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FADA_PSET1
ID   FADA_PSET1              Reviewed;         389 AA.
AC   Q3IJ24;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=PSHAa0010;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85124.1; -; Genomic_DNA.
DR   RefSeq; WP_011326742.1; NC_007481.1.
DR   AlphaFoldDB; Q3IJ24; -.
DR   SMR; Q3IJ24; -.
DR   STRING; 326442.PSHAa0010; -.
DR   EnsemblBacteria; CAI85124; CAI85124; PSHAa0010.
DR   KEGG; pha:PSHAa0010; -.
DR   eggNOG; COG0183; Bacteria.
DR   HOGENOM; CLU_031026_2_3_6; -.
DR   OMA; DYYWGMG; -.
DR   OrthoDB; 550338at2; -.
DR   BioCyc; PHAL326442:PSHA_RS00050-MON; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000006843; Chromosome I.
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..389
FT                   /note="3-ketoacyl-CoA thiolase"
FT                   /id="PRO_0000292894"
FT   ACT_SITE        91
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT   ACT_SITE        343
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT   ACT_SITE        373
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
SQ   SEQUENCE   389 AA;  40918 MW;  2BAD62B06E15D50A CRC64;
     MNNPVIVDCI RTPMGRSKGG VFKNKRAEDL SAHLMKGLLD RNPAVDPASI DDIYWGCVQQ
     TLEQGFNVAR NAALLAGIPH SVPAVTVNRL CGSSMQALHD AARAIMTGAG DTYLIGGVEH
     MGHVPMTHGN DFHPGLATSI AQAAGSMGLT AEYLATLHGI SREQQDEFAY RSHQRAQAAT
     VEGRFRREIL AMEGHAADGS LILVEDDEVI RPETTVEGLS KLRPVFNPAS GTVTAGTSSA
     LSDGASAMLV MSEAKAKELG LPIRARIKAM AVAGCDPSIM GYGPVPASKK ALAQAGITID
     DLGVVELNEA FAAQSLPVMK DLGLMDVVDE KVNLNGGAIA LGHPLGCSGS RISTSLIHLM
     EDKNVRYGLA TMCIGLGQGI ATVFERVQD
 
 
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