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G0F1A2 (G0F1A2_CUPNN) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123

Short name=AcCoA synthetase HAMAP-Rule MF_01123
Short name=Acs HAMAP-Rule MF_01123
EC=6.2.1.1 HAMAP-Rule MF_01123
Alternative name(s):
Acetate--CoA ligase HAMAP-Rule MF_01123
Acyl-activating enzyme HAMAP-Rule MF_01123
Gene names
Name:acsA3 EMBL AEI77733.1
Synonyms:acsA HAMAP-Rule MF_01123
Ordered Locus Names:CNE_1c24100 EMBL AEI77733.1
OrganismCupriavidus necator (strain ATCC 43291 / DSM 13513 / N-1) (Ralstonia eutropha) [Complete proteome] [HAMAP] EMBL AEI77733.1
Taxonomic identifier1042878 [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 By similarity. HAMAP-Rule MF_01123

Catalytic activity

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

Cofactor

Magnesium By similarity. 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. HAMAP-Rule MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site5301 By similarity HAMAP-Rule MF_01123
Metal binding5501Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5551Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3171Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3971Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5121Substrate By similarity HAMAP-Rule MF_01123
Binding site5281Substrate By similarity HAMAP-Rule MF_01123
Binding site5361Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5391Substrate By similarity HAMAP-Rule MF_01123
Binding site6001Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6251N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
G0F1A2 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: 3381FFD2F26F1B3B

FASTA66072,614
        10         20         30         40         50         60 
MSAIESVMQE HRVFNPPEGF ASQAAIPSME AYRALCDEAE RDYEGFWARH ARELLHWNKP 

        70         80         90        100        110        120 
FTKVLDESNA PFYKWFEDGE LNASYNCLDR NLQNGNADKV AIVFEADDGT VTRVTYRELH 

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

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

       250        260        270        280        290        300 
RWMEDVSAGQ PDICEAEPVS AEHPLFVLYT SGSTGKPKGV QHSTGGYLLW ALMTMKWSFD 

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

       370        380        390        400        410        420 
YTAPTAIRSL IKAAEADDKI 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

[1]"Complete Genome Sequence of the Type Strain Cupriavidus necator N-1."
Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.
J. Bacteriol. 193:5017-5017(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43291 / DSM 13513 / N-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002877 Genomic DNA. Translation: AEI77733.1.
RefSeqYP_004686214.1. NC_015726.1.

3D structure databases

ProteinModelPortalG0F1A2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEI77733; AEI77733; CNE_1c24100.
GeneID10918801.
KEGGcnc:CNE_1c24100.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01895.

Enzyme and pathway databases

BioCycCNEC1042878:GH0Z-2410-MONOMER.

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 nameG0F1A2_CUPNN
AccessionPrimary (citable) accession number: G0F1A2
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: June 11, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)