ID A0A0N0ZB67_9GAMM Unreviewed; 388 AA.
AC A0A0N0ZB67;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=3-ketoacyl-CoA thiolase/acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KPD03688.1};
DE EC=2.3.1.- {ECO:0000313|EMBL:KPD03688.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:KPD03688.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KPD03688.1};
GN ORFNames=M992_0978 {ECO:0000313|EMBL:KPD03688.1};
OS Moellerella wisconsensis ATCC 35017.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Moellerella.
OX NCBI_TaxID=1354267 {ECO:0000313|EMBL:KPD03688.1, ECO:0000313|Proteomes:UP000053226};
RN [1] {ECO:0000313|EMBL:KPD03688.1, ECO:0000313|Proteomes:UP000053226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35017 {ECO:0000313|EMBL:KPD03688.1,
RC ECO:0000313|Proteomes:UP000053226};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, 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:KPD03688.1}.
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DR EMBL; LGAA01000009; KPD03688.1; -; Genomic_DNA.
DR RefSeq; WP_053907557.1; NZ_LGAA01000009.1.
DR AlphaFoldDB; A0A0N0ZB67; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000053226; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
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,
KW ECO:0000256|RuleBase:RU003557}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000053226};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KPD03688.1}.
FT DOMAIN 4..254
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 261..387
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 344
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 374
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 388 AA; 41335 MW; A59C4E877A237014 CRC64;
MENVVIVDAI RTPMGRSKGG VFRHVRAEDL SAHLMQAIFL RNPNADKSEL NDIIWGCVQQ
TLEQGFNIAR NAALLTDIPH SVPAVTVNRL CGSSMQALHD ASRLIMTGDA HSILIGGVEH
MGHIPMTHGV DFNPKIALKI AKAAGAMGLT AEMLATIYKI SRQQQDAFAL RSHVKAAEAT
KQGQFTNEIV PIEGHDSEGN LISIDYDEVI RFDANLNDLT ALRPAFNPVN GTVTAGNSSA
LSDGASAMLI TSESYARANG LKPRARIRSM AVIGCDPSTM GYGPVPASEI ALKRAGLSLA
DIDVIELNEA FAAQSLACMK GFKLSESTIE EKVNLQGGAI ALGHPLGCSG TRITTTLLNQ
LERQQGQFGL ATMCIGLGQG ISTIIERL
//
