ID A0A1H6J468_9FLAO Unreviewed; 391 AA.
AC A0A1H6J468;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=SAMN05421793_11037 {ECO:0000313|EMBL:SEH53620.1};
OS Epilithonimonas hominis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Epilithonimonas.
OX NCBI_TaxID=420404 {ECO:0000313|EMBL:SEH53620.1, ECO:0000313|Proteomes:UP000198555};
RN [1] {ECO:0000313|Proteomes:UP000198555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19326 {ECO:0000313|Proteomes:UP000198555};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNWX01000010; SEH53620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6J468; -.
DR STRING; 420404.SAMN05421793_11037; -.
DR Proteomes; UP000198555; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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:SEH53620.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SEH53620.1}.
FT DOMAIN 4..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 268..389
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 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 391 AA; 42063 MW; 39A07E84CFF8B014 CRC64;
MEAYIVTGYR TAVGKAPKGS LRFTRPDDMA ATVIERLMKD VPNLDPARID DLIVGCAMPE
AEQGLNVARL ISLMGLDTDK VPGVTVNRYC ASGSESIAIA AAKIKAGMAE CIIAGGAESM
SYIPMGGYKP IPDTDLAKSN PDYYWGMGLT AEAVANEFKV SREEQDQFAY NSHQKAIKAI
QEGKFDNQIV PIDVKYNFLD EKEKIQTKEY AFKQDEGPRA DTSIEALAKL RPVFAANGSV
TAGNSSQTSD GAAFTMVMSE RMVKELNLTP VARLLSYSTV GVPPRIMGIG PMYAIPKALE
QAGLKQSDID LFELNEAFAS QSVAILRELN INPDIVNVNG GAIALGHPLG CTGTKLTVQL
LDEMKRRNSK YGVVTMCVGT GQGAASVFEL L
//
