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Database: UniProt
Entry: M2ZH17_PSEFD
LinkDB: M2ZH17_PSEFD
Original site: M2ZH17_PSEFD 
ID   M2ZH17_PSEFD            Unreviewed;       666 AA.
AC   M2ZH17;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE            EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN   ORFNames=MYCFIDRAFT_212387 {ECO:0000313|EMBL:EME78439.1};
OS   Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS   fungus) (Mycosphaerella fijiensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=383855 {ECO:0000313|EMBL:EME78439.1, ECO:0000313|Proteomes:UP000016932};
RN   [1] {ECO:0000313|EMBL:EME78439.1, ECO:0000313|Proteomes:UP000016932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRAD86 {ECO:0000313|EMBL:EME78439.1,
RC   ECO:0000313|Proteomes:UP000016932};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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DR   EMBL; KB446563; EME78439.1; -; Genomic_DNA.
DR   RefSeq; XP_007930821.1; XM_007932630.1.
DR   AlphaFoldDB; M2ZH17; -.
DR   STRING; 383855.M2ZH17; -.
DR   GeneID; 19337698; -.
DR   KEGG; pfj:MYCFIDRAFT_212387; -.
DR   eggNOG; KOG1254; Eukaryota.
DR   HOGENOM; CLU_006587_4_1_1; -.
DR   OrthoDB; 536at2759; -.
DR   Proteomes; UP000016932; 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:0046872; F:metal ion binding; 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; IPR005811; CoA_ligase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
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   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:UP000016932};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          48..152
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02629"
FT   DOMAIN          212..335
FT                   /note="ATP-citrate lyase/succinyl-CoA ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00549"
SQ   SEQUENCE   666 AA;  72345 MW;  4B1B70317C58A482 CRC64;
     MAQPNGTANG VNGHKQSEGL SANDNIQRFA APSRPLSPTP VHTLFHPKTR CFVYGMQTKA
     VQGMLDFDFI CKRKTPSVAG IIYTFGGQFV SKMYWGTSET LLPVYQNPEN AMAKHSDVDT
     VVNFASSRSV YSSTMELMNY PQIKCIAIIA EGVPERRARE ILHVAKKKGV TIIGPATVGG
     IKPGAFKIGN TGGMMDNIVA SKLYRKGSVG YVSKSGGMSN ELNNIVSQNT DGVYEGVAIG
     GDRYPGTTFI DHMLRYQADP ECKILLLLGE VGGVEEYRVI DAVKQGIITK PIVAWAIGTV
     ASMLKTEVQF GHAGAMANSQ LETAAVKNKS MRDAGFFVPD TFEDLPGLLA QVYNKLVSNG
     NIKPAPEPAV PKIPMDYSWA QELGMIRKPA AFISTISDDR GQELLYAGIP ITEVFKEDIG
     IGGVMSLLWF RRRLPTYASK FLEMVLMLTA DHGPAVSGAM NTIITTRAGK DLISSLVAGL
     LTIGSRFGGA LDGAAEEFTK AFDKGLSPRD FVDTMRKENK LIPGIGHRVK SRNNPDLRVT
     LVKEYCQKNF PSTKLLDYAL AVESVTTSKK DNLILNVDGC VAVCFVDLLR NSGAFSAEEA
     EDYFKMGVLN GLFVLGRSIG LIAHFLDQKR LRTGLYRHPW DDITYLLPEL GKGAPGNEGR
     VEVSVG
//
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