ID   ACL1_NEUCR              Reviewed;         670 AA.
AC   Q8X097; Q7SCH6;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Probable ATP-citrate synthase subunit 1;
DE            EC=2.3.3.8;
DE   AltName: Full=ATP-citrate (pro-S-)-lyase 1;
DE   AltName: Full=Citrate cleavage enzyme subunit 1;
GN   ORFNames=B14D6.310, NCU06785;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Catalyzes the formation of cytosolic acetyl-CoA, which is
CC       mainly used for the biosynthesis of fatty acids and sterols.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate +
CC         CoA; Xref=Rhea:RHEA:21160, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=2.3.3.8;
CC   -!- SUBUNIT: Composed of two subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL356173; CAB91740.2; -; Genomic_DNA.
DR   EMBL; CM002237; EAA34390.1; -; Genomic_DNA.
DR   RefSeq; XP_963626.1; XM_958533.3.
DR   AlphaFoldDB; Q8X097; -.
DR   SMR; Q8X097; -.
DR   STRING; 5141.EFNCRP00000006852; -.
DR   PRIDE; Q8X097; -.
DR   EnsemblFungi; EAA34390; EAA34390; NCU06785.
DR   GeneID; 3879766; -.
DR   KEGG; ncr:NCU06785; -.
DR   VEuPathDB; FungiDB:NCU06785; -.
DR   HOGENOM; CLU_006587_4_1_1; -.
DR   InParanoid; Q8X097; -.
DR   OMA; IHVPDTF; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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:0046872; F:metal ion binding; 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   Gene3D; 1.10.230.10; -; 1.
DR   Gene3D; 3.40.50.261; -; 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; IPR005811; CoA_ligase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
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; SSF48256; 1.
DR   SUPFAM; SSF51735; SSF51735; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..670
FT                   /note="Probable ATP-citrate synthase subunit 1"
FT                   /id="PRO_0000102785"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        316
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         257..277
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         308..334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         335..345
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   670 AA;  72627 MW;  3AC73BA19AA5EDFE CRC64;
     MPSATTASTN GANGASASPA PGNLSANDNI RRFAAPSRPL SPLPAHALFN DKTRCFVYGL
     QPRAVQGMLD FDFICKRSTP SVAGIIYTFG GQFVSKMYWG TSETLLPVYQ EVPKAIAKHP
     DVDVVVNFAS SRSVYSSTME LMEYPQIKTI AIIAEGVPER RAREIAYVAK KKGITIIGPA
     TVGGIKPGCF KIGNTGGMMD NIVASKLYRK GSVGYVSKSG GMSNELNNII SQTTDGVYEG
     VAIGGDRYPG TTFIDHLLRY QADPDCKILV LLGEVGGVEE YKVIDAVKQG IITKPIVAWA
     IGTCASMFKT EVQFGHAGAF ANSQLETAAT KNKSMREAGF YVPDTFEDMP ALLKQVYDKL
     VADGTIVPAP EPVVPKIPID YSWAQELGLI RKPAAFISTI SDDRGQELLY AGMPISDVFK
     EEIGIGGVMS LLWFRRRLPD YAAKFLEMVL MLTADHGPAV SGAMNTIITT RAGKDLISSL
     VAGLLTIGSR FGGALDGAAE EFTKAFDKGL SPREFVDTMR KQNKLIPGIG HRVKSRNNPD
     LRVELVKEYV KAKFPSTKLL DYALAVESVT TSKKDNLILN VDGCIAVCFV DLLRNCGAFS
     TEEAEDYLSM GVLNGLFVLG RSIGLIAHYL DQKRLRTGLY RHPWDDITYL LPSLQQPGPP
     GTEGRVEVQI