ID   A0A0C1RPJ5_9ACTN        Unreviewed;       389 AA.
AC   A0A0C1RPJ5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KIE52801.1};
GN   ORFNames=MB55_06795 {ECO:0000313|EMBL:KIE52801.1};
OS   marine actinobacterium MedAcidi-G3.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1550402 {ECO:0000313|EMBL:KIE52801.1, ECO:0000313|Proteomes:UP000031370};
RN   [1] {ECO:0000313|EMBL:KIE52801.1, ECO:0000313|Proteomes:UP000031370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT   "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL   Submitted (SEP-2014) 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:KIE52801.1}.
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DR   EMBL; JUEP01000011; KIE52801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1RPJ5; -.
DR   STRING; 1550402.MB55_06795; -.
DR   Proteomes; UP000031370; 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; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KIE52801.1}.
FT   DOMAIN          5..256
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          265..386
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        89
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        343
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        373
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   389 AA;  41237 MW;  1B50801FC8C54DC6 CRC64;
     MREAVIVDAV RTPGGKRNGK LQDWHPVDLA AHVLKALEER TGIDPSVIDD VIMGCVMQVG
     EQSLNIGRNA VLAAGWPESV PATTVDRQCG SSQQALHFAA QGVIAGAYDV AVAAGVEVMT
     RTPMGASVVK GMGFPFSETM QNRYEETGLP PQGIGAEMIA DEYGFSREDL DAFGAESQRR
     AAVATAEGRF DNEIVPVPVD VDGNLEMMTK DEGIRYETTA DSLAKLNPAF REDGKVTAGN
     SSQITDGASA VLVMSAEKAA ELGLRPRARF HTFALAGADP VTMLKGPIPA TEKVMSRSGL
     TIDDIDLFEV NEAFASVVLA WQKEHGTDLS RTNVNGGAIA LGHPLGCSGT KLMATLLNEL
     ERTEGRFGLQ TMCEGGGMAN ATIIERLDS
//