ID A0A0Q8RE58_9BURK Unreviewed; 399 AA.
AC A0A0Q8RE58;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KRB97158.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KRB97158.1};
GN ORFNames=ASE26_03760 {ECO:0000313|EMBL:KRB97158.1};
OS Duganella sp. Root198D2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736489 {ECO:0000313|EMBL:KRB97158.1, ECO:0000313|Proteomes:UP000051728};
RN [1] {ECO:0000313|EMBL:KRB97158.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRB97158.1,
RC ECO:0000313|Proteomes:UP000051728};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB97158.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRB97158.1,
RC ECO:0000313|Proteomes:UP000051728};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRB97158.1}.
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DR EMBL; LMIC01000012; KRB97158.1; -; Genomic_DNA.
DR RefSeq; WP_055939072.1; NZ_LMIC01000012.1.
DR AlphaFoldDB; A0A0Q8RE58; -.
DR Proteomes; UP000051728; 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; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919:SF138; ACETYL-COA C-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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:KRB97158.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051728};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KRB97158.1}.
FT DOMAIN 5..269
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 278..397
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 355
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 399 AA; 40913 MW; 6191AE69307D3358 CRC64;
MNDPIVIVGA ARTPMGAFQS DFASLSANDL GAVAIKAAVE RAGIKPEAVE HVYFGNCLMA
GQGQAPARQA SIKAGLPVSA GAVTLSKMCG SAMQAAIFAY DALAAGSAEV IVAGGMESMT
NAPYLVPKAR GGYRIGHGMM FDHMMYDGLE DAYTRDAKTG AGRSMGTFAE QCSAAYKFTR
EAQDNFAIES VKRAQAAQAS GAFNWEITPV TVSGRAGDVV IDKDEGPLKA RIEKIPALKP
AFAKDGTITA ASSSSINDGA AALVMMREST AKKLGANVIA KVTGHATNSL VPEQFTTAPV
GAIQKLLAKT GWKVSDVDLF EINEAFAAVP MAAMHDLDIP HSKVNVHGGA CALGHPIGAT
GARIITTLIG ALKAKGGKKG VAALCIGGGE ATAMGIELV
//