ID A0A1Q5U868_9GAMM Unreviewed; 436 AA.
AC A0A1Q5U868;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=3-ketoacyl-CoA thiolase {ECO:0000256|HAMAP-Rule:MF_01618};
DE EC=2.3.1.16 {ECO:0000256|HAMAP-Rule:MF_01618};
DE AltName: Full=ACSs {ECO:0000256|HAMAP-Rule:MF_01618};
DE AltName: Full=Acetyl-CoA acyltransferase {ECO:0000256|HAMAP-Rule:MF_01618};
DE AltName: Full=Acyl-CoA ligase {ECO:0000256|HAMAP-Rule:MF_01618};
DE AltName: Full=Beta-ketothiolase {ECO:0000256|HAMAP-Rule:MF_01618};
DE AltName: Full=Fatty acid oxidation complex subunit beta {ECO:0000256|HAMAP-Rule:MF_01618};
GN Name=fadI {ECO:0000256|HAMAP-Rule:MF_01618};
GN ORFNames=Xentx_00332 {ECO:0000313|EMBL:OKP08664.1};
OS Xenorhabdus thuongxuanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1873484 {ECO:0000313|EMBL:OKP08664.1, ECO:0000313|Proteomes:UP000186277};
RN [1] {ECO:0000313|EMBL:OKP08664.1, ECO:0000313|Proteomes:UP000186277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30TX1 {ECO:0000313|EMBL:OKP08664.1,
RC ECO:0000313|Proteomes:UP000186277};
RA Kaempfer P., Tobias N.J., Phan Ke L., Bode H.B., Glaeser S.P.;
RT "Xenorhabdus thuongxuanensis sp. nov. and Xenorhabdus eapokensis sp. nov.,
RT isolated from Steinernema species.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the final step of fatty acid oxidation in which
CC acetyl-CoA is released and the CoA ester of a fatty acid two carbons
CC shorter is formed. {ECO:0000256|HAMAP-Rule:MF_01618}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01618};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|HAMAP-Rule:MF_01618}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta chains
CC (FadI). {ECO:0000256|HAMAP-Rule:MF_01618}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01618}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|HAMAP-Rule:MF_01618,
CC 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:OKP08664.1}.
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DR EMBL; MKGR01000002; OKP08664.1; -; Genomic_DNA.
DR RefSeq; WP_074018527.1; NZ_MKGR01000002.1.
DR AlphaFoldDB; A0A1Q5U868; -.
DR OrthoDB; 8951704at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000186277; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR HAMAP; MF_01618; FadI; 1.
DR InterPro; IPR012806; Ac-CoA_C-AcTrfase_FadI.
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 NCBIfam; TIGR02446; FadI; 1.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01618};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01618};
KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01618};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|HAMAP-
KW Rule:MF_01618}; Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01618};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01618,
KW ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 15..288
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 297..434
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 99
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01618,
FT ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01618,
FT ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 422
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01618,
FT ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 436 AA; 46674 MW; 4F5322B1DA033EE7 CRC64;
MGRSSTKVIP QRERVAIVSG LRIPFAKQAT FYHGIPAVDL GKAVVSELVI RSGLSPEKID
QLVFGQVVQM PEAPNIAREI VLGAGLSVNT DAYSVSRACA TSFQAIANVA ESIMAGVVNI
GIAGGADSSS VLPIGVTKSL ARTLVDMNKA KSLTQRLKLL SRLKLRDLLP VSPAVSEYST
GLRMGDTAEQ MAKTYHISRE DQDAFAHRSH VLAAKAWEQG LLQEEIISAY FPPYSKTLAE
DNNIRKNSTL ASYAKLRPAF DRKHGTVTAA NSTPLTDGAA AVMLMRESVA KELGIVPLGY
LRSYAFSAID VWQDMLLGPS YATPLALDRA GITLNELTLI DMHEAFAAQT LTNLKMFASE
KFAREKLGRT QAIGEVDMDK FNVLGGSIAY GHPFAATGAR MVTQTLNELR RRGGGFGLTT
ACAAGGLGAA MVLEVE
//
