ID I0XLD3_9LEPT Unreviewed; 441 AA.
AC I0XLD3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:EID99690.1};
GN ORFNames=LEP1GSC185_0688 {ECO:0000313|EMBL:EID99690.1};
OS Leptospira licerasiae serovar Varillal str. VAR 010.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049972 {ECO:0000313|EMBL:EID99690.1, ECO:0000313|Proteomes:UP000004889};
RN [1] {ECO:0000313|EMBL:EID99690.1, ECO:0000313|Proteomes:UP000004889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VAR 010 {ECO:0000313|EMBL:EID99690.1};
RX PubMed=23145189; DOI=10.1371/journal.pntd.0001853;
RA Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P.,
RA Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M., Webster N.J.,
RA Vinetz J.M., Matthias M.A.;
RT "Whole Genome Analysis of Leptospira licerasiae Provides Insight into
RT Leptospiral Evolution and Pathogenicity.";
RL PLoS Negl. Trop. Dis. 6:E1853-E1853(2012).
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:EID99690.1}.
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DR EMBL; AHOO02000014; EID99690.1; -; Genomic_DNA.
DR RefSeq; WP_008593252.1; NZ_AHOO02000014.1.
DR AlphaFoldDB; I0XLD3; -.
DR PATRIC; fig|1049972.3.peg.3914; -.
DR OrthoDB; 315072at2; -.
DR Proteomes; UP000004889; 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; 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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EID99690.1}.
FT DOMAIN 9..232
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 307..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; 48190 MW; 607EBA93C1C3BB44 CRC64;
MKLEKKLAIC TPLRTPFAQI AKGLGAYPAH HLGKIVAESI IQKSGIKKED IDGVIVGEGF
PSSPNPARVI ANLIGLRDEI PSITLSNNCV SGLEAVSEAA RRIVLGEGEV FLVIGEESQT
DMPFVVKNAR LNKKTGSLEK LNKLLPDNLP EGVELRDTLE DGLGDGENSY GMQVTAEILA
QNYELSREVT DKVAFESFKR TYDASTEGKY EPFIIPIRDQ EGNMLKIDEA IELRKGLVEN
PSRMGRAMLL FDNPQSKFED FKKKYGKDLK RTHEPTVSIF NASPRSDGAA GVIITTVEKA
KSLGLKIEGL LSGWRMKGVH PNLMGLGQAV ATEGLLEDLQ LKLEDMDYIE IHEAYAATAV
AAMEQLKTDT GWDWEKSFDE KKINPNGGSI AIGHPFGATG VRLVNNAIMD LQEDPNANRV
LLTACAHGGI AGSMLIERYK D
//
