ID H2R314_PANTR Unreviewed; 1134 AA.
AC H2R314;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=ATP-citrate synthase {ECO:0000256|PIRNR:PIRNR036511};
DE EC=2.3.3.8 {ECO:0000256|PIRNR:PIRNR036511};
DE AltName: Full=ATP-citrate (pro-S-)-lyase {ECO:0000256|PIRNR:PIRNR036511};
DE AltName: Full=Citrate cleavage enzyme {ECO:0000256|PIRNR:PIRNR036511};
GN Name=ACLY {ECO:0000313|Ensembl:ENSPTRP00000044752.5,
GN ECO:0000313|VGNC:VGNC:6326};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000044752.5, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000044752.5, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000044752.5}
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|PIRNR:PIRNR036511}.
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|PIRNR:PIRNR036511};
CC -!- SUBUNIT: Homotetramer. {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 EMBL; AACZ04038960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04038961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04038962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2R314; -.
DR PaxDb; 9598-ENSPTRP00000044752; -.
DR Ensembl; ENSPTRT00000046197.5; ENSPTRP00000044752.5; ENSPTRG00000023148.5.
DR VGNC; VGNC:6326; ACLY.
DR eggNOG; KOG1254; Eukaryota.
DR GeneTree; ENSGT00940000154881; -.
DR HOGENOM; CLU_006587_2_0_1; -.
DR InParanoid; H2R314; -.
DR TreeFam; TF300560; -.
DR Proteomes; UP000002277; Chromosome 17.
DR Bgee; ENSPTRG00000023148; Expressed in fibroblast and 21 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003878; F:ATP citrate synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0006101; P:citrate metabolic process; IEA:Ensembl.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl.
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; 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; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF036511; ATP_citrt_syn; 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:UP000002277};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036511}.
FT DOMAIN 298..474
FT /note="ATP-citrate synthase citrate-binding"
FT /evidence="ECO:0000259|Pfam:PF16114"
FT DOMAIN 700..824
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 800
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
SQ SEQUENCE 1134 AA; 123378 MW; 97483BBEC53FB319 CRC64;
MGAGKSPAGP GQKPDPGKLP AAGVLRILRG SSGLWRKRRA RTSAETGRAG LSAAMSAKAI
SEQTGKELLY KFICTTSAIQ NRFKYARVTP DTDWARLLQD HPWLLSQNLV VKPDQLIKRR
GKLGLVGVNL TLDGVKSWLK PRLGQEATVG KATGFLKNFL IEPFVPHSQA EEFYVCIYAT
REGDYVLFHH EGGVDVGDVD TKAQKLLVGV DEKLNPEDIK KHLLVHAPED KKEILASFIS
GLFNFYEDLY FTYLEINPLV VTKDGVYVLD LAAKVDATAD YICKVKWGDI EFPPPFGREA
YPEEAYIADL DAKSGASLKL TLLNPKGRIW TMVAGGGASV VYSDTICDLG GVNELANYGE
YSGAPSEQQT YDYAKTILSL MTREKHPDGK ILIIGGSIAN FTNVAATFKG IVRAIRDYQG
PLKEHEVTIF VRRGGPNYQE GLRVMGEVGK TTGIPIHVFG TETHMTAIVG MALGHRPIPN
QPPTAAHTAN FLLNASGSTS TPAPSRTASF SESRADEVAP AKKAKPAMPQ DSVPSPRSLQ
GKSTTLFSRH TKAIVWGMQT RAVQGMLDFD YVCSRDEPSV AANSNYSKTL SQNKNMADAM
RKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG IPEALTRKLI KKADQKGVTI
IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV SRSGGMSNEL NNIISRTTDG
VYEGVAIGGD RYPGSTFMDH VLRYQDTPGV KMIVVLGEIG GAEEYKICRG IKEGRLTKPI
VCWCIGTCAT MFSSEVQFGH AGACANQASE TAVAKNQALK EAGVFVPRMD LGEDAEYTQQ
GSPGKICGGH QGPASLFPIS AQELGLIRKP ASFMTSICDE RGQELIYAGM PITEVFKEEM
GIGGVLGLLW FQKRLPKYSC QFIEMCLMVT ADHGPAVSGA HNTIICARAG KDLVSSLTSG
LLTIGDRFGG ALDAAAKMFS KAFDSGIIPM EFVNKMKKEG KLIMGIGHRV KSINNPDMRV
QILKDYVRQH FPATPLLDYA LEVEKITTSK KPNLILNVDG LIGVAFVDML RNCGSFTREE
ADEYIDIGAL NGIFVLGRSM GFIGHYLDQK RLKQGLYRHP WDDISYVLPE HMSM
//
