ID A0A0N1PEM5_LEPSE Unreviewed; 411 AA.
AC A0A0N1PEM5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE SubName: Full=Putative 3-ketoacyl-CoA thiolase-like protein {ECO:0000313|EMBL:KPI87383.1};
GN ORFNames=ABL78_3517 {ECO:0000313|EMBL:KPI87383.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI87383.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI87383.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI87383.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {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:KPI87383.1}.
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DR EMBL; LJSK01000090; KPI87383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1PEM5; -.
DR EnsemblProtists; KPI87383; KPI87383; ABL78_3517.
DR VEuPathDB; TriTrypDB:Lsey_0090_0010; -.
DR OMA; MTAFPEP; -.
DR OrthoDB; 1826604at2759; -.
DR Proteomes; UP000038009; 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; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 5..258
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..406
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 67
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 364
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 411 AA; 43919 MW; E60E4DA04014B549 CRC64;
MKADTLKLAT SAVAGLLNKT SLDPQEVNHI VWGNVVLDGS VHNCAREIVC DLNLPETITG
NLTSMACASG LSALAQACML IESGHADVVI AGGSDSISSI EMALPRSVMH GMMMSKKKGI
MGFFKEAGYN PAAWFPKGIA LAERSTGKTM GWHGDVIGEL NNISREEQEI FAVASHEKAA
RAEKAGYFED EIVPVSMEKN GKTVQVTKDD LLQRDTEKMK SKLSNLKPVF RRDKGTITAA
TSSALTDGGS AMLVMSEEKA KKLGFPTDVR VASWHFSGIE PYPQLLLAPV LGWGSALQKA
GLSPKDIDLF EIHEAFAAQV LATLKCLKSQ EFFDRYAKGT KAVLSEDIDR SKLNVNGSSL
AFGHPFAATG GRIVTSLASE LRRTGKRRGL VSICAAGGLG GVAILEHTPK K
//
