ID A0A495Y0D1_9MICO Unreviewed; 407 AA.
AC A0A495Y0D1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:RKT78426.1};
GN ORFNames=DFJ68_1871 {ECO:0000313|EMBL:RKT78426.1};
OS Terracoccus luteus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Terracoccus.
OX NCBI_TaxID=53356 {ECO:0000313|EMBL:RKT78426.1, ECO:0000313|Proteomes:UP000278440};
RN [1] {ECO:0000313|EMBL:RKT78426.1, ECO:0000313|Proteomes:UP000278440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44267 {ECO:0000313|EMBL:RKT78426.1,
RC ECO:0000313|Proteomes:UP000278440};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKT78426.1}.
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DR EMBL; RBXT01000001; RKT78426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495Y0D1; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000278440; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; 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:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000278440};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:RKT78426.1}.
FT DOMAIN 5..275
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 284..405
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 131..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 362
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 407 AA; 42672 MW; 7727DC12E115888C CRC64;
MPEAVIVSTA RSPFGRAFKG SLRDVRPDDL AATVVQAALD KVPALDPSLV EDVYLGCAEP
SGKHGSNMAR VVATLLGLDR TPAATVNRFC ASSAQTTRMA FHAIRAGEGD VFVSAGVECV
SQYTDWAGAG GAKADAQNPR FAEAQERTKR TAESNDTWTD PRERGELPDV YIAMGQTAEN
VATSCGIGRD RQDEWGVTSQ NRAEAAIARG FFDWEITPVT TPDGTVVTKD DGPRAGVTLE
GVQGLNPVFR PEGTVTAGNC CPLNDGAAAL VVMSDTRAKE LGLDPLARVV STAATGLSPE
VMGLGPVEAS RLALQRAGLT IGDLDLYEIN EAFAVQVLAS ADRLGMDYDR LNVNGGAIAI
GHPFGATGAR ITGTIINALR ERDGQFGLET MCVGGGQGMA VVFERLS
//
