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Reviewed, UniProtKB/Swiss-Prot B2IB12 (ACSA_BEII9)

Last modified November 3, 2009. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Bind_0053
OrganismBeijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712) [Complete proteome] [HAMAP]
Taxonomic identifier395963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBeijerinckiaceaeBeijerinckia

Protein attributes

Sequence length645 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 645645Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000137259

Sites

Active site5151 By similarity

Amino acid modifications

Modified residue6071N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2IB12-1 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 207BBEF735EE4221

FASTA64570,885
        10         20         30         40         50         60 
MSDKTYPVSA YWNERAYINA AKYKDMYKRS IEEPDLFWGE EGKRIDWIKP YTKVKNTSFD 

        70         80         90        100        110        120 
PANVDIRWFE DGITNVAYNC IDRHLATRGD QTAILFEGDD PADSRAITYK ELHDSVCRLA 

       130        140        150        160        170        180 
NVLKAHGVGK GDTVSLYLPM IPEAAFAMLA CARIGAIHSV IFGGFSPDSL AGRIEGCRSK 

       190        200        210        220        230        240 
VLITADEGLR GGRKVPLKAN ADLAIAKTGD IVQTMIVVTR TGGAVDWVEG RDVRYEEAIA 

       250        260        270        280        290        300 
AASPECPLTE VEAEHPLFIL YTSGSTGAPK GVVHCTGGYL VYASMTHQYV FDYHDGDVYW 

       310        320        330        340        350        360 
CTADVGWVTG HSYIVYGPLA NGATTLMFEG VPNYPSVSRF WEVIDKHKVT IFYTAPTAIR 

       370        380        390        400        410        420 
ALMGSGEAPV KKTSRASLRL LGSVGEPINP EAWEWYHRVV GEERCPIVDT WWQTETGGIL 

       430        440        450        460        470        480 
ITPLPGATPE KPGSATLPFF GVKPQVVDAT GAVLEGVCEG NLVIADSWPG QMRTIFGDHD 

       490        500        510        520        530        540 
RFVQSYFSTY PGKYFTGDGC RRDADGYYWI TGRVDDVINV SGHRLGTAEV ESSLVAHELV 

       550        560        570        580        590        600 
SEAAVVGYPH DIKGQGIYAY VTLMNGIEPS DRLRTELVTW VRKDIGPIAT PDVVHFATGL 

       610        620        630        640 
PKTRSGKIMR RILRKIAEKE FSALGDVSTL ADPTIVDDLI RNRLG 

« Hide

References

[1]"Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC 9039."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N. expand/collapse author list , Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001016 Genomic DNA. Translation: ACB93712.1.
RefSeqYP_001831201.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6201433.
GenomeReviewsGene locus Bind_0053 in contig CP001016_GR.
KEGGbid:Bind_0053.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAETASEHC.

Family and domain databases

HAMAPMF_01123.
[Tree]
InterProIPR011904. Ac_CoA_lig_AcsA.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACSA_BEII9
AccessionPrimary (citable) accession number: B2IB12
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: November 3, 2009
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents