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I4ERQ3 (I4ERQ3_MODMB) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 10. 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 EMBL CCH86066.1
Ordered Locus Names:MODMU_0609 EMBL CCH86066.1
OrganismModestobacter marinus (strain BC501) [Complete proteome] [HAMAP]
Taxonomic identifier1144889 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeGeodermatophilaceaeModestobacter

Protein attributes

Sequence length654 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 SAAS025110

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

Region413 – 4186Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5201 By similarity HAMAP-Rule MF_01123
Metal binding5401Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5421Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5451Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3131Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3891Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5031Substrate By similarity HAMAP-Rule MF_01123
Binding site5181Substrate By similarity HAMAP-Rule MF_01123
Binding site5261Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5291Substrate By similarity HAMAP-Rule MF_01123
Binding site5881Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6131N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
I4ERQ3 [UniParc].

Last modified September 5, 2012. Version 1.
Checksum: 51ECCF44189295FF

FASTA65471,418
        10         20         30         40         50         60 
MSETTEAHGL TNPEGGFPPP EALAAAANVG PDVYDRAAAD RVGFWEEAAR RLDWAQPWDQ 

        70         80         90        100        110        120 
ALDWSNPPFA KWFVGGKLNV AVNCVDRHVD AGHGDQVAYH WIGEPGDTRT LTYAQLKDEV 

       130        140        150        160        170        180 
CKAANALVEL GVQAGDRVAI YLPMIPEAVV AMLACARIGA VHMVVFGGFS PDALASRITD 

       190        200        210        220        230        240 
ADAKVVITAD GGYRRGAPSA LKPNVDEALT KTEGVRSVLV VRRTETDVEW TEGRDVWWHE 

       250        260        270        280        290        300 
LVDRQPAEHE AEAFDAEHPL YIMYTSGTTA KPKGILHTTG GYLTQVSYSH WAVFDIKPDT 

       310        320        330        340        350        360 
DVFWTAADVG WVTGHSYIVY GPLSNRTTSV MYEGTPETPH RGRWWEIVQE YGVTVLYTAP 

       370        380        390        400        410        420 
TTIRTFMKWG EDVPAGFDLS SLRLLGSVGE PINPEAWLWY HTHIGGGRCP IVDTWWQTET 

       430        440        450        460        470        480 
GAHMITPLPA VTTLKPGSAQ RPLPGIAASV VDEEGKPIEP GATGYLVLTE PWPAMLRTIW 

       490        500        510        520        530        540 
GDDDRYVDTY WSRYGQGVYF AGDGAKLDED GDIWLLGRVD DVMNVSGHRI STTEVESALV 

       550        560        570        580        590        600 
SHPTVAEAAV VGATDPTTGQ GIVAFVILRG DAVDSGEDLV KTLRQHVRKE IGPIASPRQI 

       610        620        630        640        650 
MVVAELPKTR SGKIMRRLLR DVAENRELGD VTTLTDSSVM ELISSKLPSS ASED 

« Hide

References

[1]"Genome sequence of radiation-resistant Modestobacter marinus strain BC501, a representative Actinobacterium that thrives on calcareous stone surfaces."
Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L., Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A., Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.
J. Bacteriol. 194:4773-4774(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BC501 EMBL CCH86066.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FO203431 Genomic DNA. Translation: CCH86066.1.
RefSeqYP_006364565.1. NC_017955.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCH86066; CCH86066; MODMU_0609.
GeneID13007694.
KEGGmmar:MODMU_0609.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01895.

Enzyme and pathway databases

BioCycMMAR477641:GLGK-607-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
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.
ProtoNetSearch...

Entry information

Entry nameI4ERQ3_MODMB
AccessionPrimary (citable) accession number: I4ERQ3
Entry history
Integrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: February 19, 2014
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)