ID C8RWR9_9RHOB Unreviewed; 391 AA.
AC C8RWR9;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EEW27012.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:EEW27012.1};
GN ORFNames=Rsw2DRAFT_0247 {ECO:0000313|EMBL:EEW27012.1};
OS Rhodobacter sp. SW2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=371731 {ECO:0000313|EMBL:EEW27012.1, ECO:0000313|Proteomes:UP000010121};
RN [1] {ECO:0000313|EMBL:EEW27012.1, ECO:0000313|Proteomes:UP000010121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SW2 {ECO:0000313|EMBL:EEW27012.1,
RC ECO:0000313|Proteomes:UP000010121};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Emerson D.;
RT "The draft genome of Rhodobacter sp. SW2.";
RL Submitted (AUG-2009) 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:EEW27012.1}.
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DR EMBL; ACYY01000001; EEW27012.1; -; Genomic_DNA.
DR RefSeq; WP_008027225.1; NZ_ACYY01000001.1.
DR AlphaFoldDB; C8RWR9; -.
DR STRING; 371731.Rsw2DRAFT_0247; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000010121; 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:SF164; ACETYL-COA 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; 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|RuleBase:RU003557,
KW ECO:0000313|EMBL:EEW27012.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010121};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EEW27012.1}.
FT DOMAIN 4..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..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; 39381 MW; 25F3451D8331BA88 CRC64;
MNDIVILSGM RTAIGSFGGA LAAVAPVDLA TVVARAAIDR AGLDAARIGS VVFGHVINTE
PRDMYLSRVA AMQAGIPETV PSMNVNRLCG SGVQAVVSAI QALLLGDADF ALAGGAESMS
RAPYLLPAAR FGVKMGDTRA IDMMTGALSC PFGSGHMGIT AENVAVECGI SREAQDAFAL
ESQNRAAMAI AEGRFASQIV PVEVKTRQGP ALFAQDEYPK ATTLAALAAL RPAFSKTGSV
TAGNASGIND GAAALVLARA SAAQAAGLQP LARVLGYAHA GVRPEVMGLG PVPAVQALLA
RTGLAIADFD LIESNEAFAA QALAVSAALG FDPAKVNPNG GAIALGHPVG ASGAIITVKA
LHELARTGSK RALITLCIGG GQGIALAIER L
//
