ID A0A013WRI7_9SPHN Unreviewed; 394 AA.
AC A0A013WRI7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EXS68733.1};
GN ORFNames=BF95_19600 {ECO:0000313|EMBL:EXS68733.1};
OS Sphingobium sp. Ant17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1461752 {ECO:0000313|EMBL:EXS68733.1, ECO:0000313|Proteomes:UP000021537};
RN [1] {ECO:0000313|EMBL:EXS68733.1, ECO:0000313|Proteomes:UP000021537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ant17 {ECO:0000313|EMBL:EXS68733.1,
RC ECO:0000313|Proteomes:UP000021537};
RA Adriaenssens E.M., Cowan D.A.;
RT "Draft genome sequence of the aromatic hydrocarbon-degrading bacterium
RT Sphingobium sp. strain Ant17 isolated from Antarctic soil.";
RL Submitted (FEB-2014) 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:EXS68733.1}.
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DR EMBL; JEMV01000062; EXS68733.1; -; Genomic_DNA.
DR RefSeq; WP_043153828.1; NZ_JEMV01000062.1.
DR AlphaFoldDB; A0A013WRI7; -.
DR STRING; 1461752.BF95_19600; -.
DR PATRIC; fig|1461752.3.peg.4421; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000021537; 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; 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; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EXS68733.1}.
FT DOMAIN 5..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 272..391
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 394 AA; 40837 MW; EEAA4D4A21F28CD3 CRC64;
MTRNVVLCAP VRTAIGSYGG SLKDMAAPRL GSIAIAETLK RAGVTGDAID TVVMGQVVQA
GAKMNPARQA AIGGGIPDTV PAMTVNRVCG SGAQAIATAA QEIMLGLTNA AVAGGMENMD
QAPYLIEKGR WGYRMGDGKL FDSMLHDGLN DAFVDQHSGW VTEDLVTKFQ ISRDAQDSWA
VRSQQRFSTA QAAGKFDSEI VAVEIPGRKG PTSFSRDEQN RPDATLESLA HLKPAFRPEG
TITAGNAPGL NTGAAAMIVA SEDWASQHGV APVGRLVAFG VGAVEPGLFG LGPVPAVRQA
LTRAGWSVSD LERVEINEAF AAIAIAVVRE LGLPEDIVNV EGGAIAHGHP IGATGAVLTT
RLLESMRRDG LRRGLVTLCI GGGQGVALAL EAVS
//
