ID   A0AAP2G7M6_9GAMM        Unreviewed;       387 AA.
AC   A0AAP2G7M6;
DT   02-OCT-2024, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2024, sequence version 1.
DT   27-NOV-2024, entry version 2.
DE   RecName: Full=3-ketoacyl-CoA thiolase {ECO:0000256|HAMAP-Rule:MF_01620};
DE            EC=2.3.1.16 {ECO:0000256|HAMAP-Rule:MF_01620};
DE   AltName: Full=Acetyl-CoA acyltransferase {ECO:0000256|HAMAP-Rule:MF_01620};
DE   AltName: Full=Beta-ketothiolase {ECO:0000256|HAMAP-Rule:MF_01620};
DE   AltName: Full=Fatty acid oxidation complex subunit beta {ECO:0000256|HAMAP-Rule:MF_01620};
GN   Name=fadA {ECO:0000256|HAMAP-Rule:MF_01620,
GN   ECO:0000313|EMBL:MBT1486996.1};
GN   ORFNames=IAF07_01015 {ECO:0000313|EMBL:MBT1486996.1}, JRZ91_01015
GN   {ECO:0000313|EMBL:QVH72005.1};
OS   Dickeya dianthicola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=204039 {ECO:0000313|EMBL:MBT1486996.1, ECO:0000313|Proteomes:UP000811537};
RN   [1] {ECO:0000313|EMBL:MBT1486996.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=16LI01 {ECO:0000313|EMBL:QVH72005.1}, and DDI_59W
RC   {ECO:0000313|EMBL:MBT1486996.1};
RA   Ge T.;
RT   "Pangenomic Analysis of Dickeya dianthicola Strains Reveals the Outbreak of
RT   Blackleg and Soft Rot of Potato in USA.";
RL   Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01620}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl-CoA + acetyl-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:0000256|HAMAP-Rule:MF_01620};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|HAMAP-Rule:MF_01620}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains
CC       (FadA). {ECO:0000256|HAMAP-Rule:MF_01620}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01620}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|HAMAP-Rule:MF_01620,
CC       ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; JAHEPW010000002; MBT1486996.1; -; Genomic_DNA.
DR   EMBL; CP069603; QVH72005.1; -; Genomic_DNA.
DR   RefSeq; WP_024109303.1; NZ_WABK01000117.1.
DR   GeneID; 49320133; -.
DR   Proteomes; UP000676146; Chromosome.
DR   Proteomes; UP000811537; Unassembled WGS sequence.
DR   CDD; cd00751; thiolase; 1.
DR   FunFam; 3.40.47.10:FF:000010; Acetyl-CoA acetyltransferase (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; IPR050215; Thiolase-like_sf_Thiolase.
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 {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_01620};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01620};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW   Rule:MF_01620};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|HAMAP-
KW   Rule:MF_01620};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_01620};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01620}.
FT   DOMAIN          5..254
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          262..386
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        91
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01620"
FT   ACT_SITE        343
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01620"
FT   ACT_SITE        373
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01620"
SQ   SEQUENCE   387 AA;  40656 MW;  513EEEE882E2A713 CRC64;
     MENAVIVDAV RTPMGRSKGG AFRQVRAETL SAHLMRSLLS RHPALEADKI DDIYWGCVQQ
     TLEQGFNVAR NAALLAEIPH SVPAVTVNRL CGSSMQALHD AARAIMVGDA GVCLVGGVEH
     MGHVPMTHGV DFHPGLGKSI AKAAVMMGLT AELLARRHHI SREMQDAFAA RSHQRAWAAT
     QSGAFRREII PTNGHNADGA LQPFDYDEVV RAETSIDALA ALRPAFDPAN GTVTAGSSSA
     LSDGAAALLV MSESRALALG LTPRVRIRAM AVVGCDPSVM GYGPVPATHK ALQRAGLSLS
     DIGLFELNEA FAAQALPCIK ALGLMDSLDD KVNLNGGAIA LGHPLGCSGA RLTATLINLM
     EQRNVEFGVA TMCIGLGQGI ATVLERV
//