ID A0A1Z5TBY0_HORWE Unreviewed; 657 AA.
AC A0A1Z5TBY0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, 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=BTJ68_06472 {ECO:0000313|EMBL:OTA33532.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA33532.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA33532.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA33532.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OTA33532.1}.
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DR EMBL; MUNK01000074; OTA33532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5TBY0; -.
DR STRING; 1157616.A0A1Z5TBY0; -.
DR VEuPathDB; FungiDB:BTJ68_06472; -.
DR InParanoid; A0A1Z5TBY0; -.
DR OrthoDB; 536at2759; -.
DR Proteomes; UP000194280; 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 Reference proteome {ECO:0000313|Proteomes:UP000194280};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..144
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 657 AA; 71631 MW; A35454BE6656F3DF CRC64;
MAPTAVPNGT GSANDNIQRF TAPSRSMSPT PEHTLFHPKT RCFVYGLQPR AVQGMLDFDF
ICKRKTPSVA GIIYTFGGQF VSKMYWGTSE TLLPVYQSSD KAMSKHSDVD TVVNFASSRS
VYQSTMELME YPQIKCIAII AEGVPERRAR EILHVAKKKG VTIIGPATVG GIKPGAFKIG
NTGGMMDNIV ASKLYRKGSV GYVSKSGGMS NELNNIIAQT TDGVYEGVAI GGDRYPGTTF
IDHLLRYQND PECKILVLLG EVGGVEEYRV IEAVKNGTIT KPVVAWAIGT VAGMLTTEVQ
FGHAGSFANS QLETANTKNS SMKEAGIHVP ETFEDLPAVL AQVYQDTVKK GVIKPQPEPA
VPKIPIDYSW AQELGLIRKP AAFISTISDD RGQELLYAGM PISDVFKENI GIGGVMSLLW
FRRRLPDYAG RFLEMVLMLT ADHGPAVSGA MNTIITTRAG KDLISALVSG LLTIGSRFGG
ALDGAAEEFT RAYDKGLSPR DFVDTMRKEN KLIPGIGHRV KSRNNPDLRV TLVKEFCQQN
FPSTKLLDYA IAVESVTTSK KDNLILNVDG CVAVCFVDLL RNCGAFSQEE AEDYLKMGVL
NGLFVLGRSI GLIAHFLDQK RLRTGLYRHP WDDITYLLPE LGRGAPGHEG RVEVNVK
//
