Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q7NSY7 (ACSA_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
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
EC=6.2.1.1
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene names
Name:acsA
Ordered Locus Names:CV_3282
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

Protein attributes

Sequence length654 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Post-translational modification

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

Sequence similarities

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

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionAMP binding

Inferred from electronic annotation. Source: InterPro

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetate-CoA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 654654Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000065288

Sites

Active site5241 By similarity

Amino acid modifications

Modified residue6191N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NSY7 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: AD8E8E873C88693B

FASTA65472,048
        10         20         30         40         50         60 
MSTLDSILKE TRSFAPSEEF RRKASISGIE AYHALCEQAD DHYLSFWGDL ARELITWKKP 

        70         80         90        100        110        120 
FSRVLDDSQA PFFKWFDDGV LNASYNCLDR HLAANANKIA IIFEADDGEV TRVTYSELHR 

       130        140        150        160        170        180 
RVCQFANGLK SLGVKKGDRV VVYMPMGIEA VVTMQACARI GAIHSVVFGG FSAGAVRDRI 

       190        200        210        220        230        240 
QDAGATVVVT ANESVRGGKN VPLKATVDEA LALEGAESVR HVVVYQRTNG GADWTDGRDV 

       250        260        270        280        290        300 
WWHKLIEGQS EACEPEWMGA EDPLFILYTS GSTGKPKGIQ HSTAGYLLGA LNSFRWVFDY 

       310        320        330        340        350        360 
KPNDVFWCTA DVGWITGHSY VCYGPLANGA TQVIFEGVPT YPDAGRFWKM IEQHKVSIFY 

       370        380        390        400        410        420 
TAPTAIRSLI KLGSDLPKQY DLSSLRVLGT VGEPINPEAW IWYYETVGGG RCPIVDTWWQ 

       430        440        450        460        470        480 
TETGSTMIAP LPGAIATKPG SCTLPLPGVI ADIVDESGAQ VEPGRGGFLV IKKPFPSLVR 

       490        500        510        520        530        540 
TIWNDPERFK KTYFPDEFDG KYYLAGDSAH RDENGYFWIM GRIDDVLNVS GHRLGTMEIE 

       550        560        570        580        590        600 
SALVANPLVA EAAVVGKPHE VKGEAVVAFV VLKGARPQGD AAKTVAAELK NWVAHEIGKI 

       610        620        630        640        650 
AQPDDIRFGE NLPKTRSGKI MRRLLRSIAK GEEITQDVST LENPQILQQL QQPL

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016825 Genomic DNA. Translation: AAQ60946.1.
RefSeqNP_902952.1. NC_005085.1.

3D structure databases

HSSPHSSP built from PDB template 1PG4 based on UniProtKB Q8ZKF6.
ProteinModelPortalQ7NSY7.
SMRQ7NSY7. Positions 16-652.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2547693.
GenomeReviewsGene locus CV_3282 in contig AE016825_GR.
KEGGcvi:CV_3282.
NMPDRfig|243365.1.peg.3282.
PATRIC21441348. VBIChrVio67196_3204.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG547964.
OMATRGTEES.
PhylomeDBQ7NSY7.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycCVIO243365:CV_3282-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
[Tree]
InterProIPR011904. Ac_CoA_lig.
IPR024597. Acyl-CoA_synth_DUF3448.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
KOK01895.
PANTHERPTHR24095:SF42. PTHR24095:SF42. 1 hit.
PfamPF00501. AMP-binding. 1 hit.
PF11930. DUF3448. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACSA_CHRVO
AccessionPrimary (citable) accession number: Q7NSY7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 15, 2003
Last modified: January 25, 2012
This is version 53 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents