ID A0A317V308_9EURO Unreviewed; 656 AA.
AC A0A317V308;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN ORFNames=BO70DRAFT_366088 {ECO:0000313|EMBL:PWY68416.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY68416.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY68416.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY68416.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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:PWY68416.1}.
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DR EMBL; MSFL01000036; PWY68416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317V308; -.
DR STRING; 1448321.A0A317V308; -.
DR VEuPathDB; FungiDB:BO70DRAFT_366088; -.
DR OrthoDB; 536at2759; -.
DR Proteomes; UP000247233; 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 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:UP000247233};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 37..146
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 71593 MW; 18E555909633894B CRC64;
MPTSAPLVNT ANGSSANDNI TRFDPPSRVL SPLNHALFHN KTRCFVYGMQ PRAVQGMLDF
DFICKRSTPS VAGIIYTFGG QFVSKMYWGT SETLLPVYQD VSKAMAKHPD VDTVVNFASS
RSVYSSTMEL MECPQIKSIA IIAEGVPERR AREILVTAKE KGITIIGPAT VGGIKPGAFK
IGNTGGMMDN IVASKLYRKG SVGYVSKSGG MSNELNNIIS QNTDGVYEGV AIGGDRYPGT
TFIDHLLRYQ AEPECKILVL LGEVGGVEEY RVIEAVKNGT ITKPIVAWAI GTCASMFKTE
VQFGHAGASA NSDLETAVAK NKAMREAGIH VPETFEDLPQ LLAEVYQDQV NKGIVKPQPE
PVVPKIPIDY SWAQELGLVR KPAAFISTIS DDRGQELLYA GMPISDVFRE DIGIGGVMAL
LWFRRRLPRY ASKFLEMVLM LTADHGPAVS GAMNTIITTR AGKDLISSLV AGLLTIGSRF
GGALDGAAEE FAKAFDKGMS PRDFVDTMRK ENKLIPGIGH RIKSRNNPDL RVELVKEYAK
KHFPSTKLLD YAIAVETVTT SKKDNLILNV DGCVAVCFVD LMRNCGAFSP EEVEDYMKMG
VLNGLFVLGR SIGLIAHYLD QKRLRTGLYR HPWDDITYLL PALQKGGSEG RVEVNV
//