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Database: UniProt
Entry: A0A2T2P4W0_CORCC
LinkDB: A0A2T2P4W0_CORCC
Original site: A0A2T2P4W0_CORCC 
ID   A0A2T2P4W0_CORCC        Unreviewed;       668 AA.
AC   A0A2T2P4W0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, 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};
GN   ORFNames=BS50DRAFT_483663 {ECO:0000313|EMBL:PSN72747.1};
OS   Corynespora cassiicola Philippines.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX   NCBI_TaxID=1448308 {ECO:0000313|EMBL:PSN72747.1, ECO:0000313|Proteomes:UP000240883};
RN   [1] {ECO:0000313|EMBL:PSN72747.1, ECO:0000313|Proteomes:UP000240883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philippines {ECO:0000313|EMBL:PSN72747.1,
RC   ECO:0000313|Proteomes:UP000240883};
RX   PubMed=29551995; DOI=10.3389/fmicb.2018.00276;
RA   Lopez D., Ribeiro S., Label P., Fumanal B., Venisse J.S., Kohler A.,
RA   de Oliveira R.R., Labutti K., Lipzen A., Lail K., Bauer D., Ohm R.A.,
RA   Barry K.W., Spatafora J., Grigoriev I.V., Martin F.M., Pujade-Renaud V.;
RT   "Genome-Wide Analysis of Corynespora cassiicola Leaf Fall Disease Putative
RT   Effectors.";
RL   Front. Microbiol. 9:276-276(2018).
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DR   EMBL; KZ678129; PSN72747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T2P4W0; -.
DR   STRING; 1448308.A0A2T2P4W0; -.
DR   Proteomes; UP000240883; 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:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   Lyase {ECO:0000313|EMBL:PSN72747.1};
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:UP000240883};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          47..156
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   668 AA;  72485 MW;  C595028CD450F1ED CRC64;
     MPSAAPVNGS TPQQAATSTD GGLSANDNIR RFAAPSRPLS PPAAHTLFHP KTRCFVYGLQ
     PRAVQGMLDF DFICKRKTPS VAGIIYTFGG QFVSKMYWGT SETLLPVYQS VEKAVAKHTD
     VDTVVNFASS RSVYSSTMEL MEFPQIKSIA IIAEGVPERR AREILYVAQK KGITIIGPAT
     VGGIKPGAFK IGNTGGMMDN IVASKLYRPG SVSYVSKSGG MSNELNNIIA NTTDGVLEGV
     AIGGDRYPGT TFIDHVLRYQ ADPDCKIIVL LGEVGGVEEY RVIEAVKSGQ VTKPIVAWAI
     GTVAGMLKTE VQFGHAGSFA NSQLETAATK NKTMREAGIY VPETFEEMPT TLAQVYQKLV
     KEGTIKPKTE PVVPKIPIDY SWAQELGLIR KPAAFISTIS DDRGQELLYA GMPISDVFKE
     NIGIGGVMSL LWFRRRLPDY ASRFLEMVLM LTADHGPAVS GAMNTIITTR AGKDLISALV
     SGLLTIGSRF GGALDGAAEE FTKAFDKGLS PRDFVDTMRK ENKLIPGIGH RIKSRNNPDL
     RVELVKEYVK KNFPSTKTLD YALAVETVTT SKKDNLILNV DGCIAVCFVD LMRNCGAFSA
     EEAEDYLRMG VLNGLFVLGR SIGLIAHFLD QKRLRTGLYR HPWDDITYLL PSLQGGAPGA
     EGRVEVSL
//
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