ID   A0A176F594_9RHOB        Unreviewed;       427 AA.
AC   A0A176F594;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KZY34983.1};
GN   ORFNames=A3731_18240 {ECO:0000313|EMBL:KZY34983.1};
OS   Roseovarius sp. HI0049.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1822235 {ECO:0000313|EMBL:KZY34983.1, ECO:0000313|Proteomes:UP000077043};
RN   [1] {ECO:0000313|EMBL:KZY34983.1, ECO:0000313|Proteomes:UP000077043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI0049 {ECO:0000313|EMBL:KZY34983.1,
RC   ECO:0000313|Proteomes:UP000077043};
RA   Sosa O.A.;
RT   "Microbial cycling of marine high molecular weight dissolved organic
RT   matter.";
RL   Submitted (MAR-2016) 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:KZY34983.1}.
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DR   EMBL; LWFA01002847; KZY34983.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176F594; -.
DR   Proteomes; UP000077043; 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; PTHR18919:SF107; 3-KETOACYL-COA THIOLASE, MITOCHONDRIAL; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KZY34983.1}.
FT   DOMAIN          5..279
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          287..425
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        383
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        413
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   427 AA;  45651 MW;  77F897787C2D96E3 CRC64;
     MSRPVYLVDG ARTPFLRARG RPGPFTPVDL AVQCGRPLLM RQPFEATAFD LVILGCVNVI
     QDEMNPARVA ALRLGMGEQQ VAFTVQINCG SGMQSIDTAY RYIREGSHEM ILAGGTEALS
     HAPLVYNREA TEWYGDMARA KGPLDKVKAM AEVRPDFFSP VIGLERGLTD PITSLNMGQT
     AEVLAHRFGI DRITADAYAV DSHKRLTAAQ KQGRLNGEVF PAFDKDGTAH EHDDGVRPDS
     SIDKLAKLNP AFEKPYGKVT PGNSSQITDG ASWTILASET AVEAHGLTPI AKIVDSEWAA
     LDPGIMGLGP VLASTPLAQR HGLSVDDVDL WEINEAFAAQ VLACLDAWQD DAFCRDVLGY
     DSAFGRIDHD KLNVDGGAIS LGHPVGTSGN RIVLHLANAL KARGAKRGIA TECIGGGQGG
     AMLLEAA
//