ACS1_YEAST
ID ACS1_YEAST Reviewed; 713 AA.
AC Q01574; D6VPG4; Q66RJ0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Acetyl-coenzyme A synthetase 1;
DE EC=6.2.1.1 {ECO:0000269|PubMed:8910545};
DE AltName: Full=Acetate--CoA ligase 1;
DE AltName: Full=Acyl-activating enzyme 1;
GN Name=ACS1; OrderedLocusNames=YAL054C; ORFNames=FUN44;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=1363452; DOI=10.1002/yea.320081207;
RA de Virgilio C., Buerckert N., Barth G., Neuhaus J.-M., Boller T.,
RA Wiemken A.;
RT "Cloning and disruption of a gene required for growth on acetate but not on
RT ethanol: the acetyl-coenzyme A synthetase gene of Saccharomyces
RT cerevisiae.";
RL Yeast 8:1043-1051(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
RC STRAIN=GRF78;
RX PubMed=7642141; DOI=10.1016/0378-1119(95)00289-i;
RA Kratzer S., Schueller H.-J.;
RT "Carbon source-dependent regulation of the acetyl-coenzyme A synthetase-
RT encoding gene ACS1 from Saccharomyces cerevisiae.";
RL Gene 161:75-79(1995).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8910545; DOI=10.1074/jbc.271.46.28953;
RA van den Berg M.A., de Jong-Gubbels P., Kortland C.J., van Dijken J.P.,
RA Pronk J.T., Steensma H.Y.;
RT "The two acetyl-coenzyme A synthetases of Saccharomyces cerevisiae differ
RT with respect to kinetic properties and transcriptional regulation.";
RL J. Biol. Chem. 271:28953-28959(1996).
RN [7]
RP INDUCTION.
RX PubMed=9252575; DOI=10.1111/j.1574-6968.1997.tb10466.x;
RA de Jong-Gubbels P., van den Berg M.A., Steensma H.Y., van Dijken J.P.,
RA Pronk J.T.;
RT "The Saccharomyces cerevisiae acetyl-coenzyme A synthetase encoded by the
RT ACS1 gene, but not the ACS2-encoded enzyme, is subject to glucose
RT catabolite inactivation.";
RL FEMS Microbiol. Lett. 153:75-81(1997).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11914276; DOI=10.1101/gad.970902;
RA Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S.,
RA Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P.,
RA Gerstein M., Roeder G.S., Snyder M.;
RT "Subcellular localization of the yeast proteome.";
RL Genes Dev. 16:707-719(2002).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [12]
RP FUNCTION.
RX PubMed=16857587; DOI=10.1016/j.molcel.2006.05.040;
RA Takahashi H., McCaffery J.M., Irizarry R.A., Boeke J.D.;
RT "Nucleocytosolic acetyl-coenzyme a synthetase is required for histone
RT acetylation and global transcription.";
RL Mol. Cell 23:207-217(2006).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 72-713 IN COMPLEX WITH THE ATP
RP ANALOG AMP.
RX PubMed=14769018; DOI=10.1021/bi035911a;
RA Jogl G., Tong L.;
RT "Crystal structure of yeast acetyl-coenzyme A synthetase in complex with
RT AMP.";
RL Biochemistry 43:1425-1431(2004).
CC -!- FUNCTION: Catalyzes the production of acetyl-CoA. Provides the acetyl-
CC CoA source for histone acetylation in the nucleus. 'Aerobic' isozyme of
CC acetyl-coenzyme A synthetase, which supports growth on nonfermentable
CC carbon sources such as glycerol and ethanol. May be required for
CC assimilation of ethanol and acetate. {ECO:0000269|PubMed:16857587,
CC ECO:0000269|PubMed:8910545}.
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 Evidence={ECO:0000269|PubMed:8910545};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177;
CC Evidence={ECO:0000305|PubMed:8910545};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.32 mM for acetate {ECO:0000269|PubMed:8910545};
CC KM=1.4 mM for ATP {ECO:0000269|PubMed:8910545};
CC Vmax=1.1 umol/min/mg enzyme {ECO:0000269|PubMed:8910545};
CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000305}. Cytoplasm.
CC Mitochondrion. Nucleus.
CC -!- INDUCTION: By acetate, acetaldehyde and ethanol. Subject to glucose
CC catabolite repression. Inactivated and degraded after addition of
CC glucose (at protein level). {ECO:0000269|PubMed:8910545,
CC ECO:0000269|PubMed:9252575}.
CC -!- DOMAIN: The FACS motif is required for catalytic activity and substrate
CC specificity. {ECO:0000250|UniProtKB:P30624}.
CC -!- MISCELLANEOUS: Present with 2890 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-25 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X66425; CAA47054.1; -; Genomic_DNA.
DR EMBL; U12980; AAC04979.1; -; Genomic_DNA.
DR EMBL; AY723758; AAU09675.1; -; Genomic_DNA.
DR EMBL; X76891; CAA54220.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06934.1; -; Genomic_DNA.
DR PIR; S51967; S30019.
DR RefSeq; NP_009347.1; NM_001178197.1.
DR PDB; 1RY2; X-ray; 2.30 A; A=72-713.
DR PDBsum; 1RY2; -.
DR AlphaFoldDB; Q01574; -.
DR SMR; Q01574; -.
DR BioGRID; 31775; 98.
DR DIP; DIP-4326N; -.
DR IntAct; Q01574; 2.
DR MINT; Q01574; -.
DR STRING; 4932.YAL054C; -.
DR MaxQB; Q01574; -.
DR PaxDb; Q01574; -.
DR PRIDE; Q01574; -.
DR EnsemblFungi; YAL054C_mRNA; YAL054C; YAL054C.
DR GeneID; 851245; -.
DR KEGG; sce:YAL054C; -.
DR SGD; S000000050; ACS1.
DR VEuPathDB; FungiDB:YAL054C; -.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000176537; -.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; Q01574; -.
DR OMA; AIKASWP; -.
DR BioCyc; MetaCyc:YAL054C-MON; -.
DR BioCyc; YEAST:YAL054C-MON; -.
DR BRENDA; 6.2.1.1; 984.
DR Reactome; R-SCE-71384; Ethanol oxidation.
DR SABIO-RK; Q01574; -.
DR EvolutionaryTrace; Q01574; -.
DR PRO; PR:Q01574; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; Q01574; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IDA:SGD.
DR GO; GO:0016880; F:acid-ammonia (or amide) ligase activity; IDA:SGD.
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; IMP:SGD.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IDA:SGD.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR GO; GO:0016573; P:histone acetylation; IGI:SGD.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Endoplasmic reticulum; Ligase;
KW Microsome; Mitochondrion; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..713
FT /note="Acetyl-coenzyme A synthetase 1"
FT /id="PRO_0000208420"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 552..600
FT /note="FACS"
FT /evidence="ECO:0000250|UniProtKB:P30624"
FT MOTIF 711..713
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 248..251
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 443..445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 467..472
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 559
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 582
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 585
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 650
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT CONFLICT 34
FT /note="Q -> R (in Ref. 1; CAA47054)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="K -> E (in Ref. 4; AAU09675)"
FT /evidence="ECO:0000305"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 166..182
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 255..262
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 335..348
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 374..379
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 397..404
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 414..420
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 448..456
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:1RY2"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:1RY2"
FT TURN 483..485
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 520..527
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 540..547
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 554..563
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 588..596
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 601..607
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 619..624
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 641..652
FT /evidence="ECO:0007829|PDB:1RY2"
FT TURN 655..657
FT /evidence="ECO:0007829|PDB:1RY2"
FT STRAND 660..664
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 678..683
FT /evidence="ECO:0007829|PDB:1RY2"
FT HELIX 702..709
FT /evidence="ECO:0007829|PDB:1RY2"
FT TURN 710..712
FT /evidence="ECO:0007829|PDB:1RY2"
SQ SEQUENCE 713 AA; 79141 MW; F282218B9A6CA3B2 CRC64;
MSPSAVQSSK LEEQSSEIDK LKAKMSQSAA TAQQKKEHEY EHLTSVKIVP QRPISDRLQP
AIATHYSPHL DGLQDYQRLH KESIEDPAKF FGSKATQFLN WSKPFDKVFI PDPKTGRPSF
QNNAWFLNGQ LNACYNCVDR HALKTPNKKA IIFEGDEPGQ GYSITYKELL EEVCQVAQVL
TYSMGVRKGD TVAVYMPMVP EAIITLLAIS RIGAIHSVVF AGFSSNSLRD RINDGDSKVV
ITTDESNRGG KVIETKRIVD DALRETPGVR HVLVYRKTNN PSVAFHAPRD LDWATEKKKY
KTYYPCTPVD SEDPLFLLYT SGSTGAPKGV QHSTAGYLLG ALLTMRYTFD THQEDVFFTA
GDIGWITGHT YVVYGPLLYG CATLVFEGTP AYPNYSRYWD IIDEHKVTQF YVAPTALRLL
KRAGDSYIEN HSLKSLRCLG SVGEPIAAEV WEWYSEKIGK NEIPIVDTYW QTESGSHLVT
PLAGGVTPMK PGSASFPFFG IDAVVLDPNT GEELNTSHAE GVLAVKAAWP SFARTIWKNH
DRYLDTYLNP YPGYYFTGDG AAKDKDGYIW ILGRVDDVVN VSGHRLSTAE IEAAIIEDPI
VAECAVVGFN DDLTGQAVAA FVVLKNKSSW STATDDELQD IKKHLVFTVR KDIGPFAAPK
LIILVDDLPK TRSGKIMRRI LRKILAGESD QLGDVSTLSN PGIVRHLIDS VKL
