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E3IPI9 (E3IPI9_DESVR) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 21. 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:acsA HAMAP-Rule MF_01123
Ordered Locus Names:Deval_2742 EMBL ADP87884.1
OrganismDesulfovibrio vulgaris (strain RCH1) [Complete proteome] [HAMAP] EMBL ADP87884.1
Taxonomic identifier573059 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length661 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

Regions

Region201 – 2044Coenzyme A By similarity HAMAP-Rule MF_01123
Region421 – 4266Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5271 By similarity HAMAP-Rule MF_01123
Metal binding5471Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5491Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5521Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3211Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3971Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5101Substrate By similarity HAMAP-Rule MF_01123
Binding site5251Substrate By similarity HAMAP-Rule MF_01123
Binding site5331Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5361Substrate By similarity HAMAP-Rule MF_01123
Binding site5941Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6191N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
E3IPI9 [UniParc].

Last modified January 11, 2011. Version 1.
Checksum: D33CE2558CB40921

FASTA66173,499
        10         20         30         40         50         60 
MSQERIESMM DEKRHFAPPA DSRGRAHVSG EAAREALVRR AAEDPEGFWG ERAAQLIDWF 

        70         80         90        100        110        120 
KPWDTVLDAD MNEPRIEWFK GGRLNVAHNC LDRHVAGNRR NKAAIIWQGE PEEDVRVLTY 

       130        140        150        160        170        180 
QMLYDEVRRF AAVLRKMGVH KGDRVSLYMP MIPELAVAML ACARIGAVHS IVFAGFSAVS 

       190        200        210        220        230        240 
LQNRIHDCEA KVVVTADAVL RAGRRIPLKV NVDEAVRQCP SVEKVVVVNR GSLEVTMEEG 

       250        260        270        280        290        300 
RDLWWHEVMA DRTLDVDRPC EEMDAEDMLF ILYTSGSTGK PKGVVHTTGG YLTYAAHTTQ 

       310        320        330        340        350        360 
WVFDVQDDDV YWCTADIGWI TGHSYIVYGP LALGATSLMF EGVPSWPSPD RFWRIVEKFR 

       370        380        390        400        410        420 
VNIFYTAPTV VRALMREGTD WTERHDLSSL RVLGSVGEPI NPEAWMWYHT HIGKGRLPIV 

       430        440        450        460        470        480 
DTWWQTETGG IMISGLPYAT TLKPGSATQP LPGVDAAIVR PDGSPAGPNE GGHLVIRKPW 

       490        500        510        520        530        540 
PGMLRGIFGS PERYRSTYFE RFPGMYESGD GARTDTDGYF WIMGRLDDVI NVSGHRMGTA 

       550        560        570        580        590        600 
EVESALVAHP SVAEAAVVGM PHAVKGEAIY AYVTLGADAE ETEELRAELR AWVRKEIGPI 

       610        620        630        640        650        660 
ATPDVLQFAE GLPKTRSGKI MRRILRKIAA GATSEFGDTS TLADPGVVSD LIEGRLQLTG 


R 

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References

[1]"Complete sequence of chromosome of Desulfovibrio vulgaris RCH1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Detter J.C., Han C., Tapia R., Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Chakraborty R., Arkin A.P. expand/collapse author list , Dehal P., Wall J.D., Deutschbauer A.M., Hazen T.C., Woyke T.
Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCH1 EMBL ADP87884.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002297 Genomic DNA. Translation: ADP87884.1.
RefSeqYP_005703522.1. NC_017310.1.

3D structure databases

ProteinModelPortalE3IPI9.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADP87884; ADP87884; Deval_2742.
GeneID12868602.
KEGGdvg:Deval_2742.
PATRIC42913287. VBIDesVul75230_2905.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01895.
OMAWVMGRVD.

Enzyme and pathway databases

BioCycDVUL573059:GLCM-2818-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 nameE3IPI9_DESVR
AccessionPrimary (citable) accession number: E3IPI9
Entry history
Integrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: February 19, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)