ID D5GBJ5_TUBMM Unreviewed; 663 AA.
AC D5GBJ5;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN ORFNames=GSTUM_00005662001 {ECO:0000313|EMBL:CAZ82001.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ82001.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ82001.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ82001.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
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DR EMBL; FN430097; CAZ82001.1; -; Genomic_DNA.
DR RefSeq; XP_002837810.1; XM_002837764.1.
DR AlphaFoldDB; D5GBJ5; -.
DR STRING; 656061.D5GBJ5; -.
DR EnsemblFungi; CAZ82001; CAZ82001; GSTUM_00005662001.
DR GeneID; 9185436; -.
DR KEGG; tml:GSTUM_00005662001; -.
DR eggNOG; KOG1254; Eukaryota.
DR HOGENOM; CLU_006587_4_1_1; -.
DR InParanoid; D5GBJ5; -.
DR OMA; HMLRYQA; -.
DR OrthoDB; 536at2759; -.
DR Proteomes; UP000006911; 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 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:UP000006911};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 42..151
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 72448 MW; FCFDE7DDC6C52A64 CRC64;
MSQASLAPPV AKSQSENLRA NDNIRRFSAP SRPRSPPAEH TLFHTKTRAF VYGLQPRACQ
GMLDFDFICK RKTPSVAAII YPFGGQFVSK MYWGTSETLL PVYQSVEKAC EKHPEVDTVV
NFASSRSVYS STLELMEKPQ IKSIAIIAEG VPERRAREIM HIAQQKNITI VGPATVGGIK
PGCYKIGNTG GMMDNIVASK LYRKGSVGYV SKSGGMSNEL NNILAEVTDG VYEGVAIGGD
RYPGTTFIDH LLRYELDPEC KILVLLGEVG GVEEYRVIEA VKNGTITKPI VAWAIGTCAS
MFKTEVQFGH AGSFANSQLE TAASKNAAMK EAGFHVPETF EEFPQTLATV YQGLVKAGTI
VPQPEPVVPK IPIDYSWAQE LGLVRKPAAF ISTISDDRGQ ELLYAGMPIS DVFKEDIGIG
GVMSLLWFRR RLPEYASKFL EMVLMLTADH GPAVSGAMNT IITTRAGKDL ISALVSGLLT
IGERFGGALD GAAAEFTGAF DKGLSPRDFV DTMRKQNKLI PGIGHRVKSR NNPDLRVELV
KEFVLKRFPS HKLLDYALAV ETVTTSKKDN LILNVDGCVA VCFVDLIRNC GAFTAEEAED
YLKMGVLNGL FVLGRSIGLI AHYLDQKRLR TGLYRHPWDD ITYLLPNLQG PSPGNEGRVE
VAI
//
