ID A0A3M9MFN7_9MICO Unreviewed; 407 AA.
AC A0A3M9MFN7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:RNI23967.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:RNI23967.1};
GN ORFNames=EFY87_06815 {ECO:0000313|EMBL:RNI23967.1};
OS Flexivirga caeni.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Flexivirga.
OX NCBI_TaxID=2294115 {ECO:0000313|EMBL:RNI23967.1, ECO:0000313|Proteomes:UP000271678};
RN [1] {ECO:0000313|EMBL:RNI23967.1, ECO:0000313|Proteomes:UP000271678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BO-16 {ECO:0000313|EMBL:RNI23967.1,
RC ECO:0000313|Proteomes:UP000271678};
RA Im W.T.;
RT "Draft genome of Simplicispira Flexivirga sp. BO-16.";
RL Submitted (NOV-2018) 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:RNI23967.1}.
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DR EMBL; RJJQ01000004; RNI23967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9MFN7; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000271678; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
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; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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:RNI23967.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000271678};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:RNI23967.1}.
FT DOMAIN 5..275
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 284..404
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 362
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 407 AA; 42476 MW; C0417B98FD211B3B CRC64;
MPEAVIVAAA RTPIGRAFKG SLKDIRPDDL SVQVIQAALD RVPGLDPKLV EDLYLGCAEP
SAEHGSNMAR VVSVLGGWDH LPGATVNRFC SSSVQTTRMA AHAIKAGEGD VFISAGVECV
SRYAAFSGAG GSKTDSQNPK FASAIARSEQ IAKDNSTWTD PRDEGNLPDI YIAMGQTAEN
VATLRGVSRE RQDEWGVTSQ NRAEQSIADG FFAREIASVT LPDGTVVSTD DGPRAGVTLE
KVSTLQPVFR ENGTVTAGNC CPLNDGAAAV VVMSDTKAKQ LGITPLARVV STGVSALSPE
IMGLGPVEAS RQALQRAGMT IADLDLYEIN EAFAAQVLPS ADDLGMDFDK LNVHGGAIAL
GHPFGSTGAR ITTTLLNGLQ EADGTLGLET MCVGGGQGMA IIYERLS
//
