ACS1_DEBHA
ID ACS1_DEBHA Reviewed; 671 AA.
AC Q6BQF2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=DEHA2E05676g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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 -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CR382137; CAG87795.1; -; Genomic_DNA.
DR RefSeq; XP_459568.1; XM_459568.1.
DR AlphaFoldDB; Q6BQF2; -.
DR SMR; Q6BQF2; -.
DR STRING; 4959.XP_459568.1; -.
DR EnsemblFungi; CAG87795; CAG87795; DEHA2E05676g.
DR GeneID; 2901869; -.
DR KEGG; dha:DEHA2E05676g; -.
DR VEuPathDB; FungiDB:DEHA2E05676g; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; Q6BQF2; -.
DR OMA; AIKASWP; -.
DR OrthoDB; 288915at2759; -.
DR Proteomes; UP000000599; Chromosome E.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
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; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..671
FT /note="Acetyl-coenzyme A synthetase 1"
FT /id="PRO_0000208411"
FT BINDING 210..213
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 405..407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 429..434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 546
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 605
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
SQ SEQUENCE 671 AA; 74416 MW; E42BB91905E81966 CRC64;
MTPHSTHVTL DHEGIIQPPA EFKERSKSKP NLADFETYSK MYKESIENPS KFFGEQALEH
LSWDRPFDEA RYPVSSEQDF ADGDIASWFV NGQLNASYNA VDRWAIKNPN KPAIIYEADE
ENEGRIITYG QLLKDVCKLA QCLTKLGIRK GDSVAVYLPM IPEALVTLLA IVRIGAVHSV
VFAGFSSSSL KDRILDASSK IVITTDESKR GGKTIETKKI VDDALKNCPD VTNVLLFKRT
GNAHIPFTEG RDLWWHEEMA KYGPYFPPVP VNSEDPLFLL YTSGSTGKPK GIQHSTAGYL
LGAAMTSKYT FDVHEDDVLF TAGDVGWITG HTYVVYGPLL CGATTVVFEG TPAHPNYSRY
WEIVDKYQVT QFYVAPTALR LLKRAGTKYI ENYKLDSLRV LGSVGEPIAA EIWHWYNDNI
GRRKCHIVDT YWQTESGSHM LAPLAGITPT KPGSASLPCF GIDAKILDPV SGKELKENDV
EGVLCVKSCW PSISRGIYND YARFIETYLK PYPNHYFSGD GAARDVDGFY WILGRVDDVV
NVSGHRLSTA EIEAALILHE SVAECAVVGY ADELTGQAVA AYVSLKSNVS EDLEVIKKEL
ILTVRKEIGP FATPKTILLV DDLPKTRSGK IMRRILRKVL AGEEDQLGDI STLSNPGVVA
QIIDVVKATR K
