ID A8X940_CAEBR Unreviewed; 1111 AA.
AC A8X940;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=ATP-citrate synthase {ECO:0000256|PIRNR:PIRNR036511};
DE EC=2.3.3.8 {ECO:0000256|PIRNR:PIRNR036511};
DE AltName: Full=ATP-citrate (pro-S-)-lyase {ECO:0000256|PIRNR:PIRNR036511};
DE AltName: Full=Citrate cleavage enzyme {ECO:0000256|PIRNR:PIRNR036511};
GN Name=acly-2 {ECO:0000313|WormBase:CBG09435};
GN ORFNames=CBG09435 {ECO:0000313|EMBL:CAP29152.2,
GN ECO:0000313|WormBase:CBG09435}, CBG_09435
GN {ECO:0000313|EMBL:CAP29152.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP29152.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP29152.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP29152.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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:0000256|ARBA:ARBA00001688,
CC ECO:0000256|PIRNR:PIRNR036511};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|PIRNR:PIRNR036511}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the succinate/malate
CC CoA ligase alpha subunit family. {ECO:0000256|ARBA:ARBA00005899,
CC ECO:0000256|PIRNR:PIRNR036511}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the succinate/malate
CC CoA ligase beta subunit family. {ECO:0000256|ARBA:ARBA00010719,
CC ECO:0000256|PIRNR:PIRNR036511}.
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DR EMBL; HE600954; CAP29152.2; -; Genomic_DNA.
DR AlphaFoldDB; A8X940; -.
DR STRING; 6238.A8X940; -.
DR WormBase; CBG09435; CBP02318; WBGene00031017; Cbr-acly-2.
DR eggNOG; KOG1254; Eukaryota.
DR HOGENOM; CLU_006587_0_1_1; -.
DR InParanoid; A8X940; -.
DR OMA; AIYSERC; -.
DR OrthoDB; 536at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003878; F:ATP citrate synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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 GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd06100; CCL_ACL-C; 1.
DR Gene3D; 3.30.470.110; -; 1.
DR Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR23118; ATP-CITRATE SYNTHASE; 1.
DR PANTHER; PTHR23118:SF51; ATP-CITRATE SYNTHASE; 1.
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; Citrate synthase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR036511};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR036511};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|PIRNR:PIRNR036511};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR036511};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR036511};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR036511};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR036511};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036511}.
FT DOMAIN 52..213
FT /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT /evidence="ECO:0000259|Pfam:PF08442"
FT DOMAIN 261..438
FT /note="ATP-citrate synthase citrate-binding"
FT /evidence="ECO:0000259|Pfam:PF16114"
FT DOMAIN 497..602
FT /note="CoA-binding"
FT /evidence="ECO:0000259|Pfam:PF02629"
FT DOMAIN 662..786
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT ACT_SITE 762
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
SQ SEQUENCE 1111 AA; 122231 MW; 6BF3C6CB4E1D22A4 CRC64;
MSAKAVSELS GKEVTFLLFV LYKHFESTGI VSAPHAFHVN AGDKFSEVSA KYEWLAQDNK
GVIKPDQLIK RRGKLGLVKI GTPAELEAWF DKTANTYIKV GQTEGRLHTF IVEPFCAHSE
DEEMYIAIYS ERCRDVIMFY EHGGVDIGDV EEKARAVHIP VQLNDNEMTI TERELDMLLG
PCKEKDIIRK FVLNLYEAYK ALHFTYLEIN PFVLTNGKIH VLDLAAKLDE TANFLCSDRW
SSRSASSRIT RSIEFPAPFG RDLTVEEQYI SDMDAKTGAS LKLTILNRQG RVWTMVAGGG
ASVVFTDTVC DLGGANELAN YGEYSGDPSE SQTYEYAKTI LSVMTEGTPR PDGKVLIIGG
SIANFTNVAK TFGGIVRAFE TFIDKLKEHK VSIYVRRGGP NYQEGLRRVK DAATKLDIPI
HVFGPETHMT AIVGAALGLT PMPTVPTAPQ TTGQFLLSPE RNTAGFERPP ASPAVTSAPV
ELPPKRSHPL HQSLFENNTK AIIWGQQHKA IQGMLDFDFV CGRHSPSVVA STYPFTGDNK
QKYYFGQKEI LIPAYKSMAK AFASHPDATV MVTFASMRSV FETVLEALQF SQIKVIAIIA
EGVPENQTRK LLKVAEDKGV TLIGPATVGG IKPGCFKIGN TGGMMDNILA SKLYRPGSVA
YVSRSGGMSN ELNNIISQNT NGVYEGIAIG GDRYPGSTYT DHVLRYQHDD RVKMIVLLGE
VGGVEEYRIV ELLKTKQITK PLVAWCIGTC ADHITSEVQF GHAGASAHGE GETAACKNTA
LRSAGALVPS SFDDLGNKIR ETYEDLLRLQ IVVPQPEQPP PAVPMDYAWA RELGLIRKPA
SFMTSICDER GEELNYAGVP ITKVLESDMG IGGVLGLLWF QKRLPPHANK FIEICLMLTA
DHGPAVSGAH NTIVCARAGK DLISSLTSGL LTIGDRFGGA LDGAARQFSE AFDQGWSPNQ
FVGEMRKRGT HIMGIGHRVK SHQIYFQINN PDKRVEILKR FAADKKEFAQ ETPLLDYALE
VEKITTAKKP NLILNVDGAI AIIFVDILRN SGMFTTAEAQ EVIEIGALNG MFVLGRSIGF
IGHYLDQSRL KQGLYRHPWD DISYIMPERN L
//
