ID A0A0V1A9D6_9BILA Unreviewed; 1088 AA.
AC A0A0V1A9D6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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|EMBL:KRY21398.1};
GN ORFNames=T12_16786 {ECO:0000313|EMBL:KRY21398.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY21398.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY21398.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY21398.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00011881,
CC ECO:0000256|PIRNR:PIRNR036511}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the succinate/malate
CC CoA ligase alpha subunit family. {ECO:0000256|PIRNR:PIRNR036511}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the succinate/malate
CC CoA ligase beta subunit family. {ECO:0000256|PIRNR:PIRNR036511}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY21398.1}.
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DR EMBL; JYDQ01000017; KRY21398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1A9D6; -.
DR Proteomes; UP000054783; 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; 1.10.580.10; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, 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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, 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:UP000054783};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036511}.
FT DOMAIN 472..581
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT ACT_SITE 746
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
SQ SEQUENCE 1088 AA; 121259 MW; E2EE96D3701917A1 CRC64;
MSSRAITEFQ AKTIVYNNID QCPLKILPIA HFDLRQSWDS FENVNHWIDQ ETRLVVKVDQ
LIKRRGKLGL LEKDVTYLSA KKWIKSKSEK EIQIGKIHGY VTNFVIEPYI SHKQEDECYV
CIYSVRSGDV VLFYHRGGID VGDVDQKSEN LFVPLEKTPS YVEIVSKLLI NLKCNVKKQL
VAEFIIKLHQ LYVNLHFTYL EINPLLVNGD DKTIYMLDIA AKLDSAADFM CRRQWGEIEF
PTPFGRQLLP EEQYVAELDS RSGASLKLTK VEFGQWSLVV VLRDTICDMG EASELANYGE
YSGAPTEVQT YEYAKTILKL MTSTKVHKSG KVLIIGGSIA NFTNVADTFK GIILALEEYR
LELIRHKVSI YVRRGGPNFQ EGLRLMKEAG KTLEIPVHVY GTDTHMTAVV GMAMGKVSHC
CKNSQPVATA SFLLNTSQST ASLSMDSEQA SSGPVDQVQF DLDKSGEANR ELFTSNTRAI
VWGMQVKAVQ SMLDFDYVCQ RKLPSVVAMT YPMTGDHKQK FYFGHKEILI PVYKSMAKAI
EKHPDASVLI NFASLRSAYD ATVEALQFPQ VRCIAIIAEG IPENFTRKLI TRAEQAGVTI
IGPATVGGIK PGCFKIGNTG GMMDNIMASK LYRPGSVAYV SRSGGMSNEL NNIISQVTNG
VYEGVAIGGD RKIFKIRYPC STFCDHLLRF EDDPKVKMMV MLGEIGGVEE YKVCELLKNG
KIKKPLVAWC IGTCASFLPS EVQFGHSGAS AAAEKETACS KNRALKDAGA HVPNTFDDLA
TCIKKIYEEL VQDGKIQLLD EKPPPAVPMD YSWARELGLI RKPSSFMSSI CDERGNELLY
AGVPISKIIS EGLGLGGVLS LLWFRRRLPD YAFKFIEMCL IVTADHGPAV SGAHNTIVCA
RAGKDLVSSL VSGLLTIGER FGGALDMAAK QFSRAYDEGL NPMEFVHKMR KEGQLIMGIG
HRVKSINNPD ARVKILHDYV VEHFPEHPLV DYAKQVEQIT TKKKPNLILN VDGIIGVAFV
DLLRKSGCFT EQEAQEYIDI GTLNGLFVLG RSIGFIGHYL DQKRLKQGLY RHPWDDITYL
MPEDSTNL
//
