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Database: UniProt
Entry: K2S2H6_MACPH
LinkDB: K2S2H6_MACPH
Original site: K2S2H6_MACPH 
ID   K2S2H6_MACPH            Unreviewed;       658 AA.
AC   K2S2H6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE            EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN   ORFNames=MPH_03487 {ECO:0000313|EMBL:EKG19227.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG19227.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG19227.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG19227.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
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:EKG19227.1}.
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DR   EMBL; AHHD01000164; EKG19227.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2S2H6; -.
DR   STRING; 1126212.K2S2H6; -.
DR   VEuPathDB; FungiDB:MPH_03487; -.
DR   eggNOG; KOG1254; Eukaryota.
DR   HOGENOM; CLU_006587_4_1_1; -.
DR   InParanoid; K2S2H6; -.
DR   OrthoDB; 536at2759; -.
DR   Proteomes; UP000007129; 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:UP000007129};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          37..146
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   658 AA;  71706 MW;  29CBEBE61E5470B8 CRC64;
     MPAANGTPNG ETLSANDNIR RFQAPSRPLS PPAQHTLFHN KTRCFVYGMQ PKAVQGMLDF
     DYICKRKQPS VAGIIYTFGG QFVSKMYWGT SETLLPVYQS VEKAIAKHSD VDTVVNFASS
     RSVYSSTMEL MEYPQIKSIA IIAEGVPERR AREIMHVAKK KGVTIIGPAT VGGIKPGAFK
     IGNTGGMMDN IVASKLYRPG SVAYVSKSGG MSNELNNIIS QTTDGVYEGV AIGGDRYPGT
     TFIDHLLRYQ ADPACKILVL LGEVGGVEEY RVIEAVKNGT ITKPIVAWAI GTVAGMLTTE
     VQFGHAGSFA NSQLETAASK NKSMKEAGIY VPDTFEDLPK ILSEVYQKLV ADGTIVAKPE
     PAVPKIPIDY SWAQELGLIR KPAAFISTIS DDRGQELLYA GMPISDVFKE NIGIGGVMSL
     LWFRRRLPDY ASKFLEMVLM LTADHGPAVS GAMNTIITTR AGKDLISALV SGLLTIGSRF
     GGALDGAAEE FTKAYDKGLS PRDFVDTMRK ENKLIPGIGH RIKSRNNPDL RVELVKEYVL
     KHFPSHKLLD YALAVETVTT SKKDNLILNV DGCIAVCFVD LVRNCGSFTQ EEAEDYLKMG
     VLNGLFVLGR SIGLIAHFLD QKRLRTGLYR HPWDDITYLL PTVGKGAPGN EGRVEVSM
//
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