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A8G3Y5 (A8G3Y5_PROM2) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 47. 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 ABV50316.1
Synonyms:acsA HAMAP-Rule MF_01123
Ordered Locus Names:P9215_07011 EMBL ABV50316.1
OrganismProchlorococcus marinus (strain MIT 9215) [Complete proteome] [HAMAP] EMBL ABV50316.1
Taxonomic identifier93060 [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
A8G3Y5 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 00F0F96C4E7DDEEB

FASTA66074,061
        10         20         30         40         50         60 
MSLDKKNSIN NILEEKRIFP PSKKFAENSN ISTQEELLSL KKQASDNPIQ FWESFAKSEL 

        70         80         90        100        110        120 
DWFKPFQTVL DKENAPFFKW FKEGKLNITY NCLDRHIKRG LGGKTALIWE GEPGDSKKYT 

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

       190        200        210        220        230        240 
ALKDRLIDGN ARFVITADGG FRKDKVIELK KAVDAAIESG ADKVVEKVVV VQRSQKNISM 

       250        260        270        280        290        300 
VDDRDFWWHE LLKDQKDHCE PEIMNSEDRL FILYTSGSTG KPKGVVHTTG GYNLWTHLTF 

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

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

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

       490        500        510        520        530        540 
WPGMMRTIHG NSERYLESYW EYISFKGEQN VYFAGDGARI DEDGYIWIMG RVDDVISVSG 

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

       610        620        630        640        650        660 
NEIGIIAKPE KIIISDFLPK TRSGKIMRRI LRSLAAGEKI 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 9215 EMBL ABV50316.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000825 Genomic DNA. Translation: ABV50316.1.
RefSeqYP_001483902.1. NC_009840.1.

3D structure databases

ProteinModelPortalA8G3Y5.
SMRA8G3Y5. Positions 21-658.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93060.P9215_07011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV50316; ABV50316; P9215_07011.
GeneID5615997.
KEGGpmh:P9215_07011.
PATRIC22990866. VBIProMar119824_0708.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAAGCAVFV.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycPMAR93060:GI08-725-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 nameA8G3Y5_PROM2
AccessionPrimary (citable) accession number: A8G3Y5
Entry history
Integrated into UniProtKB/TrEMBL: November 13, 2007
Last sequence update: November 13, 2007
Last modified: June 11, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)