ID A0A0G9MQH5_9SPHN Unreviewed; 398 AA.
AC A0A0G9MQH5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:APE28845.1, ECO:0000313|EMBL:KLE32986.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KLE32986.1};
GN ORFNames=AAW01_02975 {ECO:0000313|EMBL:KLE32986.1}, BMF35_a2016
GN {ECO:0000313|EMBL:APE28845.1};
OS Aurantiacibacter gangjinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=502682 {ECO:0000313|EMBL:KLE32986.1, ECO:0000313|Proteomes:UP000053070};
RN [1] {ECO:0000313|EMBL:KLE32986.1, ECO:0000313|Proteomes:UP000053070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K7-2 {ECO:0000313|EMBL:KLE32986.1,
RC ECO:0000313|Proteomes:UP000053070};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacr gangjinensis K7-2.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:APE28845.1, ECO:0000313|Proteomes:UP000183202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC1.15024 {ECO:0000313|EMBL:APE28845.1,
RC ECO:0000313|Proteomes:UP000183202};
RA Xu L., Wu Y.-H., Cheng H., Zhou Y.-G., Wu M., Cheng L., Xu X.-W.;
RT "Complete genome sequence of two-chromosomal Erythrobacter gangjinensis
RT CGMCC 1.15024T, isolated from seawater.";
RL Submitted (NOV-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; CP018097; APE28845.1; -; Genomic_DNA.
DR EMBL; LBHC01000001; KLE32986.1; -; Genomic_DNA.
DR RefSeq; WP_047005836.1; NZ_LBHC01000001.1.
DR AlphaFoldDB; A0A0G9MQH5; -.
DR STRING; 502682.BMF35_a2016; -.
DR KEGG; egn:BMF35_a2016; -.
DR PATRIC; fig|502682.8.peg.606; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000053070; Unassembled WGS sequence.
DR Proteomes; UP000183202; Chromosome i.
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; 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:SF144; ACYL-COA THIOLASE-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; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:KLE32986.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053070};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KLE32986.1}.
FT DOMAIN 10..267
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 276..396
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 94
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 354
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 398 AA; 41120 MW; 8E3A9E77F39BD74C CRC64;
MATFNESDPI VILSYARTPM GAMQGALADV AATDLGATAA KAAIERAGVS GDDVNRVYMG
CVLPAGLGQA PARQVAILAG LPKSAQATTV NKVCGSGMQT VIMGAESLAS GTSDVVLAGG
MESMTNAPYL LKKHRSGARI GHDKAYDHMF LDGLEDAYEE GRAMGTFAQD MADKYQLTRE
SMDEYSIASL DRANKAIESG AFADEVVPVT YTTRRGDVTV DTDEAPGKGN PDKIPQLRPA
FAKDGTITAA TSSSISDGAA AVVLSRKSVA DEKGLTPVAT VVGMTAHAQA PEEFTIAPVG
AIQKLLEQTG WSVDDVDLWE VNEAFACVAM FAMKDIGIDH AKINVNGGGT ALGHPIGASG
TRIIVTLLNA LKQQGKKRGI ASLCIGGGEA TAVAVELA
//