ID I0QLF2_9GAMM Unreviewed; 395 AA.
AC I0QLF2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EIC82125.1};
GN ORFNames=SPM24T3_23467 {ECO:0000313|EMBL:EIC82125.1};
OS Serratia sp. M24T3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=932213 {ECO:0000313|EMBL:EIC82125.1, ECO:0000313|Proteomes:UP000011072};
RN [1] {ECO:0000313|EMBL:EIC82125.1, ECO:0000313|Proteomes:UP000011072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M24T3 {ECO:0000313|EMBL:EIC82125.1,
RC ECO:0000313|Proteomes:UP000011072};
RX PubMed=22740681; DOI=10.1128/JB.00670-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Serratia sp. Strain M24T3, Isolated from Pinewood
RT Disease Nematode Bursaphelenchus xylophilus.";
RL J. Bacteriol. 194:3764-3764(2012).
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:EIC82125.1}.
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DR EMBL; AJHJ01000056; EIC82125.1; -; Genomic_DNA.
DR AlphaFoldDB; I0QLF2; -.
DR STRING; 932213.SPM24T3_23467; -.
DR PATRIC; fig|932213.3.peg.4715; -.
DR eggNOG; COG0183; Bacteria.
DR Proteomes; UP000011072; Unassembled WGS sequence.
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; IPR020613; Thiolase_CS.
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; 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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EIC82125.1}.
FT DOMAIN 6..264
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 273..394
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 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 395 AA; 41844 MW; 9FA60BEC6AEDBBF1 CRC64;
MDNIEVVILD AARTAVGSFA GSLAGVPATE LGATVIKALL EKNNISPLEV DEVIIGQVLT
AGCGQNPARQ TLINSGIPES ASALTINKVC GSGLKSLQLA YQALKNGDAD LIIAGGQENM
SMAPHILPGS RNGKKMGDWT LQDTMVKDGL WEAFNNYHMG MTAENIIDKY HITRLEQDEF
ALSSQHKAAK ALETNRFASE IIPVEVTRPR KDPLIFKSDE FPRPQTTLEG LSALRPAFKK
EGSVTAGNAS GVNDGAAMVI LTTAKKAKEL GITPLARIVA FASAGVSPEL MGTGPIAASR
KVLEKSNWSI DDLDLIESNE AFAAQAISVN REMGWDTTKV NVNGGAISLG HPIGASGTRI
FVSLIHEMQR QDLKKGLATL CIGGGMGISV TIERD
//
