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Q62AD1 (ACSA_BURMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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:BMAA1794
OrganismBurkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP]
Taxonomic identifier13373 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length660 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 – 660660Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000065279

Sites

Active site5301 By similarity

Amino acid modifications

Modified residue6251N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q62AD1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: B067B10A94777DF9

FASTA66072,282
        10         20         30         40         50         60 
MSAIESVLHE RRQFAPPAAV EKAAAISGMA AYRALAEEAE RDYEGFWARL ARETLEWRKP 

        70         80         90        100        110        120 
FGKVLDETNA PFYKWFEDGE LNASYNCLDR HVAAGLGERV AVIFEADDGT VTRVTYADLL 

       130        140        150        160        170        180 
ARVSRFANAL KKRGVGRGDR VVIYIPMSVE GIVAMQACAR IGATHSVVFG GFSSKSLHER 

       190        200        210        220        230        240 
IVDVGATALV TADEQMRGGK TLPLKSIADE ALAMGGCDAV KTVVVYRRTG GNVDWHAGRD 

       250        260        270        280        290        300 
VWMHEMVANE SDACEPEWVG AEHPLFILYT SGSTGKPKGV QHSTAGYLLW VAQTMKWTFD 

       310        320        330        340        350        360 
WKPDDVFWCT ADIGWVTGHS YITYGPLAVG ATQVVFEGVP TYPNAGRFWK MIGDHKVTVF 

       370        380        390        400        410        420 
YTAPTAIRSL IKAAEADDRV HPRSYDLSSL RIIGTVGEPI NPEAWIWYHK NVGQARCPIV 

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

       490        500        510        520        530        540 
PAMARTIWGD PERFKKSYFP EELGGRLYLA GDGTVRDKET GYFTIMGRID DVLNVSGHRL 

       550        560        570        580        590        600 
GTMEIESALV SHELVAEAAV VGRPDDTTGE AVVAFVVLKR SRPEGEEAAA LAKTLRDWVG 

       610        620        630        640        650        660 
KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEAI TQDTSTLENP AILEQLAEVR

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000011 Genomic DNA. Translation: AAU45843.1.
RefSeqYP_106348.1. NC_006349.2.

3D structure databases

HSSPHSSP built from PDB template 1RY2 based on UniProtKB Q01574.
ProteinModelPortalQ62AD1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3087408.
GenomeReviewsGene locus BMAA1794 in contig CP000011_GR.
KEGGbma:BMAA1794.
PATRIC19125824. VBIBurMal55007_5392.
TIGRBMAA1794.

Phylogenomic databases

HOGENOMHBG547964.
OMATRGTEES.
PhylomeDBQ62AD1.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycBMAL243160:BMA_A1794-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_BURMA
AccessionPrimary (citable) accession number: Q62AD1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 42 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

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