FADA_SALTY
ID FADA_SALTY Reviewed; 387 AA.
AC P0A2H7; Q9L6L6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=STM3982;
GN ORFNames=STMD1.7;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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. Involved in the aerobic and anaerobic degradation of
CC long-chain fatty acids (By similarity). {ECO:0000255|HAMAP-
CC 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; AF233324; AAF33416.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22826.1; -; Genomic_DNA.
DR RefSeq; NP_462867.1; NC_003197.2.
DR RefSeq; WP_000438778.1; NC_003197.2.
DR PDB; 3GOA; X-ray; 1.70 A; A/B=1-387.
DR PDBsum; 3GOA; -.
DR AlphaFoldDB; P0A2H7; -.
DR SMR; P0A2H7; -.
DR STRING; 99287.STM3982; -.
DR PaxDb; P0A2H7; -.
DR PRIDE; P0A2H7; -.
DR EnsemblBacteria; AAL22826; AAL22826; STM3982.
DR GeneID; 1255508; -.
DR KEGG; stm:STM3982; -.
DR PATRIC; fig|99287.12.peg.4201; -.
DR HOGENOM; CLU_031026_2_3_6; -.
DR OMA; EPMRPGT; -.
DR PhylomeDB; P0A2H7; -.
DR BioCyc; SENT99287:STM3982-MON; -.
DR UniPathway; UPA00659; -.
DR EvolutionaryTrace; P0A2H7; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0010124; P:phenylacetate catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Fatty acid metabolism;
KW Lipid degradation; Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..387
FT /note="3-ketoacyl-CoA thiolase"
FT /id="PRO_0000206391"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT ACT_SITE 373
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:3GOA"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:3GOA"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 27..41
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3GOA"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:3GOA"
FT TURN 63..67
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:3GOA"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:3GOA"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:3GOA"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3GOA"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 162..182
FT /evidence="ECO:0007829|PDB:3GOA"
FT TURN 183..188
FT /evidence="ECO:0007829|PDB:3GOA"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:3GOA"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:3GOA"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3GOA"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:3GOA"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 284..295
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:3GOA"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:3GOA"
FT HELIX 345..362
FT /evidence="ECO:0007829|PDB:3GOA"
FT STRAND 366..374
FT /evidence="ECO:0007829|PDB:3GOA"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:3GOA"
FT STRAND 378..385
FT /evidence="ECO:0007829|PDB:3GOA"
SQ SEQUENCE 387 AA; 41004 MW; 39E24805360ABD8A CRC64;
MEQVVIVDAI RTPMGRSKGG AFRNVRAEDL SAHLMRSLLA RNPSLTAATL DDIYWGCVQQ
TLEQGFNIAR NAALLAEIPH SVPAVTVNRL CGSSMQALHD AARMIMTGDA QVCLVGGVEH
MGHVPMSHGV DFHPGLSRNV AKAAGMMGLT AEMLSRLHGI SREMQDQFAA RSHARAWAAT
QSGAFKTEII PTGGHDADGV LKQFNYDEVI RPETTVEALS TLRPAFDPVS GTVTAGTSSA
LSDGAAAMLV MSESRARELG LKPRARIRSM AVVGCDPSIM GYGPVPASKL ALKKAGLSAS
DIDVFEMNEA FAAQILPCIK DLGLMEQIDE KINLNGGAIA LGHPLGCSGA RISTTLINLM
ERKDAQFGLA TMCIGLGQGI ATVFERV
