ID F9XJE1_ZYMTI Unreviewed; 664 AA.
AC F9XJE1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=MYCGRDRAFT_62567 {ECO:0000313|EMBL:EGP84439.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP84439.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP84439.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
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DR EMBL; CM001204; EGP84439.1; -; Genomic_DNA.
DR RefSeq; XP_003849463.1; XM_003849415.1.
DR AlphaFoldDB; F9XJE1; -.
DR STRING; 336722.F9XJE1; -.
DR EnsemblFungi; Mycgr3T62567; Mycgr3P62567; Mycgr3G62567.
DR GeneID; 13402444; -.
DR KEGG; ztr:MYCGRDRAFT_62567; -.
DR eggNOG; KOG1254; Eukaryota.
DR HOGENOM; CLU_006587_4_1_1; -.
DR InParanoid; F9XJE1; -.
DR OMA; HMLRYQA; -.
DR OrthoDB; 536at2759; -.
DR Proteomes; UP000008062; Chromosome 9.
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 Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 43..152
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 664
FT /evidence="ECO:0000313|EMBL:EGP84439.1"
SQ SEQUENCE 664 AA; 72146 MW; 025A4EF64C0B52F3 CRC64;
MAPATANGTN GVNGHDTNLS ANDNIQRFAA PSRPLSPQAN HTLFHPKTRC FVYGMQTKAV
QGMLDFDFIC KRKTPSVAGI IYTFGGQFVS KMYWGTSETL LPVYQTVEQA MSKHSDVDCV
VNFASSRSVY TSTMELLEFP QIKSIAIIAE GVPERRAREI LHVAKKKGVT IIGPATVGGI
KPGAFKIGNT GGMMDNIVAS KLYRKGSVGY VSKSGGMSNE LNNLVANYTD GVYEGVAIGG
DRYPGTTFID HMLRYEADPN CKILLLLGEV GGVEEYRVIE AVKAGVIKKP IVAWAIGTVA
SMLKTEVQFG HAGSLANSLL ETAATKNSSM REAGFYVPNT FEELPEMLST VYQKLVKAGT
IVPAPEPGVP KIPIDYSWAQ ELGLIRKPAA FISTISDDRG QELLYAGLPI SDVFRDNIGI
GGVMSLLWFR RRLPDYASKF LEMVLMLTAD HGPAVSGAMN TIITTRAGKD LISALVAGLL
TIGSRFGGAL DGAAEEFTRA FDKGLSPRDF VDTMRKENKL IPGIGHRVKS RNNPDLRVSL
VKEYCQANFP NTKLLDYALA VESVTTSKKD NLILNVDGCV AVCFVDLLRN SGAFSNEEAE
DYLKMGVLNG LFVLGRSIGL IAHFLDQKRL RTGLYRHPWD DITYLLPELG KGAPGNEGRV
EVDM
//
