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B8EPJ0 (ACSA_METSB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase
Short name=AcCoA synthetase
Short name=Acs
EC=6.2.1.1
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene names
Name:acsA
Ordered Locus Names:Msil_1226
OrganismMethylocella silvestris (strain BL2 / DSM 15510 / NCIMB 13906) [Complete proteome] [HAMAP]
Taxonomic identifier395965 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Beijerinckiaceae › Methylocella ›

Protein attributes

Sequence length645 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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 645645Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123
PRO_1000164051

Regions

Region409 – 4146Substrate binding By similarity

Sites

Active site5151 By similarity
Metal binding5351Magnesium; via carbonyl oxygen By similarity
Metal binding5371Magnesium; via carbonyl oxygen By similarity
Metal binding5401Magnesium; via carbonyl oxygen By similarity
Binding site3091Coenzyme A By similarity
Binding site3851Substrate; via amide nitrogen By similarity
Binding site4981Substrate By similarity
Binding site5131Substrate By similarity
Binding site5211Coenzyme A By similarity
Binding site5241Substrate By similarity
Binding site5821Coenzyme A

Amino acid modifications

Modified residue6071N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B8EPJ0 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 79DAA68C78D3C927

FASTA64570,912
        10         20         30         40         50         60 
MSDKVYPVTA EWSKSAYVDA AKYKSMYESS VSEPDKFWGE HGKRIDWVKP YTKVKNTSFD 

        70         80         90        100        110        120 
PHNVSIKWFE DGVTNVSTNC IDRHLATLGD QTAIIWEGDD PNESKHITYK QLHEEVCRLA 

       130        140        150        160        170        180 
NVLKSYGISK GDTVTIYLPM IPEAAYAMLA CARIGAIHSI VFGGFSADSL GGRIEGCKSK 

       190        200        210        220        230        240 
LIITADEGYR GGRKVPLKVN ADAAIKKVDG IVETMIVVRR TGGKVAWTEG RDVWYDEALA 

       250        260        270        280        290        300 
KASPDCPAAE MNAEDPLFIL FTSGSTGAPK GVVHSTGGYL VWASMTHQYV FDYRPGEVYW 

       310        320        330        340        350        360 
CTADVGWVTG HSYIVYGPLA NGATTLMFEG VPSYPTISRF WDVVDKHQVN IFYTAPTAIR 

       370        380        390        400        410        420 
SLMGAGDGPV KATSRKTLRV LGSVGEPINP EAWEWYYRVV GEERCPIVDT WWQTETGGIL 

       430        440        450        460        470        480 
ISPLPGATAL KPGSATQPFF GVQPQVVDAA GEVLEGPCSG NLVIADSWPA QMRTLFNDHE 

       490        500        510        520        530        540 
RFVQAYFSAY PGKYFTGDGC RRDEDGYYWI TGRVDDVINV SGHRLGTAEV ESSLVAHIKV 

       550        560        570        580        590        600 
AEAAVVGYPH DLKGQGIYAY VTLMTGIEPS EELRKELVSW VRKDIGPIAS PDIVHFAPGL 

       610        620        630        640 
PKTRSGKIMR RILRKIAEKE FSALGDTSTL ADPSVVDDLI RERAN

« Hide

References

[1]"Complete sequence of Methylocella silvestris BL2."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Forester B., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Dunfield P.F., Dedysh S.N., Liesack W. expand/collapse author list , Stott M.B., Smirnova A.V., Alam M., Chen Y., Murrell J.C., Richardson P.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BL2 / DSM 15510 / NCIMB 13906.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001280 Genomic DNA. Translation: ACK50195.1.
RefSeqYP_002361557.1. NC_011666.1.

3D structure databases

ProteinModelPortalB8EPJ0.
ModBaseSearch...

Protein-protein interaction databases

STRING395965.Msil_1226.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK50195; ACK50195; Msil_1226.
GeneID7092299.
KEGGmsl:Msil_1226.
PATRIC22597937. VBIMetSil55537_1347.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAPPIKRSC.
ProtClustDBPRK00174.

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 nameACSA_METSB
AccessionPrimary (citable) accession number: B8EPJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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