ID A2SL81_METPP Unreviewed; 394 AA.
AC A2SL81;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:ABM96320.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:ABM96320.1};
GN OrderedLocusNames=Mpe_A3367 {ECO:0000313|EMBL:ABM96320.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM96320.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM96320.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM96320.1; -; Genomic_DNA.
DR RefSeq; WP_011830941.1; NC_008825.1.
DR AlphaFoldDB; A2SL81; -.
DR STRING; 420662.Mpe_A3367; -.
DR KEGG; mpt:Mpe_A3367; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_1_4; -.
DR BioCyc; MetaCyc:MONOMER-19852; -.
DR Proteomes; UP000000366; Chromosome.
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; 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; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:ABM96320.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ABM96320.1}.
FT DOMAIN 7..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 272..392
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 40673 MW; BCF1D46A8F783F4C CRC64;
MSTDDPVVIV SAARTPIGGL LGDLAALAAW ELGAVAIRAA VERAGVPGDA VDEVLMGNCL
MAGQGQAPAR QAARKAGLPD SAGAVTLSKM CGSGMRALMF GHDMLAAGSA EVVVAGGMES
MTNAPHLSFV RKGLKYGAAV LYDHMALDGL EDAYERGKSM GVFAEQCVSY YSFRREAMDA
FAVASTQRAI AAHNDGSFDW EIAPVTLAGR AGDVTVDRDE QPFKAKLDKI TALKPAFGKD
GTITAATSSS ISDGAAALVL MRASTARARG LAPIAVLRAH AVHAQAPAWF STAPAGAIRK
VLQKTGWSVR DVDLWEINEA FAAVTMAAMT DFELPHERVN VHGGACALGH PIGASGARIV
VTLLGALQRR GLRRGVAALC IGGGEATALA VELP
//
