ACS2_YEAST
ID ACS2_YEAST Reviewed; 683 AA.
AC P52910; D6VYE8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Acetyl-coenzyme A synthetase 2 {ECO:0000303|PubMed:8910545};
DE EC=6.2.1.1 {ECO:0000269|PubMed:8910545};
DE AltName: Full=Acetate--CoA ligase 2 {ECO:0000303|PubMed:8910545};
DE AltName: Full=Acyl-activating enzyme 2 {ECO:0000303|PubMed:8910545};
GN Name=ACS2 {ECO:0000303|PubMed:8910545}; OrderedLocusNames=YLR153C;
GN ORFNames=L9634.10;
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].
RX PubMed=7649171; DOI=10.1111/j.1432-1033.1995.tb20751.x;
RA van den Berg M.A., de Steensma H.Y.;
RT "ACS2, a Saccharomyces cerevisiae gene encoding acetyl-coenzyme A
RT synthetase, essential for growth on glucose.";
RL Eur. J. Biochem. 231:704-713(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
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 [5]
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 [6]
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 [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-506, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Catalyzes the production of acetyl-CoA. Provides the acetyl-
CC CoA source for histone acetylation in the nucleus. 'Anaerobic' isozyme
CC of acetyl-coenzyme A synthetase, which is required for growth on
CC fermentable carbon sources such as glucose. May be involved in the PDH
CC (pyruvate dehydrogenase complex) bypass. {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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.8 mM for acetate {ECO:0000269|PubMed:8910545};
CC KM=1.3 mM for ATP {ECO:0000269|PubMed:8910545};
CC Vmax=0.34 umol/min/mg enzyme {ECO:0000269|PubMed:8910545};
CC -!- PATHWAY: Carbohydrate metabolism; pyruvate metabolism.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly nuclear.
CC -!- MISCELLANEOUS: Present with 225000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S79456; AAB35143.1; -; Genomic_DNA.
DR EMBL; U53879; AAB82387.1; -; Genomic_DNA.
DR EMBL; Z73325; CAA97725.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09464.1; -; Genomic_DNA.
DR PIR; S65002; S65002.
DR RefSeq; NP_013254.1; NM_001182040.1.
DR AlphaFoldDB; P52910; -.
DR SMR; P52910; -.
DR BioGRID; 31422; 353.
DR DIP; DIP-992N; -.
DR IntAct; P52910; 45.
DR MINT; P52910; -.
DR STRING; 4932.YLR153C; -.
DR iPTMnet; P52910; -.
DR MaxQB; P52910; -.
DR PaxDb; P52910; -.
DR PRIDE; P52910; -.
DR EnsemblFungi; YLR153C_mRNA; YLR153C; YLR153C.
DR GeneID; 850846; -.
DR KEGG; sce:YLR153C; -.
DR SGD; S000004143; ACS2.
DR VEuPathDB; FungiDB:YLR153C; -.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000176537; -.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; P52910; -.
DR OMA; SPDIWEW; -.
DR BioCyc; MetaCyc:YLR153C-MON; -.
DR BioCyc; YEAST:YLR153C-MON; -.
DR BRENDA; 6.2.1.1; 984.
DR Reactome; R-SCE-71384; Ethanol oxidation.
DR SABIO-RK; P52910; -.
DR UniPathway; UPA00231; -.
DR PRO; PR:P52910; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P52910; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
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: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; IMP:SGD.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniPathway.
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 ATP-binding; Cytoplasm; Isopeptide bond; Ligase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..683
FT /note="Acetyl-coenzyme A synthetase 2"
FT /id="PRO_0000208421"
FT BINDING 206..209
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 325
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 401..403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 425..430
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 425..430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 516
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 531
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 539
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 612
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 506
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
SQ SEQUENCE 683 AA; 75492 MW; 418439EDCDF308F3 CRC64;
MTIKEHKVVY EAHNVKALKA PQHFYNSQPG KGYVTDMQHY QEMYQQSINE PEKFFDKMAK
EYLHWDAPYT KVQSGSLNNG DVAWFLNGKL NASYNCVDRH AFANPDKPAL IYEADDESDN
KIITFGELLR KVSQIAGVLK SWGVKKGDTV AIYLPMIPEA VIAMLAVARI GAIHSVVFAG
FSAGSLKDRV VDANSKVVIT CDEGKRGGKT INTKKIVDEG LNGVDLVSRI LVFQRTGTEG
IPMKAGRDYW WHEEAAKQRT YLPPVSCDAE DPLFLLYTSG STGSPKGVVH TTGGYLLGAA
LTTRYVFDIH PEDVLFTAGD VGWITGHTYA LYGPLTLGTA SIIFESTPAY PDYGRYWRII
QRHKATHFYV APTALRLIKR VGEAEIAKYD TSSLRVLGSV GEPISPDLWE WYHEKVGNKN
CVICDTMWQT ESGSHLIAPL AGAVPTKPGS ATVPFFGINA CIIDPVTGVE LEGNDVEGVL
AVKSPWPSMA RSVWNHHDRY MDTYLKPYPG HYFTGDGAGR DHDGYYWIRG RVDDVVNVSG
HRLSTSEIEA SISNHENVSE AAVVGIPDEL TGQTVVAYVS LKDGYLQNNA TEGDAEHITP
DNLRRELILQ VRGEIGPFAS PKTIILVRDL PRTRSGKIMR RVLRKVASNE AEQLGDLTTL
ANPEVVPAII SAVENQFFSQ KKK
