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A1W1D6 (ACSA_CAMJJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. 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:CJJ81176_1522
OrganismCampylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) [Complete proteome] [HAMAP]
Taxonomic identifier354242 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length657 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 – 657657Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000065287

Sites

Active site5211 By similarity

Amino acid modifications

Modified residue6171N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1W1D6 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: F1E77BA491B3D0F5

FASTA65773,958
        10         20         30         40         50         60 
MLNQNNQELF KPSKEFSRNA RIKNLCEYYD LCDEAKEDFE GFWKRQAFEK 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 
IRMLHADAPN 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 VVSILDTIKG ESLFAFVVLS PASSCDLGGA IETLKELNDI LRVEIGPIAK 

       610        620        630        640        650 
IEKILYTPGL PKTRSGKIMR RILRTIARGE EIKQDISTLE DSKVVETIVK LAKAEFE

« Hide

References

[1]Fouts D.E., Nelson K.E., Sebastian Y.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 81-176.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000538 Genomic DNA. Translation: EAQ72526.1.
RefSeqYP_001001177.1. NC_008787.1.

3D structure databases

ProteinModelPortalA1W1D6.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1W1D6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4682781.
GenomeReviewsGene locus CJJ81176_1522 in contig CP000538_GR.
KEGGcjj:CJJ81176_1522.
PATRIC20053022. VBICamJej103413_1518.
TIGRCJJ81176_1522.

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHBG547964.
OMAKGKPYML.
PhylomeDBA1W1D6.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycCJEJ354242:CJJ81176_1522-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_CAMJJ
AccessionPrimary (citable) accession number: A1W1D6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 36 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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