0000313|EMBL:ANN76092.1, ECO:0000313|Proteomes:UP000091926};
RN [1] {ECO:0000313|EMBL:ANN76092.1, ECO:0000313|Proteomes:UP000091926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU10664 {ECO:0000313|EMBL:ANN76092.1,
RC ECO:0000313|Proteomes:UP000091926};
RA LiPuma J.J., Spilker T.;
RT "Complete genome sequences of Bordetella bronchialis and Bordetella
RT flabilis.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP016172; ANN76092.1; -; Genomic_DNA.
DR RefSeq; WP_066653492.1; NZ_CP016172.1.
DR AlphaFoldDB; A0A193G7X8; -.
DR STRING; 463014.BAU07_02215; -.
DR KEGG; bfz:BAU07_02215; -.
DR OrthoDB; 6139495at2; -.
DR Proteomes; UP000091926; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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 NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ANN76092.1}.
FT DOMAIN 5..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..393
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 40886 MW; 7DBF8BF88D6773DA CRC64;
MGKEVYVVSA VRTAIGRFGG GLKTVPPAEL ATTVVREAVR RAGVVPDSVG HISMGTVITT
DPRDIYMSRI AALDAGLPQE ISAFNVNRLC GSGLQAIVSS AQSILLGDCD VAVGAGSESM
SRAGYLVQSA RWGARMGDSA MLDLMLNALH DPFHQVHMGI TAENVAERFG ITRRMMDELA
VTSHQRAAAA IAAGRFKDQI VPVPVATRQG VVHFDTDEHV KPDTTLEVLA AMKPAFKKEG
GTVTAGNASG VNDGAAAVVL VSAEAAKIQN LKPVARLVGY ACAGVEPAIM GTGPIPATRR
LLARVGLKVA DLDVIESNEA FAAQACAVSR ELGFDPGRVN PNGSGISLGH PIGATGAIIT
TKALHELHRI GGRYALVTMC IGGGQGIAAI FERV
//
