ID A0A0A1YGB1_9PSED Unreviewed; 393 AA.
AC A0A0A1YGB1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KFX68952.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KFX68952.1};
GN ORFNames=TMS3_0115825 {ECO:0000313|EMBL:KFX68952.1};
OS Pseudomonas taeanensis MS-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1395571 {ECO:0000313|EMBL:KFX68952.1, ECO:0000313|Proteomes:UP000030063};
RN [1] {ECO:0000313|EMBL:KFX68952.1, ECO:0000313|Proteomes:UP000030063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS-3 {ECO:0000313|EMBL:KFX68952.1,
RC ECO:0000313|Proteomes:UP000030063};
RX PubMed=24407626;
RA Lee S.Y., Kim S.H., Lee D.G., Shin S., Yun S.H., Choi C.W., Chung Y.H.,
RA Choi J.S., Kahng H.Y., Kim S.I.;
RT "Draft Genome Sequence of Petroleum Oil-Degrading Marine Bacterium
RT Pseudomonas taeanensis Strain MS-3, Isolated from a Crude Oil-Contaminated
RT Seashore.";
RL Genome Announc. 2:0-0(2014).
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:KFX68952.1}.
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DR EMBL; AWSQ01000004; KFX68952.1; -; Genomic_DNA.
DR RefSeq; WP_025166182.1; NZ_AWSQ01000004.1.
DR AlphaFoldDB; A0A0A1YGB1; -.
DR STRING; 1395571.TMS3_0115825; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000030063; 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:UP000030063};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KFX68952.1}.
FT DOMAIN 4..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..392
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 393 AA; 40369 MW; 963C5E05D4A0C222 CRC64;
MQEVVIVAAT RTAIGSFQGA LAGIPATELG AAVIRQLLAQ TDLNGAEVDE VILGHVLTAG
AGQNTARQAA IKAGLPHAVP ALTLNKVCGS GLKALHLGAQ AIRCGDAEVI IAGGMENMSL
APYVMPKART GLRMGHSQLI DSMITDGLWD AFNDYHMGIT AENLVDKYAI TREAQDAFAA
ASQQKACAAI EAGRFVEEIT PLLIAQRKGE PLAFATDEQP RAGTSAESLG KLKPAFKKDG
SVTAGNASSL NDGAAAVLLM SASKAQALGL PVLARIAGYA NAGVDPAIMG IGPVSATRRC
LEKAEWSLEQ LDLIEANEAF AAQALAVGQE LGWDASKVNV NGGAIALGHP IGASGCRVLV
TLLHEMIKRD AKKGLATLCI GGGQGVAMAI ERA
//
