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I4CUB2 (I4CUB2_PSEST) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 7. 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
ORF Names:A458_12170 EMBL AFM33669.1
OrganismPseudomonas stutzeri CCUG 29243 EMBL AFM33669.1
Taxonomic identifier1196835 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

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

Region411 – 4166Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5171 By similarity HAMAP-Rule MF_01123
Metal binding5371Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5391Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5421Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3111Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3351Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3871Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5001Substrate By similarity HAMAP-Rule MF_01123
Binding site5151Substrate By similarity HAMAP-Rule MF_01123
Binding site5231Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5261Substrate By similarity HAMAP-Rule MF_01123
Binding site5841Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6091N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
I4CUB2 [UniParc].

Last modified September 5, 2012. Version 1.
Checksum: D85BB766C8B3B657

FASTA65171,716
        10         20         30         40         50         60 
MSAASVYPVR PEVAAQSLTN EASYKAMYQQ SVINPEGFWR EQAARLNWIR PFTEVKRTSF 

        70         80         90        100        110        120 
DDHHVDIKWF ADGTLNVSAN CLDRHLAERG DQLAIIWEGD DPSEHREITY RELHQEVSKF 

       130        140        150        160        170        180 
ANALRGQDVH RGDVVTIYMP MIPEAAVAML ACARIGAIHS VVFGGFSPEA LAGRIIDGQS 

       190        200        210        220        230        240 
KIVITADEGV RGGKPVPLKG NVDEALTNPQ TSCVKKIIVV RRTGADIRWH SHRDICYDDL 

       250        260        270        280        290        300 
MRVAGEVCAP KEMGAEEPLF ILYTSGSTGK PKGVLHTCGG YLLYAALTHE RVFDYRPGEV 

       310        320        330        340        350        360 
YWCTADIGWI TGHSYLIYGP LANGATTLMY EGVPNHPDVT RIARIIDKHK VNILYTAPTA 

       370        380        390        400        410        420 
IRAMMAEGAA AVEGADGSSL RLLGTVGEPI NPEAWHWYYE TVGQSRCPIV DTWWQTETGG 

       430        440        450        460        470        480 
ILISPLPGAT TLKPGSATRP MFGVVPGLVD NLGNLLEGPA EGNLVILDSW PGQMRTIYKD 

       490        500        510        520        530        540 
HDRFVDTYFK TFRGMYFTGD GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESAMVAHA 

       550        560        570        580        590        600 
KVAEAAAVGV PHKLKGQAIY VYVTLVSGVQ PSDALRQELQ QWVRKEIGPI AVPDVIQWAP 

       610        620        630        640        650 
GLPKTRSGKI MRRLLRKIAT DDYDALGDTS TLADPGVVDQ LIEAHEAVRK R

« Hide

References

[1]"Complete Genome Sequence of the Naphthalene-Degrading Bacterium Pseudomonas stutzeri AN10 (CCUG 29243)."
Brunet-Galmes I., Busquets A., Pena A., Gomila M., Nogales B., Garcia-Valdes E., Lalucat J., Bennasar A., Bosch R.
J. Bacteriol. 194:6642-6643(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: CCUG 29243 EMBL AFM33669.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP003677 Genomic DNA. Translation: AFM33669.1.
RefSeqYP_006458092.1. NC_018028.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFM33669; AFM33669; A458_12170.
GeneID13145759.
KEGGpsc:A458_12170.

Phylogenomic databases

KOK01895.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR024597. Acyl-CoA_synth_DUF3448.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR025110. DUF4009.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF11930. DUF3448. 1 hit.
PF13193. DUF4009. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameI4CUB2_PSEST
AccessionPrimary (citable) accession number: I4CUB2
Entry history
Integrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: April 3, 2013
This is version 7 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info