FADA_ACIAD
ID FADA_ACIAD Reviewed; 390 AA.
AC Q6FF69;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=3-ketoacyl-CoA thiolase {ECO:0000255|HAMAP-Rule:MF_01620};
DE EC=2.3.1.16 {ECO:0000255|HAMAP-Rule:MF_01620};
DE AltName: Full=Acetyl-CoA acyltransferase {ECO:0000255|HAMAP-Rule:MF_01620};
DE AltName: Full=Beta-ketothiolase {ECO:0000255|HAMAP-Rule:MF_01620};
DE AltName: Full=Fatty acid oxidation complex subunit beta {ECO:0000255|HAMAP-Rule:MF_01620};
GN Name=fadA {ECO:0000255|HAMAP-Rule:MF_01620}; OrderedLocusNames=ACIAD0334;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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:0000255|HAMAP-Rule:MF_01620}.
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:0000255|HAMAP-Rule:MF_01620};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000255|HAMAP-Rule:MF_01620}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains
CC (FadA). {ECO:0000255|HAMAP-Rule:MF_01620}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01620}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01620}.
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DR EMBL; CR543861; CAG67288.1; -; Genomic_DNA.
DR RefSeq; WP_004920543.1; NC_005966.1.
DR AlphaFoldDB; Q6FF69; -.
DR SMR; Q6FF69; -.
DR STRING; 62977.ACIAD0334; -.
DR EnsemblBacteria; CAG67288; CAG67288; ACIAD0334.
DR GeneID; 45232841; -.
DR KEGG; aci:ACIAD0334; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_2_6; -.
DR OMA; DYYWGMG; -.
DR OrthoDB; 550338at2; -.
DR BioCyc; ASP62977:ACIAD_RS01565-MON; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000000430; 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; -; 2.
DR HAMAP; MF_01620; FadA; 1.
DR InterPro; IPR012805; FadA.
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 Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR TIGRFAMs; TIGR02445; fadA; 1.
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; Cytoplasm; Fatty acid metabolism; Lipid degradation;
KW Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..390
FT /note="3-ketoacyl-CoA thiolase"
FT /id="PRO_0000206368"
FT ACT_SITE 95
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT ACT_SITE 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
SQ SEQUENCE 390 AA; 41215 MW; D8E3050256548E62 CRC64;
MTNLNPRDVV IVDGVRSAMG KSKNGMFRNV RADSLSAELV RALVARNQFD VNEVEDLIWG
CVNQTLEQGM NIGRNIVLLA DLPKTVAGQT VNRLCGSSMQ AIHTAAAQIA TNQGDIFIIG
GVEHMGHVGM MHGIDLNPEA SKHYAKASNM MGLTAEMLGR MNGIGREEQD AFGVESHRRA
WAATQEGRFK NEIVGVEGHD ANGFKILCDI DEVIRPDANL EAFKALRPVF DPKGGTVTAA
TSSALSDGAS AMLLMSAERA QALGLKPRAV IRSMAVAGCD AAIMGYGPVP ATQKALKRAG
LSVADIQTVE LNEAFAAQGL SVLKGLGLYE KQDIVNLNGG AIALGHPLGC SGARITTTLL
NVMEQQDTQI GLATMCIGLG QGIATVIERV
