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A7HSR8 (ACSA_PARL1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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:Plav_1331
OrganismParvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966) [Complete proteome] [HAMAP]
Taxonomic identifier402881 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeParvibaculum

Protein attributes

Sequence length647 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 – 647647Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000073044

Sites

Active site5141 By similarity

Amino acid modifications

Modified residue6061N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7HSR8 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 43419A3302E5FBE3

FASTA64771,661
        10         20         30         40         50         60 
MSDEIFPVPA EWKKRAIVDA EKYRHMYEAS INDPESFWRR EGLRIDWMKP YTKIKDTSFD 

        70         80         90        100        110        120 
PHNVSIKWFE DGTLNASVNC IDRHLERRAG QVAIIWEGDD PSIDRKITYR ELHDEVCRFA 

       130        140        150        160        170        180 
NVLKARGVKK GDRVTIYMPM IPEAAYAMLA CARIGAVHSV VFGGFSPDSL AGRIVDCASS 

       190        200        210        220        230        240 
CVITADEGVR GGRKIPLKAN TDEALKKCPG VKSVIVVKHT GGAVAMEKGR DVWYAEEAAK 

       250        260        270        280        290        300 
VSATCAPEEM NAEDPLFILY TSGSTGKPKG VLHTTGGYMV YASMTHQYVF DYHDGDIYWC 

       310        320        330        340        350        360 
TADVGWVTGH SYILYGPLAN GATTLMFEGV PNYPDASRCW QVIDKHEVNI FYTAPTALRA 

       370        380        390        400        410        420 
LMREGEEPVK KTSRKSLRLL GSVGEPINPE AWLWYHRVVG DGRCPIVDTW WQTETGGILI 

       430        440        450        460        470        480 
SPLPGAIATK PGSATKPFFG VQPVIVDAEG NVQEGATTGN LCIDDSWPGQ MRTVYGDHQR 

       490        500        510        520        530        540 
FVETYFIQYP GRYFTGDGCR RDEDGYYWIT GRVDDVLNVS GHRMGTAEVE SALVAHPKVA 

       550        560        570        580        590        600 
EAAVVGYPHD IKGQGIYAYV TLIAGEAATE ELRKELVTWV RKEIGPIASP DLIQFAPGLP 

       610        620        630        640 
KTRSGKIMRR ILRKIAEDDF SNLGDTSTLA DPSVVTDLVD NRQNKAG 

« Hide

References

[1]"Complete genome sequence and annotation of Parvibaculum lavamentivorans DS-1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DS-1 / DSM 13023 / NCIMB 13966.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000774 Genomic DNA. Translation: ABS62951.1.
RefSeqYP_001412608.1. NC_009719.1.

3D structure databases

ProteinModelPortalA7HSR8.
SMRA7HSR8. Positions 8-643.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7HSR8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5454434.
GenomeReviewsGene locus Plav_1331 in contig CP000774_GR.
KEGGpla:Plav_1331.
PATRIC22864268. VBIParLav90819_1372.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHBG547964.
OMAGVEHEVS.

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_PARL1
AccessionPrimary (citable) accession number: A7HSR8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: September 11, 2007
Last modified: January 25, 2012
This is version 30 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