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-APR-2013, entry version 89.
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 (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ADP + phosphate + acetyl-CoA + oxaloacetate =
CC ATP + citrate + CoA.
CC -!- SUBUNIT: Composed of two subunits (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha
CC subunit family.
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DR EMBL; AL356173; CAB91740.2; -; Genomic_DNA.
DR EMBL; AABX02000033; 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 EnsemblFungi; EFNCRT00000006861; EFNCRP00000006852; EFNCRG00000006849.
DR GeneID; 3879766; -.
DR KEGG; ncr:NCU06785; -.
DR eggNOG; COG0372; -.
DR HOGENOM; HOG000151479; -.
DR KO; K01648; -.
DR OMA; NVDGTIG; -.
DR OrthoDB; EOG4CC78H; -.
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: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; Citrate_synthase_core; 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; 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 (By similarity).
FT NP_BIND 308 334 ATP (By similarity).
FT REGION 335 345 CoA-binding (Potential).
FT ACT_SITE 316 316 Tele-phosphohistidine intermediate (By
FT similarity).
FT METAL 274 274 Magnesium (By similarity).
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
//
