ID A3SQD6_ROSNI Unreviewed; 355 AA.
AC A3SQD6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EAP75345.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:EAP75345.1};
GN ORFNames=ISM_09491 {ECO:0000313|EMBL:EAP75345.1};
OS Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=89187 {ECO:0000313|EMBL:EAP75345.1, ECO:0000313|Proteomes:UP000005954};
RN [1] {ECO:0000313|EMBL:EAP75345.1, ECO:0000313|Proteomes:UP000005954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-591 / DSM 15170 / ISM
RC {ECO:0000313|Proteomes:UP000005954};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-2005) 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:EAP75345.1}.
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DR EMBL; AALY01000003; EAP75345.1; -; Genomic_DNA.
DR AlphaFoldDB; A3SQD6; -.
DR STRING; 89187.ISM_09491; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_5; -.
DR Proteomes; UP000005954; 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|RuleBase:RU003557,
KW ECO:0000313|EMBL:EAP75345.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005954};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EAP75345.1}.
FT DOMAIN 3..224
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 233..354
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 52
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 311
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 341
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 355 AA; 37276 MW; 931660890115E67D CRC64;
MCERAGVDKG DVSETILGQV LTAGQGQNPA RQAHVNAGLP IESAAWGINQ VCGSGLRAVA
LGAQHIMLGD AKIVAAGGQE NMTLSPHVAH LRAGHKMGDV KYIDSMIRDG LWDAFNGYHM
GQTAENVAEK WQISREQQDE FALASQNKAE AAQKAGKFDD EIVPFTVSTR KGDIVVDKDE
YIRHGATLEA MQKMRPAFTK DGSVTAANAS GLNDGAAATL LMSAEEAEKR GITPLARIVS
YATAGLDPAI MGVGPVNASR KALEKAGWKA SDLDLVEANE AFAAQACAVN KEMGWDPEVV
NVNGGAIAIG HPIGASGCRV LNTLLFEMQR RDAKKGLATL CIGGGMGVAL CVERG
//
