ID F0YJG1_AURAN Unreviewed; 1127 AA.
AC F0YJG1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 ORFNames=AURANDRAFT_72443 {ECO:0000313|EMBL:EGB04787.1};
OS Aureococcus anophagefferens (Harmful bloom alga).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC Aureococcus.
OX NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN [1] {ECO:0000313|EMBL:EGB04787.1, ECO:0000313|Proteomes:UP000002729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT "Niche of harmful alga Aureococcus anophagefferens revealed through
RT ecogenomics.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
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; GL833147; EGB04787.1; -; Genomic_DNA.
DR RefSeq; XP_009040523.1; XM_009042275.1.
DR AlphaFoldDB; F0YJG1; -.
DR EnsemblProtists; EGB04787; EGB04787; AURANDRAFT_72443.
DR GeneID; 20228708; -.
DR KEGG; aaf:AURANDRAFT_72443; -.
DR eggNOG; KOG1254; Eukaryota.
DR InParanoid; F0YJG1; -.
DR OMA; MDYAWAK; -.
DR OrthoDB; 536at2759; -.
DR Proteomes; UP000002729; Unassembled WGS sequence.
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; 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:UP000002729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036511}.
FT DOMAIN 255..430
FT /note="ATP-citrate synthase citrate-binding"
FT /evidence="ECO:0000259|Pfam:PF16114"
FT DOMAIN 678..803
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT ACT_SITE 778
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
SQ SEQUENCE 1127 AA; 121470 MW; F07BE2D9795D8EEA CRC64;
MAAKPVREYF GKQLLAKYLG EASGGEFEFE GRGMLVKSGA SDPASPSSWA ALLAAHPWAR
DARLVAKPDQ LIKRRGKAGL LAIDKSFDEC RAWVDARMNA TIDVEGVEGV LHTFLVEPFV
PHAQADEYYV CVVSNREGEE LLFCKDGGVD VGDVDAKAKR LQVPLGESAA PDALAAALLD
GVPEARKPKL ARFLATLLGV YRQLHFVYME INPIVFEEGG KITPLDLAAK LDETAAFLVQ
NKWGPGVDFP APFGRAEFPE EAYIRSMDAK TGASLKLTIL NVAGRVWTMV AGGGASVVYA
DTICDLGFAH ELANYGEYSG APNDEQTYNY ARTILGLMTR TRRDDGKVLI VGGGIANFTD
VAATFRGLIK ALRAFKDELK AGGVKIYVRR AGPNYQEGLR MMLRLRDETG LHVRVFGPEQ
DAVAPCAIAL GLKAEDSLPD FDPDAESKVA TVADAAPADA TILKRSFSSG SLTQFDATLS
SMASVQFTAE TRCLVYGLQQ RAVPKSTTGR VIPAKLQTSL ARQRAVQGML DFDFMCKRKK
PSVAAMVYPF QGNHYVKFYW GTEETLVPVY TSIAEAASKH GDASCLVNFA SYRSVYDTCM
ETFKLSAQIR TVAIIAEGVP EAQTRDIAAA AEEAGVGLVG PATVGGIKPG CFRIGNTGGM
LDNIVMSKLY RPGSVCYVSK SGGMSNELNN IIARSSDGVC EGVAIGGDRY PGSRFIDHLL
RYNDNPDCQI LVLLGEVGGV DEYDVCAALE SGRIDKPLVA WCIGTCASAF SFEVQFGHAG
ACARGLGEAA VDKNAALAKA GAVVPRSFAE FGARLSEVYA LLVDRGTIVP RPEPEVPKVP
MDYTWAKRLG MVRKPANFIS TISDDRGEEL TYGGMRISDV FKEDLGVGGV LSLLWFKKRL
PPYATKFIEM ILMVTADHGP AVSGARGAAR EQSDSTHNTI VSTRAGKDLV SSLVSGLLTI
GPRFGGALDG AATMMTDACD RGMSGKQFVD DCKREGKLIM GIGHRIKSVE NPDMRVEIIK
KYAQAHFPKT PTLDFALEVE AVTTAKRSTL ILNVDGCIAV CFVDLLRHCG AMTVEEADEL
IANGCLNGLF VLGRSLGFIG HHLDQKRLKQ PLYRHPWDDI SYIGGDM
//
