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Database: UniProt
Entry: A0A0G2IDQ8_9EURO
LinkDB: A0A0G2IDQ8_9EURO
Original site: A0A0G2IDQ8_9EURO 
ID   A0A0G2IDQ8_9EURO        Unreviewed;       659 AA.
AC   A0A0G2IDQ8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE            EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN   ORFNames=EMCG_05691 {ECO:0000313|EMBL:KKZ68703.1};
OS   Emmonsia crescens UAMH 3008.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX   NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ68703.1, ECO:0000313|Proteomes:UP000034164};
RN   [1] {ECO:0000313|Proteomes:UP000034164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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:KKZ68703.1}.
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DR   EMBL; LCZI01000065; KKZ68703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2IDQ8; -.
DR   VEuPathDB; FungiDB:EMCG_05691; -.
DR   Proteomes; UP000034164; 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; 1.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
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; PF00285; Citrate_synt; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF48256; Citrate synthase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          38..147
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   659 AA;  72097 MW;  8F542647F3800662 CRC64;
     MPSTVPLANT ANGNLSANDN IRRFVAPSRP FTPLEHNLFH NKTRCFVYGM QPRAVQGMLD
     FDFICKRTTP SVAGIIYTFG GQFVSKMYWG TSETLLPVYQ EVEKAIAKHP DVDTVVNFAS
     SRSVYTSTME LMQFPQIKSI AIIAEGVPER RAREIMVAAK EKGITIIGPA TVGGIKPGAF
     RIGNTGGMMD NIVASKLYRK GSVGYVSKSG GMSNELNNII SQNTDGVYEG VAIGGDRYPG
     TTFIDHLLRY QADPECKILV LLGEVGGVEE YRVIEAVRDG TITKPIVAWA IGTCASLFKT
     EVQFGHAGAS ANSELETAVM KNKCMREAGI HVPDTFEELP QLLAEVYKKL VKQGTIKPQP
     EPVPPKIPID YAWAQELGLI RKPAAFISTI SDDRGQELLY AGMPISDVFR EDIGIGGVMS
     LLWFRRRLPV YASKFLEMVL MLTADHGPAV SGAMNTIITT RAGKDLISAL VSGLLTIGSR
     FGGALDGAAE EFTKAFDKGL SPRDFVDTMR KENKLIPGIG HKVKSRANPD LRVELVKEFV
     HKNFPNHKLL DYAIAVETVT TSKKDNLILN VDGCVAVCFV DLLRNCGAFS PEEAEDYLSM
     GVLNGLFVLG RSIGLIAHFL DQKRLRTGLY RHPWDDITYL LPTLQKGAPG AEGRVEVTL
//
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