ID A0A0C1JD00_9RHOB Unreviewed; 391 AA.
AC A0A0C1JD00;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KIC46325.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KIC46325.1};
GN ORFNames=RA28_00490 {ECO:0000313|EMBL:KIC46325.1};
OS Ruegeria sp. ANG-S4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1577904 {ECO:0000313|EMBL:KIC46325.1, ECO:0000313|Proteomes:UP000031326};
RN [1] {ECO:0000313|Proteomes:UP000031326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S4 {ECO:0000313|Proteomes:UP000031326};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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:KIC46325.1}.
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DR EMBL; JWLK01000001; KIC46325.1; -; Genomic_DNA.
DR RefSeq; WP_039522508.1; NZ_JWLK01000001.1.
DR AlphaFoldDB; A0A0C1JD00; -.
DR STRING; 1577904.RA28_00490; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000031326; 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; 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 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|RuleBase:RU003557,
KW ECO:0000313|EMBL:KIC46325.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031326};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KIC46325.1}.
FT DOMAIN 4..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 268..390
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 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 391 AA; 40179 MW; 4E19CF67FC79B9BB CRC64;
MSEIVILDGA RTAIGTFGGA LASTAPIDLA TVATEAALER SGVEGAQIGH VVFGHVINTE
PRDMYLSRVA AMQAGIPNGT PAMNVNRLCG SGAQAIVSAV QSLMLGDADF AVAGGAESMS
RSPYIVPQAR WGAKMGDVTS LDMMLGALNC PFGTGHMGVT AENVADEHQI SREQMDGFAM
ASQTRAAAAI ESGFFDSQIT PVQIKVKREM VDFKVDEHPK ATTTEALAGL RPVFKKDGRV
TAGNASGIND GAAAMVLATA DAAEKAGLKP KARILGYAHA GVRPEVMGIG PVPVVRNLMD
RTGLAVSDFD VIESNEAFAA QALAVNQELG LDASKVNPNG GAIALGHPVG ATGAIITLKA
LYELERTGGT KGLITMCIGG GQGIAIAIER L
//
