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A1WY97 (ACSA_HALHL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:Hhal_1895
OrganismHalorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1)) [Complete proteome] [HAMAP]
Taxonomic identifier349124 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeHalorhodospira

Protein attributes

Sequence length645 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 – 645645Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000065291

Sites

Active site5141 By similarity

Amino acid modifications

Modified residue6061N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1WY97 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: A49FA72EB504C8DC

FASTA64571,771
        10         20         30         40         50         60 
MSETKVYPVP ETIQRDAHLN FEQYQEMYNR SIQDPEGFWS EQADKFLDWF SKWGTTCHWD 

        70         80         90        100        110        120 
LAKGDIRFFE GGTLNVAYNC VDRHLETRGD QTAIIWEGDE PDQDEHITYR DLYERVGRLA 

       130        140        150        160        170        180 
NALKARGVKK GDRVCIYLPM VPEAAVAMLA CARIGAVHSI VFGGFSPEAL RDRIQDADAE 

       190        200        210        220        230        240 
VVITSDEGVR GGRSIPLKAN TDKALEGCPN VKTVFVVRRT GGDIAWNDGR DVWFHEACAE 

       250        260        270        280        290        300 
ASPDCPPEHM DAEDPLFILY TSGSTGKPKG VQHSTAGYLL GTAMTHKYIF DYQDGEVYWC 

       310        320        330        340        350        360 
TADVGWVTGH SYIVYGPLAN GAKTLMFEGV PTYPDAGRFW QVVDKHEVSI FYTAPTAIRA 

       370        380        390        400        410        420 
LMGQGDDHVK KTSRKSLRIL GTVGEPINPE AWEWYYHTIG EDRCPIVDTW WQTETGSILI 

       430        440        450        460        470        480 
APLPGAMDLK PGSATLPFFG VEPQLVDDKG NVLEGATNGN LVINRAWPSM MRTIYGDHER 

       490        500        510        520        530        540 
FFNTYLAAYP GKYFTGDGAR RDEDGYYWIT GRVDDVINVS GHRMGTAEVE SALVLHDKVS 

       550        560        570        580        590        600 
EAAVVGYPHD VKGQGIYAYV TLMAGEEPSD ELKQELVKLC IQEIGPIAKP DIIQFAPGLP 

       610        620        630        640 
KTRSGKIMRR ILRKVASNEL DSLGDTSTLA DPTVVDTLIE DRANQ 

« Hide

References

[1]"Complete sequence of Halorhodospira halophila SL1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 244 / SL1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000544 Genomic DNA. Translation: ABM62659.1.
RefSeqYP_001003461.1. NC_008789.1.

3D structure databases

ProteinModelPortalA1WY97.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1WY97.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4710685.
GenomeReviewsGene locus Hhal_1895 in contig CP000544_GR.
KEGGhha:Hhal_1895.
PATRIC22098083. VBIHalHal112047_1869.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHBG547964.
OMADGFYWIL.
PhylomeDBA1WY97.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycHHAL349124:HHAL_1895-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_HALHL
AccessionPrimary (citable) accession number: A1WY97
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 33 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