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Database: UniProt
Entry: A0A0D1YXS1_9EURO
LinkDB: A0A0D1YXS1_9EURO
Original site: A0A0D1YXS1_9EURO 
ID   A0A0D1YXS1_9EURO        Unreviewed;       677 AA.
AC   A0A0D1YXS1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE            EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN   ORFNames=PV11_02941 {ECO:0000313|EMBL:KIV87392.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV87392.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV87392.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV87392.1,
RC   ECO:0000313|Proteomes:UP000053599};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala sideris CBS121828.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN846951; KIV87392.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D1YXS1; -.
DR   HOGENOM; CLU_006587_4_1_1; -.
DR   OrthoDB; 536at2759; -.
DR   Proteomes; UP000053599; 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   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:UP000053599};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          60..165
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02629"
FT   DOMAIN          225..348
FT                   /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00549"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   677 AA;  73702 MW;  F539B1341CDB6BF6 CRC64;
     MPSTMDGAPA PLSNGVPKID IPAGNASPGS DAPFSANDNI RRFEAPSRAL SPAPHALFHN
     KTRCFVYGMQ PKAVQGMLDF DFICKRSTPS VAGIIYTFGG QFVSKMYWGT SETLLPVYQG
     VDKAFEKHPD VDTIVNFASS RSVYSSTMEL MNIPQIRTIA IIAEGVPERR AREIMVKSKE
     KGITIVGPAT VGGIKPGAFK IGNTGGMLDN IVASKLYRKG SVGYVSKSGG MSNELNNIIA
     QNTDGVYEGI AIGGDRYPGT TFIDHLLRYQ NEPDCKILLL LGEVGGVEEY RVIEAVKNGQ
     ITKPIVAWAI GTCASMFKTE VQFGHAGASA NSQLETAVVK NQSMREAGFF VPDTFEDMPT
     LLAEVYQKLV KQGNIKPAPE PVVPKIPMDY AWAQELGLIR KPAAFISTIS DDRGQELLYA
     GMPISDVFKE DIGIGGVMSL LWFRRRLPAY ASKFLEMVLM LTADHGPAVS GAMNTIITTR
     AGKDLISSLV AGLLTIGSRF GGALDGAAEE FSRASDKGLS PREFVDIMRK ENKLIPGIGH
     RIKSRNNPDL RVELVKDFVL KHFPSHKLLD YALAVETLTT AKKDSLILNV DGCIAVSFVD
     LLRNCGAFSA EEAEDYMKMG VLNGLFVLGR SIGLIAHYLD QKRNRQGLYR HPWDDITYLL
     PTFAKGQNSE GRVEVSV
//
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