ID A0A3Q1JNL0_ANATE Unreviewed; 1104 AA.
AC A0A3Q1JNL0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
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:ENSATEP00000032318.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000032318.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000032318.2}
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 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; A0A3Q1JNL0; -.
DR Ensembl; ENSATET00000032792.2; ENSATEP00000032318.2; ENSATEG00000022150.2.
DR GeneTree; ENSGT00940000154881; -.
DR Proteomes; UP000265040; Unplaced.
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:UP000265040};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036511}.
FT DOMAIN 495..604
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 448..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 763
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
SQ SEQUENCE 1104 AA; 121619 MW; 013DFA8B550C93E4 CRC64;
MSAKAISEQT GKEFLYKYIC TSAAVKNRFH YASVTAETDW NLLKQEHPWL LTERLVVKPD
QLIKRRGKLG LVGINLDLQG VQEWLKTHLM KETTVGKAKG LLKNFLIEPF VPHTQEEEFY
VCIYATREGD HVLFHHEGGV EVGDVDAKAQ RLMVAVDNKL SEHQVTEQLL TQVPDDKKQV
LASFIVGLFN LYEDLYFTYL EINPLVVTQN GVYILDMAAK IDATADYICK AKWGDLEFPP
PFGREAYPEE AYIADLDAKS GASLKLTLLN PRGRIWTMVA GGGASVVYSD TICDLGGVDE
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHVQGKVLII GGSIANFTNV AATFKGIVRA
IKDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMALG
HRPIPNQPPM DAHTANFLLN ASNSGMTPAT TRTASFSEPR TPNDTTPAKK SKAGLPLNFS
LFLYHLVHLA KATTLFSKRT KSIVWGMQTR AVQGMLDFDY VCSRDEPSVA AMVYPFTGDH
KQKFYWGHKE ILLPVYKNMA DAMKKHSEVD VLISFASLRS AFDSTVEAMQ YSQIHTIAII
AEGIPEAQTR KMIKMADEKG ITIIGPATVG GIKPGCFKIG NTGGMLDNIL ASKLYRPGSV
AYVSRSGGMS NELNNIISRT TDGVYEGVAI GGDRYPGSTF MDHVLRYQDT PGIKMIVVLG
EVGGTEEYKI CQGIREGRIT KPVVCWCIGT CATMFASEVQ FGHAGACANQ ASETAVAKNQ
ALRDAGAFVP KSFDELGNVI RTVYDDLVAN GTIIPAQEVP PPTVPMDYSW ARELGLIRKP
ASFMTSICDE RGQELIYAGM PITEVFKEEM GLGGVLGLLW FQRRLPRYAC QFIEMCLMVT
ADHGPAVSGA HNTIVCARAG KDLISSLTSG LLTIGDRFGG ALDAAAKQFS KAFDSGMLPM
EFVNKMKKDG KLIMGIGHRV KSINNPDMRV QILKDFVKQH FTSTQLLDYA LDVEKITTSK
KPNLILNVDG FIGVAFVDLL RTCGGFTRDE ADEFVEIGAL NGIFVLGRSM GFIGHYLDQK
RLKQGLYRHP WDDISYVLPE HMSM
//
