FADA_YERPN
ID FADA_YERPN Reviewed; 387 AA.
AC Q1CNA0; D1Q190;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=YPN_0197;
GN ORFNames=YP516_0163;
OS Yersinia pestis bv. Antiqua (strain Nepal516).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=377628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL Submitted (APR-2009) 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: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; CP000305; ABG16530.1; -; Genomic_DNA.
DR EMBL; ACNQ01000001; EEO78644.1; -; Genomic_DNA.
DR RefSeq; WP_002211545.1; NZ_ACNQ01000001.1.
DR AlphaFoldDB; Q1CNA0; -.
DR SMR; Q1CNA0; -.
DR EnsemblBacteria; ABG16530; ABG16530; YPN_0197.
DR GeneID; 66843329; -.
DR KEGG; ypn:YPN_0197; -.
DR HOGENOM; CLU_031026_2_2_6; -.
DR OMA; DYYWGMG; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000008936; 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; Transferase.
FT CHAIN 1..387
FT /note="3-ketoacyl-CoA thiolase"
FT /id="PRO_0000292913"
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 387 AA; 40917 MW; 1690502C07AE9F63 CRC64;
MENVVIIDAV RTPMGRSKGG AFRHVRAEDL SAHLMRAVIS RNPGLNAAEI DDIYWGCVQQ
TLEQGFNIAR NASLLAEIPH SVPAVTVNRL CGSSMQALHD GARAIMVGDA KISLIGGVEH
MGHVPMNHGV DFHPGMGRTV AKAAGMMGLT AEMLAKIHNI SRQSQDEFAF RSHQRAYAAT
QAGHFAKEIV ATNGHDAEGV LKRFDFDEVI RPETNLSGLA ALRPAFDPVN GTVTAGTSSA
LSDGASAMLI MSESRAKSLG LTPRARIRSM AVVGCDPSIM GYGPVPASQL ALKRAGLELA
DIGLFELNEA FAAQSLACLK GLGLLESMDD KVNLNGGAIA LGHPLGCSGA RISTTLLNLM
ERRDVQFGLA TMCIGLGQGI ATVFERL
