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Database: UniProt
Entry: Q8X097
LinkDB: Q8X097
Original site: Q8X097 
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   01-OCT-2014, entry version 97.
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
OS   1257 / FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   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.,
RA   Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
RA   Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the
RT   Neurospora 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.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   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.,
RA   Paulsen I., 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
CC       is mainly used for the biosynthesis of fatty acids and sterols.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ADP + phosphate + acetyl-CoA + oxaloacetate =
CC       ATP + citrate + CoA.
CC   -!- SUBUNIT: Composed of two subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha
CC       subunit family. {ECO:0000305}.
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DR   EMBL; AL356173; CAB91740.2; -; Genomic_DNA.
DR   EMBL; CM002237; EAA34390.1; -; Genomic_DNA.
DR   RefSeq; XP_963626.1; XM_958533.2.
DR   UniGene; Ncr.10806; -.
DR   ProteinModelPortal; Q8X097; -.
DR   STRING; 5141.NCU06785.1; -.
DR   PRIDE; Q8X097; -.
DR   EnsemblFungi; EFNCRT00000006861; EFNCRP00000006852; EFNCRG00000006849.
DR   GeneID; 3879766; -.
DR   KEGG; ncr:NCU06785; -.
DR   eggNOG; COG0372; -.
DR   HOGENOM; HOG000151479; -.
DR   KO; K01648; -.
DR   OMA; RVKSRNN; -.
DR   OrthoDB; EOG7HB5JK; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR   GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.230.10; -; 1.
DR   Gene3D; 1.10.580.10; -; 1.
DR   Gene3D; 3.40.50.261; -; 1.
DR   Gene3D; 3.40.50.720; -; 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-like.
DR   InterPro; IPR016141; Citrate_synthase-like_core.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR005810; CoA_lig_alpha.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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   PRINTS; PR01798; SCOASYNTHASE.
DR   SUPFAM; SSF48256; SSF48256; 2.
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; Complete proteome; Cytoplasm; Lipid biosynthesis;
KW   Lipid metabolism; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN         1    670       Probable ATP-citrate synthase subunit 1.
FT                                /FTId=PRO_0000102785.
FT   NP_BIND     257    277       ATP. {ECO:0000250}.
FT   NP_BIND     308    334       ATP. {ECO:0000250}.
FT   REGION      335    345       CoA-binding. {ECO:0000255}.
FT   ACT_SITE    316    316       Tele-phosphohistidine intermediate.
FT                                {ECO:0000250}.
FT   METAL       274    274       Magnesium. {ECO:0000250}.
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
//
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