Acetyl-coenzyme A synthetase 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q01574 (ACS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 122. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acetyl-coenzyme A synthetase 1
EC=6.2.1.1

Alternative name(s):
Acetate--CoA ligase 1
Acyl-activating enzyme 1

Gene names

Name:	ACS1
Ordered Locus Names:	YAL054C
ORF Names:	FUN44

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	713 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the production of acetyl-CoA. Provides the acetyl-CoA source for histone acetylation in the nucleus. "Aerobic" isozyme of acetyl-coenzyme A synthetase, which supports growth on nonfermentable carbon sources such as glycerol and ethanol. May be required for assimilation of ethanol and acetate. Ref.6 Ref.12
Catalytic activity	ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
Subcellular location	Microsome Potential. Cytoplasm. Mitochondrion. Nucleus Ref.8 Ref.9 Ref.11.
Induction	By acetate, acetaldehyde and ethanol. Subject to glucose catabolite repression. Inactivated and degraded after addition of glucose (at protein level). Ref.6 Ref.7
Miscellaneous	Present with 2890 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.
Caution	It is uncertain whether Met-1 or Met-25 is the initiator.
Biophysicochemical properties	Kinetic parameters: K_M=0.32 mM for acetate Ref.6 K_M=1.4 mM for ATP V_max=1.1 µmol/min/mg enzyme

Ontologies

Keywords
Cellular component	Cytoplasm Endoplasmic reticulum Microsome Mitochondrion Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetate fermentation Inferred from mutant phenotype Ref.1. Source: SGD acetyl-CoA biosynthetic process Inferred from direct assay Ref.6. Source: SGD acetyl-CoA biosynthetic process from acetate Inferred from electronic annotation. Source: InterPro histone acetylation Inferred from genetic interaction Ref.12. Source: SGD
Cellular_component	cytosol Inferred from direct assay PubMed 9711835. Source: SGD endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD mitochondrion Inferred from direct assay Ref.11 PubMed 16823961. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	AMP binding Inferred from electronic annotation. Source: InterPro ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate-CoA ligase activity Inferred from direct assay Ref.6. Source: SGD acid-ammonia (or amide) ligase activity Inferred from direct assay PubMed 18305111. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
SRP1	Q02821	1	EBI-2128,EBI-1797
YAT1	P80235	1	EBI-2128,EBI-3928
YLR049C	Q12110	1	EBI-2128,EBI-33635

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 713

713

Acetyl-coenzyme A synthetase 1

PRO_0000208420

Regions

Nucleotide binding

467 – 472

AMP

Motif

711 – 713

Microbody targeting signal Potential

Sites

Binding site

559

AMP

Binding site

574

AMP

Experimental info

Sequence conflict

Q → R in CAA47054. Ref.1

Sequence conflict

328

K → E in AAU09675. Ref.4

Secondary structure

713

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q01574 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: F282218B9A6CA3B2
Show »

FASTA

713

79,141

        10         20         30         40         50         60 
MSPSAVQSSK LEEQSSEIDK LKAKMSQSAA TAQQKKEHEY EHLTSVKIVP QRPISDRLQP 

        70         80         90        100        110        120 
AIATHYSPHL DGLQDYQRLH KESIEDPAKF FGSKATQFLN WSKPFDKVFI PDPKTGRPSF 

       130        140        150        160        170        180 
QNNAWFLNGQ LNACYNCVDR HALKTPNKKA IIFEGDEPGQ GYSITYKELL EEVCQVAQVL 

       190        200        210        220        230        240 
TYSMGVRKGD TVAVYMPMVP EAIITLLAIS RIGAIHSVVF AGFSSNSLRD RINDGDSKVV 

       250        260        270        280        290        300 
ITTDESNRGG KVIETKRIVD DALRETPGVR HVLVYRKTNN PSVAFHAPRD LDWATEKKKY 

       310        320        330        340        350        360 
KTYYPCTPVD SEDPLFLLYT SGSTGAPKGV QHSTAGYLLG ALLTMRYTFD THQEDVFFTA 

       370        380        390        400        410        420 
GDIGWITGHT YVVYGPLLYG CATLVFEGTP AYPNYSRYWD IIDEHKVTQF YVAPTALRLL 

       430        440        450        460        470        480 
KRAGDSYIEN HSLKSLRCLG SVGEPIAAEV WEWYSEKIGK NEIPIVDTYW QTESGSHLVT 

       490        500        510        520        530        540 
PLAGGVTPMK PGSASFPFFG IDAVVLDPNT GEELNTSHAE GVLAVKAAWP SFARTIWKNH 

       550        560        570        580        590        600 
DRYLDTYLNP YPGYYFTGDG AAKDKDGYIW ILGRVDDVVN VSGHRLSTAE IEAAIIEDPI 

       610        620        630        640        650        660 
VAECAVVGFN DDLTGQAVAA FVVLKNKSSW STATDDELQD IKKHLVFTVR KDIGPFAAPK 

       670        680        690        700        710 
LIILVDDLPK TRSGKIMRRI LRKILAGESD QLGDVSTLSN PGIVRHLIDS VKL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and disruption of a gene required for growth on acetate but not on ethanol: the acetyl-coenzyme A synthetase gene of Saccharomyces cerevisiae." de Virgilio C., Buerckert N., Barth G., Neuhaus J.-M., Boller T., Wiemken A. Yeast 8:1043-1051(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / GRF88.
[2]	"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae." Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K. Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	"Carbon source-dependent regulation of the acetyl-coenzyme A synthetase-encoding gene ACS1 from Saccharomyces cerevisiae." Kratzer S., Schueller H.-J. Gene 161:75-79(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59. Strain: GRF78.
[6]	"The two acetyl-coenzyme A synthetases of Saccharomyces cerevisiae differ with respect to kinetic properties and transcriptional regulation." van den Berg M.A., de Jong-Gubbels P., Kortland C.J., van Dijken J.P., Pronk J.T., Steensma H.Y. J. Biol. Chem. 271:28953-28959(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
[7]	"The Saccharomyces cerevisiae acetyl-coenzyme A synthetase encoded by the ACS1 gene, but not the ACS2-encoded enzyme, is subject to glucose catabolite inactivation." de Jong-Gubbels P., van den Berg M.A., Steensma H.Y., van Dijken J.P., Pronk J.T. FEMS Microbiol. Lett. 153:75-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[8]	"Subcellular localization of the yeast proteome." Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S., Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P., Gerstein M., Roeder G.S., Snyder M. Genes Dev. 16:707-719(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
[12]	"Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription." Takahashi H., McCaffery J.M., Irizarry R.A., Boeke J.D. Mol. Cell 23:207-217(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP." Jogl G., Tong L. Biochemistry 43:1425-1431(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 72-713 IN COMPLEX WITH AMP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X66425 Genomic DNA. Translation: CAA47054.1.
U12980 Genomic DNA. Translation: AAC04979.1.
AY723758 Genomic DNA. Translation: AAU09675.1.
X76891 Genomic DNA. Translation: CAA54220.1.
BK006935 Genomic DNA. Translation: DAA06934.1.

PIR

S30019. S51967.

RefSeq

NP_009347.1. NM_001178197.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RY2	X-ray	2.30	A	72-713	[»]

ProteinModelPortal

Q01574.

SMR

Q01574. Positions 74-713.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4326N.

IntAct

Q01574. 4 interactions.

MINT

MINT-525275.

STRING

4932.YAL054C.

Proteomic databases

PaxDb

Q01574.

PeptideAtlas

Q01574.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YAL054C; YAL054C; YAL054C.

GeneID

851245.

KEGG

sce:YAL054C.

Organism-specific databases

SGD

S000000050. ACS1.

Phylogenomic databases

eggNOG

COG0365.

GeneTree

ENSGT00690000101993.

HOGENOM

HOG000229981.

K01895.

OMA

PEAMEST.

OrthoDB

EOG4M0J8W.

Enzyme and pathway databases

SABIO-RK

Q01574.

Gene expression databases

Genevestigator

Q01574.

GermOnline

YAL054C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011904. Ac_CoA_lig.
IPR024597. Acyl-CoA_synth_DUF3448.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR025110. DUF4009.
[Graphical view]

Pfam

PF00501. AMP-binding. 1 hit.
PF11930. DUF3448. 1 hit.
PF13193. DUF4009. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02188. Ac_CoA_lig_AcsA. 1 hit.

PROSITE

PS00455. AMP_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

EvolutionaryTrace

Q01574.

NextBio

968180.

Entry information

Entry name

ACS1_YEAST

Accession

Primary (citable) accession number: Q01574
Secondary accession number(s): D6VPG4, Q66RJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	September 1, 2009
Last modified:	April 3, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome I

Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents