ID A0A0V1BQD1_TRISP Unreviewed; 1143 AA.
AC A0A0V1BQD1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
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 Name=ACLY {ECO:0000313|EMBL:KRY39073.1};
GN ORFNames=T01_4784 {ECO:0000313|EMBL:KRY39073.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY39073.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY39073.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY39073.1};
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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:KRY39073.1}.
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DR EMBL; JYDH01000021; KRY39073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1BQD1; -.
DR STRING; 6334.A0A0V1BQD1; -.
DR eggNOG; KOG1254; Eukaryota.
DR InParanoid; A0A0V1BQD1; -.
DR Proteomes; UP000054776; 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; 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; 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.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054776};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 489..598
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT ACT_SITE 787
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
FT NON_TER 1143
FT /evidence="ECO:0000313|EMBL:KRY39073.1"
SQ SEQUENCE 1143 AA; 127408 MW; C7B7B29A4607CD17 CRC64;
MSSRAITEFQ AKTIVYNNID QCPLKILPIA HFDLRQSWDS FENVNHWIDQ ETRLVVKVDQ
LIKRRGKLGL LEKDVTYLSA KKWIKSKSEK EIQIGKIHGY VTNFVIEPYI SHKEEDECYV
CIYSVRSGDV VLFYHRGGID VGDVDQKSEN LFIPLEKTPS YVEIVSKLLI NLKCNVKKQL
VAEFIIKLYQ LYVNLHFTYL EINPLLVNGD DKTIYMLDIA AKLDSAADFM CRRQWGEIEF
PTPFGRQLLP EEQYVAELDS RSGASLKLTV LNKEGRIWTM VAGGGASFLF YLLYFSNSYS
DTICDMGEAS ELANYGEYSG APTEVQTYEY AKTILKLMTS TKVHKSGKVL IIGGSIANFT
NVADTFKGII LALEEYRLEL IRHKVSIYVR RGGPNFQEGL RLMKEAGKTL EIPVHVYGTD
THMTAVVGMA MGKVSHCCKN PQPVATASFL LNTSQSTASL SMDSEQASSG PVDQVQFDLD
KSGEANRELF TSNTRAIVWG MQVKAVQSML DFDYVCQRKL PSVVAMTYPM TGDHKQKFYF
GHKEILIPVY KSMAKAIEKH PDASVLINFA SLRSAYDATV EALQFPQVRC IAIIAEGIPE
NFTRKLITRA EQAGVTIIGP ATVGGIKPGC FKIGNTGGMM DNIMASKLYR PGSVAYVSRS
GGMSNELNNI ISQVTNGVYE GVAIGGDRKI FKIRYPCSTF CDHLLRFEDD PKVKMMVMLG
EIGGVEEYKV CELLKNGKIK KPLVAWCIGT CASFLPSEMV IMNCLNKCRQ CKNRTVKVGV
GLVQFGHSGA SAAAEKETAC SKNRALKDAG AHVPNTFDDL ATCIKKIYEE LVQDGKIQLL
DEKPPPAVPM DYSWARELGL IRKPSSFMSS ICDERGNELL YAGVPISKII SEGLGLGGVL
SLLWFRRRLP DYAFKFIEMC LIVTADHGPA VSGAHNTIVC ARAGKDLVSS LVSGLLTILN
KSTRANGKLT YKGERFGGAL DMAAKQFSRA YDEGLNPMEF VHKMRKEGQL IMGIGHRVKS
INNPDARVKI LHDYVVEHFP EHPLVDYAKQ VEQITTKKKP NLILNVDGII GVAFVDLLRK
SGCFTEQEAQ EYIDIGTLNG LFVLGRSIGF IGHYLDQKRL KQGLYRHPWD DITYLMPEDS
TNL
//
