FADA_PSESM
ID FADA_PSESM Reviewed; 391 AA.
AC Q87ZB3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 109.
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=PSPTO_3516;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO56991.1; -; Genomic_DNA.
DR RefSeq; NP_793296.1; NC_004578.1.
DR RefSeq; WP_007245350.1; NC_004578.1.
DR AlphaFoldDB; Q87ZB3; -.
DR SMR; Q87ZB3; -.
DR STRING; 223283.PSPTO_3516; -.
DR EnsemblBacteria; AAO56991; AAO56991; PSPTO_3516.
DR GeneID; 1185181; -.
DR KEGG; pst:PSPTO_3516; -.
DR PATRIC; fig|223283.9.peg.3601; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_2_6; -.
DR OMA; YAYESHQ; -.
DR OrthoDB; 550338at2; -.
DR PhylomeDB; Q87ZB3; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000002515; 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..391
FT /note="3-ketoacyl-CoA thiolase"
FT /id="PRO_0000206386"
FT ACT_SITE 95
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
SQ SEQUENCE 391 AA; 41720 MW; E0572722AF7EBE9B CRC64;
MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AEDMSAHLIS KLLERNNKVD PAEVEDVIWG
CVNQTLEQGW NIARMASLLT QIPHTSAAQT VSRLCGSSMS ALHTAAQAIM TNNGDVFVIG
GVEHMGHVSM MHGVDPNPHM SLHAAKASGM MGLTAEMLGK MHGITREQQD AFGLRSHQLA
HKATLEGKFK DEIIPMQGYD ENGFLRVFDY DETIRPDTTL ESLAALKPAF NPKGGTVTAG
TSSQITDGAS CMIVMSAQRA QDLGIQPLAV IRSMAVAGVD PAIMGYGPVP ATQKALKRAG
LSISDIDFFE LNEAFAAQAL PVLKDLKVLD KMNEKVNLHG GAIALGHPFG CSGARISGTL
LNVMKQNGGT FGVSTMCIGL GQGIATVFER V
