(data stored in ACNUC7421 zone)

SWISSPROT: FADA_PSEHT

ID   FADA_PSEHT              Reviewed;         389 AA.
AC   Q3IJ24;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 84.
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=PSHAa0010;
OS   Pseudoalteromonas haloplanktis (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.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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: Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
CC       {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 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01620}.
DR   EMBL; CR954246; CAI85124.1; -; Genomic_DNA.
DR   RefSeq; WP_011326742.1; NC_007481.1.
DR   ProteinModelPortal; Q3IJ24; -.
DR   SMR; Q3IJ24; -.
DR   STRING; 326442.PSHAa0010; -.
DR   EnsemblBacteria; CAI85124; CAI85124; PSHAa0010.
DR   GeneID; 32565508; -.
DR   KEGG; pha:PSHAa0010; -.
DR   eggNOG; ENOG4105CHU; Bacteria.
DR   eggNOG; COG0183; LUCA.
DR   HOGENOM; HOG000012239; -.
DR   KO; K00632; -.
DR   OMA; CGGTESM; -.
DR   OrthoDB; POG091H0I7B; -.
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-EC.
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; Q3IJ24.
DR   SWISS-2DPAGE; Q3IJ24.
KW   Acyltransferase; Complete proteome; Cytoplasm; Fatty acid metabolism;
KW   Lipid degradation; Lipid metabolism; Reference proteome; Transferase.
FT   CHAIN         1    389       3-ketoacyl-CoA thiolase.
FT                                /FTId=PRO_0000292894.
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   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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