ID M3EQT2_9LEPT Unreviewed; 441 AA.
AC M3EQT2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:EMF83413.1};
GN ORFNames=LEP1GSC188_1958 {ECO:0000313|EMBL:EMF83413.1};
OS Leptospira weilii serovar Topaz str. LT2116.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1088540 {ECO:0000313|EMBL:EMF83413.1, ECO:0000313|Proteomes:UP000011770};
RN [1] {ECO:0000313|EMBL:EMF83413.1, ECO:0000313|Proteomes:UP000011770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2116 {ECO:0000313|EMBL:EMF83413.1,
RC ECO:0000313|Proteomes:UP000011770};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Tulsiani S.M., Graham G.C., Burns M.-A.,
RA Dohnt M.F., Smythe L.D., McKay D.B., Craig S.B., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) 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:EMF83413.1}.
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DR EMBL; AHOR02000013; EMF83413.1; -; Genomic_DNA.
DR AlphaFoldDB; M3EQT2; -.
DR Proteomes; UP000011770; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000011770};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EMF83413.1}.
FT DOMAIN 13..233
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 306..438
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 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 425
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 441 AA; 47228 MW; CC9BDAB7FF1805C2 CRC64;
MKLTKPLALC TPRRTPFAQI AKALGPYPGH HLGKIVAEDI LAKSKLKPSQ IDGVVVGEGF
SNAPNSARVI ANLVGMRDEI ACITVANNCV SGMEAVAEAA RRIILGEGEV FLAIGEESQT
SMPFIVKNAR LNKKAGSLDK LKKLLPDNLP EGVELRDTLE DGLGDGETSY GMQVTAEIVA
QNYALSREVQ DKVAFESFKR ALEASKAGRY APYIIPMKDD EGNELAIDEA VGLREGLVEN
PTRMGRAMLM FDNPGMKFEE FKTKYAKDLK KSHGPTVSIF NASPRSDGAA GVIVTTVEKA
KELGLTIEAV ISGWHMKGVH PNNMGIGQAE ATKALLADVG LKIQDIDYVE IHEAFAATAV
GALEQIKMDT GWDWEKSFDA KKINPNGGSI AIGHPFGATG IRLIANAIMD LKEDSSANKV
VITACAHGGI AGSMLIERFK G
//
