ID A0A443SH59_9ACAR Unreviewed; 883 AA.
AC A0A443SH59;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
DE Flags: Fragment;
GN ORFNames=B4U80_07623 {ECO:0000313|EMBL:RWS26815.1};
OS Leptotrombidium deliense.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombiculoidea; Trombiculidae; Leptotrombidium.
OX NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS26815.1, ECO:0000313|Proteomes:UP000288716};
RN [1] {ECO:0000313|EMBL:RWS26815.1, ECO:0000313|Proteomes:UP000288716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-UT {ECO:0000313|EMBL:RWS26815.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
CC -!- SIMILARITY: In the C-terminal section; belongs to the succinate/malate
CC CoA ligase alpha subunit family. {ECO:0000256|ARBA:ARBA00005899}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the succinate/malate
CC CoA ligase beta subunit family. {ECO:0000256|ARBA:ARBA00010719}.
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:RWS26815.1}.
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DR EMBL; NCKV01002456; RWS26815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443SH59; -.
DR STRING; 299467.A0A443SH59; -.
DR EnsemblMetazoa; LDEU005225-RA; LDEU005225-PA; LDEU005225.
DR VEuPathDB; VectorBase:LDEU005225; -.
DR Proteomes; UP000288716; 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: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; 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; 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; IPR017866; Succ-CoA_synthase_bsu_CS.
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 PRINTS; PR01798; SCOASYNTHASE.
DR SUPFAM; SSF48256; Citrate synthase; 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; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 3: Inferred from homology;
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:UP000288716};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..209
FT /note="ATP-citrate synthase citrate-binding"
FT /evidence="ECO:0000259|Pfam:PF16114"
FT DOMAIN 276..380
FT /note="CoA-binding"
FT /evidence="ECO:0000259|Pfam:PF02629"
FT DOMAIN 440..564
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT REGION 237..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RWS26815.1"
SQ SEQUENCE 883 AA; 96183 MW; 9BECD3AEB5D17E23 CRC64;
IYILDLAAKL DATAEFVCKQ QWGEITFPPP FGRDAFPEEA YIADLDSKSG ASLKLTILNR
NGRIWTMVAG GGASVIYADT ICELGGASEL ANYGEYSGAP TEQQTYEYAK TILSLMTKEV
HPDGKILIIG GGIANFTNVA ATFKGIVKAL REFQPKLIEH QVSIFVRRAG PNYQEGLRVI
REVGNTLGVP VHVFGAETHM TAVVAMAMGK REIPEMPEPN VTTANFLLPG MQSNNTGDIP
KSSSFPNSGS GSPTLQSRIS PTSMTASPQK QLFSPKTKSI VWGMQVRAVQ SMLDFDFVCS
RKEWSVAAMV YPFTGDHKLK FYWGHKEILI PCYKNMADAM KKHPEADVMI SFASLRSAYE
STLETLEYPQ IRTIAIIAEG IPENMTRKVN KLAKSKGVTI IGPATVGGIK PGSFKIGNTG
GMMDNILSSR LYRPGSVAYV SRSGGMSNEL NNIISRATNG VAEGVAIGGD RYPGTTFIDH
LFRYENDPNI KMMVLLGEVG GVEEYEVCEA IKSGKITKPV VAWCIGTCSG MFTSEVQFGH
AGACANSDRE TALAKNKALA EAGVHVPSTF DELGNVVKKV FDGLVETGVI VLTPEIPPPT
VPMDYNWARE LGLIRKPASF MTSICDERGH ELLYAGIPIT TVIKEELGIG GTLSLLWFQR
RLPAYACKFL EMCLMVTADH GPAVSGAHNT IVCARAGKDL VSSLVSGLLT IGDRFGGALD
GAARQFSDAY SSGMIPHEFV NSMRKKGQLI MGIGHRVKSI NNPDMRVKLM KEYVKQTFPA
TPILDYALEV EKITTSKKPN LILNVDGMIG VAIVDLLYHS GCFTPEEAQE YIEIGALNGL
FVLGRSIGFI GHFLDQKRLK QGLYRHPWDD ISYVLPETQF AQR
//
