Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis.

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation2 Publications

Cofactori

Mg2+UniRule annotation1 Publication

Kineticsi

  1. KM=0.15 mM for ATP (at pH 8.5 and 37 degrees Celsius)1 Publication
  2. KM=0.2 mM for CoA (at pH 8.5 and 37 degrees Celsius)1 Publication
  3. KM=0.2 mM for acetate (at pH 8.5 and 37 degrees Celsius)1 Publication
  1. Vmax=100 nmol/min/mg enzyme (at pH 8.5 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 8.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei311Coenzyme AUniRule annotation1
Binding sitei335Coenzyme AUniRule annotation1
Binding sitei500ATPUniRule annotation1
Binding sitei515ATPUniRule annotation1
Binding sitei523Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei526ATPUniRule annotation1
Metal bindingi537Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi539Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi542Magnesium; via carbonyl oxygenUniRule annotation1
Binding sitei584Coenzyme AUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi387 – 389ATPUniRule annotation3
Nucleotide bindingi411 – 416ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ACS-MONOMER
MetaCyc:ACS-MONOMER
SABIO-RKiP27550

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
Short name:
AcCoA synthetaseUniRule annotation
Short name:
AcsUniRule annotation
Alternative name(s):
Acetate--CoA ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
Gene namesi
Name:acsUniRule annotation
Synonyms:yfaC
Ordered Locus Names:b4069, JW4030
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11448 acs

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene grow as well as wild-type cells at high concentrations (>25 mM) of acetate as the sole carbon source, but grow poorly on lower concentrations (<10 mM).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002083621 – 652Acetyl-coenzyme A synthetaseAdd BLAST652

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei609N6-acetyllysine; by autocatalysisUniRule annotation1 Publication1

Post-translational modificationi

Autoacetylated. Deacetylation by CobB activates the enzyme.

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP27550
PaxDbiP27550
PRIDEiP27550

PTM databases

iPTMnetiP27550

Expressioni

Inductioni

By CRP and FNR, in response to rising cAMP levels, falling oxygen partial pressure and changes in carbon flux. May also be induced by acetate.1 Publication

Interactioni

Subunit structurei

Forms a 1:1 complex with CobB/NAD-dependent deacetylase.

Protein-protein interaction databases

BioGridi4262675, 22 interactors
IntActiP27550, 7 interactors
STRINGi316385.ECDH10B_4259

Structurei

3D structure databases

ProteinModelPortaliP27550
SMRiP27550
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni191 – 194Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108IQF Bacteria
COG0365 LUCA
HOGENOMiHOG000229981
InParanoidiP27550
KOiK01895
PhylomeDBiP27550

Family and domain databases

CDDicd05966 ACS, 1 hit
HAMAPiMF_01123 Ac_CoA_synth, 1 hit
InterProiView protein in InterPro
IPR011904 Ac_CoA_lig
IPR032387 ACAS_N
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
PfamiView protein in Pfam
PF16177 ACAS_N, 1 hit
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
TIGRFAMsiTIGR02188 Ac_CoA_lig_AcsA, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit

Sequencei

Sequence statusi: Complete.

P27550-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQIHKHTIP ANIADRCLIN PQQYEAMYQQ SINVPDTFWG EQGKILDWIK
60 70 80 90 100
PYQKVKNTSF APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD
110 120 130 140 150
DASQSKHISY KELHRDVCRF ANTLLELGIK KGDVVAIYMP MVPEAAVAML
160 170 180 190 200
ACARIGAVHS VIFGGFSPEA VAGRIIDSNS RLVITSDEGV RAGRSIPLKK
210 220 230 240 250
NVDDALKNPN VTSVEHVVVL KRTGGKIDWQ EGRDLWWHDL VEQASDQHQA
260 270 280 290 300
EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAALTFK YVFDYHPGDI
310 320 330 340 350
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMAQVVDKHQ
360 370 380 390 400
VNILYTAPTA IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK
410 420 430 440 450
KIGNEKCPVV DTWWQTETGG FMITPLPGAT ELKAGSATRP FFGVQPALVD
460 470 480 490 500
NEGNPLEGAT EGSLVITDSW PGQARTLFGD HERFEQTYFS TFKNMYFSGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP KIAEAAVVGI
560 570 580 590 600
PHNIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD
610 620 630 640 650
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM

PS
Length:652
Mass (Da):72,094
Last modified:October 1, 1993 - v2
Checksum:iF464062B6E82C099
GO

Sequence cautioni

The sequence AAA24715 differs from that shown. Reason: Frameshift at position 323.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00006 Genomic DNA Translation: AAC43163.1
U00096 Genomic DNA Translation: AAC77039.1
AP009048 Genomic DNA Translation: BAE78071.1
M87509 Genomic DNA Translation: AAA24715.1 Frameshift.
PIRiD65215
RefSeqiNP_418493.1, NC_000913.3
WP_000078239.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC77039; AAC77039; b4069
BAE78071; BAE78071; BAE78071
GeneIDi948572
KEGGiecj:JW4030
eco:b4069
PATRICifig|1411691.4.peg.2635

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00006 Genomic DNA Translation: AAC43163.1
U00096 Genomic DNA Translation: AAC77039.1
AP009048 Genomic DNA Translation: BAE78071.1
M87509 Genomic DNA Translation: AAA24715.1 Frameshift.
PIRiD65215
RefSeqiNP_418493.1, NC_000913.3
WP_000078239.1, NZ_LN832404.1

3D structure databases

ProteinModelPortaliP27550
SMRiP27550
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262675, 22 interactors
IntActiP27550, 7 interactors
STRINGi316385.ECDH10B_4259

PTM databases

iPTMnetiP27550

Proteomic databases

EPDiP27550
PaxDbiP27550
PRIDEiP27550

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77039; AAC77039; b4069
BAE78071; BAE78071; BAE78071
GeneIDi948572
KEGGiecj:JW4030
eco:b4069
PATRICifig|1411691.4.peg.2635

Organism-specific databases

EchoBASEiEB1417
EcoGeneiEG11448 acs

Phylogenomic databases

eggNOGiENOG4108IQF Bacteria
COG0365 LUCA
HOGENOMiHOG000229981
InParanoidiP27550
KOiK01895
PhylomeDBiP27550

Enzyme and pathway databases

BioCyciEcoCyc:ACS-MONOMER
MetaCyc:ACS-MONOMER
SABIO-RKiP27550

Miscellaneous databases

PROiPR:P27550

Family and domain databases

CDDicd05966 ACS, 1 hit
HAMAPiMF_01123 Ac_CoA_synth, 1 hit
InterProiView protein in InterPro
IPR011904 Ac_CoA_lig
IPR032387 ACAS_N
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
PfamiView protein in Pfam
PF16177 ACAS_N, 1 hit
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
TIGRFAMsiTIGR02188 Ac_CoA_lig_AcsA, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiACSA_ECOLI
AccessioniPrimary (citable) accession number: P27550
Secondary accession number(s): Q2M6N5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 1, 1993
Last modified: November 7, 2018
This is version 153 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again