ID   A0A1I7Z5V5_9BILA        Unreviewed;       613 AA.
AC   A0A1I7Z5V5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE            EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
OS   Steinernema glaseri.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC   Steinernema.
OX   NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g23071.t1};
RN   [1] {ECO:0000313|WBParaSite:L893_g23071.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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:ARBA00001688};
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DR   WBParaSite; L893_g23071.t1; L893_g23071.t1; L893_g23071.
DR   Proteomes; UP000095287; Unplaced.
DR   GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 3.30.470.110; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR032263; Citrate-bd.
DR   InterPro; IPR002020; Citrate_synthase.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR23118; ATP-CITRATE SYNTHASE; 1.
DR   PANTHER; PTHR23118:SF42; ATP-CITRATE SYNTHASE; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF16114; Citrate_bind; 1.
DR   Pfam; PF02629; CoA_binding; 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.
PE   4: Predicted;
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          25..209
FT                   /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT                   /evidence="ECO:0000259|Pfam:PF08442"
FT   DOMAIN          251..428
FT                   /note="ATP-citrate synthase citrate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16114"
FT   DOMAIN          504..597
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02629"
FT   REGION          428..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  67912 MW;  A4BDB5DB0D0AD183 CRC64;
     MSAKAVSEFT GKELLYRHLA DAGYVDKPKA FPIAENESFQ DAARGCEWIQ SQKAVIKPDQ
     LIKRRGKHGL VKIGSAEEVQ QWFEANRGQY VQVGKTRGRL THFIVEPFVA HTEQDELYVA
     IFSKRNEDVI LFYEHGGVEI GDVDSKARSV SVPVQLVDSK MEVSSADLDK LVGKLPGGKE
     KLVKDFVQRL YKIYRENHFT YLEINPLVVV ENKVYILDLA AKLDETALFL CSEMWKTREG
     ENVDFPAPFG RDLSKEEKYI AELDAKTGAS LKLTVLNREG SIWTMVAGGG SSVVFTDTIC
     DLGGAQELAN YGEYSGDPSE TQTFEYAKTI LSMMTEGAKR EDGKVLIIGG SIANFTNVAM
     TFKGIVRALE AFASQLKEHN VTVYVRRGGP NYQEGLRKMK DLSVKIGIPI HVYGPETHMT
     AIVGAAMKPP NETREAXXXX PSPPSAPQTT GQFLLAPERN TGGTVPSAPA VNSPTALDDD
     SRPDQIPEVV EIDGHRTQIS KIFDRNTKAI VWGQQVKAIQ GMLDFDFVCG RESPSVVAST
     YPFTGDHKQK FYFGHKEIFV PAYKSMEKAF VQHPDASVLV TFASLRSVFE TVMQALEFPQ
     LKPSSSTPTP PFW
//