ID A0A1Y4D020_9FIRM Unreviewed; 393 AA.
AC A0A1Y4D020;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00044137};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
DE AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000256|ARBA:ARBA00030755};
GN ORFNames=B5F80_00695 {ECO:0000313|EMBL:OUO48891.1};
OS Megasphaera sp. An286.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1965622 {ECO:0000313|EMBL:OUO48891.1, ECO:0000313|Proteomes:UP000195529};
RN [1] {ECO:0000313|EMBL:OUO48891.1, ECO:0000313|Proteomes:UP000195529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An286 {ECO:0000313|EMBL:OUO48891.1,
RC ECO:0000313|Proteomes:UP000195529};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO48891.1}.
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DR EMBL; NFIY01000001; OUO48891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4D020; -.
DR Proteomes; UP000195529; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000195529};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OUO48891.1}.
FT DOMAIN 4..261
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..390
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 393 AA; 40496 MW; 54D2A35A50856794 CRC64;
MKEVVIVSAC RTAIGKFGGS LKDVPAADLG AIVIEEAIKR AGIDKAIVDE VVMGNVLQAA
QGQNPARQAM IKAGLPVETP AMTINKVCGS GLRCVSLAAQ MIKAGDADVI VAGGMENMSA
APYAIPKARY GYRMGNGVLV DTMIKDGLWD AFNDYHMGIT AENVAEQFGV SREDQDALGA
RSQQKACEAI KSGAFKDQIV PVVIHGKKGD TVFDTDEFPR EGTTVESLAK LKPAFKKGGT
VTAGNASGIN DGAAAFVVMS AEKAAELGLK PMAKVVSYAS AGVDPSIMGI GPVPSSRKAL
EKAGLTADDL SLVEANEAFA AQSVYVVREL GLDMSKVNIH GGAIALGHPI GASGARILVT
LLYGLKEVGG KYGLATLCIG GGQGTACIVE NID
//
