ID A0A196MNQ3_9SPHN Unreviewed; 386 AA.
AC A0A196MNQ3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:OAN56726.1};
GN ORFNames=A7Q26_19370 {ECO:0000313|EMBL:OAN56726.1};
OS Sphingobium sp. TCM1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=453246 {ECO:0000313|EMBL:OAN56726.1, ECO:0000313|Proteomes:UP000078322};
RN [1] {ECO:0000313|EMBL:OAN56726.1, ECO:0000313|Proteomes:UP000078322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCM1 {ECO:0000313|EMBL:OAN56726.1,
RC ECO:0000313|Proteomes:UP000078322};
RA Takahashi S.;
RT "Draft Genome Sequences of Sphingobium sp. strain TCM1 and Sphingomonas sp.
RT strain TDK1, Haloalkyl Organophosphorus Flame Retardant-Degrading
RT Bacteria.";
RL Submitted (MAY-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}.
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:OAN56726.1}.
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DR EMBL; LXVX01000011; OAN56726.1; -; Genomic_DNA.
DR RefSeq; WP_066859018.1; NZ_LXVX01000011.1.
DR AlphaFoldDB; A0A196MNQ3; -.
DR STRING; 453246.A7Q26_19370; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000078322; 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; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000078322};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OAN56726.1}.
FT DOMAIN 5..255
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 263..384
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 342
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 372
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 386 AA; 40197 MW; C30509FF115A5285 CRC64;
MAQAYIVEAV RTPGGKRKGA LAGSHPADIG AVVLNALVDR TGVDPAAIDD VILGCVTQAG
EQAFAFGRNV VLASKLPQSV PAVTIDRQCG SSQQALHFAA QAVMSGTQDL VIAAGAESMT
RVPMMSNFTL HAQAGMGDGP WPRSIQQRFG IAEFSQFHGA QAIADKYGFT REDMDGFAMR
SHHKAAAAIA AGAFDREIVP VETLQGPFVQ DEGVRADSSM EALAGLKTLA EGGTITAGNA
SQMTDGASAV LVASEAALKR FNLTPLARIH NLTVTAGDPV IMLEEPIPAT RRALVRAGLK
LDDIDLFEVN EAFAAIPMAW LQAIGADPDK LNVHGGAIAL GHPLGASGTK LMATMIHALR
ARGKRYGLQT MCEGGGIANV TIVEAL
//
