SUR5_CAEEL
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 03-AUG-2022, entry version 131.
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; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9671465; DOI=10.1128/mcb.18.8.4556;
RA Gu T., Orita S., Han M.;
RT "Caenorhabditis elegans SUR-5, a novel but conserved protein, negatively
RT 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 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 investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Activates acetoacetate to acetoacetyl-CoA (By similarity).
CC Negatively regulates let-60 Ras activity during vulval induction.
CC {ECO:0000250, ECO:0000269|PubMed:9671465}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetoacetate + ATP + CoA = acetoacetyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:16117, ChEBI:CHEBI:13705,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57286,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:456215; EC=6.2.1.16;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9671465}. Nucleus
CC {ECO:0000269|PubMed:9671465}.
CC -!- TISSUE SPECIFICITY: Present in most cells of the organism.
CC {ECO:0000269|PubMed:9671465}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AY091467; AAM44123.1; -; mRNA.
DR EMBL; FO081579; CCD72541.1; -; Genomic_DNA.
DR PIR; T34321; T34321.
DR RefSeq; NP_509229.1; NM_076828.5.
DR AlphaFoldDB; Q21166; -.
DR SMR; Q21166; -.
DR BioGRID; 45917; 9.
DR STRING; 6239.K03A1.5; -.
DR EPD; Q21166; -.
DR PaxDb; Q21166; -.
DR PeptideAtlas; Q21166; -.
DR EnsemblMetazoa; K03A1.5.1; K03A1.5.1; WBGene00006351.
DR GeneID; 180992; -.
DR KEGG; cel:CELE_K03A1.5; -.
DR UCSC; K03A1.5; c. elegans.
DR CTD; 180992; -.
DR WormBase; K03A1.5; CE04713; WBGene00006351; sur-5.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000156044; -.
DR HOGENOM; CLU_000022_3_3_1; -.
DR InParanoid; Q21166; -.
DR OMA; WYSSTGW; -.
DR OrthoDB; 899666at2759; -.
DR PhylomeDB; Q21166; -.
DR Reactome; R-CEL-77111; Synthesis of Ketone Bodies.
DR SignaLink; Q21166; -.
DR PRO; PR:Q21166; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006351; Expressed in larva and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030729; F:acetoacetate-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR005914; Acac_CoA_synth.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 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; Lipid metabolism;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..700
FT /note="Acetoacetyl-CoA synthetase"
FT /id="PRO_0000315791"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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