ID I0WFD2_9FLAO Unreviewed; 393 AA.
AC I0WFD2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=W5A_07177 {ECO:0000313|EMBL:EID75098.1};
OS Imtechella halotolerans K1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Imtechella.
OX NCBI_TaxID=946077 {ECO:0000313|EMBL:EID75098.1, ECO:0000313|Proteomes:UP000005938};
RN [1] {ECO:0000313|EMBL:EID75098.1, ECO:0000313|Proteomes:UP000005938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1 {ECO:0000313|EMBL:EID75098.1,
RC ECO:0000313|Proteomes:UP000005938};
RX PubMed=22740661; DOI=10.1128/JB.00506-12;
RA Kumar S., Vikram S., Subramanian S., Raghava G.P., Pinnaka A.K.;
RT "Genome Sequence of the Halotolerant Bacterium Imtechella halotolerans
RT K1T.";
RL J. Bacteriol. 194:3731-3731(2012).
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:EID75098.1}.
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DR EMBL; AJJU01000007; EID75098.1; -; Genomic_DNA.
DR RefSeq; WP_008238912.1; NZ_AJJU01000007.1.
DR AlphaFoldDB; I0WFD2; -.
DR STRING; 946077.W5A_07177; -.
DR PATRIC; fig|946077.3.peg.1451; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000005938; 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 Reference proteome {ECO:0000313|Proteomes:UP000005938};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EID75098.1}.
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; 42464 MW; E2416BF52D524186 CRC64;
MKTAYIVKAY RTAVGKAPRG LFRFKRPDEL AAETIEYMMK ELPQLDKKRI DDVIVGNAMP
EAEQGLNVAR LISLMGLKVE DVPGVTVNRY CASGLETIAI ATAKIQSGMA DCIIAGGAES
MSYIPMGGYK PTPDYKIAKE GHEDYYWGMG LTAEAVANQF NVSREDQDIF AYNSHQKAIK
AISEGRFKDQ IVPITVEQVY IDDQGKKATK TYTVNTDEGP RADTSVEVLS KLRPVFAADG
SVTAGNSSQM SDGAAFVLVM SEEMVKELNL EPIARLVSYA AAGVEPRIMG IGPVKAIPKA
LQQAGMTKEQ IDLIELNEAF ASQSLAVTRE LNLNPEIINV NGGAIALGHP LGCTGAKLSV
QLFDEMRKRG NKYGMVTMCV GTGQGAAGIY ELM
//