ID Q4WM99_ASPFU Unreviewed; 724 AA.
AC Q4WM99;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN ORFNames=AFUA_6G10650 {ECO:0000313|EMBL:EAL88915.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL88915.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL88915.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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:EAL88915.1}.
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DR EMBL; AAHF01000006; EAL88915.1; -; Genomic_DNA.
DR RefSeq; XP_750953.1; XM_745860.1.
DR AlphaFoldDB; Q4WM99; -.
DR STRING; 330879.Q4WM99; -.
DR SwissPalm; Q4WM99; -.
DR EnsemblFungi; EAL88915; EAL88915; AFUA_6G10650.
DR GeneID; 3508258; -.
DR KEGG; afm:AFUA_6G10650; -.
DR eggNOG; KOG1254; Eukaryota.
DR HOGENOM; CLU_006587_4_1_1; -.
DR InParanoid; Q4WM99; -.
DR OMA; HMLRYQA; -.
DR OrthoDB; 536at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003878; F:ATP citrate synthase activity; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
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 Acyltransferase {ECO:0000313|EMBL:EAL88915.1};
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 Lyase {ECO:0000313|EMBL:EAL88915.1};
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:UP000002530};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAL88915.1}.
FT DOMAIN 116..213
FT /note="CoA-binding"
FT /evidence="ECO:0000259|Pfam:PF02629"
FT DOMAIN 273..396
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
SQ SEQUENCE 724 AA; 78829 MW; 19169C13EB46A3D2 CRC64;
MVQPSPPSRI PPRAALARYC TNTVSSGKVS SSPQLLDIVE PPPPSTQPSC PHLLLSLALP
MAISTPMTTS LASSLPAECS LLLLTLSSTT RRDASYSKCF LAANRVNGWA DGYHSGMQPR
AVQGMLDFDF ICKRSTPSVA GIIYTFGGQF VSKMYWGTSE TLLPVYQDVA KAMAKHPDVD
TVVNFASSRS VYSSTMELMN YPQIKSIAII AEGVPERRAR EIMVTAKEKG ITIIGPATVG
GIKPGAFKIG NTGGMMDNIV ASKLYRKGSV GYVSKSGGMS NELNNIISQT TDGVHEGIAI
GGDRYPGTTF IDHLLRYQAD PDCKILLLLG EVGGVEEYRV IEAVKNGTIT KPLVAWAIGT
CASMFKTEVQ FGHAGASANS QLETAVYKNK AMREAGIHVP DTFEELPQLL KQVYEDQVKK
GVIKPQPEPQ VPKIPIDYSW AQELGLIRKP AAFISTITDD RGQELLYAGM PISDVFKEDI
GIGGVMSLLW FRRRLPRYAS KFLEMVLMLT ADHGPAVSGA MNTIITTRAG KDLISALVSG
LLTIGSRFGG ALDGAAEEFT KAFDKGMSPR DFVDTMRKEN KLIPGIGHRV KSRNNPDLRV
ELVKEFAKKH FPSTKLLDYA IAVETVTTSK KDNLILNVDG CVAVCFVDLM RNCGAFSPEE
VEDYMKMGVL NGLFVLGRSI GLIAHYLDQK RLRTGLYRHP WDDITYLLPT LQKGGAEGRV
EVNI
//
