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E8S8F1 (E8S8F1_MICSL) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 22. 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:ML5_0403 EMBL ADU05955.1
OrganismMicromonospora sp. (strain L5) [Complete proteome] [HAMAP] EMBL ADU05955.1
Taxonomic identifier648999 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeMicromonospora

Protein attributes

Sequence length662 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

Region410 – 4156Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5241 By similarity HAMAP-Rule MF_01123
Metal binding5441Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5461Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5491Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3101Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3861Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5071Substrate By similarity HAMAP-Rule MF_01123
Binding site5221Substrate By similarity HAMAP-Rule MF_01123
Binding site5301Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5331Substrate By similarity HAMAP-Rule MF_01123
Binding site5951Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6201N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
E8S8F1 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: 31D50DC26ECEAAFB

FASTA66271,800
        10         20         30         40         50         60 
MSEALANLLN ETRQFPPPAE LAANANVTAE AYEEAAGDRL AFWERQAGRL AWAQPWEQVL 

        70         80         90        100        110        120 
DWSNAPFAKW FTGGRLNVAY NCLDRHVEAG LGDKVAIHWE GEPGDTRTVT YADLHKLTCQ 

       130        140        150        160        170        180 
AANALTELGV TAGDRVAIYL PMIPEAAVAM LACARIGATH SVVFGGFSAD ALTNRIQDAS 

       190        200        210        220        230        240 
AKVVITADGG FRRGKPSALK PTVDEAVANC PSVEHVLVVR RTGEEVAWSA KDHWWHETVE 

       250        260        270        280        290        300 
TASPEHEAQA FDAEHPLFIL YTSGTTARPK GILHTTGGYL TQTSYTTHAV FDLKPETDVY 

       310        320        330        340        350        360 
WCTADIGWVT GHSYIVYGPL SNGATQVMYE GTPDTPHKGR FWEVVDKYKV TILYTAPTLI 

       370        380        390        400        410        420 
RTMMKWGEDI PAGYDLSSLR LLGSVGEPIN PEAWIWYRQH VGRGELPVVD TWWQTETGAI 

       430        440        450        460        470        480 
MISPLPGVTE AKPGSAMSPL PGIVADVVDD QGQSVPNGGG GYLVLKEPWP SMLRTIWGDD 

       490        500        510        520        530        540 
NRFLETYWSR FGAGANTGDE WVYFAGDGAK KDDDGHIWLL GRVDDVMLVS GHNISTTEVE 

       550        560        570        580        590        600 
SALVSHPSVA EAAVVGATDP TTGQAIVAFA IPRGSAEISG DAGEQLIAEL RNHVAKTLGP 

       610        620        630        640        650        660 
IAKPRQIMLV PELPKTRSGK IMRRLLRDVA ENRSLGDVTT LQDSSVMELI SSGMSGGKSD 


ED 

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References

[1]"Complete sequence of Micromonospora sp. L5."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., De Hoff P.L., Hirsch A.M., Woyke T.
Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002399 Genomic DNA. Translation: ADU05955.1.
RefSeqYP_004080106.1. NC_014815.1.

3D structure databases

ProteinModelPortalE8S8F1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADU05955; ADU05955; ML5_0403.
GeneID10055885.
KEGGmil:ML5_0403.
PATRIC45268612. VBIMicSp154089_0413.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000229981.
KOK01895.
OMAAWIWYRD.

Enzyme and pathway databases

BioCycMSP648999:GHVN-411-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 nameE8S8F1_MICSL
AccessionPrimary (citable) accession number: E8S8F1
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: June 11, 2014
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)