ID A0A3B3Q7H0_9TELE Unreviewed; 1092 AA.
AC A0A3B3Q7H0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=ATP-citrate synthase {ECO:0000256|ARBA:ARBA00015259, ECO:0000256|PIRNR:PIRNR036511};
DE EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639, ECO:0000256|PIRNR:PIRNR036511};
DE AltName: Full=ATP-citrate (pro-S-)-lyase {ECO:0000256|ARBA:ARBA00030151, ECO:0000256|PIRNR:PIRNR036511};
DE AltName: Full=Citrate cleavage enzyme {ECO:0000256|ARBA:ARBA00030982, ECO:0000256|PIRNR:PIRNR036511};
GN Name=ACLY {ECO:0000313|Ensembl:ENSPKIP00000002597.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000002597.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000002597.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the cleavage of citrate into oxaloacetate and
CC acetyl-CoA, the latter serving as common substrate for de novo
CC cholesterol and fatty acid synthesis. {ECO:0000256|ARBA:ARBA00002797}.
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:ARBA00000727};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21162;
CC Evidence={ECO:0000256|ARBA:ARBA00000727};
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 AlphaFoldDB; A0A3B3Q7H0; -.
DR STRING; 1676925.ENSPKIP00000002597; -.
DR Ensembl; ENSPKIT00000026545.1; ENSPKIP00000002597.1; ENSPKIG00000020389.1.
DR GeneTree; ENSGT00940000154881; -.
DR OrthoDB; 536at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:InterPro.
DR GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; 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:SF42; ATP-CITRATE SYNTHASE; 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 SMART; SM00881; CoA_binding; 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|PIRNR:PIRNR036511};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR036511};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036511};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 483..592
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 447..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 751
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
SQ SEQUENCE 1092 AA; 119924 MW; 43AF960F47E0AD18 CRC64;
MSAKAISEQT GKEFLYKYIC TSAAVQNRFK YASVTADTDW VRLAQEHPWL LTERLVIKPD
QLIKRRGKLG LVGVNLDLKG VQDWLRPRLM KETTVAKAKG ILKNFLIEPF VAHKQEEEFY
ICIYAAREGD YVLFHHEGGV DVGDVDAKAQ KLLLGVDKKL TEDAVKGRLL THVPADKRAV
LASFVVGLFN LYEELFFTYL EINPLVVTKD GVFVLDMAAK IDATADYICK AKWGDIEFPP
PFGREAYPEE AYIADLDAKS GASLKLTLLN PRGRIWTMVA GGGASVVYSD TICDLGGVDE
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHRDGKVLII GGSIANFTNV AATFKGIVRA
IKDYQVPLQE HEVSIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMALG
HRPIPNQPPA AAHTANFLLN TSASVSTPGT SRTASFSEPK AASSASPAKK SKPSVPPVKA
TTLFSKETKA IVWGMQTRAV QGMLDFDYVC SREEPSVAAM VYPFTGDHKQ KFYWGHKEIL
LPVYKNMGDA MKKHPEVDVL ISFASLRSAF ESTMETMQYH QIRTIAIIAE GIPEAHTRRL
IKRADEKGVT IIGPATVGGI KPGCFKIGNT GGMLDNILAS KLYRPGSVAY VSRSGGMSNE
LNNIVSRNTD GVFEGVAIGG DRYPGSTFMD HVLRYQDTPE VKMIVVLGEI GGTEEYKIGQ
GIKSGRITKP VVCWCIGTCA TMFSSEVQFG HAGACANQAS ETAVAKNQAL MEAGAFVPRS
FDELGDIIKK VYDDLVASRV IIPAMEVPPP TVPMDYSWAR ELGLIRKPAS FMTSICDERG
QELLYAGMPI TEVFKEEMGL GGVLGLLWFQ RRLPRYACHF IEMCLMVTAD HGPAVSGAHN
TIICARAGKD LISSLTSGLL TIGDRFGGAL DAAAKEFSKA FDSGLLPMEF VNKMKKEGRL
IMGIGHRVKS INNPDMRVQI LKDFVKQHFP ATQLLDYALD VEKITTSKKP NLILNVDGFI
GVAFVDLLRT CGGFTRDEAD EFVEIGALNG IFVLGRSMGF IGHYLDQKRL KQGLYRHPWD
DISYVLPEHM SM
//
