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D7BFC2 (D7BFC2_MEISD) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 22. 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:Mesil_1588 EMBL ADH63475.1
OrganismMeiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) (Thermus silvanus) [Complete proteome] [HAMAP] EMBL ADH63475.1
Taxonomic identifier526227 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeMeiothermus

Protein attributes

Sequence length651 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 SAAS SAAS020845

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

Regions

Region416 – 4216Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5231 By similarity HAMAP-Rule MF_01123
Metal binding5431Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5451Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5481Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3161Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3401Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3921Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5061Substrate By similarity HAMAP-Rule MF_01123
Binding site5211Substrate By similarity HAMAP-Rule MF_01123
Binding site5291Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5321Substrate By similarity HAMAP-Rule MF_01123
Binding site5901Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6151N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
D7BFC2 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: D8E7C2C5D25B4AF0

FASTA65172,374
        10         20         30         40         50         60 
MDQSADRIEA VLKEERVFYP SEDFKRSALL AKPEEYQALY EESLRDPEGF WGRFAGEFHW 

        70         80         90        100        110        120 
FEPWKKVLEW NVPYAKWFVG GKTNLTYNAL DRHLASRRNK AAIVFEGEPG DSRVLTYHDL 

       130        140        150        160        170        180 
HREVSKFANV LKGLGVNKGD RVTIYLPMIP EAAIAMLACA RIGAIHSVVF GGFSASALAE 

       190        200        210        220        230        240 
RINDAQSAVL VTADGGWRRG SVVPLKANAD EALASTESVR HVVVVRRVGQ EVPMLPGRDH 

       250        260        270        280        290        300 
WYHELMASAS DRCEAEPLDS EHPLFILYTS GSTGKPKGVM HTTAGYMAYV ALTARYVFDL 

       310        320        330        340        350        360 
KETDTYFCTA DVGWVTGHSY VVYGLLLNGA TTLMYEGAPN WPDEGRIWNI IDKYGVSILY 

       370        380        390        400        410        420 
TAPTAIRAFM KWGEQWPLKY RLSSLRLLGS VGEPINPEAW LWYYHVIGKG RCPIVDTWWQ 

       430        440        450        460        470        480 
TETGGIMITT LPGVHPMKPG HAGKPFFGVE PDIVDTSGKT ITGADEGGHL IIKRPWPSML 

       490        500        510        520        530        540 
RTVWGDPERY ERQYWSQYPG NYFTGDGARR DSDGYYLIMG RVDDVLNVSG HRLGTMEVES 

       550        560        570        580        590        600 
ALVSHPAVAE AAVVGRPDPI KGEGIVAFVT LKAGYTPSDA LSAELKAHVV KAIGAIARPD 

       610        620        630        640        650 
EIRFTEAMPK TRSGKIMRRL LRQIAAGESE IKGDTSTLED RSVVERLKAA Q 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002042 Genomic DNA. Translation: ADH63475.1.
RefSeqYP_003684983.1. NC_014212.1.

3D structure databases

ProteinModelPortalD7BFC2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADH63475; ADH63475; Mesil_1588.
GeneID9251092.
KEGGmsv:Mesil_1588.
PATRIC38191955. VBIMeiSil18825_1623.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000229981.
KOK01895.
OMAWVMGRVD.

Enzyme and pathway databases

BioCycMSIL526227:GJ9Q-1617-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 nameD7BFC2_MEISD
AccessionPrimary (citable) accession number: D7BFC2
Entry history
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: February 19, 2014
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)