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Protein

Acetyl-coenzyme A synthetase 1

Gene

ACS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.

Kineticsi

  1. KM=0.32 mM for acetate1 Publication
  2. KM=1.4 mM for ATP1 Publication
  1. Vmax=1.1 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei367Coenzyme ABy similarity1
Binding sitei559ATP1
Binding sitei574ATP1
Binding sitei582Coenzyme A; via carbonyl oxygenBy similarity1
Binding sitei585ATPBy similarity1
Binding sitei650Coenzyme ABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi443 – 445ATP3
Nucleotide bindingi467 – 472ATP6

GO - Molecular functioni

  • acetate-CoA ligase activity Source: SGD
  • acid-ammonia (or amide) ligase activity Source: SGD
  • AMP binding Source: InterPro
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • acetate fermentation Source: SGD
  • acetyl-CoA biosynthetic process Source: SGD
  • acetyl-CoA biosynthetic process from acetate Source: InterPro
  • histone acetylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:YAL054C-MONOMER.
YEAST:YAL054C-MONOMER.
BRENDAi6.2.1.1. 984.
ReactomeiR-SCE-77111. Synthesis of Ketone Bodies.
SABIO-RKQ01574.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetase 1 (EC:6.2.1.1)
Alternative name(s):
Acetate--CoA ligase 1
Acyl-activating enzyme 1
Gene namesi
Name:ACS1
Ordered Locus Names:YAL054C
ORF Names:FUN44
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:YAL054C.
SGDiS000000050. ACS1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • endoplasmic reticulum Source: UniProtKB-KW
  • mitochondrion Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002084201 – 713Acetyl-coenzyme A synthetase 1Add BLAST713

Proteomic databases

MaxQBiQ01574.
PRIDEiQ01574.

Expressioni

Inductioni

By acetate, acetaldehyde and ethanol. Subject to glucose catabolite repression. Inactivated and degraded after addition of glucose (at protein level).2 Publications

Interactioni

Protein-protein interaction databases

BioGridi31775. 41 interactors.
DIPiDIP-4326N.
IntActiQ01574. 4 interactors.
MINTiMINT-525275.

Structurei

Secondary structure

1713
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi75 – 85Combined sources11
Helixi87 – 98Combined sources12
Beta strandi113 – 115Combined sources3
Helixi133 – 137Combined sources5
Helixi139 – 142Combined sources4
Beta strandi148 – 154Combined sources7
Beta strandi162 – 165Combined sources4
Helixi166 – 182Combined sources17
Beta strandi191 – 194Combined sources4
Helixi200 – 211Combined sources12
Beta strandi215 – 218Combined sources4
Helixi225 – 235Combined sources11
Beta strandi238 – 245Combined sources8
Helixi255 – 262Combined sources8
Beta strandi271 – 275Combined sources5
Beta strandi287 – 292Combined sources6
Helixi293 – 297Combined sources5
Beta strandi316 – 320Combined sources5
Beta strandi323 – 326Combined sources4
Beta strandi328 – 332Combined sources5
Helixi335 – 348Combined sources14
Beta strandi356 – 359Combined sources4
Helixi366 – 371Combined sources6
Helixi374 – 379Combined sources6
Beta strandi381 – 386Combined sources6
Helixi397 – 404Combined sources8
Beta strandi408 – 412Combined sources5
Helixi414 – 420Combined sources7
Beta strandi427 – 430Combined sources4
Beta strandi438 – 441Combined sources4
Helixi448 – 456Combined sources9
Beta strandi461 – 463Combined sources3
Beta strandi465 – 467Combined sources3
Turni472 – 474Combined sources3
Beta strandi478 – 480Combined sources3
Turni483 – 485Combined sources3
Beta strandi503 – 506Combined sources4
Beta strandi508 – 510Combined sources3
Beta strandi520 – 527Combined sources8
Helixi540 – 547Combined sources8
Beta strandi549 – 551Combined sources3
Beta strandi554 – 563Combined sources10
Beta strandi569 – 571Combined sources3
Beta strandi581 – 583Combined sources3
Helixi588 – 596Combined sources9
Beta strandi601 – 607Combined sources7
Beta strandi619 – 624Combined sources6
Helixi641 – 652Combined sources12
Turni655 – 657Combined sources3
Beta strandi660 – 664Combined sources5
Helixi678 – 683Combined sources6
Helixi702 – 709Combined sources8
Turni710 – 712Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RY2X-ray2.30A72-713[»]
ProteinModelPortaliQ01574.
SMRiQ01574.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01574.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni248 – 251Coenzyme A bindingBy similarity4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi711 – 713Microbody targeting signalSequence analysis3

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229981.
InParanoidiQ01574.
KOiK01895.
OMAiEGRIITY.
OrthoDBiEOG092C0Z1N.

Family and domain databases

CDDicd05966. ACS. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q01574-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPSAVQSSK LEEQSSEIDK LKAKMSQSAA TAQQKKEHEY EHLTSVKIVP
60 70 80 90 100
QRPISDRLQP AIATHYSPHL DGLQDYQRLH KESIEDPAKF FGSKATQFLN
110 120 130 140 150
WSKPFDKVFI PDPKTGRPSF QNNAWFLNGQ LNACYNCVDR HALKTPNKKA
160 170 180 190 200
IIFEGDEPGQ GYSITYKELL EEVCQVAQVL TYSMGVRKGD TVAVYMPMVP
210 220 230 240 250
EAIITLLAIS RIGAIHSVVF AGFSSNSLRD RINDGDSKVV ITTDESNRGG
260 270 280 290 300
KVIETKRIVD DALRETPGVR HVLVYRKTNN PSVAFHAPRD LDWATEKKKY
310 320 330 340 350
KTYYPCTPVD SEDPLFLLYT SGSTGAPKGV QHSTAGYLLG ALLTMRYTFD
360 370 380 390 400
THQEDVFFTA GDIGWITGHT YVVYGPLLYG CATLVFEGTP AYPNYSRYWD
410 420 430 440 450
IIDEHKVTQF YVAPTALRLL KRAGDSYIEN HSLKSLRCLG SVGEPIAAEV
460 470 480 490 500
WEWYSEKIGK NEIPIVDTYW QTESGSHLVT PLAGGVTPMK PGSASFPFFG
510 520 530 540 550
IDAVVLDPNT GEELNTSHAE GVLAVKAAWP SFARTIWKNH DRYLDTYLNP
560 570 580 590 600
YPGYYFTGDG AAKDKDGYIW ILGRVDDVVN VSGHRLSTAE IEAAIIEDPI
610 620 630 640 650
VAECAVVGFN DDLTGQAVAA FVVLKNKSSW STATDDELQD IKKHLVFTVR
660 670 680 690 700
KDIGPFAAPK LIILVDDLPK TRSGKIMRRI LRKILAGESD QLGDVSTLSN
710
PGIVRHLIDS VKL
Length:713
Mass (Da):79,141
Last modified:September 1, 2009 - v2
Checksum:iF282218B9A6CA3B2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti34Q → R in CAA47054 (PubMed:1363452).Curated1
Sequence conflicti328K → E in AAU09675 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS51967. S30019.
RefSeqiNP_009347.1. NM_001178197.1.

Genome annotation databases

EnsemblFungiiYAL054C; YAL054C; YAL054C.
GeneIDi851245.
KEGGisce:YAL054C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS51967. S30019.
RefSeqiNP_009347.1. NM_001178197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RY2X-ray2.30A72-713[»]
ProteinModelPortaliQ01574.
SMRiQ01574.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31775. 41 interactors.
DIPiDIP-4326N.
IntActiQ01574. 4 interactors.
MINTiMINT-525275.

Proteomic databases

MaxQBiQ01574.
PRIDEiQ01574.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAL054C; YAL054C; YAL054C.
GeneIDi851245.
KEGGisce:YAL054C.

Organism-specific databases

EuPathDBiFungiDB:YAL054C.
SGDiS000000050. ACS1.

Phylogenomic databases

GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229981.
InParanoidiQ01574.
KOiK01895.
OMAiEGRIITY.
OrthoDBiEOG092C0Z1N.

Enzyme and pathway databases

BioCyciMetaCyc:YAL054C-MONOMER.
YEAST:YAL054C-MONOMER.
BRENDAi6.2.1.1. 984.
ReactomeiR-SCE-77111. Synthesis of Ketone Bodies.
SABIO-RKQ01574.

Miscellaneous databases

EvolutionaryTraceiQ01574.
PROiQ01574.

Family and domain databases

CDDicd05966. ACS. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACS1_YEAST
AccessioniPrimary (citable) accession number: Q01574
Secondary accession number(s): D6VPG4, Q66RJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: September 1, 2009
Last modified: November 30, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2890 molecules/cell in log phase SD medium.1 Publication

Caution

It is uncertain whether Met-1 or Met-25 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome I
    Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.