ID A0A093FN91_TYTAL Unreviewed; 1087 AA.
AC A0A093FN91;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=N341_08522 {ECO:0000313|EMBL:KFV58125.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV58125.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV58125.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV58125.1};
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; KK397667; KFV58125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093FN91; -.
DR Proteomes; UP000054190; 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; 1.10.580.10; Citrate Synthase, domain 1; 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; IPR016142; Citrate_synth-like_lrg_a-sub.
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|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 478..587
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 437..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 746
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV58125.1"
FT NON_TER 1087
FT /evidence="ECO:0000313|EMBL:KFV58125.1"
SQ SEQUENCE 1087 AA; 119818 MW; 2756CBDA97CE7C81 CRC64;
AMSAKAISEQ TGKEFLYKYI CTSSAIQNRF KYARVTPVTD WARLTQDHPW LLSERLVVKP
DQLIKRRGKL GLVGINLTLD QVKVWLKQRL GQETTIANAK GILKNFLIEP FVPHRQEEEF
YVCIYAAREG DYVLFHHEGG VDVGDVDAKA QKLLVAVDEK LNESDVKKYL LQHAPANKKD
ILASFICGLF NLYEDLYFTY LEINPLVVTN DGVYILDLAA KIDATADYIC KVKWGDVEFP
PPFGREAYPE ATYIADLDAK SGASLKLTIL NPKGRIWTMV AGGGASVVYS DTICDLGGVN
ELANYGEYSG APSEQQTYDY AKTILSLMTR EKHPEGKCRA AQLPCAVCFF QGIVRAIKDY
QGPLKEHEVR IFVRRGGPNY QEGLRVMGEV GKTTGIPIHV FGTETHMTAI VGMALGHRPI
PNQPPAAAHT ANFLLNASGS PSTPAPSRTA SFSESKPDDI APAKKAKPTA PLGKATTLFS
RHTKAIIWGM QTRAVQGMLD FDYICSRDEP SVAAMVYPFT GDHRQKFYWG HKEILIPVYK
NMSDAMRKHP EVDVLINFAS LRSAYDSTVE TMNYPQIRTI AIIAEGIPEA LTRKLIKTAD
KKGVTIIGPA TVGGIKPGCF KIGNTGGMLD NILASKLYRP GSVAYVSRSG GMSNELNNII
SRTTDGVYEG VAIGGDRYPG STFMDHVLRY EDTPGVKMIV VLGEIGGTEE YKICRGIKEG
RITKPVVCWC IGTCATMFSS EVQFGHAGAC ANQASETAVA KNQALKEAGV FVPRSFDELG
EVIQSVYQDL VARRVIEPAE EVPPPTVPMD YSWARELGLI RKPASFMTSI CDERGQELIY
AGMPITEVFK EEMGIGGVLG LLWFQRRLPK YACQFIEMCL MVTADHGPAV SGAHNTIVCA
RAGKDLVSSL TSGLLTIGDR FGGALDAAAK MFSKAFDSGI IPMEFVNKMK KEGKLIMGIG
HRVKSINNPD MRVQILKDYV KQHFPATPLL DYALEVEKIT TSKKPNLILN VDGFIGVAFV
DVLRNCGSFT REEADEYIDI GALNGIFVLG RSMGFIGHYL DQKRLKQGLY RHPWDDISYV
LPEHMTM
//
