ID F4HBC2_GALAU Unreviewed; 435 AA.
AC F4HBC2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=3-ketoacyl-CoA thiolase {ECO:0000313|EMBL:AEC17489.1};
GN OrderedLocusNames=UMN179_01472 {ECO:0000313|EMBL:AEC17489.1};
OS Gallibacterium anatis (strain UMN179) (Pasteurella anatis).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Gallibacterium.
OX NCBI_TaxID=1005058 {ECO:0000313|EMBL:AEC17489.1, ECO:0000313|Proteomes:UP000006908};
RN [1] {ECO:0000313|EMBL:AEC17489.1, ECO:0000313|Proteomes:UP000006908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN179 {ECO:0000313|EMBL:AEC17489.1,
RC ECO:0000313|Proteomes:UP000006908};
RX PubMed=21602325; DOI=10.1128/JB.05177-11;
RA Johnson T.J., Fernandez-Alarcon C., Bojesen A.M., Nolan L.K., Trampel D.W.,
RA Seemann T.;
RT "Complete genome sequence of Gallibacterium anatis strain UMN179, isolated
RT from a laying hen with peritonitis.";
RL J. Bacteriol. 193:3676-3677(2011).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP002667; AEC17489.1; -; Genomic_DNA.
DR RefSeq; WP_013746261.1; NC_015460.1.
DR AlphaFoldDB; F4HBC2; -.
DR STRING; 1005058.UMN179_01472; -.
DR KEGG; gan:UMN179_01472; -.
DR PATRIC; fig|1005058.3.peg.1465; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_6; -.
DR Proteomes; UP000006908; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 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; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 15..286
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 295..433
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 435 AA; 48161 MW; 9C74432149354C89 CRC64;
MSEQPVLTTS KGARVAVVDG IRTPFIKKNT LFKEARAKDL GAMVANELLS RLAVPKDKIE
QVVFGQVIQD PDIPNLSREI SLLLNMPKAQ SYTVSSSCPT GLQVLINLSN SILMGNTHYA
LAGGADSLSN APIRLNSHLI QLFRDVMAAK SYEEKYRLLR QITWQDFKLQ ALNLKDPLTQ
LSLSAVSEQM AQDFHLSRQE LDEYAARSHR LAYQAWQSGE LRQQVMVSFP PPYKDFVVSD
NQIEKHVKPE FYQKFKPFNG KNYGTATDWN TSHSCDGAAA VLLMNEHTAK AEGLNILGYI
RHYTMTANDV WKNMFVGVTY SIAKVLQNAN MRLSDLDLID IHETSSAQIL SNLKLIESET
FARQHLNRST AIGNIDMSKL NILGGSLAYG NPRAVSSLRL IIQSLYALKQ RGGGRSLIAS
SGLGGIGGAM ILESE
//
