ID D5H242_LACCS Unreviewed; 387 AA.
AC D5H242;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00044137};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
DE AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000256|ARBA:ARBA00030755};
GN Name=atoB {ECO:0000313|EMBL:CBL50077.1};
GN OrderedLocusNames=LCRIS_00630 {ECO:0000313|EMBL:CBL50077.1};
OS Lactobacillus crispatus (strain ST1).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=748671 {ECO:0000313|EMBL:CBL50077.1, ECO:0000313|Proteomes:UP000002371};
RN [1] {ECO:0000313|EMBL:CBL50077.1, ECO:0000313|Proteomes:UP000002371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST1 {ECO:0000313|EMBL:CBL50077.1,
RC ECO:0000313|Proteomes:UP000002371};
RX PubMed=20435723; DOI=10.1128/JB.00399-10;
RA Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., Auvinen P.,
RA Edelman S., Westerlund-Wikstrom B., Korhonen T.K., Paulin L., Kankainen M.;
RT "Genome sequence of Lactobacillus crispatus ST1.";
RL J. Bacteriol. 192:3547-3548(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ST1;
RA Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., Auvinen P.,
RA Edelman S., Westerlund-Wikstroem B., Korhonen T.K., Paulin L.,
RA Kankainen M.;
RT "Genome Sequence of Lactobacillus crispatus ST1.";
RL Submitted (MAR-2010) 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; FN692037; CBL50077.1; -; Genomic_DNA.
DR RefSeq; WP_013086022.1; NC_014106.1.
DR AlphaFoldDB; D5H242; -.
DR KEGG; lcr:LCRIS_00630; -.
DR PATRIC; fig|748671.3.peg.609; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_9; -.
DR Proteomes; UP000002371; 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; -; 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 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; 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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:CBL50077.1}.
FT DOMAIN 4..255
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 263..384
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 342
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 372
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 387 AA; 41236 MW; A69A0F2AC0D3E80D CRC64;
MKDIYIVAAK RTPFGKYRGF FKDASAIDLG VMALKGTMKA GNIKPADVQA LFMGNVLDTG
LGENMARQVA LHSGMSEASA AVTINEVCGS SLKALRLAQG QMELGDLDLV AVGGSESMTN
APYFVKKENK NDPADHLVST MLNDGLMDAF SGKHMGITAE NVAEKYHVSR QDMDEFALQS
HQKAAAAVKS GFFDNEILDV EIDGQSLDHD EPIRPDTTLE ALSNLKPVFK ADGEVTAGNS
SPLTDGASML VLATKEKMKE LGLTPIAKLG EFAEAGFDPA LMGYTPYYAV KKLLKKTGRN
FDDYDIIELN EAFAAQSVAV ARDLQIPTDK LNIMGGAIAL GHPLGATGTR LVASAISGLK
KRKGRRALVT LCIGGGQAIA YEIENAE
//
