ID A0A267EDT4_9PLAT Unreviewed; 1109 AA.
AC A0A267EDT4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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};
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 ORFNames=BOX15_Mlig026952g1 {ECO:0000313|EMBL:PAA58989.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA58989.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA58989.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA58989.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA58989.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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:PAA58989.1}.
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DR EMBL; NIVC01002311; PAA58989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267EDT4; -.
DR STRING; 282301.A0A267EDT4; -.
DR Proteomes; UP000215902; 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; 1.10.580.10; 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 PRINTS; PR01798; SCOASYNTHASE.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 497..606
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT ACT_SITE 765
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PAA58989.1"
SQ SEQUENCE 1109 AA; 119945 MW; CC5F3529E0F93D35 CRC64;
SAKAIYENKG KELLYKHLKS DGLSAMPSII VTGETNWQTL ESENDWLKSG KLVCKPDQLI
KRRGKLGLVC AGSDLAGVQQ FVRARVDKPF EIGKTQGLLK RFIIEPFVAH EQNEEFYLCI
LSERQHDIIL FHHEGGVDIG NVEDKALRLE VPIDTKAADC NIASLLTGIK DAQVQSLLLN
FIADLHRVYC DLHFTYLEVN PLVVRAGRIH ILDLAARLDQ CAEYLCKSAW GSNVDFPPPF
GREAFPEEAY IAELDARSGA SLKLTVLNPE GRVWTMVAGG GASVIYADTV CDMGSASELA
NYGEYSGAPT EEQTYEYAKT LLSLMTRTVR PDGKVLIIGG GIANFTNVAA TFKGIVRALR
QYQAQLVKCG AEIFVRRAGP NYQEGLRVMR ELGENLGVQI HVFGPETHMT AIVGMALGKR
PIPDKPDAAK PATTANFLLP TSENSATAAA AASARAAAAG TAAAGASVAT AASSASGATS
GVDGLSGASG GAPDAPLFNP GTKCIVWGMQ QRSVQNCLDF DFVCSRREPS VVAIVYPFVG
NHNQKYYWGH NEILIPVYKQ MSDAMRKHPD ASVMVNFASL RSAYDSTLEA LQFPQIRVIA
IIAEGIPENL SRRLALRAAE KSVTVIGPAT VGGVKPGCFK IGNTGGMMDN ILNSKLYRPG
SVAYVSRSGG MSNELNNIIA LNADGVLEGV AIGGDRYPGS TFLDHLLRYQ ADPGAQMLVV
LGEVGGQEEW RIADALRDGR ITKPMVAWCI GTCAGLLGSE VQFGHAGACA NSGQETASAK
NAALAAAGAH VPASFDQLGE TIRCVYEDLV GRGVIVPKEE PAPPTVPMDY SWARELGLIR
KPSSFMTSIC DERGQELLYA GVPITEIINR DFGIGGVLSL LWFQRRLPKY ACKFIEMCLI
ITADHGPAVS GAHNTIVCAR AGKDLVSCLT SGLLTIGDRF GGALDGAAKQ FSHGVDTGLI
PMEFVNEMRK RGELIMGIGH RVKSINNPDM RVEILKKFAL ENFPASPMLH YALEVEKITT
SKKPNLILNV DGMIGVAMVD LLRHCGCFTR EEADEFIEIG ALNGMFVLGR SMGFIGHYLD
QRRLKQGLYR HPWDDISYVM PEQSQWAPW
//
