ID FADA_PSEU5 Reviewed; 391 AA.
AC A4VKA4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 01-MAY-2013, entry version 49.
DE RecName: Full=3-ketoacyl-CoA thiolase;
DE EC=2.3.1.16;
DE AltName: Full=Acetyl-CoA acyltransferase;
DE AltName: Full=Beta-ketothiolase;
DE AltName: Full=Fatty acid oxidation complex subunit beta;
GN Name=fadA; Synonyms=foaB; OrderedLocusNames=PST_1727;
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501;
RA Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W.,
RA Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D.,
RA Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Complete genome sequence of the metabolically versatile and root-
RT associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta
CC chains (FadA) (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the thiolase family.
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DR EMBL; CP000304; ABP79405.1; -; Genomic_DNA.
DR RefSeq; YP_001172247.1; NC_009434.1.
DR ProteinModelPortal; A4VKA4; -.
DR SMR; A4VKA4; 2-391.
DR STRING; 379731.PST_1727; -.
DR EnsemblBacteria; ABP79405; ABP79405; PST_1727.
DR GeneID; 5097811; -.
DR KEGG; psa:PST_1727; -.
DR PATRIC; 19963921; VBIPseStu31643_1735.
DR eggNOG; COG0183; -.
DR HOGENOM; HOG000012239; -.
DR KO; K00632; -.
DR OMA; AIMTNNG; -.
DR ProtClustDB; PRK08947; -.
DR BioCyc; PSTU379731:GJER-1726-MONOMER; -.
DR UniPathway; UPA00659; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:HAMAP.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.47.10; -; 4.
DR HAMAP; MF_01620; FadA; 1; -.
DR InterPro; IPR012805; FadA.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR016038; Thiolase-like_subgr.
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 PANTHER; PTHR18919; PTHR18919; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 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; Complete proteome; Cytoplasm; Fatty acid metabolism;
KW Lipid degradation; Lipid metabolism; Transferase.
FT CHAIN 1 391 3-ketoacyl-CoA thiolase.
FT /FTId=PRO_0000323551.
FT ACT_SITE 95 95 Acyl-thioester intermediate (By
FT similarity).
FT ACT_SITE 347 347 Proton acceptor (By similarity).
FT ACT_SITE 377 377 Proton acceptor (By similarity).
SQ SEQUENCE 391 AA; 41738 MW; 10443DF8691148DA CRC64;
MSLNPRDAVI VDFGRTPMGR SKGGMHRNTR AETMSAQLID GLLARNPKID PAEVEDVIWG
CVNQTLEQGW NIARMASLLT RIPHTSAGQT VSRLCGSSMS ALHTAVQAIQ TNNGDVFVIG
GVEHMGHVSM MHGVDPNPQL SLHAAKASGM MGLTAEMLGK MHGITREAQD QFGYRSHQLA
WKATQEGKFK DEIIPMEGHD ENGFLKVFDY DETIRPETTL EGLAELKPAF NPKGGTVTAG
TSSQITDGAS CMIVMSAQRA KDLGLQPMAV VRAMALAGVD PAIMGYGPVP STQKALKRAG
LTMDDISHVE LNEAFAAQAL PVLKDLKLLD KMEEKVNLHG GAIALGHPFG CSGARISGTL
LNVMKQNNGT LGVATMCIGL GQGISTVFER L
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