Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P31638 (ACSA_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase

Short name=AcCoA synthetase
Short name=Acs
EC=6.2.1.1
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene names
Name:acsA
Synonyms:acoE
Ordered Locus Names:H16_A2525
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA 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. Although acetate is the preferred substrate of AcsA, propionate is also used, but at a diminished rate compared with that of acetate. Fatty acids with more than three carbon atoms are usually not accepted as substrates by AcsA. Ref.1

Catalytic activity

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01123

Pathway

Ketone degradation; acetoin degradation. HAMAP-Rule MF_01123

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 660660Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123
PRO_0000208353

Sites

Active site5301 By similarity
Metal binding5501Magnesium; via carbonyl oxygen By similarity
Metal binding5551Magnesium; via carbonyl oxygen By similarity
Binding site3171Coenzyme A By similarity
Binding site3971Substrate; via amide nitrogen By similarity
Binding site5121Substrate By similarity
Binding site5281Substrate By similarity
Binding site5361Coenzyme A By similarity
Binding site5391Substrate By similarity
Binding site6001Coenzyme A

Amino acid modifications

Modified residue6251N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P31638 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: EA03022F82C5C502

FASTA66072,602
        10         20         30         40         50         60 
MSAIESVMQE HRVFNPPEGF ASQAAIPSME AYQALCDEAE RDYEGFWARH ARELLHWTKP 

        70         80         90        100        110        120 
FTKVLDQSNA PFYKWFEDGE LNASYNCLDR NLQNGNADKV AIVFEADDGS VTRVTYRELH 

       130        140        150        160        170        180 
GKVCRFANGL KALGIRKGDR VVIYMPMSVE GVVAMQACAR LGATHSVVFG GFSAKSLQER 

       190        200        210        220        230        240 
LVDVGAVALI TADEQMRGGK ALPLKAIADD ALALGGCEAV RNVIVYRRTG GKVAWTEGRD 

       250        260        270        280        290        300 
RWMEDVSAGQ PDTCEAEPVS AEHPLFVLYT SGSTGKPKGV QHSTGGYLLW ALMTMKWTFD 

       310        320        330        340        350        360 
IKPDDLFWCT ADIGWVTGHT YIAYGPLAAG ATQVVFEGVP TYPNAGRFWD MIARHKVSIF 

       370        380        390        400        410        420 
YTAPTAIRSL IKAAEADEKI HPKQYDLSSL RLLGTVGEPI NPEAWMWYYK NIGNERCPIV 

       430        440        450        460        470        480 
DTFWQTETGG HMITPLPGAT PLVPGSCTLP LPGIMAAIVD ETGHDVPNGN GGILVVKRPW 

       490        500        510        520        530        540 
PAMIRTIWGD PERFRKSYFP EELGGKLYLA GDGSIRDKDT GYFTIMGRID DVLNVSGHRM 

       550        560        570        580        590        600 
GTMEIESALV SNPLVAEAAV VGRPDDMTGE AICAFVVLKR SRPTGEEAVK IATELRNWVG 

       610        620        630        640        650        660 
KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEEI TQDTSTLENP AILEQLKQAQ 

« Hide

References

« Hide 'large scale' references
[1]"Identification and molecular characterization of the acetyl coenzyme A synthetase gene (acoE) of Alcaligenes eutrophus."
Priefert H., Steinbuechel A.
J. Bacteriol. 174:6590-6599(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY.
[2]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97217 Genomic DNA. Translation: AAA21945.1.
AM260479 Genomic DNA. Translation: CAJ93612.1.
PIRA45736.
RefSeqYP_726980.1. NC_008313.1.

3D structure databases

ProteinModelPortalP31638.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_A2525.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ93612; CAJ93612; H16_A2525.
GeneID4247141.
KEGGreh:H16_A2525.
PATRIC35234555. VBIRalEut6770_2916.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAAHERYEN.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-2492-MONOMER.
MetaCyc:MONOMER-13637.
UniPathwayUPA00040.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACSA_CUPNH
AccessionPrimary (citable) accession number: P31638
Secondary accession number(s): Q0K8Q9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 14, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways