ID A0A3Q3EEZ1_9LABR Unreviewed; 1056 AA.
AC A0A3Q3EEZ1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ATP-citrate synthase {ECO:0000256|ARBA:ARBA00015259};
DE EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
DE AltName: Full=ATP-citrate (pro-S-)-lyase {ECO:0000256|ARBA:ARBA00030151};
DE AltName: Full=Citrate cleavage enzyme {ECO:0000256|ARBA:ARBA00030982};
GN Name=ACLY {ECO:0000313|Ensembl:ENSLBEP00000005933.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000005933.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000005933.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 -!- SIMILARITY: In the C-terminal section; belongs to the succinate/malate
CC CoA ligase alpha subunit family. {ECO:0000256|ARBA:ARBA00005899}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the succinate/malate
CC CoA ligase beta subunit family. {ECO:0000256|ARBA:ARBA00010719}.
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DR AlphaFoldDB; A0A3Q3EEZ1; -.
DR Ensembl; ENSLBET00000006234.1; ENSLBEP00000005933.1; ENSLBEG00000004457.1.
DR GeneTree; ENSGT00940000154881; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
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; 1.10.230.10; 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; 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; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 483..592
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 442..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..469
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 1056 AA; 116206 MW; 5DC7456938745C94 CRC64;
MSAKAISEQT GKDFLYKYIC TSAAVQNRFR YANVTPETDF DRLAKEHPWL LTERLVVKPD
QLIKRRGKLG LVGVNLDLNS VREWLKSRLM RETTVGKAKG ILKNFLIEPF VQHKQEEEFY
VCIYATREGD YVLFHHEGGV DVGDVDAKAK KLLIGVDEKI SEDSVKKMLL TNVPNDKKSV
LASFIVGLFN LYEDLFFTYL EINPLVVTKD GVYVLDMAAK IDATADYICK AKWGDVEFPP
PFGREAYPEE AYIADLDAKS GASLKLTLLN PRGRIWTMVA GGGASVVYSD TICDLGGVDE
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPDGKVLII GGSIANFTNV AATFKGIVRA
IRDYQGPLKE HEVTLFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMALG
HRPIPNQPPV AAHTANFLLN SSGSTSTPAS SRTASFSDNR TNVQSSPAKK AKTGGPAVKA
TTLFSKQTKS IVWGMQTRAV QGMMDFDYVC SREEPSVAAM VYPFTGDHKQ KFYWGHKEIL
IPVYKNMGDA MKKHPDVDVL ISFASLRSAF DSTMETMQYP QIHTIAIIAE GIPEAHTRKI
IKAADEKGVT IIGPATVGGI KPGCFKIGNT GGMLDNILAS KLYRPGSVAY VSRSGGMSNE
LNNIISRTTD GVFEGVAIGG DRYPGSVFTD HVLRYQDTPG VKMIVVLGEI GGTEEYKICE
AIKEGRITKP VVCWCIGTCA TMFSSEVQFG HAGACANQAS ETAVSKNEAL KEAGAFVPRS
FDELGEIIKS VYDDLVAKGV IQPAAEMPPP TVPMDYSWAR ELGLIRKPAS FMTSICDERG
QELIYAGMPI TEVFKSEIGL GGTLGLLWFQ RSKHSCFPLC VAFSDCQGTP VSSSRCRNKH
FSKAFDSGML PMEFVNKMKK DGKLIMGIGH RVKSINNPDM RVQILKDFVK QHFPSSQLLD
YALDVEKITT SKKPNLILNV DGFIGVAFVD LLRTCGGFTR DEADEFVEIG ALNGIFVLGR
SMGFIGHYLD QKRLKQGLYR HPWDDISYVL PEHMSM
//
