ID A0A0J9XIH0_GEOCN Unreviewed; 642 AA.
AC A0A0J9XIH0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN ORFNames=BN980_GECA18s02562g {ECO:0000313|EMBL:CDO57118.1},
GN DV451_003501 {ECO:0000313|EMBL:KAF5098222.1};
OS Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Geotrichum.
OX NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO57118.1, ECO:0000313|Proteomes:UP000242525};
RN [1] {ECO:0000313|EMBL:CDO57118.1, ECO:0000313|Proteomes:UP000242525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO57118.1,
RC ECO:0000313|Proteomes:UP000242525};
RA Casaregola S.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF5098222.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMA-70 {ECO:0000313|EMBL:KAF5098222.1};
RX PubMed=32457706;
RA Perkins V., Vignola S., Lessard M.H., Plante P.L., Corbeil J.,
RA Dugat-Bony E., Frenette M., Labrie S.;
RT "Phenotypic and Genetic Characterization of the Cheese Ripening Yeast
RT Geotrichum candidum.";
RL Front. Microbiol. 11:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF5098222.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMA-70 {ECO:0000313|EMBL:KAF5098222.1};
RA Perkins V., Lessard M.-H., Dugat-Bony E., Frenette M., Labrie S.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CCBN010000018; CDO57118.1; -; Genomic_DNA.
DR EMBL; QQZK01000077; KAF5098222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9XIH0; -.
DR STRING; 1173061.A0A0J9XIH0; -.
DR OrthoDB; 536at2759; -.
DR Proteomes; UP000242525; Unassembled WGS sequence.
DR Proteomes; UP000750522; 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:0016874; F:ligase 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; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:CDO57118.1};
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:UP000750522};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..120
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 642 AA; 70302 MW; 77A26FB2C1270E88 CRC64;
MSEQFQLPYE LFNNKTRAFV YGLQPRACQG MLDFDFICKR ETPSVAGVIY PFGGQFVTKM
YWGTKETLLP VYQEVEKAMA KHPDVDVVVN FASSRSVYSS TLELLQYPQI KTIAIIAEGV
PERRAREILY KAQKKGVTII GPATVGGIKP GCFKIGNTGG MMDNIVASKL YRPGSVAYVS
KSGGMSNELN NIIANTTNGV YEGVAIGGDR YPGTTFIDHI LRYEADPNCK IIVLLGEVGG
VEEYRVIEAV KNGSIKKPIV AWAIGTCASM FKTEVQFGHA GSMANSDLET AKSKNAAMKA
AGFFVPNTFE DFPETLALVY ESLVKKKVII PEPEPEVPKI PIDYSWAQEL GLIRKPAAFI
STISDDRGQE LLYAGIPISE VFKEDIGIGG VMSLLWFRRR LPSYAAKFLE MVLMLTADHG
PAVSGAMNTI ITTRAGKDLI SSLVSGLLTI GTRFGGALDG AATEFTNAFD KGLSPRQFVD
TMRKQNKLIP GIGHKVKSRN NPDFRVELVK EFVKKNFPAT NLLDYALAVE EVTTSKKDNL
ILNVDGCIAV SFVDLMRSSG AFTPEEVEEY LKNGVLNGLF VLGRSIGLIA HHLDQKRLKT
GLYRHPWDDI TYLVGQDAVQ NKRVEVDAKG VSKAASKKGP AK
//
