ID   A0A124IH96_9SPHN        Unreviewed;       422 AA.
AC   A0A124IH96;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KUO52641.1};
GN   ORFNames=APF78_04360 {ECO:0000313|EMBL:KUO52641.1};
OS   Sphingomonadales bacterium BRH_c3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX   NCBI_TaxID=1734408 {ECO:0000313|EMBL:KUO52641.1, ECO:0000313|Proteomes:UP000061825};
RN   [1] {ECO:0000313|EMBL:KUO52641.1, ECO:0000313|Proteomes:UP000061825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c3 {ECO:0000313|EMBL:KUO52641.1};
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:KUO52641.1}.
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DR   EMBL; LOET01000125; KUO52641.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124IH96; -.
DR   Proteomes; UP000061825; 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; -; 2.
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; PTHR43365; BLR7806 PROTEIN; 1.
DR   PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KUO52641.1}.
FT   DOMAIN          5..236
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          294..416
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        92
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        373
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        403
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   422 AA;  44885 MW;  0E308850F8E1CD99 CRC64;
     MGEAYIIDAV RTPRGIGKQG KGALAAEHPQ HLAATVLKAI KDRNHLDTTT VDDVIWSVST
     QDGMQGGDMG RMASLDAGYD ITSSGMTLDR FCGGGITSVN LAAAQVMSGM ADCVVAGGTE
     MMSLTAQMAK EKMQAGIKPP MMGSYNERLQ KVHPQSHQGI CGDAIASMEG ITREELDEVG
     YRSQQRAAEA IAEGRFAKSI IPVVDDEGNV ILDHDEYPRP QTTREGLAQL EPAFTKIADV
     PIDAEGTTFR KLVNQKYPDL EIRNFHHAGN SSGVVDGAAA VLVTSKEYAQ SHGLKPRARI
     VATANMGDDP TLMLNAPVPA ARRVLEKAGL TLEDIDLFEI NEAFAVVAAK FVRDLGLDWD
     KVNVNGGSIA LGHPIGATGS ILIGTIIDEL ERRGGRYGLV TMCAAGGMAP AIIVERVTDF
     AD
//