ID A8LD76_FRASN Unreviewed; 388 AA.
AC A8LD76;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=Franean1_4577 {ECO:0000313|EMBL:ABW13950.1};
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW13950.1};
RN [1] {ECO:0000313|EMBL:ABW13950.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW13950.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT "Complete sequence of Frankia sp. EAN1pec.";
RL Submitted (AUG-2007) 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 ---------------------------------------------------------------------------
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; CP000820; ABW13950.1; -; Genomic_DNA.
DR AlphaFoldDB; A8LD76; -.
DR STRING; 298653.Franean1_4577; -.
DR KEGG; fre:Franean1_4577; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_1_11; -.
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; 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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:ABW13950.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ABW13950.1}.
FT DOMAIN 5..257
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 265..386
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 86
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 344
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 374
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 388 AA; 39938 MW; 7D5D870B463918A5 CRC64;
MAQAVIVSAV RTPIATSFKG TLRDTSAEEL ATAVVRAAVD RSGLAPEDVD DVILAEELAG
GGDIARYAAF AAGLTAAPGQ AVNRHCAASL AAVGNAAATI RAGMDRAVVA GGTHSSSMNP
RLSWRVPGSD EPRAGFNPTF PYYEGATDDV TLAVGWNTAQ EVGITRAEMD AWAKRSHDRA
IAAIDAGVFD DEIVPIDVVV AGEKVRFAVD EHPRRTSTLE KLATLKPLHP EIEGFGITAG
NASGVNDAAA ALMLVTDDLA RDRGLTPLAR VRAWAALGVA PHRTGMAGVE VIPRVLERAG
IGVADVDAWE INEAFASVPI AACRLLGIPD DLVNQYGSGC SLGHPVAASG ARMLTTLTHH
LRRRGGGIAV AAMCAAGGQG GAVVIEAP
//
