ACL1_SORMK
ID ACL1_SORMK Reviewed; 674 AA.
AC O93988; D1ZRT9; F7VPZ5;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=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 Name=ACL1; Synonyms=ACL; ORFNames=SMAC_06775;
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX PubMed=9858569; DOI=10.1128/mcb.19.1.450;
RA Nowrousian M., Masloff S., Poeggeler S., Kueck U.;
RT "Cell differentiation during sexual development of the fungus Sordaria
RT macrospora requires ATP citrate lyase activity.";
RL Mol. Cell. Biol. 19:450-460(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX PubMed=10794176; DOI=10.1007/s002940050518;
RA Nowrousian M., Kueck U., Loser K., Weltring K.-M.;
RT "The fungal acl1 and acl2 genes encode two polypeptides with homology to
RT the N- and C-terminal parts of the animal ATP citrate lyase polypeptide.";
RL Curr. Genet. 37:189-193(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
CC -!- FUNCTION: Catalyzes the formation of cytosolic acetyl-CoA, which is
CC mainly used for the biosynthesis of fatty acids and sterols.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; AJ224922; CAA12224.1; -; Genomic_DNA.
DR EMBL; AJ243817; CAB76165.1; -; Genomic_DNA.
DR EMBL; CABT02000003; CCC07573.1; -; Genomic_DNA.
DR RefSeq; XP_003344998.1; XM_003344950.1.
DR AlphaFoldDB; O93988; -.
DR SMR; O93988; -.
DR STRING; 771870.O93988; -.
DR PRIDE; O93988; -.
DR EnsemblFungi; CCC07573; CCC07573; SMAC_06775.
DR GeneID; 10802343; -.
DR KEGG; smp:SMAC_06775; -.
DR VEuPathDB; FungiDB:SMAC_06775; -.
DR eggNOG; KOG1254; Eukaryota.
DR HOGENOM; CLU_006587_4_1_1; -.
DR InParanoid; O93988; -.
DR OMA; IHVPDTF; -.
DR OrthoDB; 349367at2759; -.
DR Proteomes; UP000001881; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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; 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..674
FT /note="ATP-citrate synthase subunit 1"
FT /id="PRO_0000102787"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 320
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 261..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 312..338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 339..349
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255"
SQ SEQUENCE 674 AA; 72985 MW; 7E75CF2D415E4A61 CRC64;
MPSATSTNGA NGNGNGNGAS ASPAPGNLSA NDNIRRFAAP SRPLSPLPAH ALFNEKTRCF
VYGLQPRAVQ GMLDFDFICK RSTPSVAGII YTFGGQFVSK MYWGTSETLL PVYQEVQKAI
AKHPDVDVVV NFASSRSVYS STMELMEHPQ IKTIAIIAEG VPERRAREIA YVAKKKGITI
IGPATVGGIK PGCFKIGNTG GMMDNIVASK LYRKGSVGYV SKSGGMSNEL NNIISQTTDG
VYEGVAIGGD RYPGTTFIDH LLRYQADPAC KILVLLGEVG GVEEYKVIEA VKQGIITKPI
VAWAIGTCAS MFKTEVQFGH AGAFANSQLE TAATKNKSMR EAGFYVPDTF EDMPALLKQV
YDKLVADGTI VPAPEPVVPK IPIDYSWAQE LGLIRKPAAF ISTISDDRGQ ELLYAGMPIS
DVFREEIGIG GVMSLLWFRR RLPDYAAKFL EMVLMLTADH GPAVSGAMNT IITTRAGKDL
ISSLVAGLLT IGSRFGGALD GAAEEFTKAF DKGLSPREFV DTMRKQNKLI PGIGHRVKSR
NNPDLRVELV KEYVKAKFPS SKLLDYALAV ETVTTSKKDN LILNVDGCIA VCFVDLLRNC
GAFSTEEAED YLSMGVLNGL FVLGRSIGLI AHYLDQKRLR TGLYRHPWDD ITYLLPSLQQ
PGPPGTEGRV EVQI
