ID A0A1Y5RAU1_9RHOB Unreviewed; 393 AA.
AC A0A1Y5RAU1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Beta-ketothiolase BktB {ECO:0000313|EMBL:SLN13140.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:SLN13140.1};
GN Name=bktB {ECO:0000313|EMBL:SLN13140.1};
GN ORFNames=PSA7680_00240 {ECO:0000313|EMBL:SLN13140.1};
OS Pseudoruegeria aquimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoruegeria.
OX NCBI_TaxID=393663 {ECO:0000313|EMBL:SLN13140.1, ECO:0000313|Proteomes:UP000193409};
RN [1] {ECO:0000313|EMBL:SLN13140.1, ECO:0000313|Proteomes:UP000193409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7680 {ECO:0000313|EMBL:SLN13140.1,
RC ECO:0000313|Proteomes:UP000193409};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFQ01000001; SLN13140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5RAU1; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000193409; Unassembled WGS sequence.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
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 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; 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|RuleBase:RU003557,
KW ECO:0000313|EMBL:SLN13140.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193409};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SLN13140.1}.
FT DOMAIN 4..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..390
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 89
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 393 AA; 40434 MW; 9E36A28A3E99DE11 CRC64;
MEPVVIVSAA RTAIGSFGGS LKSLSPTELG ATTAKAAIER AGLTADAVEQ SFYGNVIHTE
ARDMYISRTV AMAAGVPESS PALTVNRLCG SGLQAVVSAI QVLMLGDAKI ALAGGTESMS
RAGYLLPAAR WGQKMGDTGA IDMMTAALHD PFGHGHMGIT AENISEQYGI DRAAQDAFAL
ESHRRAAAAI EAGHFKEQIV PVTVTERRKE VVFDTDEHVR PNATLADMEK LRPVFKKDGT
VTAGNASGIN DGAASLVLMT ESEAKARGLA PLARVVSYGH AGVDPKIMGM GPVPAMENAM
KRAGITADDL DVVESNEAFA AQACAVSQQL GLDPAKVNPN GGAVALGHPV GASGAIIATK
LLYELKRTGG RYGAATMCIG GGQGIALIVE NAG
//
