ID A0A0N1H8G0_9EURO Unreviewed; 454 AA.
AC A0A0N1H8G0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 08-OCT-2025, 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=AB675_986 {ECO:0000313|EMBL:KPI38204.1};
OS Cyphellophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI38204.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI38204.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI38204.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the succinate/malate
CC CoA ligase alpha subunit family. {ECO:0000256|ARBA:ARBA00005899}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the succinate/malate
CC CoA ligase beta subunit family. {ECO:0000256|ARBA:ARBA00010719}.
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:KPI38204.1}.
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DR EMBL; LFJN01000020; KPI38204.1; -; Genomic_DNA.
DR RefSeq; XP_017998167.1; XM_018150442.1.
DR AlphaFoldDB; A0A0N1H8G0; -.
DR STRING; 1664694.A0A0N1H8G0; -.
DR GeneID; 28742311; -.
DR VEuPathDB; FungiDB:AB675_986; -.
DR OrthoDB; 5295093at2759; -.
DR Proteomes; UP000038010; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 FunFam; 3.40.50.261:FF:000004; ATP-citrate synthase subunit; 1.
DR Gene3D; 3.30.470.110; -; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR InterPro; IPR032263; Citrate-bd.
DR InterPro; IPR056749; Citrate_synth_N.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF16114; Citrate_bind; 1.
DR Pfam; PF24948; Citrate_synth_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
PE 3: Inferred from homology;
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..229
FT /note="ATP-citrate synthase ATP-grasp"
FT /evidence="ECO:0000259|Pfam:PF24948"
FT DOMAIN 265..442
FT /note="ATP-citrate synthase citrate-binding"
FT /evidence="ECO:0000259|Pfam:PF16114"
SQ SEQUENCE 454 AA; 49457 MW; 41AC46DE88F0F305 CRC64;
MSAKSILEAD GKAILNYHLT RAPLVKPSPL KSTGQHNAPS KLASIYFPED EQRRGKSGLL
ALNKTWPEAR AWIETKARKE QQVEHVVGTL SQFLVEPFVP HPQDTEYYIN INSVRDGDWI
LFTHEGGVDV GDVDAKAEKV LIPVDLKNFP SHQELAKALL KNVPKGVHNV LLDFIIRLYS
VYVDSQFTYL EINPLVVIPN ADATSAEVHF LDLAAKLDQT ADFECGVKWA IARSPAALGL
PGVKTDGKVS IDVGPPIEFP APFGREMSKE EKYISDMDAK TGASLKLTVL NASGRIWTLV
AGGGASVVYA DAIASAGFVS ELANYGEYSG APTETQTYNY ARTVLDLMLR APMHKEGKVL
FIGGGIANFT NVASTFKGVI RALREVAPVL NEHGTQIWVR RAGPNYQEGL KNIKAVGEEL
KLNMHVFGPE MHVSGIVPLA LNGKTTTVPE FGTM
//
