ID W1SA64_9SPHN Unreviewed; 395 AA.
AC W1SA64;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ETI64008.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:ETI64008.1};
GN ORFNames=C100_09685 {ECO:0000313|EMBL:ETI64008.1};
OS Sphingobium sp. C100.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1207055 {ECO:0000313|EMBL:ETI64008.1, ECO:0000313|Proteomes:UP000018867};
RN [1] {ECO:0000313|EMBL:ETI64008.1, ECO:0000313|Proteomes:UP000018867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C100 {ECO:0000313|EMBL:ETI64008.1,
RC ECO:0000313|Proteomes:UP000018867};
RX PubMed=24482512;
RA Dong C., Bai X., Lai Q., Xie Y., Chen X., Shao Z.;
RT "Draft Genome Sequence of Sphingobium sp. Strain C100, a Polycyclic
RT Aromatic Hydrocarbon-Degrading Bacterium from the Deep-Sea Sediment of the
RT Arctic Ocean.";
RL Genome Announc. 2:0-0(2014).
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:ETI64008.1}.
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DR EMBL; AYOY01000138; ETI64008.1; -; Genomic_DNA.
DR AlphaFoldDB; W1SA64; -.
DR STRING; 1207055.C100_09685; -.
DR PATRIC; fig|1207055.3.peg.1814; -.
DR eggNOG; COG0183; Bacteria.
DR Proteomes; UP000018867; 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:ETI64008.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018867};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ETI64008.1}.
FT DOMAIN 9..265
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 275..395
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 93
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 352
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 395 AA; 40573 MW; 69E782A3A213FFFB CRC64;
MRIKALSDIV ITAAKRTPVG SFLGAFAATP AHELGRQAIL AALAQANVAP EEVDEVILGQ
VLTAAQGQNP ARQAAVNAGI PVERTAIGLN QLCGSGLRAV ALAAQAIRAG DANIMLAGGQ
ESMSMAPHAQ MLRAGAKMGP VTLVDTMIHD GLTDAFNNYH MGMTAENLAE KYQISREAQD
AFAVASQNKA EAARAAGRFA DEILPVTVKG RKGDTIVDQD EYIRAGATIE AMQNLRPAFK
KDGTVTAGNA SGINDGAAAL VLMTADNAAK RGANVLGRIA GFATCGVDPS IMGIGPAPAS
RKALEKAGWS VADLDLIEAN EAFAAQALSV GQELGWNPEK VNVNGGAIAI GHPIGASGAR
VLTTLLYEMA KRDAKKGLAT LCIGGGMGVA MCIER
//
