ID A0A0V1PK45_9BILA Unreviewed; 1050 AA.
AC A0A0V1PK45;
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:KRZ96596.1};
GN ORFNames=T08_7804 {ECO:0000313|EMBL:KRZ96596.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ96596.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ96596.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ96596.1};
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:KRZ96596.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDM01000007; KRZ96596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1PK45; -.
DR Proteomes; UP000054924; 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; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF036511; ATP_citrt_syn; 2.
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:UP000054924};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 472..581
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT ACT_SITE 756
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
FT NON_TER 1050
FT /evidence="ECO:0000313|EMBL:KRZ96596.1"
SQ SEQUENCE 1050 AA; 116836 MW; B4791455DB32362C CRC64;
MSSRAITEFQ AKTIVYNNID RCPLKILPIA HFDLRQSWDS FENVNHWIDQ ETRLVVKVDQ
LIKRRGKLGL LEKDVTYLSA KKWIKSKSEK EIQIGKIHGY VTNFVIEPYI SHKQEDECYV
CIYSVRSGDV VLFYHRGGID VGDVDQKSEN LFIPLEKTPS 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
CKNPQPVATA SFLLNTSQST ASLSMDSEQA SSGPVDQVQF GLDKSGEANR ELFTSNTRAI
VWGMQVKAVQ SMLDFDYVCQ RKLPSVVAMT YPMTGDHKQK FYFGHKEILI PVYKSMAKAI
EKHPDASVLI NFASLRSAYD ATVEALQFPQ VRCIAIIAEG IPENFTRKLI TRAEQAGVTI
IGPATVGGIK PGCFKIGNTG GMMDNIMASK LYRPGSVAYV SRSGGMSNEL NNIISQVTNG
VYEGVAIGGD RKILKIRYPC STFCDHLLRF EDDPKVKMMV MLGEIGGVEE YKVCELLKNG
KIKKPLVAWC IGTCASFLPS ENRAVKVGVG LVQFGHSGAS AAAEKETACS KNRALKDAGA
HVPNTFDDLA TCIKKIYEEL VQDGKIQLLD EKPPPAVPMD YSWARELGLI RKPSSFMSSI
CDERGNELLY AGVPISKIIS EGLGLGGVLS LLWFRRRLPD YAFKFIEMCL IVTADHGPAV
SGAHNTIVCA RAGKDLVSSL VSGLLTIINN PDARVKILHD YVVEHFPEHP LVDYAKQVEQ
ITTKKKPNLI LNVDGIIGVA FVDLLRKSGC FTEQEAQEYI DIGTLNGLFV LGRSIGFIGH
YLDQKRLKQG LYRHPWDDIT YLMPEDSTNL
//
