ID C1D2D4_DEIDV Unreviewed; 431 AA.
AC C1D2D4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Putative acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase) {ECO:0000313|EMBL:ACO47573.1};
GN OrderedLocusNames=Deide_1p01300 {ECO:0000313|EMBL:ACO47573.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OG Plasmid pDeide1 {ECO:0000313|Proteomes:UP000002208}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47573.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO47573.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RC PLASMID=pDeide1 {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001115; ACO47573.1; -; Genomic_DNA.
DR RefSeq; WP_012694696.1; NC_012527.1.
DR AlphaFoldDB; C1D2D4; -.
DR KEGG; ddr:Deide_1p01300; -.
DR HOGENOM; CLU_031026_2_2_0; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000002208; Plasmid pDeide1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF2; 3-OXOADIPYL-COA_3-OXO-5,6-DEHYDROSUBERYL-COA THIOLASE; 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 Plasmid {ECO:0000313|EMBL:ACO47573.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ACO47573.1}.
FT DOMAIN 18..298
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 306..428
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 103
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 415
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 431 AA; 45311 MW; CDD8878F6885E7C1 CRC64;
MNPPHSSTSV QQLHDRDVVI VSAVRSPIGA LRGALGTVRP DDLAAMVIRE AVSRAGAAPD
QIEEVILGCA NQAGEDNRNV ARMAALLAGF PHEVAGLTVN RLCASGLSAI NTAARAIRNG
DGDVYVAGGV ESMTRAPLSM PKGAQPFANG NVTAYDTTLG WRYPNPAMEA LFPLEAMGET
AENIVDRSRA GEIVGGEITR EHQDAYALES QRRAVTALNA GVYREEIMAI EVKGRRGTTL
FDTDEHPRYT REGNSFALAT SMDTLAGLRP AFRKNGTVTA GNASGLNDGA AAVVLMSAGH
ARKLGLKPLA RWVGAASAGV DPRVMGLGPV PATRKLMDRL GMTLAEVDLV EINEAFAAQA
IACMRELSVP HDRLNVHGGA IALGHPLGMS GARLVTTLTH ELHRRSARYG VVALCVGVGQ
GEAALIERVE A
//
