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C6BJD4 (C6BJD4_RALP1) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123

Short name=AcCoA synthetase HAMAP-Rule MF_01123
Short name=Acs HAMAP-Rule MF_01123
EC=6.2.1.1 HAMAP-Rule MF_01123
Alternative name(s):
Acetate--CoA ligase HAMAP-Rule MF_01123
Acyl-activating enzyme HAMAP-Rule MF_01123
Gene names
Name:acsA HAMAP-Rule MF_01123
Ordered Locus Names:Rpic12D_1775 EMBL ACS63057.1
OrganismRalstonia pickettii (strain 12D) [Complete proteome] [HAMAP] EMBL ACS63057.1
Taxonomic identifier428406 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA By similarity. HAMAP-Rule MF_01123

Catalytic activity

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01123

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family. HAMAP-Rule MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site5301 By similarity HAMAP-Rule MF_01123
Metal binding5501Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5551Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3171Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3971Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5121Substrate By similarity HAMAP-Rule MF_01123
Binding site5281Substrate By similarity HAMAP-Rule MF_01123
Binding site5361Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5391Substrate By similarity HAMAP-Rule MF_01123
Binding site6001Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6251N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
C6BJD4 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 5656BD9158B10654

FASTA66072,595
        10         20         30         40         50         60 
MAGIESVLQE TRVFNPPESF VKQANIAGMD AYRALCAEAE KDYEGFWARL AHEHLLWHKP 

        70         80         90        100        110        120 
FSKVLDESNA PFYKWFEDGE LNASYNCLER NLENGNADKV AIIFETDDGN VSRITYRELH 

       130        140        150        160        170        180 
ARVCRFANGL KALGIKKGDR VVIYMPMSVE GIVAMQACAR IGATHSVVFG GFSAKSLQER 

       190        200        210        220        230        240 
IVDVGAVALI TADEQMRGGK ALPLKAIADE ALAMEGTGAV KHVIVYRRTN GNVNWVEGRD 

       250        260        270        280        290        300 
RAMDEVEAGQ PDTCEVTPVS AEHPLFILYT SGSTGKPKGV QHSTGGYLLW ALLTMQWTFD 

       310        320        330        340        350        360 
LKPDDIFWCT ADIGWVTGHS YIAYGPLAAG ATQVVFEGVP TYPNAGRFWD MIQRHKVNTF 

       370        380        390        400        410        420 
YTAPTAIRSL IKAAEADEKV HPKQYDLSSL RLLGTVGEPI NPEAWMWYHT NIGGGRCPIV 

       430        440        450        460        470        480 
DTFWQTETGG HMMTPLPGAT PLVPGSCTLP LPGIMAAVVD ETGHDVPNGQ GGILVVKRPW 

       490        500        510        520        530        540 
PSMIRTIWGD PERFKKSYFP EELGGKLYLA GDGSIRDKET GYFTIMGRID DVLNVSGHRM 

       550        560        570        580        590        600 
GTMEIESALV ANPIVAEAAV VGRPDDMTGE AICAFVVLKR ARPDGDEAKQ IANELRNWVG 

       610        620        630        640        650        660 
KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEDI TQDTSTLENP AILDQLKETR 

« Hide

References

[1]"Complete sequence chromosome 1 of Ralstonia pickettii 12D."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ovchinnikova G., Marsh T., Richardson P.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 12D EMBL ACS63057.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001644 Genomic DNA. Translation: ACS63057.1.
RefSeqYP_002981729.1. NC_012856.1.

3D structure databases

ProteinModelPortalC6BJD4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING428406.Rpic12D_1775.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS63057; ACS63057; Rpic12D_1775.
GeneID8019431.
KEGGrpf:Rpic12D_1775.
PATRIC20242597. VBIRalPic57998_2388.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAGGCEAVT.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycRPIC428406:GH9Y-1808-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC6BJD4_RALP1
AccessionPrimary (citable) accession number: C6BJD4
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: June 11, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)