ID F9UGF3_9GAMM Unreviewed; 394 AA.
AC F9UGF3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EGV16636.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:EGV16636.1};
GN ORFNames=ThimaDRAFT_4006 {ECO:0000313|EMBL:EGV16636.1};
OS Thiocapsa marina 5811.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV16636.1, ECO:0000313|Proteomes:UP000005459};
RN [1] {ECO:0000313|EMBL:EGV16636.1, ECO:0000313|Proteomes:UP000005459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5811 {ECO:0000313|EMBL:EGV16636.1,
RC ECO:0000313|Proteomes:UP000005459};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., Frigaard N.-U.,
RA Bryant D., Woyke T.J.;
RT "The draft genome of Thiocapsa marina 5811.";
RL Submitted (JUN-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFWV01000015; EGV16636.1; -; Genomic_DNA.
DR RefSeq; WP_007194878.1; NZ_AFWV01000015.1.
DR AlphaFoldDB; F9UGF3; -.
DR STRING; 768671.ThimaDRAFT_4006; -.
DR PATRIC; fig|768671.3.peg.4230; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 1402717at2; -.
DR Proteomes; UP000005459; 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; -; 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 Reference proteome {ECO:0000313|Proteomes:UP000005459};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EGV16636.1}.
FT DOMAIN 5..264
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 89
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; 40836 MW; 94B19FC5C6668261 CRC64;
MSDNIVIVDA GRTAVGTFGG SLSSLPATDI GAAVLKALME RTGISPDQVD EVILGQVLTA
GVGQNPARQT TLNAGLPHSV PAMTINKVCG SGLKAVHLAM QAVACGDADI VIAGGQESMS
QSAHVLPRSR EGQRMGDWSM KDTMIVDGLW DAFNQYHMGV TAENIAKKYA FTRDAQDAFA
AASQQKAEAA IKSGRFADEI VPVSIPQRKG DPVVFATDEF PRPGTTAETL GKLRPAFDKA
GTVTAGNASG INDGAAMVVV MKESKAKELG LKPMARLVAF ASAGVDPAIM GTGPIPASTK
CLEKAGWTPK DLDLIEANEA FAAQAMSVNH EMGWDLSKVN VNGGAISIGH PIGASGARVL
VTLLYEMQKR DAKKGLATLC IGGGQGVALA VERV
//
