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Reviewed, UniProtKB/Swiss-Prot A8FNJ7 (ACSA_CAMJ8)

Last modified November 3, 2009. Version 16. 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: C8J_1436
OrganismCampylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828) [Complete proteome] [HAMAP]
Taxonomic identifier407148 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length657 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 – 657657Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000073043

Sites

Active site5211 By similarity

Amino acid modifications

Modified residue6171N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8FNJ7-1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 5F0EB3B36C18B459

FASTA65773,824
        10         20         30         40         50         60 
MLNQNNQELF KPSKEFSRNA RIKNLCEYYD LCDEAKEDFE GFWKRQALEK IEWFSPFSRV 

        70         80         90        100        110        120 
LNEDKAPFYK WFEGGTLNVS YQCLDRHMKT RRNKAALIFE GEMGDYEVYT YRRLLHETCK 

       130        140        150        160        170        180 
AANLLKKFGV KKGDRVVIYM PMIPETAIVM LACARIGAIH SVVFGGFSPE ALRDRIIDAG 

       190        200        210        220        230        240 
AKLVVTADGA FRRGKPYMLK PAVDKALSEG CESVEKVLIV IRNNEPIEYI KGRDYVYNEL 

       250        260        270        280        290        300 
VKNESYKCEP EIMDSEDLLF LLYTSGSTGK PKGVMHASAG YILWAQMTME WVFDIKDYDN 

       310        320        330        340        350        360 
YWCSADVGWI TGHTYVVYGP LACGATTIMH EGTPTYPNSG RWWRMIEEYQ ISKFYTSPTA 

       370        380        390        400        410        420 
IRMLHADAPD EPRKYDLSTL EVLGTVGEPI NPSAWKWFYD EIGGTKSPIV DTWWQTETGG 

       430        440        450        460        470        480 
HMITPLPGAT PLKPGCATLP LPGIFAEVID EEGNKKDEGE DGLLCITKPW PSMIRGIWGN 

       490        500        510        520        530        540 
DERYIESYFS QAKKDGKAVY FSGDGAFYDK NGYITITGRT DDVVNVAGHR IGTAEIESAI 

       550        560        570        580        590        600 
AKHPSVAESA VVSILDAIKG ESLFAFVVLS PASSCDLGGA IETLKELNDI LRVEIGPIAK 

       610        620        630        640        650 
IEKILYTPGL PKTRSGKIMR RILRTIARGE EIKQDISTLE DSGVVETIVK LAKAEFE 

« Hide

References

[1]"The complete genome sequence of Campylobacter jejuni strain 81116 (NCTC11828)."
Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M., van Vliet A.H.M.
J. Bacteriol. 189:8402-8403(2007) [PubMed: 17873037] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000814 Genomic DNA. Translation: ABV53034.1.
RefSeqYP_001483011.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA8FNJ7.

Genome annotation databases

GeneID5618493.
GenomeReviewsGene locus C8J_1436 in contig CP000814_GR.
KEGGcju:C8J_1436.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMATGGYNLY.

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_CAMJ8
AccessionPrimary (citable) accession number: A8FNJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: November 13, 2007
Last modified: November 3, 2009
This is version 16 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