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Database: UniProt
Entry: A0A1X1BW46_9GAMM
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Original site: A0A1X1BW46_9GAMM 
ID   A0A1X1BW46_9GAMM        Unreviewed;       387 AA.
AC   A0A1X1BW46;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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:ORM52786.1};
GN   ORFNames=HA41_10710 {ECO:0000313|EMBL:ORM52786.1};
OS   Pantoea conspicua.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=472705 {ECO:0000313|EMBL:ORM52786.1, ECO:0000313|Proteomes:UP000193933};
RN   [1] {ECO:0000313|EMBL:ORM52786.1, ECO:0000313|Proteomes:UP000193933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24534 {ECO:0000313|EMBL:ORM52786.1,
RC   ECO:0000313|Proteomes:UP000193933};
RX   PubMed=28255640;
RA   Palmer M., Steenkamp E.T., Coetzee M.P., Chan W.Y., van Zyl E.,
RA   De Maayer P., Coutinho T.A., Blom J., Smits T.H., Duffy B., Venter S.N.;
RT   "Phylogenomic resolution of the bacterial genus Pantoea and its
RT   relationship with Erwinia and Tatumella.";
RL   Antonie Van Leeuwenhoek 0:0-0(2017).
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:ORM52786.1}.
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DR   EMBL; MLFN01000026; ORM52786.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1BW46; -.
DR   STRING; 472705.GCA_001743465_03388; -.
DR   OrthoDB; 9764638at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000193933; 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          4..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                   ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        343
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01620,
FT                   ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        373
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01620,
FT                   ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   387 AA;  41226 MW;  1333E5291CC928D9 CRC64;
     MENVVIIDAV RTPMGRSKGG AFRHVRAEDL SAHLMRELLS RNPAINPASL DDIVWGCVQQ
     TLEQGFNIAR NAALLAEIPH SVPATTVNRL CGSSMQALHD AARAIMVGDA HNCLIGGVEH
     MGHVPMSHGV DFHPGLGRTV AKAAGMMGLT AEMLARMHHI SREQQDAFAL RSHQRAWQAT
     QRGDFKSEIV ATAGHDSDGI LKRYDYDEVI REETSAEGLA ALRPAFDPVN GTVTAGTSSA
     LSDGAAAMLV MSESRARELG LTPRARIRSM AVVGCDPSIM GYGPVPASKL ALKRAGLSVN
     DIDVFELNEA FAAQTLPCIK DLGLLDRLDE KVNLNGGAIA LGHPLGCSGA RISTTLLNIM
     ARRDAQFGLA TMCIGLGQGI ATVFERL
//
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