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Database: UniProt
Entry: W1J088_9GAMM
LinkDB: W1J088_9GAMM
Original site: W1J088_9GAMM 
ID   W1J088_9GAMM            Unreviewed;       392 AA.
AC   W1J088;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 53.
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:CDL82880.1};
GN   ORFNames=XCR1_1730004 {ECO:0000313|EMBL:CDL82880.1};
OS   Xenorhabdus cabanillasii JM26.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=1427517 {ECO:0000313|EMBL:CDL82880.1, ECO:0000313|Proteomes:UP000019197};
RN   [1] {ECO:0000313|EMBL:CDL82880.1, ECO:0000313|Proteomes:UP000019197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JM26 {ECO:0000313|EMBL:CDL82880.1,
RC   ECO:0000313|Proteomes:UP000019197};
RA   Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT   "Draft genome sequence and annotation of the entomopathogenic bacterium,
RT   Xenorhabdus cabanillasi strain JM26.";
RL   Submitted (NOV-2013) 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=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: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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDL82880.1}.
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DR   EMBL; CBXE010000083; CDL82880.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1J088; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000019197; Unassembled WGS sequence.
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 {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          9..259
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          267..391
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        96
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01620,
FT                   ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        348
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01620,
FT                   ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        378
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01620,
FT                   ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   392 AA;  41733 MW;  3D3575DAC9E57CFB CRC64;
     MRSENMENVV IIDGIRTPMG RSKGGVFRQI RAEDLSAHLM KSILKRNPSV QPEHIDDISW
     GCVQQTLEQG FNIARNSALL AGIPHSVPAV TVNRLCGSSM QSLHDSARMI MTGDANIALI
     GGVEHMGHVP MTHGVDFHPK LSRNVAKAAG VMGLTAEMLA KMYGISREIQ DEFAMRSHQR
     AAQATESKAF AGEIASIQGH DADGNLKLID FDEVIRPDTN LKDLAALRPV FDPVTGSVTA
     GNSSALSDGA SAMLIMSESK ARELGLTPRA RIRSMAVVGC DPSIMGYGPV PATQMALKKA
     GLNLSDIGMI ELNEAFAAQS LACIKGLKLL DSMDDRINLN GGAIALGHPL GCSGARITTT
     LLNLMERKDV QFGLATMCIG LGQGIATIVE RV
//
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