ID A0A0T5NYY9_9RHOB Unreviewed; 390 AA.
AC A0A0T5NYY9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KRS14100.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KRS14100.1};
GN ORFNames=XM53_04905 {ECO:0000313|EMBL:KRS14100.1};
OS Roseovarius atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1641875 {ECO:0000313|EMBL:KRS14100.1, ECO:0000313|Proteomes:UP000051295};
RN [1] {ECO:0000313|EMBL:KRS14100.1, ECO:0000313|Proteomes:UP000051295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R12B {ECO:0000313|EMBL:KRS14100.1,
RC ECO:0000313|Proteomes:UP000051295};
RA Li G., Lai Q., Shao Z., Yan P.;
RT "The draft genome sequence of Roseovarius sp.R12b.";
RL Submitted (APR-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:KRS14100.1}.
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DR EMBL; LAXJ01000003; KRS14100.1; -; Genomic_DNA.
DR RefSeq; WP_057790865.1; NZ_LAXJ01000003.1.
DR AlphaFoldDB; A0A0T5NYY9; -.
DR STRING; 1641875.XM53_04905; -.
DR PATRIC; fig|1641875.4.peg.2999; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000051295; 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; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919:SF138; ACETYL-COA C-ACETYLTRANSFERASE; 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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:KRS14100.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KRS14100.1}.
FT DOMAIN 4..259
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 268..389
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 86
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 390 AA; 40345 MW; F429AA2378DCA38C CRC64;
MKDVVIAGAA RTPMGGFQGD FDGVEASILG GAAIAAALKD AGATTVGELL MGCVLPAGQG
QAPARQAGFK AGLGEDVPAT TLNKMCGSGM KAAMIGFDQI ALGHTDTMVT GGMESMSNAP
YLLPKMRGGA RIGHGQVIDH MFLDGLEDAY DKGRLMGTFA EDCAEKYQFT REAQDAYAIG
SLEGALEAQK SGAFAGEIAP VTLETRKGTV VVETDEQPGK ARPEKIPQLK PAFREGGTVT
AANSSSISDG AAALVLASHE AAEAQGLKVR ARILGHASHA QAPGWFTTAP VPAAQKLLER
IGWDKDDVDL WEVNEAFAVV PMAFMHEMGL PREKVNVHGG ACALGHPIGA SGARIMVTLL
NALEKRDLKR GVAAICIGGG EGTAIAIERV
//
