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A0KNI2 (ACSA_AERHH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:AHA_3344
OrganismAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]
Taxonomic identifier380703 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length648 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 – 648648Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000065265

Sites

Active site5161 By similarity

Amino acid modifications

Modified residue6081N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0KNI2 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 73B767E59C45A687

FASTA64871,342
        10         20         30         40         50         60 
MSESKVYPVK AHISNGALLD KAGYEAMYRA SVQDPDAFWG EQGKILDWMK PYTRVKNTSY 

        70         80         90        100        110        120 
DPGHVSIKWY EDGLLNVSAN CLDRHLAQRG DKVAIIWEGD NPAEDRKLTY RELHTEVCKF 

       130        140        150        160        170        180 
ANVLKAQGVH RGDVVCLYMP MVPEAAIAML ACTRIGAVHS IVFGGFSPEA LAGRIIDSGS 

       190        200        210        220        230        240 
SIVITADEGL RGGRPVPLKK NVDEALTNPE TKVNNVIVLK RTGGNIAWHN HRDIWWHDAV 

       250        260        270        280        290        300 
ATVSADCPPE AMGAEDPLFI LYTSGSTGKP KGVLHTTGGY LVYATLTFKY IFDYHEEDIY 

       310        320        330        340        350        360 
WCTADVGWVT GHSYLVYGPL ANGATTIMFE GVPNYPATNR MSQVVDKHQV SILYTAPTAI 

       370        380        390        400        410        420 
RALMAKGNEA VADTSRSSLR IMGSVGEPIN PEAWEWYYRT IGEERCPIVD TWWQTETGGI 

       430        440        450        460        470        480 
LISPLPGVTD LKPGSATRPF FGVQPALVDN MGEPLEGATE GNLVITDSWP GQMRTVFGDH 

       490        500        510        520        530        540 
ERFEQTYFST FPGRYFTGDG ARRDEDGYYW ITGRVDDVLN VSGHRMGTAE IESALVSHPK 

       550        560        570        580        590        600 
IAEAAVVGVP HEIKGQGIYA YVTLIAGEEP SRELHKEVKE WVRKEIGAIA TPDVIHWAEG 

       610        620        630        640 
LPKTRSGKIM RRILRKIATG ETDSLGDIST LADPGVVDKL IREKSEAA 

« Hide

References

[1]"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.
J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 7966 / NCIB 9240.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000462 Genomic DNA. Translation: ABK37083.1.
RefSeqYP_857833.1. NC_008570.1.

3D structure databases

ProteinModelPortalA0KNI2.
SMRA0KNI2. Positions 7-644.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0KNI2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4490124.
GenomeReviewsGene locus AHA_3344 in contig CP000462_GR.
KEGGaha:AHA_3344.
PATRIC20784316. VBIAerHyd135212_3340.
TIGRAHA_3344.

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHBG547964.
OMALIQWAGG.
PhylomeDBA0KNI2.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycAHYD196024:AHA_3344-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_AERHH
AccessionPrimary (citable) accession number: A0KNI2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 35 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