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Reviewed, UniProtKB/Swiss-Prot Q17WR1 (ACSA_HELAH)

Last modified November 3, 2009. Version 25. 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: Hac_1156
OrganismHelicobacter acinonychis (strain Sheeba) [Complete proteome] [HAMAP]
Taxonomic identifier382638 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length662 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 – 662662Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000065292

Sites

Active site5271 By similarity

Amino acid modifications

Modified residue6231N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q17WR1-1 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 84B19724456B64F0

FASTA66274,921
        10         20         30         40         50         60 
MQLDDDLEFA KKIFNPNRAF AKQARIKNMC EYKDLVHEAN ENYENFWGEL AKQKLTWFKP 

        70         80         90        100        110        120 
FDKVLNSDNA PFFKWFENGK INVSYNCIDR HLKDKKNKVA IIFEGEMGDY NAITYRKLHS 

       130        140        150        160        170        180 
EVNKTANLLK NEFNIKKGDR VIIYMPMIAE SVYMMLACTR IGAIHSIVFA GFSPEALRDR 

       190        200        210        220        230        240 
INDAQAKLVI TADGTFRKGK PYMLKPALDK ALANNTCPSV EKTLIVIRNA KEIDYVRGRD 

       250        260        270        280        290        300 
FVYNEMVNYQ SDKCEPEMMD SEDPLFLLYT SGSTGKPKGV QHSSAGYLLW AQMTMEWVFD 

       310        320        330        340        350        360 
IRDNDNFWCT ADIGWITGHT YVVYGPLACG ATTLILEGTM SYPDYGRWWR MIEEYRVDKF 

       370        380        390        400        410        420 
YTSPTAIRML HAKGENEPSK YNLDSLKVLG TVGEPINPTA WKWFYEKIGN SQCSIVDTWW 

       430        440        450        460        470        480 
QTETGGHIIS PLPGATPIRA SCATLPLPGI HAEVLNEDGS KTKPGEQGFL CITKPWPSMI 

       490        500        510        520        530        540 
RNIWGDEKRY IDSYFSQIQL NGEYVYLSGD GAIVDENGYI TIIGRTDDIV NVSGHRIGTA 

       550        560        570        580        590        600 
EVESAISKHE MVVECAVVGI PDTIKGEGLF AFVVLCDGAK CNLGESLELL KEMNHILAVE 

       610        620        630        640        650        660 
IGKIAKLDNV MYVPGLPKTR SGKIMRRILK SIVKKEPITQ DLSTLEDVNV VKEIINIAQM 


EE 

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References

[1]"Who ate whom? Adaptive Helicobacter genomic changes that accompanied a host jump from early humans to large felines."
Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., Gressmann H., Achtman M., Schuster S.C.
PLoS Genet. 2:1097-1110(2006) [PubMed: 16789826] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM260522 Genomic DNA. Translation: CAJ99915.1.
RefSeqYP_664914.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ17WR1.

Genome annotation databases

GeneID4177696.
GenomeReviewsGene locus Hac_1156 in contig AM260522_GR.
KEGGhac:Hac_1156.
NMPDRfig|382638.8.peg.1123.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ17WR1.
OMATGGYNLY.

Enzyme and pathway databases

BioCycHACI382638:HAC_1156-MON.

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_HELAH
AccessionPrimary (citable) accession number: Q17WR1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 25, 2006
Last modified: November 3, 2009
This is version 25 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