ID FADA_CHRSD Reviewed; 392 AA.
AC Q1QUW9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 116.
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=Csal_2392;
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
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; CP000285; ABE59739.1; -; Genomic_DNA.
DR RefSeq; WP_011507685.1; NC_007963.1.
DR AlphaFoldDB; Q1QUW9; -.
DR SMR; Q1QUW9; -.
DR STRING; 290398.Csal_2392; -.
DR KEGG; csa:Csal_2392; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_2_6; -.
DR OrthoDB; 9764638at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000000239; 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 NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR NCBIfam; TIGR02445; fadA; 1.
DR PANTHER; PTHR43853:SF11; 3-KETOACYL-COA THIOLASE FADA; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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 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; Reference proteome; Transferase.
FT CHAIN 1..392
FT /note="3-ketoacyl-CoA thiolase"
FT /id="PRO_0000292887"
FT ACT_SITE 95
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
SQ SEQUENCE 392 AA; 41321 MW; CC657D205AE37DDF CRC64;
MSLNPRDIVV VDAVRTAMAK AKHGAFRNVR AENLSAAVMQ ALFDRNANLV PAEVDDVIWG
CVNQTLEQSM NIARNAAIMT GIPRTVPAQT VNRLCGSSMS ALHIATANIK AGMGDFYIIG
GVEHMEHVPM THGVDVNPAA SKYAAKAAMM MGLTAELLGK MHGVGREEQD AFGVRSHQRA
QAANENGYFD NEIVGVEGHD ADGFLRLIDR DEVIRQDANL EDMGKLKPVF DPKGGTVTAG
TSSALSVGAS ALAVMSYERA QALGLEPLAR VVSTGVAGCD ASIMGYGPVP ATQKALKSAG
LAIDDIQTVE LNEAFAAQSI PVLKDLGLRE RMDDAVNLHG GAIALGHPLG CSGARICTTL
LNVMRQQDTT LGLATMCIGM GQGVATVFER LK
//
