ID A0A3S3Q397_9FLAO Unreviewed; 393 AA.
AC A0A3S3Q397;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=EPI11_16450 {ECO:0000313|EMBL:RWW92213.1};
OS Flavobacterium cerinum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2502784 {ECO:0000313|EMBL:RWW92213.1, ECO:0000313|Proteomes:UP000287527};
RN [1] {ECO:0000313|EMBL:RWW92213.1, ECO:0000313|Proteomes:UP000287527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1E403 {ECO:0000313|EMBL:RWW92213.1,
RC ECO:0000313|Proteomes:UP000287527};
RA Zhang R., Du Z.-J.;
RT "Flavobacterium sp. nov.,isolated from freshwater.";
RL Submitted (JAN-2019) 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:RWW92213.1}.
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DR EMBL; SBII01000013; RWW92213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3Q397; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000287527; 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:RWW92213.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000287527};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:RWW92213.1}.
FT DOMAIN 5..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..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; 42402 MW; 256BBA0590D79845 CRC64;
MKTAYIVKAY RTAVGKAPKG VFRFKRPDEL AAETIQFIMN ELPDFDKTRI DDVMVGNAMP
EAEQGLNFAR LISLMGLKID DVPGVTVNRY CASGLETIAM ATAKIQSGMA ECIIAGGAES
MSYIPMGGYK PVPDYQAAKN GHEDYYWGMG LTAEAVAKQF KVSREDQDQF GYMSHQKALK
AQAEGKFDKQ IVPITVEQIY VDENGKKATK SYTVTKDEGP RADTSLEALG KLRPVFAADG
SVTAGTSSQM SDGAAFVMVM SEDMVKELNL EPIARMVSYA AAGVEPRIMG IGPVKAIPKA
LKMAGLQLKD IELFELNEAF ASQSLAVMRE LGINQDLVNV NGGAIALGHP LGCTGAKLSV
QLFDEMKRRN NKYGIVTMCV GTGQGAAGVY EIL
//