ID A0A0N7J8H5_9BURK Unreviewed; 416 AA.
AC A0A0N7J8H5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Beta-ketothiolase BktB {ECO:0000313|EMBL:ALK88208.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:ALK88208.1};
GN Name=bktB_1 {ECO:0000313|EMBL:ALK88208.1};
GN ORFNames=L63ED372_00987 {ECO:0000313|EMBL:ALK88208.1};
OS Limnohabitans sp. 63ED37-2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1678128 {ECO:0000313|EMBL:ALK88208.1, ECO:0000313|Proteomes:UP000059510};
RN [1] {ECO:0000313|EMBL:ALK88208.1, ECO:0000313|Proteomes:UP000059510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=63ED37-2 {ECO:0000313|EMBL:ALK88208.1,
RC ECO:0000313|Proteomes:UP000059510};
RA Ahn J.-H., Kim S.B.;
RT "Limnohabitans sp. 2 strains.";
RL Submitted (JUN-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}.
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DR EMBL; CP011774; ALK88208.1; -; Genomic_DNA.
DR RefSeq; WP_062403971.1; NZ_CP011774.1.
DR AlphaFoldDB; A0A0N7J8H5; -.
DR STRING; 1678128.L63ED372_00987; -.
DR KEGG; lih:L63ED372_00987; -.
DR PATRIC; fig|1678128.3.peg.983; -.
DR OrthoDB; 6139495at2; -.
DR Proteomes; UP000059510; Chromosome.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
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 PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:ALK88208.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059510};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ALK88208.1}.
FT DOMAIN 17..281
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 291..411
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 98
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 369
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 399
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 416 AA; 43443 MW; D4D230610A09BE6E CRC64;
MSAKGFFNAF ADVWMHEGVR TPMVDYCGAL GHISPTDLGI KAAREALKRA GIAATEIGSV
ITGNMAPGDF DQFVLPRHIG LYAGVPQEVP AIMVQRICGT GFELFRQAGE QIEAGVCEAA
LVVGTESMTR NPIAAFDHRT GFKLGAPVGF KDFMWEALKD PAAGINMIQT AENLAKKYSI
TREEVDQFAC DSFAKAVAAQ AAGFHAGEIV PVVTEKFELE GYIARGIKLQ GKVTEVNADT
HPRISPADVL GKLRPVYEGG VQTGGNSSAL VDAAAACVVT SGTYAKANGK KPLARVVAAA
AVGVPPEIMG IGPAPAIRLL LERTGLKLSD IGRFEINEAQ GAQTLAVGRE LGLDLSKLNV
NGGAIALGHP LAATGVRLTI TLARELQRSG LRYGISSACV GGGQGIALLI ENPEAV
//