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Q9RRL7 (ACSA_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. 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:DR_2471
OrganismDeinococcus radiodurans
Taxonomic identifier1299 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length649 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
Reference 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 – 649649Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_0000208361

Sites

Active site5231 By similarity

Amino acid modifications

Modified residue6121N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RRL7 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 044D1DE306E85137

FASTA64972,138
        10         20         30         40         50         60 
MTHPNDHIDA MLHETRVIHP SAEFQAGTRV SRAEYERRYR QSLDQPDDFW SEVAHDLHWM 

        70         80         90        100        110        120 
KDWDRVLDWQ EPHAQWFVGG QTNIAYNALD RNVQRGLGDK RAIIWEGEDG EVRTYTYAEL 

       130        140        150        160        170        180 
LREVCKAANA LEELGVVAGD RVTLYMPLIP EAAIAMLACA RIGAVHSIVF GGFSVSALAD 

       190        200        210        220        230        240 
RINNAQSKLL ITADAGYRRG KPVTLKINAD EAAKLAPCLE HVLVVKRAGI PLEWWTEGRD 

       250        260        270        280        290        300 
LWWHDVVDRQ SDQHEATALD SEHPLFILYT SGSTGAPKGV QHTTGGYMVG TYLTTQTVFD 

       310        320        330        340        350        360 
LRDDDIYWCT ADIGWITGHS YSVYGPLLNG ATVVMYEGAP NQPDWGRFWD IVQKHRVTIL 

       370        380        390        400        410        420 
YTAPTAIRSF MQHGDEIPGR YDLASLRLLG SVGEPINPEA WMWYYRVIGG ERCPVVDTWW 

       430        440        450        460        470        480 
QTETGSIMLT TLPGAFPSKP GSAGLPMFGV EPALMTRDGE EIGDDDGGLL VIKRPWPSML 

       490        500        510        520        530        540 
RTVYGDDERY RKSYWGEIPH VYFAGDGARR DHDGYYTIVG RVDDVLNVSG HRLGTMEIES 

       550        560        570        580        590        600 
ALVAHPDVSE AAVVGRPDPV KGESVVAYVL LQDGHTADPA ALRAHVSSEI GALARPDAIY 

       610        620        630        640 
IADALPKTRS GKIMRRFLRQ LAAGQPVQGD TSTLEDPTVL ERLQASPAL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000513 Genomic DNA. Translation: AAF12014.1.
PIRD75270.
RefSeqNP_296191.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RRL7.
SMRQ9RRL7. Positions 21-645.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1797778.
GenomeReviewsGene locus DR_2471 in contig AE000513_GR.
KEGGdra:DR_2471.
NMPDRfig|243230.1.peg.2650.
PATRIC21632662. VBIDeiRad64572_2707.
TIGRDR_2471.

Phylogenomic databases

HOGENOMHBG547964.
OMANDHIDAM.
PhylomeDBQ9RRL7.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycDRAD243230:DR_2471-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_DEIRA
AccessionPrimary (citable) accession number: Q9RRL7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 67 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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