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K0CWU1 (K0CWU1_ALTME) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 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
Ordered Locus Names:AMEC673_16675 EMBL AFT76017.1
OrganismAlteromonas macleodii (strain English Channel 673) [Complete proteome] [HAMAP] EMBL AFT76017.1
Taxonomic identifier1004788 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

Protein attributes

Sequence length648 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 SAAS011904

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

Region191 – 1944Coenzyme A By similarity HAMAP-Rule MF_01123
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 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
K0CWU1 [UniParc].

Last modified November 28, 2012. Version 1.
Checksum: B044EA01F57280B0

FASTA64871,668
        10         20         30         40         50         60 
MTASKTYPVP ENILQSTHLT ASQYDEMYKQ SVEQPEAFWA EHASMLEWYQ KPTKIKNTMF 

        70         80         90        100        110        120 
GENDVSIKWF EDGELNASYN CIDRHLADNA TKVAFHWEGD SPEDSQDITY QQVHYEVCKL 

       130        140        150        160        170        180 
ANALKEMGVA KGDRVAIYMP MVPEAAYAML ACARIGAVHS VIFGGFSPNA IADRINDSNA 

       190        200        210        220        230        240 
KVVITADEGR RAGRSIPLKA NVDKALAGDA CPSITHVLVH KLTGGDVDWN AKHDVWWHDA 

       250        260        270        280        290        300 
VDGVSAQCEP EVMNAEDPLF ILYTSGSTGT PKGVVHTTGG YLLYSAMTFK YAFDYKEDDV 

       310        320        330        340        350        360 
YWCTADVGWI TGHSYMVYGP MVNAASQVFF EGVPTYPDVK RIAQVVEKYK VNSLYTAPTA 

       370        380        390        400        410        420 
IRALMAHGDV PTEGCDVSSL RLLGTVGEPI NPEAWEWYHR VIGMSRCPII DTWWQTETGG 

       430        440        450        460        470        480 
HMILPLPGAT ELKPGSATRP FFGIQPALFD ADGNELEGAA EGNLVIKDSW PSQARTVYGD 

       490        500        510        520        530        540 
HQRFINTYFS AYKGVYFTGD GARCDEDGFY WITGRVDDVL NVSGHRLGTA EIESALVAHP 

       550        560        570        580        590        600 
KVAEAAVVGF PHDIKGQGIY VYVTPNEGVE ANEALTKELK AWVRQELSPI ATPDMIQWSR 

       610        620        630        640 
GLPKTRSGKI MRRILRKIAA NEHEQLGDTS TLADPSVVDT LIEERLNK 

« Hide

References

[1]"Genomes of surface isolates of Alteromonas macleodii: the life of a widespread marine opportunistic copiotroph."
Lopez-Perez M., Gonzaga A., Martin-Cuadrado A.B., Onyshchenko O., Ghavidel A., Ghai R., Rodriguez-Valera F.
Sci. Rep. 2:696-696(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: English Channel 673.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003844 Genomic DNA. Translation: AFT76017.1.
RefSeqYP_006800394.1. NC_018678.1.

3D structure databases

ProteinModelPortalK0CWU1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFT76017; AFT76017; AMEC673_16675.
GeneID13741805.
KEGGamg:AMEC673_16675.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01895.
OMADISWING.

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 nameK0CWU1_ALTME
AccessionPrimary (citable) accession number: K0CWU1
Entry history
Integrated into UniProtKB/TrEMBL: November 28, 2012
Last sequence update: November 28, 2012
Last modified: June 11, 2014
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)