ID A0A1B9G506_9TREE Unreviewed; 1149 AA.
AC A0A1B9G506;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN ORFNames=I302_03757 {ECO:0000313|EMBL:OCF26080.1};
OS Kwoniella bestiolae CBS 10118.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF26080.1, ECO:0000313|Proteomes:UP000092730};
RN [1] {ECO:0000313|EMBL:OCF26080.1, ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF26080.1,
RC ECO:0000313|Proteomes:UP000092730};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus bestiolae CBS10118.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|Proteomes:UP000092730};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI894020; OCF26080.1; -; Genomic_DNA.
DR RefSeq; XP_019047150.1; XM_019190402.1.
DR AlphaFoldDB; A0A1B9G506; -.
DR STRING; 1296100.A0A1B9G506; -.
DR GeneID; 30208156; -.
DR VEuPathDB; FungiDB:I302_03757; -.
DR OrthoDB; 536at2759; -.
DR Proteomes; UP000092730; 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; 3.30.470.110; -; 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; 2.
DR InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR InterPro; IPR032263; Citrate-bd.
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; PF16114; Citrate_bind; 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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000092730};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 287..464
FT /note="ATP-citrate synthase citrate-binding"
FT /evidence="ECO:0000259|Pfam:PF16114"
FT DOMAIN 538..643
FT /note="CoA-binding"
FT /evidence="ECO:0000259|Pfam:PF02629"
FT DOMAIN 703..826
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT REGION 474..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1149 AA; 124309 MW; EF037BB5BDD90114 CRC64;
MSTKAIREFD AKQLVSYWLN RSPTPIATKT ESSLSAAQVA QVEWDPVTKQ LSPPIKPGQG
LPDWVFTSKL VGKPDQLIKR RGKAGLLCLN KGWEETGAWI EQRAGKPVTV ESTTGTLNTF
IIEPFCPHPA ETEYYVCINS TREGDWILFT HEGGVDVGDV DAKALKLLLP VGEEFPAREH
LISTLLAHVA PAKQDVLADF LIRLYAVYVD LHFAYLEINP LVVLDAAEGK PSEIHYLDMA
AKLDQTADFL CGPKWAVARD TVTASSSSAA IKADRGPPMV WPAPFGRDLT KEEAYIQKLD
ASTGASLKLT VLNQAGRVWT MVAGGGASVV YSDAIAAAGF AHELANYGEY SGAPTEGQTY
EYAKTIIDLI VRGEPHPEGK VLIIGGGAAN FSDVAATFKG IIRALKQFKE GLLRHKVSIW
VRRAGPNYQE GLKAMRLCGE SIGVPMKVYG PESPITAIVP MALGIQRPAS AATRDVTPIA
SSPASPSANG STPLPGSAEP QAVGSVKADG SREQPNDHIV RFETEKLGSR PWFRPFDEHT
RSFVFGLQPR AIQGMLDFDF SCGRKTPSVA AMIYPFGGHH IQKFYWGTKE TLLPVYTSVG
EAIKKHPDVD VVVNFSSSRS VYASTLDILT YPQIKAIGII AEGVPERHAR ELLHLAVKKE
VIIIGPATVG GIKPGCFRIG NTGGMMDNLI ACKLYRPGSV GYVSKSGGMS NELNNILSYT
TNGVYEGVAI GGDRYPGTSF IDHLLRYEAD PECKLLLLLG EVGGTEEYRV IEAVKKGIIK
KPIVAWAIGT CAKMFTSEVQ FGHAGSMANS DLETADAKNR AMKAAGFIVP DTFEDLPEVL
KATYQKLVSA GAITVKAEIE PPQIPMDYQW ASKLGLIRKP AAFISTISDE RGQELMYAGM
RISDVFKEEL GIGGVISLLW FKRRLPAFAC KFIEMVLQLT ADHGPAVSGA MNTIITARAG
KDLISSLVAG LLTIGDRFGG ALDGAAAEFS RGVSSGLTPR EFVDQNRKAN KLIPGIGHKI
KSKTNPDLRV TLVVDYVKKH FPSHKTLDFA LAVEDVTTQK ANTLILNVDG AIAASFCDLL
SGSGAFTEEE AAEYLKSGTL NGLFVLGRSI GFIGHYLDQR LLKQPLYRHP ADDIFINMQE
RVVFQPGSA
//
