Skip Header

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

Reviewed, UniProtKB/Swiss-Prot Q9KWA3 (ACSA_AGRRH)

Last modified June 16, 2009. Version 40. 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
ORF Names: riorf81
Encoded onPlasmid pRi1724
OrganismAgrobacterium rhizogenes
Taxonomic identifier359 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium

Protein attributes

Sequence length652 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 termPlasmid
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_0000208351

Sites

Active site5171 By similarity

Amino acid modifications

Modified residue6091N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KWA3-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 5B97DF7EAB99A8FB

FASTA65271,992
        10         20         30         40         50         60 
MSEKIYPVAK PVESHALINK AEYQEWYAES VADPEQFWGK HGKRIDWFKP YTSVKDTSFT 

        70         80         90        100        110        120 
GDVSIKWFED GETNVSYNCI DRHLATNGDQ VAIIWEGDDP SLDRKITYRE LYEHVCRMAN 

       130        140        150        160        170        180 
VLKKHGVKKG DRVTIYMPMV PEAAYAMLAC ARIGAIHSVV FGGFSPEALG GRIVDCQSTF 

       190        200        210        220        230        240 
VITCDEGLRG GKPVPLKANV DKAIDIAARG HVMVKNVLVI RRTGSPLSWA PGRDLWHHEE 

       250        260        270        280        290        300 
AATVSADCPP EPMKAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASMTHE YVFDYQHGDI 

       310        320        330        340        350        360 
YWCTADVGWV TGHSYIVYGP LANCATTLMF EGIPTFPDAG RFWDVIDKHK VNIFYTAPTA 

       370        380        390        400        410        420 
IRSLMGAGDD FVKRSSRSSL RLLGSVGEPI NPEAWEWYYH TVGDGRCPVV DTWWQTETGG 

       430        440        450        460        470        480 
IMITPLPGAT DLKPGSATRP FFGIRPELVD AEGKLIEGAA DGNLCIADSW PGQARSVYGD 

       490        500        510        520        530        540 
HERFIQTYFS TYEGKYFTGD GCRRDADGYY WITGRVDDVL NVSGHRLGTA EVESALVSHH 

       550        560        570        580        590        600 
LVSEAAVVGY PHNIKGQGIY CYVTLMAGSE GSEELRQQLV KHVRAEIGPI ASPDKIQFAP 

       610        620        630        640        650 
GLPKTRSGKI MRRILRKIAE DDFGSLGDTS TLADPAVVDD LIANRQNRAE AA 

« Hide

References

[1]"Analysis of unique variable region of a plant root inducing plasmid, pRi1724, by the construction of its physical map and library."
Moriguchi K., Maeda Y., Satou M., Kataoka M., Tanaka N., Yoshida K.
DNA Res. 7:157-163(2000) [PubMed: 10907845] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MAFF03-01724.
[2]"The complete nucleotide sequence of a plant root-inducing (Ri) plasmid indicates its chimeric structure and evolutionary relationship between tumor-inducing (Ti) and symbiotic (Sym) plasmids in Rhizobiaceae."
Moriguchi K., Maeda Y., Satou M., Hardayani N.S.N., Kataoka M., Tanaka N., Yoshida K.
J. Mol. Biol. 307:771-784(2001) [PubMed: 11273700] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MAFF03-01724.

Cross-references

Sequence databases

AB039932 Genomic DNA. Translation: BAA97792.1.
AP002086 Genomic DNA. Translation: BAB16200.1.
RefSeqNP_066662.1.

3D structure databases

HSSPHSSP built from PDB template 1PG4 based on UniProtKB Q8ZKF6.
ModBaseSearch...

Genome annotation databases

GeneID874783.

Enzyme and pathway databases

BRENDA6.2.1.1. 2198.

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_AGRRH
AccessionPrimary (citable) accession number: Q9KWA3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 40 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