FADA_PSEFR
ID FADA_PSEFR Reviewed; 391 AA.
AC P28790;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
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}; Synonyms=faoB;
OS Pseudomonas fragi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=296;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=B-0771;
RX PubMed=1607366; DOI=10.1093/oxfordjournals.jbchem.a123722;
RA Sato S., Hayashi M., Imamura S., Ozeki Y., Kawaguchi A.;
RT "Primary structures of the genes, faoA and faoB, from Pseudomonas fragi B-
RT 0771 which encode the two subunits of the HDT multienzyme complex involved
RT in fatty acid beta-oxidation.";
RL J. Biochem. 111:8-15(1992).
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 -!- INTERACTION:
CC P28790; P28793: fadB; NbExp=4; IntAct=EBI-1039311, EBI-1039318;
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; D10390; BAA01228.1; -; Genomic_DNA.
DR PIR; JS0624; JS0624.
DR PDB; 1WDK; X-ray; 2.50 A; C/D=2-391.
DR PDB; 1WDL; X-ray; 3.50 A; C/D=2-391.
DR PDB; 1WDM; X-ray; 3.80 A; C/D=2-391.
DR PDB; 2D3T; X-ray; 3.40 A; C/D=2-391.
DR PDBsum; 1WDK; -.
DR PDBsum; 1WDL; -.
DR PDBsum; 1WDM; -.
DR PDBsum; 2D3T; -.
DR AlphaFoldDB; P28790; -.
DR SMR; P28790; -.
DR DIP; DIP-29090N; -.
DR IntAct; P28790; 1.
DR STRING; 1136138.JH604622_gene1073; -.
DR DrugBank; DB08249; 3,6,9,12,15-PENTAOXATRICOSAN-1-OL.
DR PRIDE; P28790; -.
DR eggNOG; COG0183; Bacteria.
DR BRENDA; 2.3.1.16; 5123.
DR UniPathway; UPA00659; -.
DR EvolutionaryTrace; P28790; -.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Direct protein sequencing;
KW Fatty acid metabolism; Lipid degradation; Lipid metabolism; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..391
FT /note="3-ketoacyl-CoA thiolase"
FT /id="PRO_0000206380"
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"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:1WDK"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:1WDK"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1WDK"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1WDK"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1WDK"
FT TURN 67..71
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:1WDK"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1WDK"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:1WDK"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:1WDK"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:1WDK"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 166..185
FT /evidence="ECO:0007829|PDB:1WDK"
FT TURN 186..192
FT /evidence="ECO:0007829|PDB:1WDK"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1WDK"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:1WDK"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1WDK"
FT STRAND 246..256
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 257..262
FT /evidence="ECO:0007829|PDB:1WDK"
FT STRAND 268..278
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1WDK"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 316..325
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:1WDK"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:2D3T"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:1WDK"
FT HELIX 349..366
FT /evidence="ECO:0007829|PDB:1WDK"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:1WDK"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:1WDK"
FT STRAND 382..389
FT /evidence="ECO:0007829|PDB:1WDK"
SQ SEQUENCE 391 AA; 41606 MW; 3C5F24D816DB9EA5 CRC64;
MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AEDMSAHLIS KVLERNSKVD PGEVEDVIWG
CVNQTLEQGW NIARMASLMT QIPHTSAAQT VSRLCGSSMS ALHTAAQAIM TGNGDVFVVG
GVEHMGHVSM MHGVDPNPHM SLYAAKASGM MGLTAEMLGK MHGISREQQD AFAVRSHQLA
HKATVEGKFK DEIIPMQGYD ENGFLKIFDY DETIRPDTTL ESLAALKPAF NPKGGTVTAG
TSSQITDGAS CMIVMSAQRA KDLGLEPLAV IRSMAVAGVD PAIMGYGPVP ATQKALKRAG
LNMADIDFIE LNEAFAAQAL PVLKDLKVLD KMNEKVNLHG GAIALGHPFG CSGARISGTL
LNVMKQNGGT FGLSTMCIGL GQGIATVFER V
