ID A0A0M0BTJ6_9ARCH Unreviewed; 432 AA.
AC A0A0M0BTJ6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KON31675.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KON31675.1};
GN ORFNames=AC477_04010 {ECO:0000313|EMBL:KON31675.1};
OS miscellaneous Crenarchaeota group-1 archaeon SG8-32-1.
OC Archaea; Candidatus Bathyarchaeota; MCG-1.
OX NCBI_TaxID=1685124 {ECO:0000313|EMBL:KON31675.1, ECO:0000313|Proteomes:UP000037237};
RN [1] {ECO:0000313|EMBL:KON31675.1, ECO:0000313|Proteomes:UP000037237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8-32-1 {ECO:0000313|EMBL:KON31675.1};
RA Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA Teske A.P.;
RT "New insights into the roles of widespread benthic archaea in carbon and
RT nitrogen cycling.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982}.
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:KON31675.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFWU01000094; KON31675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0BTJ6; -.
DR PATRIC; fig|1685124.3.peg.784; -.
DR Proteomes; UP000037237; Unassembled WGS sequence.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
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; 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; 2.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 2.
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:0000313|EMBL:KON31675.1};
KW Transferase {ECO:0000313|EMBL:KON31675.1}.
FT DOMAIN 6..47
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 83..301
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 308..429
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 432 AA; 46472 MW; E17E8420D1FB39DC CRC64;
MRNEEIVIAG GVRTAIGKFG GSLKDFTAVQ LGSKVIGEVL RKNKLRPIPP NENVMFQPKH
LEHGMIELET KFYDWDDSFE EIAVDEVIMG NVLQAGQGQN VARQATIYGG LPKEVNAFTV
NKVCASGLKA ISLAAQAIMT NSANIIIAGG MESMSNAPYG LPRARWGYIM DLNGQGGIND
LMVLDGLFES FYGYHMGITA ENIAEKYSIS RREQDELGII SHQRALQAIK DGLFKQEITP
ICVPQRKADP IVFDTDERPM ETSIEKMSKL PSIFKKDGTV TAGNSSGIND AAAAVLVMKE
EEAKQYSLKP LARIIGFASG AIDPAYMGVG PVPAIHRALN VAGLSLDDLG LIELNEAFAS
QTLACLKELG IGLDNTNMYG SGISLGHPIG CTGARLVVTL LNAMKRNNIE YGLASMCIGG
GQGMAMVFEL TH
//
