ID   A0A124IHW8_9SPHN        Unreviewed;       421 AA.
AC   A0A124IHW8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Acetyl-CoA acyltransferase {ECO:0000313|EMBL:KUO54631.1};
GN   ORFNames=APF82_01415 {ECO:0000313|EMBL:KUO54631.1};
OS   Sphingomonadales bacterium BRH_c42.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX   NCBI_TaxID=1734407 {ECO:0000313|EMBL:KUO54631.1, ECO:0000313|Proteomes:UP000054281};
RN   [1] {ECO:0000313|EMBL:KUO54631.1, ECO:0000313|Proteomes:UP000054281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c42 {ECO:0000313|EMBL:KUO54631.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) 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:KUO54631.1}.
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DR   EMBL; LOEX01000079; KUO54631.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124IHW8; -.
DR   Proteomes; UP000054281; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR   PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:KUO54631.1};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KUO54631.1}.
FT   DOMAIN          8..269
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          279..419
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        87
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        376
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        407
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   421 AA;  44354 MW;  6BE492CECEE183D9 CRC64;
     MSRFAEPVFV AAGLRTPFGR GGGALAAYNA ISLSVPVVQA MAAQAEPDLL VWGTVIPNLG
     WSNIARETWL DAKLNPTVPA FSVVLACSTS MTATFAAAGM LGEGTDLTMV GGSEVMSRPS
     IALTAEASKR LTDLFAQDAM AALAALQSLA PSDYVLPTKG WANRITGRTM GDHMEETAKA
     WRVSREAQDN WALKSHQRAV AGWERGFFDD LVIPLPELAR DANPRADTSP ERLAALKPAF
     DRDSGWGTLT AGNSSPITDG AAGCWVATEA GVARLPAGTP YARLVDYEVS AVDFHTEGLL
     MAPSYGIPRL LARHQLGFSD IALWEIHEAF AAQVLANVAA ITDPEWVRAT AGVQAAMGDF
     DWDRVNPNGG SVALGHPFGA TGARDLSQAV KELWAMPPGS RAIVSICADG GQGTVALLER
     G
//