ID A0A0S8IAS8_9CHLR Unreviewed; 404 AA.
AC A0A0S8IAS8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KPK94566.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KPK94566.1};
GN ORFNames=AMJ88_03510 {ECO:0000313|EMBL:KPK94566.1};
OS Anaerolineae bacterium SM23_ 63.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703387 {ECO:0000313|EMBL:KPK94566.1, ECO:0000313|Proteomes:UP000051685};
RN [1] {ECO:0000313|EMBL:KPK94566.1, ECO:0000313|Proteomes:UP000051685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_ 63 {ECO:0000313|EMBL:KPK94566.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK94566.1}.
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DR EMBL; LJUS01000007; KPK94566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8IAS8; -.
DR PATRIC; fig|1703387.3.peg.813; -.
DR Proteomes; UP000051685; 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; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
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; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:KPK94566.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KPK94566.1}.
FT DOMAIN 11..269
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 278..401
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 95
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 359
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 404 AA; 42373 MW; 6F4AA8EA895FCC4A CRC64;
MTNEHNPRDP VILSAVRTPT GRFQGALGSL SATQLGAIAI AEAVLRAGLS DPSEIDEVLM
GNVVSAGLGQ APARQAAIFA GLPPTVGAST INKVCGSSLK AGMFAAQAIK AGDADLIVAG
GMESMSNAPY LVHGRGGQLR YGHAQLVDAL LHDGLWDPFE DWVMGMAAEW IGEQYEVTRE
AMDHWAFESQ QKSITAMDAG KFDEEIVPVE VPGRKGQVTV VEKDESPRRD TTLEKLSALK
PVFKDDGSVT AGNSSTLNDG AAAVIYASRA KAEALSIKPL ARVIGYAQAA VPPIELFIAP
ARAIPKLLEK IGWDLSDVDL IELNEAFAAQ VLADGYALAD AGWDWEKVNV NGGAVALGHP
IGASGARVLT TLIYALRDRG LKRGIASLCL GGGEAVAMAI EIEQ
//
