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A3PBZ3 (A3PBZ3_PROM0) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 51. 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:acs EMBL ABO17268.1
Synonyms:acsA HAMAP-Rule MF_01123
Ordered Locus Names:P9301_06451 EMBL ABO17268.1
OrganismProchlorococcus marinus (strain MIT 9301) [Complete proteome] [HAMAP] EMBL ABO17268.1
Taxonomic identifier167546 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

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

Regions

Region422 – 4276Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5331 By similarity HAMAP-Rule MF_01123
Metal binding5531Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5551Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5581Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3221Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3981Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5161Substrate By similarity HAMAP-Rule MF_01123
Binding site5311Substrate By similarity HAMAP-Rule MF_01123
Binding site5391Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5421Substrate 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
A3PBZ3 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 8EC977BFDFF2C40D

FASTA66074,035
        10         20         30         40         50         60 
MTLDKKNSIN NILEEKRIFP PSKKFAENSN ISTQEELLSL KKQASDNPIQ FWESFAKSEL 

        70         80         90        100        110        120 
DWFEPFQTVL DNENAPFFKW FKEGKLNITY NCLDRHIKRG LGGKTALIWE GEPGDSKKYT 

       130        140        150        160        170        180 
YEELLKEVCR AANALKAIGV KKGDLVCIYM PMIPEAMFAM LACARIGAPH SVVFGGFSSE 

       190        200        210        220        230        240 
ALKDRLIDGN ARYVITADGG FRKDKVIELK QAVDAAIENG ADKVVEKVVV VQRTKKNISM 

       250        260        270        280        290        300 
VDDRDLWWHE LVKDQKDQCE PEIMSSEDRL FILYTSGSTG KPKGVVHTTG GYNLWSHLTF 

       310        320        330        340        350        360 
KWIFDLKDDD IYWCTADVGW ITGHSYIVYG PLSNGATTLM YEGVPRRSNL GAFWEIVQKY 

       370        380        390        400        410        420 
KVSIFYTAPT AIRAFMKSGR EIPDKYNLES LRLLGTVGEP INPEAWMWYK DVIGKDKCPI 

       430        440        450        460        470        480 
VDTWWQTETG GVMISPLPGV VATKPGSATF PLPGIEVEIV DKDGDKVKEN EGGYLIIKKP 

       490        500        510        520        530        540 
WPGMMRTIHG NSKRYLESYW EYISFKGEKN VYFAGDGARI DEDGYIWIMG RVDDVISVSG 

       550        560        570        580        590        600 
HRLGTMEIES ALVSHKSVAE SAVVGKKDDL KGEVIVAFVS LEKDVNGSSE LVEDLKKHVV 

       610        620        630        640        650        660 
NEIGIIAKPE KIIISDSLPK TRSGKIMRRI LRSLAGGEKI SGDISTLEDS SVLEKLKELS 

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References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9301 EMBL ABO17268.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000576 Genomic DNA. Translation: ABO17268.1.
RefSeqYP_001090869.1. NC_009091.1.

3D structure databases

ProteinModelPortalA3PBZ3.
SMRA3PBZ3. Positions 21-658.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167546.P9301_06451.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO17268; ABO17268; P9301_06451.
GeneID4911088.
KEGGpmg:P9301_06451.
PATRIC22994885. VBIProMar103344_0631.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAWVMGRVD.
OrthoDBEOG68WR2H.
ProtClustDBCLSK921911.

Enzyme and pathway databases

BioCycPMAR167546:GH1Y-665-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 nameA3PBZ3_PROM0
AccessionPrimary (citable) accession number: A3PBZ3
Entry history
Integrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: February 19, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)