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Reviewed, UniProtKB/Swiss-Prot Q056J9 (ACSA_LEPBL)

Last modified June 16, 2009. Version 18. 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: LBL_0125
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain L550) [Complete proteome] [HAMAP]
Taxonomic identifier355276 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length654 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 – 654654Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000085002

Sites

Active site5211 By similarity

Amino acid modifications

Modified residue6131N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q056J9-1 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 2A51CC717429B00A

FASTA65473,402
        10         20         30         40         50         60 
MAKERIVLPS AEFKKNSNIT LKDYKSLYKE SIENPNKFWA KEANRLTWFK KWTKVLNHDF 

        70         80         90        100        110        120 
KNAKVEWFKG GKLNVSYNCL DRHISTPLKN KAALIWEGDN PSESKVLTYY DVYREVNRFA 

       130        140        150        160        170        180 
NVLKKYGVKK GDRVLVYLPM IPELAITILA CTRIGAIHSV VFGGFSPEAL QSRIDDCKPK 

       190        200        210        220        230        240 
LIVTADGGFR GGKPIELKRN VDIALEKSKE DVKTVIVVRR TGNESGLVWK DGRDYWYHFL 

       250        260        270        280        290        300 
ISDPDLSPYC KPESMDAEDP LFILYTSGST GKPKGVLHTT GGYLLGVNLT FHYVFDIKPE 

       310        320        330        340        350        360 
DTYWCTADIG WVTGHSYLVY GPLSNGASSV MFEGVPSYPD AGRFWDVIDK YGVNIFYTAP 

       370        380        390        400        410        420 
TAIRALMREG LTHVQKRNLS SLRLLGSVGE PINPEAWEWY FKIIGKEKCP IVDTWWQTET 

       430        440        450        460        470        480 
GSIMITALPG AIPQKPGSAT LPFFGVQPVL VDNDGKEIND KGEVSGNLCI KSPWPSMMRG 

       490        500        510        520        530        540 
VYGDSKRFFD TYFSQFKGYY FTGDGARRDK DGYYWITGRV DDVINVSGHR IGSAEVESAL 

       550        560        570        580        590        600 
VENRSVAEAA VVGFPHDIKG QGIYAYVTVK EGIATNDTLK KELVAIVEKV IGKIARPDVI 

       610        620        630        640        650 
HWAPSLPKTR SGKIMRRILR KIASGEFEGL GDTSTLADPS VVQKLIEDKR KFHS 

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed: 16973745] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000348 Genomic DNA. Translation: ABJ77746.1.
RefSeqYP_796679.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4408535.
GenomeReviewsGene locus LBL_0125 in contig CP000348_GR.
KEGGlbl:LBL_0125.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAQ056J9. TGGYNLY.

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_LEPBL
AccessionPrimary (citable) accession number: Q056J9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 14, 2006
Last modified: June 16, 2009
This is version 18 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