ID A0A255GL88_9ACTN Unreviewed; 383 AA.
AC A0A255GL88;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:OYO16579.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:OYO16579.1};
GN ORFNames=CGZ93_17605 {ECO:0000313|EMBL:OYO16579.1};
OS Enemella dayhoffiae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Enemella.
OX NCBI_TaxID=2016507 {ECO:0000313|EMBL:OYO16579.1, ECO:0000313|Proteomes:UP000216311};
RN [1] {ECO:0000313|EMBL:OYO16579.1, ECO:0000313|Proteomes:UP000216311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 130396 {ECO:0000313|EMBL:OYO16579.1,
RC ECO:0000313|Proteomes:UP000216311};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-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:OYO16579.1}.
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DR EMBL; NMVQ01000047; OYO16579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255GL88; -.
DR OrthoDB; 4440515at2; -.
DR Proteomes; UP000216311; 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; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43365; BLR7806 PROTEIN; 1.
DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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 ECO:0000313|EMBL:OYO16579.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216311};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OYO16579.1}.
FT DOMAIN 5..252
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 260..382
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 89
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 369
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 383 AA; 40194 MW; 5B14D381E1A29EAC CRC64;
MGEAYIVDAV RTPVARRGGD LANLHPADLG AHSLRALVER TGIDPAAVED VILGCVDTIG
GQAGDVARTA WLVAGLPEEV PGTTIDRQCG SSQQAVHFAA QAVLSGTSDL VVAGGLQQMS
SIPISAAMLT GQQYGYDDPF TGSTGWRARY GTEPPSQFRS AQMIADRWKC DRAAMERFAL
ASHEKALAAI DAGRFDDEIA PVGDFAVDSC PRRGTSLEKM AALDPLEDGG SITAAVASQI
CDASAALLIA SERGVRTHGL TPMARVHHLS VRGADPVWML TAPIPATAHA LQRTGLDIDD
IDLFEVNEAF ASVVLAWLAE SGADPDRVNV NGGAIALGHP LGATGARLMT TMLHELRRRG
GRYGLQVMCE GGGQANVTIV ERL
//
