(data stored in ACNUC29543 zone)

SWISSPROT: FADA_ACIBT

ID   FADA_ACIBT              Reviewed;         390 AA.
AC   A3M1H9;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   08-MAY-2019, entry version 79.
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};
GN   OrderedLocusNames=A1S_0305;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
CC   -!- FUNCTION: Catalyzes the final step of fatty acid oxidation in
CC       which acetyl-CoA is released and the CoA ester of a fatty acid two
CC       carbons 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
CC       chains (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
CC       family. {ECO:0000255|HAMAP-Rule:MF_01620}.
DR   EMBL; CP000521; ABO10773.2; -; Genomic_DNA.
DR   SMR; A3M1H9; -.
DR   PRIDE; A3M1H9; -.
DR   EnsemblBacteria; ABO10773; ABO10773; A1S_0305.
DR   KEGG; acb:A1S_0305; -.
DR   HOGENOM; HOG000012239; -.
DR   KO; K00632; -.
DR   UniPathway; UPA00659; -.
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;
DR   PRODOM; A3M1H9.
DR   SWISS-2DPAGE; A3M1H9.
KW   Acyltransferase; Cytoplasm; Fatty acid metabolism; Lipid degradation;
KW   Lipid metabolism; Transferase.
FT   CHAIN         1    390       3-ketoacyl-CoA thiolase.
FT                                /FTId=PRO_0000292883.
FT   ACT_SITE     95     95       Acyl-thioester intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01620}.
FT   ACT_SITE    346    346       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01620}.
FT   ACT_SITE    376    376       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01620}.
SQ   SEQUENCE   390 AA;  41132 MW;  A59F51928FC3ED8B CRC64;
     MATLNPRDVV IVDGVRSAMG KSKNGMFRNV RADSLSAELV RALIARNQFD VNEVEDLIWG
     CVNQTLEQGM NIGRNIGLLA GLPKTVAGQT VNRLCGSSMQ AIHTAAAQIA TNQGDIFIIG
     GVEHMGHVGM MHGIDLNPEA SKHYAKASNM MGLTAEMLGR MNGITREEQD TFGVESHRRA
     WAATQEGRFK NEIIGVEGHD ANGFKILCDI DEVIRPDANL EAFKALKPVF DPKGGSVTAA
     TSSALSDGAS AMLLMSAERA QALGLKPRAV IRSMAVAGCD AAIMGYGPVP ATQKALKRAG
     LSIADIQTVE LNEAFAAQGL SVLKGLGLYD KQDIVNLNGG AIALGHPLGC SGARITTTLL
     NVMEQQDTQI GLATMCIGLG QGIATVIERV
//

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