ID   SUR5_CAEEL              Reviewed;         700 AA.
AC   Q21166;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Acetoacetyl-CoA synthetase;
DE            EC=6.2.1.16;
DE   AltName: Full=Suppressor of activated let-60 Ras protein 5;
GN   Name=sur-5; ORFNames=K03A1.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   MEDLINE=98336261; PubMed=9671465;
RA   Gu T., Orita S., Han M.;
RT   "Caenorhabditis elegans SUR-5, a novel but conserved protein,
RT   negatively regulates LET-60 Ras activity during vulval induction.";
RL   Mol. Cell. Biol. 18:4556-4564(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Activates acetoacetate to acetoacetyl-CoA (By
CC       similarity). Negatively regulates let-60 Ras activity during
CC       vulval induction.
CC   -!- CATALYTIC ACTIVITY: ATP + acetoacetate + CoA = AMP + diphosphate +
CC       acetoacetyl-CoA.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Present in most cells of the organism.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
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DR   EMBL; AY091467; AAM44123.1; -; mRNA.
DR   EMBL; U41625; AAA83327.1; -; Genomic_DNA.
DR   PIR; T34321; T34321.
DR   RefSeq; NP_509229.1; -.
DR   UniGene; Cel.22610; -.
DR   Ensembl; K03A1.5; Caenorhabditis elegans.
DR   GeneID; 180992; -.
DR   KEGG; cel:K03A1.5; -.
DR   WormBase; WBGene00006351; sur-5.
DR   WormPep; K03A1.5; CE04713.
DR   OMA; Q21166; WAHGDYA.
DR   BRENDA; 6.2.1.16; 672.
DR   NextBio; 911894; -.
DR   ArrayExpress; Q21166; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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; Complete proteome; Cytoplasm; Fatty acid metabolism;
KW   Ligase; Lipid metabolism; Nucleotide-binding; Nucleus.
FT   CHAIN         1    700       Acetoacetyl-CoA synthetase.
FT                                /FTId=PRO_0000315791.
SQ   SEQUENCE   700 AA;  78339 MW;  6821FD4A33275CF7 CRC64;
     MTAVSANGKT TEKHENGAHT NGTTNGTTNG SMNGNEISHV QKLQPVYYKP PQNLETFELS
     LRNHFEEKTN KKFADYREFH RFTCDNYGIF WEDLLKLSDV KLHQNYNQVI DHNLKINERP
     RWFNGATLNY TENVIERGTA TDIAVLNASI EETVTEYTYD NLRKDVYRIA TSLRNYGIGP
     GDTVCGFVPN TYDTLVAVFA TAAVGAAWCS ASVDFGPAGV LDRFRQVHPK VLFTVNHVTY
     KKKLIDQTDK INEIVKELPT LEKIVVSDTF TSVKFDATKY NQSDKFSSLE EFKTPIADVV
     LPFVYTPVPF SDPLFVMFSS GTTGIPKAMV HTVGGTLLKH IEEHLVQGDS KKHDRMFFYT
     TCGWMMYNWM ISFLYSKGSV VLFDECPLAP DTHIIMKIAA KTQSTMIGMG AKLYDEYLRL
     QIPFNTLYDL SKIHTVYSTG SPLKKECFAY INTYIAPGAL IASISGGTDI IGCFVGGIKS
     LSITPGECQC LFLGMDIKSF NYMDEEIINS DEQGELVCVT PFPSMPSHFL NDTDGKKYRD
     AYFARLEPFW AHGDFVRVNH STGGVEMLGR SDATLNRGGV RIGTAEIYSV VEKIPHIADC
     IVAGRLVEEG MDEEVLLFVK MVPGQELTHS IQAAIVSKLR NDMSPRHVPN KIYAVDDIPY
     TSSGKKVEVA VKQIVSGKAV QKASSIRNPE SLDHFVQYRL
//