ID A0A3N4U2C6_9BURK Unreviewed; 394 AA.
AC A0A3N4U2C6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:RPE64993.1};
GN ORFNames=EDC62_2117 {ECO:0000313|EMBL:RPE64993.1};
OS Tibeticola sediminis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Tibeticola.
OX NCBI_TaxID=1917811 {ECO:0000313|EMBL:RPE64993.1, ECO:0000313|Proteomes:UP000272193};
RN [1] {ECO:0000313|EMBL:RPE64993.1, ECO:0000313|Proteomes:UP000272193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101684 {ECO:0000313|EMBL:RPE64993.1,
RC ECO:0000313|Proteomes:UP000272193};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-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:RPE64993.1}.
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DR EMBL; RKQL01000005; RPE64993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4U2C6; -.
DR OrthoDB; 6139495at2; -.
DR Proteomes; UP000272193; Unassembled WGS sequence.
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; 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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000272193};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:RPE64993.1}.
FT DOMAIN 5..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 272..393
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 41386 MW; ACD45756D9108AF4 CRC64;
MRREVVIASG VRTAIGTYGG SLKDVPPTEL ASLVVRESLA RAGVEGKDVG HVVFGHVVNT
EPKDMYLSRV AALNGGCPEE TPAYNVNRLC GSGLQAIVSA SQSILLGDCD VAIGGGAENM
SRAPYASLNT RWGARMGDTK LVDMMVGALH DPFHTIHMGV TAEHVAERYR ISREQQDALA
VESHQRAQRA TEAGYFKSQI VPVMLKGRKG ETAFDTDEHF RPNCTLADLA KLKPVFVKEN
GTVTAGNASG INDAAAAVVL MEAHAAKARG VQPLARLVAY AHAGVDPKYM GIGPVPASKL
ALQRAGLTVN DLDVVEANEA FAAQACAVTC ELGLDPAKVN PNGSGISLGH PIGATGALIT
VKAIHELHRI QGRYALVTMC IGGGQGIAAI FERL
//