ID AACS_XENTR Reviewed; 672 AA. AC Q28BL6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Acetoacetyl-CoA synthetase; DE EC=6.2.1.16; GN Name=aacs; ORFNames=TEgg036g05.1; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Egg; RG Sanger Xenopus tropicalis EST/cDNA project; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Activates acetoacetate to acetoacetyl-CoA (By CC similarity). CC -!- CATALYTIC ACTIVITY: ATP + acetoacetate + CoA = AMP + diphosphate + CC acetoacetyl-CoA. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR942772; CAJ81897.1; -; mRNA. DR RefSeq; NP_001039244.1; -. DR UniGene; Str.12148; -. DR GeneID; 734109; -. DR KEGG; xtr:734109; -. DR Xenbase; XB-FEAT-490084; aacs. DR HOVERGEN; Q28BL6; -. DR BRENDA; 6.2.1.16; 279072. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR005914; Acac_CoA_synth. DR InterPro; IPR000873; AMP-dep_Synth/Lig. DR Pfam; PF00501; AMP-binding; 1. DR TIGRFAMs; TIGR01217; ac_ac_CoA_syn; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 2: Evidence at transcript level; KW ATP-binding; Cytoplasm; Fatty acid metabolism; Ligase; KW Lipid metabolism; Nucleotide-binding. FT CHAIN 1 672 Acetoacetyl-CoA synthetase. FT /FTId=PRO_0000315790. SQ SEQUENCE 672 AA; 75168 MW; 5C2A9077295F3D2A CRC64; MSDKGELMEE IMEAKVMWYP DSKKITQMDQ FRNRVNRNLG LRLANYNELY QWSVEFYPEF WAEFWDFSGI VYSKTYDEVI DRSKGIADVP EWFKGSRLNY AENLLKHKEN DKIALYSARE GKENIEKVTF AELRRDVALF AAAMRKMGIK TGDRVAGYLP NCIQTVEAML AAASIGAIWS ATSPDFGVNG VLDRFSQIQP KLILSVESVI YNGKEHCHLE KLQHVVKGLP DLKKVVVIPY VLPKEKIDIS KIPNSMFLDE FLATGKVGDQ SPQLEFEQLP FNHPLYIMYS SGTTGAPKCM VHSAGGTLIK HLTEHILHGS TTSSDVIMYY TTAGWMMWNW LITAVATGAS LVLYDGSPLV PSLNVLWDLV DRLGITILGT GAKWLAVLED KGLKPCNTHS LQTLHTILST GSPLKPQSYE YVYKHIKSNV LLGSVSGGTD IIACFMGQNV SVPVYKGEIQ ARHLGMAIEA WNEEGEAVLG ESGELVCLKP LPSQPTHFWN DENGSKYQKA YFAKFPGVWA HGDYCKINPK TGGIVMLGRS DGTLNPNGVR FGSSEIYNIV EAFVEVSDSL CVPQYNKDGD ERVILFLKMA DKFEFSKELL KRIKDAIRVA LSARHVPALI LETKDIPYTI SGKKVEVAVK QVIAGKEVPH RGAFSNPQSL DLYRNIPELQ NF //