ID A0A0G0AFT7_TRIHA Unreviewed; 653 AA.
AC A0A0G0AFT7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN ORFNames=THAR02_04023 {ECO:0000313|EMBL:KKP03874.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP03874.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(2015).
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:KKP03874.1}.
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DR EMBL; JOKZ01000095; KKP03874.1; -; Genomic_DNA.
DR OMA; HMLRYQA; -.
DR OrthoDB; 536at2759; -.
DR Proteomes; UP000034112; 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; 1.10.230.10; 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; 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 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:UP000034112};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 32..141
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 653 AA; 71413 MW; 57871846CFFB1BB8 CRC64;
MSGSKDLLSA NDRIQRFAAP SRPLSPLPAH ALFSEKTRCF VYGLQPRAVQ GMLDFDFICK
RKTPSVAGII YTFGGQFVSK MYWGTSETLL PVYQQVDKAI AKHPDVDVVV NFASSRSVYS
STMELMECPQ IKTIAIIAEG VPERRAREIA HVAKKKGVTI IGPATVGGIK PGSFKIGNTG
GMMDNIVASK LYRKGSVGYV SKSGGMSNEL NNIISQNTDG VYEGVAIGGD RYPGTTFIDH
LLRYQADPDC KILVLLGEVG GVEEYKVIDA VKQGIITKPI VAWAIGTCAS MFKTEVQFGH
AGSFANSQLE TATVKNQSMR DAGFHVPKTF EDMPAVLKEV YDKLVKEGTI VPRAEPVVPK
IPIDYSWAQE LGLIRKPAAF ISTISDDRGQ ELLYAGMPIS DVFKEEIGVG GVMSLLWFRR
RLPDYASKFL EMVLMLTADH GPAVSGAMNT IITTRAGKDL ISALVSGLLT IGSRFGGALD
GAAEEFTKAF DKNLSPRDFV DSMRKQNKLI PGIGHRIKSR NNPDLRVELV KEYVKAKFPS
HKLLDYALAV ETVTTSKKDS LILNVDGCIA VCFVDLMRNC GAFSAEEAED YLSMGVLNGL
FVLGRSIGLI AHFLDQKRLR TGLYRHPWDD ITYLLPNLNE GQPSGQGRVE VQM
//