ID A0A1W1UE45_9PAST Unreviewed; 393 AA.
AC A0A1W1UE45;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:SMB79330.1};
GN ORFNames=SAMN05660772_00332 {ECO:0000313|EMBL:SMB79330.1};
OS Pasteurella testudinis DSM 23072.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=1122938 {ECO:0000313|EMBL:SMB79330.1, ECO:0000313|Proteomes:UP000192408};
RN [1] {ECO:0000313|EMBL:SMB79330.1, ECO:0000313|Proteomes:UP000192408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23072 {ECO:0000313|EMBL:SMB79330.1,
RC ECO:0000313|Proteomes:UP000192408};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWWV01000002; SMB79330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1UE45; -.
DR STRING; 1122938.SAMN05660772_00332; -.
DR Proteomes; UP000192408; 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; -; 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; PTHR18919:SF164; ACETYL-COA ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SMB79330.1}.
FT DOMAIN 4..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..392
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 393 AA; 40951 MW; 14778ABBE295BAC0 CRC64;
MENIVIVSAV RTPIGSFNGA LATVSAVDLG ALVIEEVLKR ANVAADQVDE VIMGNVLQAG
LGQNPARQAA LKAGIQQQAA ALTINKVCGS GLKSVVLGAQ AIRSGDADVV VVGGMENMSQ
APYLLSSKVR LGARMGNLTL QDTMIEDGLT CAINHYHMGI TAENIAEHYA LSRQQQDEFA
LRSQTLAAQA VRSGVFDAEI IPVPVKTRKG ETLFSRDEHP KFDSTLEQLA ALKPAFKKEG
TVTAGNASGI NDGAAALLLM RESQALAAGL QPLARIRSYA SAGNDPAVMG LGPIQATQNA
LQKANLNLDD MDLIEANEAF AAQFLGVGKA LHFDMNKTNV HGGAIALGHP IGASGARILV
TLLYGMRARG AKLGLATLCI GGGQGISMVL ERV
//
