ID A0A329ZZ36_9HELI Unreviewed; 393 AA.
AC A0A329ZZ36;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:RAX59190.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:RAX59190.1};
GN ORFNames=CCZ01_00125 {ECO:0000313|EMBL:RAX59190.1};
OS Helicobacter sp. 15-1451.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=2004995 {ECO:0000313|EMBL:RAX59190.1, ECO:0000313|Proteomes:UP000251881};
RN [1] {ECO:0000313|EMBL:RAX59190.1, ECO:0000313|Proteomes:UP000251881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15-1451 {ECO:0000313|EMBL:RAX59190.1,
RC ECO:0000313|Proteomes:UP000251881};
RX PubMed=29225701; DOI=10.1186/s13099-017-0220-y;
RA Feng Y., Mannion A., Madden C.M., Swennes A.G., Townes C., Byrd C.,
RA Marini R.P., Fox J.G.;
RT "Cytotoxic Escherichia coli strains encoding colibactin and cytotoxic
RT necrotizing factor (CNF) colonize laboratory macaques.";
RL Gut Pathog. 9:71-71(2017).
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:RAX59190.1}.
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DR EMBL; NHYN01000001; RAX59190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329ZZ36; -.
DR OrthoDB; 4565318at2; -.
DR Proteomes; UP000251881; Unassembled WGS sequence.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
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; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 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 ECO:0000313|EMBL:RAX59190.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000251881};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:RAX59190.1}.
FT DOMAIN 5..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..392
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 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; 41334 MW; 6D24BF1A1900FB05 CRC64;
MQKEVVIVGA KRTAIGSFLG SLKGVSAVEL ASIVSKDLLS ELNLEPNLID EVILGQILQA
GLGQNPARQV LINSGIDESK GAYCINKLCG SGLKAIDLAY QSILLGENDI VLAGGSENMS
ASPYLLESVR EGYKMGDKQV IDSMIKDALT CAMEGYHMGI TAENLAKEYN ISREEQDEFA
LHSQFKAKKA LDSNAFAGEI SPVVLKSKKG ENVFTQDEFV RGDISKESLA KLRPAFDKNG
SVTAGNASGI NDGAAMAIVM SKDKAQDLGL PILATIKAIA SVGVPPRIMG IGAAMAAKKV
LEKASMKIED IDLIEANEAF AAQSLACIKE LKPNLERLNI NGGAIALGHP VGASGARIVA
TLLNAMKKQN KQFGLATLCV GGGQGIAAIF ERS
//
