ID C7BSK5_PHOAA Unreviewed; 436 AA.
AC C7BSK5;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
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 ECO:0000313|EMBL:CAQ83508.1};
GN OrderedLocusNames=PAU_01416 {ECO:0000313|EMBL:CAQ83508.1};
OS Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
OS (Xenorhabdus luminescens (strain 2)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=553480 {ECO:0000313|EMBL:CAQ83508.1, ECO:0000313|Proteomes:UP000002747};
RN [1] {ECO:0000313|EMBL:CAQ83508.1, ECO:0000313|Proteomes:UP000002747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43949 / 3105-77 {ECO:0000313|Proteomes:UP000002747};
RX PubMed=19583835; DOI=10.1186/1471-2164-10-302;
RA Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
RA Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
RA Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
RA Harris D., Thompson N.R., Quail M., Parkhill J., ffrench-Constant R.H.;
RT "Comparative genomics of the emerging human pathogen Photorhabdus
RT asymbiotica with the insect pathogen Photorhabdus luminescens.";
RL BMC Genomics 10:302-302(2009).
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}.
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DR EMBL; FM162591; CAQ83508.1; -; Genomic_DNA.
DR AlphaFoldDB; C7BSK5; -.
DR STRING; 291112.PAU_01416; -.
DR KEGG; pay:PAU_01416; -.
DR eggNOG; COG0183; Bacteria.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000002747; Chromosome.
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 296..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; 46779 MW; F3A1A0FEAB7BC4BD CRC64;
MSRPLTKVTQ QGDRIAIVSG LRIPFAKQAT SYHGIPAVDL GKSVVNELVA RSGLLPEKID
QLVFGQVVQM PEAPNIAREI VLGTGLSVNT DAYSVSRACA TSFQAIANVA ESIMAGTVNI
GIAGGADSSS VLPIGVTKSL ARTLVDMNKA KSLPQRLKLL SRLKFRDLLP VSPAVAEYST
GLRMGDTAEQ MAKTYRISRE DQDALAHRSH ILAAKAWEQG LLSDEVMTAH FPPYREALPE
DNNIRKNSVL TSYAKLRPAF DRKYGTVTVA NSTPLTDGAA AVMLMRESVA KEWGIKPLGY
LRSYAFSAID VWQDMLLGPS YATPIALERA GITLKDLTLI DMHEAFAAQT LANLKMFASD
EFARNKLGRA QAIGEVDMDK FNVLGGSIAY GHPFAATGAR MVTQVLNELR RRGGGLGLTT
ACAAGGLGTA MVLEVE
//
