ID M3HIM9_LEPBO Unreviewed; 349 AA.
AC M3HIM9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:EMF97950.1};
GN ORFNames=LEP1GSC123_4178 {ECO:0000313|EMBL:EMF97950.1};
OS Leptospira borgpetersenii str. 200701203.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193007 {ECO:0000313|EMBL:EMF97950.1, ECO:0000313|Proteomes:UP000011783};
RN [1] {ECO:0000313|EMBL:EMF97950.1, ECO:0000313|Proteomes:UP000011783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200701203 {ECO:0000313|EMBL:EMF97950.1,
RC ECO:0000313|Proteomes:UP000011783};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA Vinetz J.M., Sutton G.G., 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:EMF97950.1}.
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DR EMBL; AKWO02000106; EMF97950.1; -; Genomic_DNA.
DR AlphaFoldDB; M3HIM9; -.
DR BioCyc; LBOR1193007:G11KN-1818-MONOMER; -.
DR Proteomes; UP000011783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
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; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011783};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EMF97950.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 329..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..176
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 226..348
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 37
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 305
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 335
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 349 AA; 37177 MW; 4D8F3A4B85A57E74 CRC64;
MGCVSQVDDQ AACIARYAVM SALWPNSVPG YTVNRFCGSG LQAVNNAANH VQSGSMQIAL
GGGVESMSRV KMGADMNGRD FNIGNPNIQK HYNLVPQGIS ADLIATKFGI SREEADRFAE
SSQIKADKAI KEGYFKKSIV PVKIEDGTIV DTDENPRIES TFEWLSDLAP VFKTIGEKEL
DAIALKSYPE IPKINHIHTL GNSSGIVDGA ASVLLASDEG IKKYGLKPRA KIVAMASTGE
DPTIMLTGPV SASKKALAIA GLKADDIDLW EINEAFASVV LYTQKSLNIP LEKINVNGGS
ISLGHPLGAT GAILLGTALD ELERRQKRYA LITLCIGGGM GIATIIERM
//
