(data stored in ACNUC7421 zone)

SWISSPROT: FADA_AERHH

ID   FADA_AERHH              Reviewed;         387 AA.
AC   A0KEL0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 85.
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=AHA_0138;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK39512.1; -; Genomic_DNA.
DR   RefSeq; WP_011704164.1; NC_008570.1.
DR   RefSeq; YP_854675.1; NC_008570.1.
DR   SMR; A0KEL0; -.
DR   STRING; 380703.AHA_0138; -.
DR   PRIDE; A0KEL0; -.
DR   EnsemblBacteria; ABK39512; ABK39512; AHA_0138.
DR   GeneID; 4490319; -.
DR   KEGG; aha:AHA_0138; -.
DR   PATRIC; fig|380703.7.peg.131; -.
DR   eggNOG; ENOG4105CHU; Bacteria.
DR   eggNOG; COG0183; LUCA.
DR   HOGENOM; HOG000012239; -.
DR   KO; K00632; -.
DR   OMA; DYYWGMG; -.
DR   BioCyc; AHYD380703:G1G7B-138-MONOMER; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000000756; 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;
DR   PRODOM; A0KEL0.
DR   SWISS-2DPAGE; A0KEL0.
KW   Acyltransferase; Complete proteome; Cytoplasm; Fatty acid metabolism;
KW   Lipid degradation; Lipid metabolism; Reference proteome; Transferase.
FT   CHAIN         1    387       3-ketoacyl-CoA thiolase.
FT                                /FTId=PRO_0000292884.
FT   ACT_SITE     91     91       Acyl-thioester intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01620}.
FT   ACT_SITE    343    343       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01620}.
FT   ACT_SITE    373    373       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01620}.
SQ   SEQUENCE   387 AA;  40900 MW;  FD0D22C742642BC6 CRC64;
     MKDVVIVDCI RTPMGRSKGG AFRNVRAEDL SAHLMKSILL RNPNLDPNEI EDIYWGCVQQ
     TLEQGFNIAR NAALLAGIPK QVGAVTVNRL CGSSMQALHD ASRAIQVGDG DIFIIGGVEH
     MGHVPMSHGV DFHPGMAKSV AKASGMMGLT AEMLGKLHGI SRQQQDEFAA RSHRRAHAAT
     VEGRFAKEIV GLEGHDASGA RFFYDYDEVI RPETTVETLS QLRPVFDPVN GTVTAGTSSA
     LSDGAAAMLV MSADRAKALG LTPRAKIRAM AVAGCDAAIM GYGPVPATQK ALKRAGLTIG
     DIDLFELNEA FAAQSLPCVK DLGLQDVVDE KVNLNGGAIA LGHPLGCSGA RISTTLLNLM
     EEKDATLGVA TMCIGLGQGI ATVFERV
//

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