ID A0A0W0VE21_9GAMM Unreviewed; 424 AA.
AC A0A0W0VE21;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KTD18388.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KTD18388.1};
GN ORFNames=Ljor_2694 {ECO:0000313|EMBL:KTD18388.1};
OS Legionella jordanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=456 {ECO:0000313|EMBL:KTD18388.1, ECO:0000313|Proteomes:UP000055035};
RN [1] {ECO:0000313|EMBL:KTD18388.1, ECO:0000313|Proteomes:UP000055035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL-540 {ECO:0000313|EMBL:KTD18388.1,
RC ECO:0000313|Proteomes:UP000055035};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTD18388.1}.
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DR EMBL; LNYJ01000011; KTD18388.1; -; Genomic_DNA.
DR RefSeq; WP_058472052.1; NZ_RDQQ01000005.1.
DR AlphaFoldDB; A0A0W0VE21; -.
DR STRING; 456.Ljor_2694; -.
DR PATRIC; fig|456.5.peg.2887; -.
DR OrthoDB; 1402717at2; -.
DR Proteomes; UP000055035; Unassembled WGS sequence.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000055035};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KTD18388.1}.
FT DOMAIN 6..274
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 282..422
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 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 410
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 424 AA; 46545 MW; 82FC756C7D23BDD6 CRC64;
MKTRPVYIAG GIRTPFVKSM TRYQSISTQD LLIASLQALV DKMQLAGKIV GDVGLGAVIN
SPFNWNLARE AVLGSKLNPH TPAYTLQRAC GTSLETTLQI ALKIANFQME DGIAGGVDTN
SDVPVMFPNN FTQKLLRTKQ SKGVLEKFKT LLSFRFKDFK PEFPAVVEPR TGLSMGEHTE
KMVKDWNISR KDQDELALHS HQKAWRAYEE GFYDDLVFDY LGLKRDTILR PDTNIEQLAK
LKPAFDRSGK GTLTAGNSTP LTDGSAAVYL VSEDKANQFH LPILARFVDA QVAAVDFVHG
EGLLMAPTIA VSQLLQRNQL SLQDFDFYEI HEAFAGQVLC TLKAWESEEY CKRVLHLDHP
LGQIDRQKMN IKGGSLALGH PFAATGARIV SSLAKVLHQA GKGRGLISIC TAGGMGVAAI
LEAV
//
