ACS1_CANGA
ID ACS1_CANGA Reviewed; 704 AA.
AC Q6FLU2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=CAGL0L00649g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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 -!- 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}.
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DR EMBL; CR380958; CAG61772.1; -; Genomic_DNA.
DR RefSeq; XP_448802.1; XM_448802.1.
DR AlphaFoldDB; Q6FLU2; -.
DR SMR; Q6FLU2; -.
DR STRING; 5478.XP_448802.1; -.
DR EnsemblFungi; CAG61772; CAG61772; CAGL0L00649g.
DR GeneID; 2891117; -.
DR KEGG; cgr:CAGL0L00649g; -.
DR CGD; CAL0136172; CAGL0L00649g.
DR VEuPathDB; FungiDB:CAGL0L00649g; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; Q6FLU2; -.
DR OMA; AIKASWP; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0005829; C:cytosol; IDA:CGD.
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..704
FT /note="Acetyl-coenzyme A synthetase 1"
FT /id="PRO_0000208407"
FT MOTIF 702..704
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 239..242
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 434..436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 458..463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 550
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 573
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 576
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 641
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
SQ SEQUENCE 704 AA; 79263 MW; 9E3D72E57E80536A CRC64;
MSPSAIAEKK QVDNIQEIKD KNQEPAHHEY EHLTNVGVVK QKPIDHRLKD NIKTHYSPHL
DGLQEYKRQY QESIENPEKF FSEKARSFMN WFRDFDRVFV PDVDNPTKPS FENNAWFLNG
QLNTCYNCVD RHALKTPNKT AIIYEADEPG EGYSMSYKEL LEKVCQVAQI LKYSMNVKKG
DTVAVYMPMI PEALITLLAI SRIGAIHSVV FAGFSSNSLR DRINDAGSRV VITADESNRG
GKIIETKRIV DDALRETPQV EHVLVYRRTN NPQVNFQAPR DLDWETERKK YKTYFPCEPV
DSEHPLFLLY TSGSTGTPKG VQHSTAGYLL GALLTMRYTF DVHQEDVFFT AGDIGWITGH
TYCVYGPLLY GCTTLVFEGT PAYPNFSRYW EIIDKHQVTQ FYVAPTALRL LKRAGDSFID
GFSLKSLRCL GSVGEPIAAE VWEWYSDKIG KNEIPIVDTY WQTESGSHLV TPLAGGVTPM
KPGSASLPFF GIETVILDPT TGEEINDSHA EGVLAIKRPW PSFARTIWKN HDRFLDTYLN
PYKGYYFTGD GAARDKDGYI WILGRVDDVV NVSGHRLSTA EIEAAIIEDR MVAECAVVGF
NDDLTGQAVA AFVVLKDKST WASASEEELQ DIKKHLILTV RKDIGPFAAP KLIVLVDDLP
KTRSGKIMRR ILRKILAGES DQLGDVSTLS NPGVVKHLID SVKL
