ACS1_KLULA
ID ACS1_KLULA Reviewed; 707 AA.
AC O60011; Q6CY43;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Acetyl-coenzyme A synthetase 1;
DE EC=6.2.1.1;
DE AltName: Full=Acetate--CoA ligase 1;
DE AltName: Full=Acyl-activating enzyme 1;
GN Name=ACS1; OrderedLocusNames=KLLA0A03333g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=12489122; DOI=10.1002/yea.936;
RA Zeeman A.-M., Steensma H.Y.;
RT "The acetyl co-enzyme A synthetase genes of Kluyveromyces lactis.";
RL Yeast 20:13-23(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: May be required for assimilation of ethanol and acetate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456215; EC=6.2.1.1;
CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC16713.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF061265; AAC16713.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CR382121; CAH02734.1; -; Genomic_DNA.
DR RefSeq; XP_451146.1; XM_451146.1.
DR AlphaFoldDB; O60011; -.
DR SMR; O60011; -.
DR STRING; 28985.XP_451146.1; -.
DR EnsemblFungi; CAH02734; CAH02734; KLLA0_A03333g.
DR GeneID; 2896335; -.
DR KEGG; kla:KLLA0_A03333g; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; O60011; -.
DR OMA; AIKASWP; -.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016880; F:acid-ammonia (or amide) ligase activity; IEA:EnsemblFungi.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019654; P:acetate fermentation; IEA:EnsemblFungi.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR GO; GO:0016573; P:histone acetylation; IEA:EnsemblFungi.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding; Endoplasmic reticulum; Ligase; Microsome; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..707
FT /note="Acetyl-coenzyme A synthetase 1"
FT /id="PRO_0000208414"
FT MOTIF 705..707
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 242..245
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 437..439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 461..466
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 553
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 568
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 576
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 644
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT CONFLICT 687..707
FT /note="GDVSTLSNPGIVKHLIDSVKL -> ATSPHYPTLVSLST (in Ref. 1;
FT AAC16713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 78420 MW; 9663996B9AD44C91 CRC64;
MSPAVDTAST AKDPISVMKS NASAAAADQI KTHEYEHLTS VPIVQPLPIT DRLSSEAAQK
YKPNLPGGFE EYKSLHKESL ENPAKFYHER AQLLNWFKPY DQVFIPDTEG KPTFENNAWF
TNGQLNACYN LVDRHAFTQP NKVAILYEAD EPGQGYSLTY AELLEQVCKV AQILQYSMNV
KKGDTVAVYM PMIPQALITL LAITRIGAIH SVVFAGFSSN SLRDRINDAY SKTVITTDES
KRGGKTIETK RIVDEALKDT PQVTNVLVFK RTHNENIKYI PGRDLDWDEE VKKYKSYTPC
EPVDSEHPLF LLYTSGSTGA PKGVQHSTAG YLLQALLSMK YTFDIQNDDI FFTAGDIGWI
TGHTYCVYGP LLQGCTTLVF EGTPAYPNFS RYWEIVDKYQ VTQFYVAPTA LRLLKRAGDS
FTEGFSLKSL RSLGSVGEPI AAEVWEWYSE KIGKNELPIV DTYWQTESGS HLVTPLAGGA
TPMKPGAAAF PFFGIDLAVL DPTTGIEQTG EHAEGVLAIK RPWPSFARTI WKNNDRFLDT
YLKPYPGYYF TGDGVARDKD GFFWILGRVD DVVNVSGHRL STAEIEAAII EDDMVAECAV
VGFNDELTGQ AVAAFVVLKN KSSLTAASES ELQDIKKHLI ITVRKDIGPF AAPKLIVLVD
DLPKTRSGKI MRRILRKILA GESDQLGDVS TLSNPGIVKH LIDSVKL
