ACLY_CAEEL
ID ACLY_CAEEL Reviewed; 1106 AA.
AC P53585;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Probable ATP-citrate synthase {ECO:0000250|UniProtKB:P53396};
DE EC=2.3.3.8 {ECO:0000250|UniProtKB:P53396};
DE AltName: Full=ATP-citrate (pro-S-)-lyase {ECO:0000250|UniProtKB:P53396};
DE AltName: Full=Citrate cleavage enzyme {ECO:0000250|UniProtKB:P53396};
GN Name=acly-1 {ECO:0000312|WormBase:D1005.1};
GN ORFNames=D1005.1 {ECO:0000312|WormBase:D1005.1};
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 [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: ATP-citrate synthase is the primary enzyme responsible for
CC the synthesis of cytosolic acetyl-CoA in many tissues.
CC {ECO:0000250|UniProtKB:P53396}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate +
CC CoA; Xref=Rhea:RHEA:21160, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=2.3.3.8;
CC Evidence={ECO:0000250|UniProtKB:P53396};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P53396}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53396}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the succinate/malate
CC CoA ligase beta subunit family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the succinate/malate
CC CoA ligase alpha subunit family. {ECO:0000305}.
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DR EMBL; FO080989; CCD68276.1; -; Genomic_DNA.
DR PIR; T29496; T29496.
DR RefSeq; NP_508280.1; NM_075879.4.
DR AlphaFoldDB; P53585; -.
DR SMR; P53585; -.
DR BioGRID; 45435; 9.
DR DIP; DIP-26861N; -.
DR IntAct; P53585; 5.
DR STRING; 6239.D1005.1; -.
DR iPTMnet; P53585; -.
DR EPD; P53585; -.
DR PaxDb; P53585; -.
DR PeptideAtlas; P53585; -.
DR EnsemblMetazoa; D1005.1.1; D1005.1.1; WBGene00016995.
DR GeneID; 180485; -.
DR KEGG; cel:CELE_D1005.1; -.
DR UCSC; D1005.1; c. elegans.
DR CTD; 180485; -.
DR WormBase; D1005.1; CE06997; WBGene00016995; acly-1.
DR eggNOG; KOG1254; Eukaryota.
DR GeneTree; ENSGT00940000154881; -.
DR HOGENOM; CLU_006587_0_1_1; -.
DR InParanoid; P53585; -.
DR OMA; ANFLCAD; -.
DR OrthoDB; 349367at2759; -.
DR PhylomeDB; P53585; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-75105; Fatty acyl-CoA biosynthesis.
DR PRO; PR:P53585; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00016995; Expressed in material anatomical entity and 5 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003878; F:ATP citrate synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
DR Gene3D; 3.40.50.261; -; 2.
DR InterPro; IPR014608; ATP-citrate_synthase.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR InterPro; IPR032263; Citrate-bd.
DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR005811; CoA_ligase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF16114; Citrate_bind; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF036511; ATP_citrt_syn; 1.
DR SUPFAM; SSF48256; SSF48256; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52210; SSF52210; 1.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..1106
FT /note="Probable ATP-citrate synthase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000102784"
FT REGION 442..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 760
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P16638"
FT BINDING 358
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000250|UniProtKB:P53396"
FT BINDING 360
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000250|UniProtKB:P53396"
FT BINDING 391
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000250|UniProtKB:P53396"
FT BINDING 701..721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 718
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q84LB6"
FT BINDING 752..778
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 779..789
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1106 AA; 121616 MW; 49BEE17983BDEB3F CRC64;
MSAKAVSELS GKEVLYKYFE PSGLLSAPHA FHVKAGENFD EIANKYEWLA RDNKGVIKPD
QLIKRRGKLG LVKIGTPQEL KAWFEKTGDS YVRVGQTEGR LHTFIVEPFC AHTEKDEMYI
AIYSERFRDV IMFYEQGGVD IGDVEEKART VSVPVQLNEN AMTPSDEELT TLLGPLKDSD
IVRRFVVELY KAYKDLHFTY LEINPFVLLN NQIHVLDLAA RLDETANFLC ADKWKSRLTP
YGGPNHVEFP APFGRDLTSE EQYISEMDAK TGASLKLTIL NRKGRVWTMV AGGGASVVFT
DTVCDLGGAS ELANYGEYSG DPSESQTYEY AKTLLSVMTE GTPRPDGKVL IIGGSIANFT
NVAKTFGGIV RAFETFVSKL KEHKVTIFVR RGGPNYQEGL RRIKDAATKL ELPIHVFGPE
THMTAIVGAA LGVKPMPTVP TAPQTTGQFL LSPERNTGGT ERAPPSPAAN ATPTEHPLTT
AQQNKLKSFR GLFEDDTKAI IWGQQAKAIQ GMLDFDYVCR RSSPSVVAST YPFTGDNKQK
YYFGQKEILI PAYKSMAKAF ATHPDASIMV TFASMRSVFE TVLEALEFPQ IKVIAIIAEG
VPENQTRKLL KIAHDRGVTL VGPATVGGIK PGCFKIGNTG GMMDNILASK LYRPGSVAYV
SRSGGMSNEL NNIISQNTNG VYEGIAIGGD RYPGSTYTDH VIRYQNDDRV KMIVLLGEVG
GVEEYKIVDL LKQKKVTKPL VAWCIGTCAD HITSEVQFGH AGASANALGE TAACKNAALR
ASGALVPESF DDLGNKIRQT YDELVSQQII VPQPEVPPPA VPMDYAWARE LGLIRKPASF
MTSICDERGE ELNYAGVPIT KVLESDMGIG GVLGLLWFQK RLPPHANKFI EICLMLTADH
GPAVSGAHNT IVCARAGKDL ISSLTSGLLT IGDRFGGALD GAARQFSEAF DQGWSANQFV
SEMRKKGKHI MGIGHRVKSI NNPDKRVEIL KRFAMDKKEF AQETPLFEYA LEVEKITTAK
KPNLILNVDG AIAILFVDIL RHSGMFTKQE AEETIEIGSL NGLFVLGRSI GFIGHYLDQS
RLKQGLYRHP WDDISYIMPE SNLVKF
