ID A0A1H8EJ19_9BACL Unreviewed; 390 AA.
AC A0A1H8EJ19;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acetyl-CoA acetyltransferases {ECO:0000313|EMBL:SEN19406.1};
GN ORFNames=SAMN05444955_10719 {ECO:0000313|EMBL:SEN19406.1};
OS Lihuaxuella thermophila.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Lihuaxuella.
OX NCBI_TaxID=1173111 {ECO:0000313|EMBL:SEN19406.1, ECO:0000313|Proteomes:UP000199695};
RN [1] {ECO:0000313|EMBL:SEN19406.1, ECO:0000313|Proteomes:UP000199695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46701 {ECO:0000313|EMBL:SEN19406.1,
RC ECO:0000313|Proteomes:UP000199695};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOCQ01000007; SEN19406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8EJ19; -.
DR STRING; 1173111.SAMN05444955_10719; -.
DR Proteomes; UP000199695; 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; -; 1.
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; 2.
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:UP000199695};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SEN19406.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 362..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..251
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 260..381
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 368
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 390 AA; 41727 MW; E67453E247010EFB CRC64;
MQDRDAVIID AVRTPIGRKK GSLSRTRPDE MAAFLLKELV SRNRLNPSEV EDIKMGCVTQ
IGEQGYNIGR LAALIAGFPV EVCGVSVNRM CGSSLETLAQ AAHAIMAGMA DCVIAAGVES
MNRVPMGSDG GSFSERLLER YNIIPQGFSA ELIAEKWNLS REELDQFSLD SHRKAIQAQK
EGRFANEIIP IECQTSAGEP MLLTEDETPR PDTSLETLAG LRPSFQSDGK VTAGNSSQIS
DGAAAVLLTS RKKAESLGLT PRARVVATAL AGVDPEIMLT GIIPATKKVL ERAGLTLDEI
DVFEVNEAFA SVVLAWQREI GPDPEKVNPN GGAIALGHPL GASGARMTAT LINELERREG
RYGLATMCIG FGMAVAVILE REGRHGSKTL
//
