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Q12X88 (Q12X88_METBU) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 54. 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:Mbur_0999 EMBL ABE51938.1
OrganismMethanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M) [Complete proteome] [HAMAP] EMBL ABE51938.1
Taxonomic identifier259564 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides

Protein attributes

Sequence length649 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

Region409 – 4146Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5161 By similarity HAMAP-Rule MF_01123
Metal binding5361Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5381Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5411Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3091Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3851Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site4991Substrate By similarity HAMAP-Rule MF_01123
Binding site5141Substrate By similarity HAMAP-Rule MF_01123
Binding site5221Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5251Substrate 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
Q12X88 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 4C72352FF0A22D0B

FASTA64972,668
        10         20         30         40         50         60 
MTETIESLLK EQQEFHPSAD FVKQANMNDP HIYEKAEADI EGFWEGLAGN IDWFKKWDTV 

        70         80         90        100        110        120 
LDWQPPHAKW FSGGKLNASY NCLDRHVQKH GDKPALIWEG EMENSETYTY KELRDATARF 

       130        140        150        160        170        180 
AAGLKELGVK KGDVVTIYLP MVPEAVISML ACSRIGAPHS VVFAGFSSEA LAQRVEDAHS 

       190        200        210        220        230        240 
RFVITCNGYF HKGNLIQQKE RADKGLENAP AVEKVIVVDH AANIIPMKEE RDIWWNDLIH 

       250        260        270        280        290        300 
NVDSECEPEH MDSEDTLFIM YTSGTTGRPK GVVHTTGGYM VGTNVTSNWI FDLKDDDIFW 

       310        320        330        340        350        360 
CTADVGWITG HSYLVYGPLS NGATIVMHEG APDYPDKGRF WDIVEKYGVT IFYTAPTAIR 

       370        380        390        400        410        420 
TFMKWGDEIP AKYDLSSLRL LGSVGEPINP KAWLWYYETI GKSKCPIVDT WWQTETGMIM 

       430        440        450        460        470        480 
ISPLPGITTM RPGTATRPFP GIKANILDDE GNEVPMGSGG YLALQNPWPS MIRTINGDEQ 

       490        500        510        520        530        540 
RFIDTYWSKW GADTYLTGDG ARKDEDGNFW ILGRLDDVIK VSGHRLGTME IESALVSHPS 

       550        560        570        580        590        600 
VAEAAVDGKV DEIKGEVICA YVILESSCDD QCSILEDELK QHVVDEIGPI ARPKMIIFTE 

       610        620        630        640 
ELPKTRSGKI MRRVLKAITN GTEIGDISTL QDPAVVEDLK RKVNEIGEQ 

« Hide

References

[1]"Complete sequence of Methanococcoides burtonii DSM 6242."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6242 / NBRC 107633 / OCM 468 / ACE-M.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000300 Genomic DNA. Translation: ABE51938.1.
RefSeqYP_565688.1. NC_007955.1.

3D structure databases

ProteinModelPortalQ12X88.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259564.Mbur_0999.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE51938; ABE51938; Mbur_0999.
GeneID3998104.
KEGGmbu:Mbur_0999.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAQTAILFE.

Enzyme and pathway databases

BioCycMBUR259564:GHBZ-1022-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 nameQ12X88_METBU
AccessionPrimary (citable) accession number: Q12X88
Entry history
Integrated into UniProtKB/TrEMBL: August 22, 2006
Last sequence update: August 22, 2006
Last modified: June 11, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)