Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot B2JD61 (ACSA_BURP8)

Last modified November 3, 2009. Version 10. 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: Bphy_1938
OrganismBurkholderia phymatum (strain DSM 17167 / STM815) [Complete proteome] [HAMAP]
Taxonomic identifier391038 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length660 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 – 660660Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000137261

Sites

Active site5301 By similarity

Amino acid modifications

Modified residue6251N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2JD61-1 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: BDC68F538B23A5BF

FASTA66072,379
        10         20         30         40         50         60 
MSAIESVLQE RRVFQPSAEV AAQATVSGMD AYKALVAEAE RDYEGFWGRL ARETLSWNKP 

        70         80         90        100        110        120 
FTKVLDESNA PFYKWYDDGE LNASYNSIDR HVEAGNGERV AIIFEADDGT ITNVTYNDLL 

       130        140        150        160        170        180 
QRVSRFANAL KQRGIKKGDR VVIYMPMSVE GIVAMQACAR IGATHSVVFG GFSSKSLNER 

       190        200        210        220        230        240 
LVDVGAVALV TSDEQMRGGK ALPLKNIADE ALAMGGCEAV KSVIVYQRTG GKIGWDDKRD 

       250        260        270        280        290        300 
LWMHEITASE SDHCPPEWVG AEHPLFILYT SGSTGKPKGV QHSTGGYLLW AAQTMKWTFD 

       310        320        330        340        350        360 
WKPTDVFWCT ADIGWVTGHS YITYGPLTLG GTQVVFEGVP TYPNAGRFWD MIQKHKVTVF 

       370        380        390        400        410        420 
YTAPTAIRSL IKAAEADPKV HPKSYDLSTL RIIGTVGEPI NPEAWVWYYE NVGGSRCPIV 

       430        440        450        460        470        480 
DTWWQTETGG HMITPLPGAT PLVPGSCTLP LPGIMAAVVD ETGQDVPNGQ GGILVVKRPW 

       490        500        510        520        530        540 
PSMIRTIWGD PERYKKSYFP EELGGTLYLA GDGSVRDKET GYFTIMGRID DVLNVSGHRL 

       550        560        570        580        590        600 
GTMEIESALV ANPLVAEAAV VGRPDDTTGE AVCAFVVLKR ARPEGEEAAK IAADLRNWVG 

       610        620        630        640        650        660 
KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEEI TQDVSTLENP AILDQLGESR 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia phymatum STM815."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Bruce D., Goodwin L., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Bacher J., Blanchard J., Cohan F., James E., Lawrence J., Lizotte-Waniewski M., Moulin L., Rainey P., Riley M., Souza V., Wertz J., Young P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001043 Genomic DNA. Translation: ACC71117.1.
RefSeqYP_001858163.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6243427.
GenomeReviewsGene locus Bphy_1938 in contig CP001043_GR.
KEGGbph:Bphy_1938.

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_BURP8
AccessionPrimary (citable) accession number: B2JD61
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: November 3, 2009
This is version 10 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