ACS1_ASHGO
ID ACS1_ASHGO Reviewed; 694 AA.
AC Q758X0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=ADR408W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS52327.1; -; Genomic_DNA.
DR RefSeq; NP_984503.1; NM_209856.1.
DR AlphaFoldDB; Q758X0; -.
DR SMR; Q758X0; -.
DR STRING; 33169.AAS52327; -.
DR EnsemblFungi; AAS52327; AAS52327; AGOS_ADR408W.
DR GeneID; 4620668; -.
DR KEGG; ago:AGOS_ADR408W; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; Q758X0; -.
DR OMA; AIKASWP; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IBA:GO_Central.
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:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
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..694
FT /note="Acetyl-coenzyme A synthetase 1"
FT /id="PRO_0000208403"
FT MOTIF 692..694
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 229..232
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 424..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 448..453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 563
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 631
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
SQ SEQUENCE 694 AA; 76809 MW; 901542DF3FD3A31F CRC64;
MVTSAGVGHA EYNNGADVQH ADYAHLTSVG QVEQKPLGGR LGALAEYYKP NVASMEEYRA
MHAQSITDPA AFYGERARTY VDWFRPFDAV FLPGPDGRPS FDNNAWFVNG QLNACYNLVD
RHAARTPDKV AIIYEADEPG EGYSLTYREL LAQVCKVAQV LQYSMGVRKG DTVAVYMPMI
PQALVTLLAI SRIGAIHSVV FAGFSSNSLR DRINDARSEV VVTTDESKRG GKIIETKRIV
DDAIKETPQL RKVLVYKRTC NPSVSYVADR DLDWDTEVKK YKSYCPCEPV DSEHPLFLLY
TSGSTGAPKG VQHSTAGYLL QAYLSMLYSF DVHSDDIFFT AGDIGWITGH TYVVYGPLFS
GCTTVVFEGT PAYPSYSRYW DIIDKYSVTQ FYVAPTALRL LKRAGDSYVD GYSLRTLRSL
GTVGEPIAAE VWEWYYTVIG KREIPVIDTY WQTESGAHLV TPLAGGSTPM KPGSASFPFF
GIDLAILDPQ TGEELLGPNV EGVLAVKQPW PSFTRTIWNN HDRYLDTYLN PYKGYYFAGD
GAARDSQGFI WILGRVDDVV NVSGHRLSTA EVEAAIIQES MVAECAVVGF ADELTGQAIA
AFVVLKQKSS WNTASERELQ EIKKHLILSV RRDIGPFAAP KLIVLVDDLP KTRSGKIMRR
ILRKILAGEA DQLGDVSTLS NPGIVKHLIE SVKF
