ID A1VKD8_POLNA Unreviewed; 416 AA.
AC A1VKD8;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ABM36116.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:ABM36116.1};
GN OrderedLocusNames=Pnap_0797 {ECO:0000313|EMBL:ABM36116.1};
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM36116.1, ECO:0000313|Proteomes:UP000000644};
RN [1] {ECO:0000313|Proteomes:UP000000644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644};
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(2009).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP000529; ABM36116.1; -; Genomic_DNA.
DR RefSeq; WP_011800211.1; NC_008781.1.
DR AlphaFoldDB; A1VKD8; -.
DR STRING; 365044.Pnap_0797; -.
DR KEGG; pna:Pnap_0797; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_4; -.
DR OrthoDB; 6139495at2; -.
DR Proteomes; UP000000644; Chromosome.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
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:ABM36116.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000644};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ABM36116.1}.
FT DOMAIN 16..281
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 291..411
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 98
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 369
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 399
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 416 AA; 43310 MW; 35C4242A0B7E38B2 CRC64;
MAHTGFFNAF DDIWMLAGVR TPMVDYCGAL GHISPTDLGI KVAREVLARA GVPGAHIGSV
IAGNMAPGDF DQFFLPRHIG LYAGVPVDVP ALMAQRICGT GFELFRQAGE QIQGGACEAA
LVVGTESMTR NPIAAFDHRT GFKLGAPVGF KDYMWEALKD PAAGINMIQT AENLAKKYGI
QREEVDEFAS SSFARAVAAQ QSGFHAGEIV PIVTEKFELE GYKPRGIRLQ GKTTEVALDT
HARLSPADVL ARLKPVYEGG VQTGGNSAAL VDAAAAAVVS SGAYARAQGK TPLARVVASA
VVGVPPEIMG IGPAPAIQLL LARTGLSLAQ IGRFEINEAQ GAQTLAVGRE LGLDLSRLNV
NGGAIALGHP LAATGVRLTI TLAREMKRAG VRWGIASACI GGGQGIALLL ENPEAA
//
