ID A0A091FSK2_9AVES Unreviewed; 1075 AA.
AC A0A091FSK2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
DE Flags: Fragment;
GN ORFNames=N303_00607 {ECO:0000313|EMBL:KFO72149.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO72149.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO72149.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO72149.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL447298; KFO72149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091FSK2; -.
DR STRING; 55661.A0A091FSK2; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
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; 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 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:UP000053760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 466..575
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 425..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 734
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO72149.1"
FT NON_TER 1075
FT /evidence="ECO:0000313|EMBL:KFO72149.1"
SQ SEQUENCE 1075 AA; 118361 MW; E16A5B97C8200D31 CRC64;
KYICTSSAIQ NRFKYARVTP DTDWARLTQD HPWLLSERLV VKPDQLIKRR GKLGLVGINL
TLDQVKVWLK QRLGQETTIA NAKGILKNFL IEPFVPHKQE EEFYVCIYAA REGDYVLFHH
EGGVDVGDVD AKAQKLLVAV DEKLSESDVK KHLLQHAPAH KKDVLASFIC GLFNLYEDLY
FTYLEINPLV VTNDGVYILD LAAKIDATAD YICKMKWGDV EFPPPFGREA YPEATYIADL
DAKSGASLKL TILNPKGRIW TMVAGGGASV VYSDTICDLG GVNELANYGE YSGAPSEQQT
YDYAKTILSL MTREKHPEGK ILIIGGSIAN FTNVAATFKG IVRAIKDYQG PLKEHEVRIF
VRRGGPNYQE GLRVMGEVGK TTGIPIHVFG TETHMTAIVG MALGHRPIPN QPPAAAHTAN
FLLNASGSPS TPAPSRTASF SESRPDDIAP AKKAKPTAPL GKATTLFSRH TKAIIWGMQT
RAVQGMLDFD YICSRDEPSV AAMVYPFTGD HRQKFYWGHK EILIPVYKNM SDAMKKHPEV
DVLINFASLR SAYDSTVETM NYPQIRTIAI IAEGIPEALT RKLIKTADKK GVTIIGPATV
GGIKPGCFKI GNTGGMLDNI LASKLYRPGS VAYVSRSGGM SNELNNIISR TTDGVYEGVA
IGGDRYPGST FMDHVLRYED TPGVKMIVVL GEIGGTEEYK ICRGIKEGRI TKPVVCWCIG
TCATMFSSEV QFGHAGACAN QTSETAVAKN QALREAGVFV PRSFDELGEV IQSVYQDLVA
KRVIEPAEEV PPPTVPMDYS WARELGLIRK PASFMTSICD ERGQELIYAG MPITEVFKEE
MGIGGVLGLL WFQRRLPKYA CQFIEMCLMV TADHGPAVSG AHNTIVCARA GKDLVSSLTS
GLLTIGDRFG GALDAAAKMF SKAFDSGIIP MEFVNKMKKE GKLIMGIGHR VKSLNNPDMR
VQILKDYVKQ HFPATPLLDY ALEVEKITTS KKPNLILNVD GFIGVAFVDV LRNCGSFTRE
EADEYIDIGA LNGIFVLGRS MGFIGHYLDQ KRLKQGLYRH PWDDISYVLP EHMTM
//
