Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q6G1W0 (ACSA_BARHE)

Last modified February 9, 2010. Version 34. 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: BH15410
OrganismBartonella henselae (Rochalimaea henselae) [Complete proteome] [HAMAP]
Taxonomic identifier38323 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length652 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)
   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 – 652652Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000065270

Sites

Active site5171 By similarity

Amino acid modifications

Modified residue6091N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6G1W0-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 9091B62C2E782DFD

FASTA65273,577
        10         20         30         40         50         60 
MSEKIYPIPD NIKKNALIDE ETYQQWYQES INDPESFWAK HGQCIEWFKP YTKVKNTSFN 

        70         80         90        100        110        120 
GDVSIQWYED GITNVAYNCI DRHLKTHGDK IALIWEGDNP YHDKKITYNE LYEHVCRFAN 

       130        140        150        160        170        180 
ILKNHGVKKG DKVTIYLTMI PEAAYAMLAC ARIGAIHSVI FAGFSPEAIA GRIVDCESTF 

       190        200        210        220        230        240 
IITANQGLRG GKQINLKDSV DHAIEIAARQ NVHVDQVMVI RRTCGPIHWV EGRDFWYHEE 

       250        260        270        280        290        300 
VSHTKTDCPA EKMNAEDPLF ILYTSGSTGK PKGVLHTTAG YLVYASMTHK YVFDYHAGEI 

       310        320        330        340        350        360 
YWCTADIGWI TGHSYLVYGP LCNAATTLMF EGTPTFPDNG RFWEIVDKHQ VNIFYTAPTA 

       370        380        390        400        410        420 
IRALMGAGNS FVERSKRTSL RLLGSVGEPI NPEAWEWFYH TVGNNHCPIL DTWWQTETGG 

       430        440        450        460        470        480 
HMITPLPGAT PLKAGSATRP FFGVQLQIID AEGNVLEGET EGNLCIIDSW PGQMRTLYND 

       490        500        510        520        530        540 
HERFIQTYFS TYKGKYFTGD GCRRDSDGYY WITGRVDDIL NVSGHRLGTA EIESALVSHP 

       550        560        570        580        590        600 
AVSEAAVVGY PHTIKGQGIY SFITLMEGTA PSEELHQELI RHVRKEIGSI AILDKVQFAP 

       610        620        630        640        650 
QLPKTRSGKI MRRILRKIAE NNFDNLGDIS TLSEPQVIDD LIANRQNREI TA 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49882 / Houston 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897699 Genomic DNA. Translation: CAF28304.1.
RefSeqYP_034237.1.

3D structure databases

HSSPHSSP built from PDB template 1PG4 based on UniProtKB Q8ZKF6.
SMRQ6G1W0. Positions 6-646.
ModBaseSearch...

Genome annotation databases

GeneID2866062.
GenomeReviewsGene locus BH15410 in contig BX897699_GR.
KEGGbhe:BH15410.
NMPDRfig|283166.1.peg.1365.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG547964.
OMATRVKNTS.
PhylomeDBQ6G1W0.

Enzyme and pathway databases

BioCycBHEN283166:BH15410-MONOMER.
BRENDA6.2.1.1. 277357.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
[Tree]
InterProIPR011904. Ac_CoA_lig_AcsA.
IPR020845. AMP-binding_CS.
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_BARHE
AccessionPrimary (citable) accession number: Q6G1W0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 19, 2004
Last modified: February 9, 2010
This is version 34 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