ID A0A3Q4HRR8_NEOBR Unreviewed; 1101 AA.
AC A0A3Q4HRR8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ENSNBRP00000024926.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000024926.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000024926.1}
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; A0A3Q4HRR8; -.
DR STRING; 32507.ENSNBRP00000024926; -.
DR Ensembl; ENSNBRT00000025578.1; ENSNBRP00000024926.1; ENSNBRG00000019018.1.
DR GeneTree; ENSGT00940000154881; -.
DR OMA; TLETMQY; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000019018; Expressed in liver and 4 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
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; 1.10.230.10; 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; 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|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}; Magnesium {ECO:0000256|PIRNR:PIRNR036511};
KW Metal-binding {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:UP000261580};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036511}.
FT DOMAIN 492..601
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 443..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 760
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
SQ SEQUENCE 1101 AA; 120987 MW; 5817B581DEBCB03E CRC64;
MSAKAISEQT GKEFLYKYIC TSAAIQNRFR YANVTPETNF DRLAQEHPWL LTERLVVKPD
QLIKRRGKLG LVGVNLDLKG VKEWLKPRLM KETTVGKAKG VLKNFLIEPF VPHKQEEEFY
VCIYATREGD YVLFHHEGGV DVGDVDAKAQ KLLIKVDEKI SEDLVKKDLL THVPNDKKVI
LASFIVGLFN LYEDLFFTYL EINPLVVTKD GVYVLDMAAK IDATADYICK AKWGDVEFPP
PFGREAYPEE AYIADLDAKS GASLKLTLLN PRGRIWTMVA GGGASVVYSD TICDLGGVNE
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHSDGKVLII GGSIANFTNV AATFKGIVRA
IRDYQEPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMALG
HRPIANLPPI AAHTANFLLN SNSSTSTPVS SRTASFSENK GKVESSPAKK PKTGAPVVSK
SFPFSVGKAT TLFTKHTKSI VWGMQTRAVQ GMLDFDYICS RAEPSVAAMV YPFTGDHKQK
FYWGHKEILL PVYKNMSDAM KKHPDVDVLI NFASLRSAFD STIETMQYPQ IRTIAIIAEG
IPEAHTRKLI KTADEKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV
SRSGGMSNEL NNIISRTTDG VFEGVAIGGD RYPASVFTDH VLRYQDTPGV KMIVVLGEIG
GTEEYKICQA IKQGRITKPV VCWCIGTCAT MFSSEVQFGH AGACANQASE TAVAKNKALK
EAGAFVPKSF DELGDIIKSV YDDLVAKGVI QPAEELPPPT VPMDYSWARE LGLIRKPASF
MTSICDERGQ ELIYAGMPIT EVFKSEIGLG GTLGLLWFQR RLPRYACQFI EMCLMVTADH
GPAVSGAHNT IVCARAGKDL ISSLTSGLLT IGDRFGGALD AAAKQFSKAF DSGMLPMEFV
NKMKKDGKLI MGIGHRVKSI NNPDMRVQIL KDFVKQHFPS TQLLDYALEV EKITTSKKPN
LILNVDGFIG VAFVDLLRTC GGFTRDEADE FVEIGALNGI FVLGRSMGFI GHYLDQKRLK
QGLYRHPWDD ISYVLPEHMS M
//
