ID A0A3B3BET9_ORYME Unreviewed; 1092 AA.
AC A0A3B3BET9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000003684.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000003684.1}
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; A0A3B3BET9; -.
DR Ensembl; ENSOMET00000010435.1; ENSOMEP00000003684.1; ENSOMEG00000004730.1.
DR GeneTree; ENSGT00940000154881; -.
DR OMA; AIYSERC; -.
DR Proteomes; UP000261560; 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; 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:SF42; 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 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|ARBA:ARBA00022723,
KW 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 ACT_SITE 751
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
SQ SEQUENCE 1092 AA; 119893 MW; 84C8912679550D0A CRC64;
MSAKAISEQT GKEFLYKHIS PSAAVQNRFH YATVTAETDW DRLTQENQWL LTKRLVVKPD
QLIKRRGKLG LVGINLDLQG VKDWVKTHMM KDTTVGRAKG VLKNFLIEPF VPHKQEEEFY
VCIYAVREGD VVLFHHEGGV EVGDVDAKAL KLTVAVNDKI SEEQVKEQLL SHVPEDKKGV
LASFIVGLFN LYEDLYFTYL EINPLVVTSD GVYVLDMAAK IDATADFICK SKWGDVEFPP
PFGREAYPEE AYIADLDAKS GASLKLTLLN PQGRIWTMVA GGGASVVYSD TICDLGGVDE
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPQGKVLII GGSIANFTNV AATFKGIVRA
IKDYQEPLKE HEVKIFVRRG GPNYQEGLRV MGEIGKTTGI PIHVFGTETH MTAIVGMALG
HRPIPNLPPM AAHTANFLLN ASNNTVTPAN TRTASFSEPK MANDVSPAKK SKAGLPAAKA
TTLFSNHTKA IVWGMQTRAV QGMLDFDYVC SREEPSVAAM VYPFTGDHKQ KFYWGHKEIL
LPVYKNMADA MKKHPQVDVM ISFASLRSAF DSTVEAMQYP QIHTIAIIAE GIPEAQTRKM
IKMADEKGVT IIGPATVGGI KPGCFKIGNT GGMLDNILAS KLYRPGSVAY VSRSGGMSNE
LNNIISRTTD GVYEGVAIGG DRYPGSTFMD HVLRYQDTPG IKMIVVLGEI GGTDEYKICQ
GIKEDRITKP VVCWCIGTCA TMFASEVQFG HAGACANQAS ETAVAKNQAL RDAGAYVPKS
FDELGDLIRT VYDELVASGT IVPAQEVPPP TVPMDYSWAR ELGLIRKPAS FMTSICDERG
QELIYAGMGI TEVFKEEMGI GGVLGLLWFQ RRLPRYACQF IEMCLMVTAD HGPAVSGAHN
TIVCARAGKD LISSLTSGLL TIGDRFGGAL DAAAKQFSKA FDSGMLPMDF VNKMKKDGKL
IMGIGHRVKS INNPDMRVQI LKDFVKQHFP STQLLDYALD VEKITTSKKP NLILNVDGFI
GVSFVDLLRT CGGFTRDEAD EFVEIGALNG IFVLGRSMGF IGHYLDQKRL KQGLYRHPWD
DISYVLPEHM SM
//
