ID A0A432CBJ2_9FLAO Unreviewed; 393 AA.
AC A0A432CBJ2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=EKM02_12485 {ECO:0000313|EMBL:RTY98152.1};
OS Flavobacterium sp. RSP49.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2497487 {ECO:0000313|EMBL:RTY98152.1, ECO:0000313|Proteomes:UP000272024};
RN [1] {ECO:0000313|EMBL:RTY98152.1, ECO:0000313|Proteomes:UP000272024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSP49 {ECO:0000313|EMBL:RTY98152.1,
RC ECO:0000313|Proteomes:UP000272024};
RA Liu Q., Xin Y.-H.;
RT "Flavobacterium sp. nov., isolated from glacier ice.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:RTY98152.1}.
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DR EMBL; RYDN01000031; RTY98152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432CBJ2; -.
DR Proteomes; UP000272024; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase 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; IPR020615; Thiolase_acyl_enz_int_AS.
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; 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; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:RTY98152.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:RTY98152.1}.
FT DOMAIN 5..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..390
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 393 AA; 42021 MW; 703059242CE9FAEC CRC64;
MKTAYIVKAY RTAVGKAPKG VFRFKRPDEL AAETIQFMMN ELPDFDKKRI DDVMVGNAMP
EAEQGLNVGR LISLMGLKIE DVPGVTVNRY CASGLETIGM ATAKIQSGMA DCIIAGGAES
MSFIPMGGYK PTPDYAVAKA GNEDYYWGMG LTAEAVAKQF NVSRADQDEF AYNSHLKALK
AQAEGKFDKQ IVPIRVEQTF INENGKKETK SYIVNKDEGP RAGTSVEALA GLRPVFEANG
SVTAGNSSQM SDGAAFVLIM SEEMVKELNL TPIARLVNFA SAGVEPRIMG IGPVKAIPKA
LKQAGLTLND VDLIELNEAF ASQSLAVIRE LGLNPDIVNV NGGAIAMGHP LGCTGAKLSV
QLFDEMKKRG NKYGIVSMCV GTGQGTAGVY ELL
//