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D7A5Y5 (D7A5Y5_STAND) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 26. 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:Snov_2812 EMBL ADH90100.1
OrganismStarkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB 9113) [Complete proteome] [HAMAP] EMBL ADH90100.1
Taxonomic identifier639283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeStarkeya

Protein attributes

Sequence length652 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 SAAS SAAS020845

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 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 site3101Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3341Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3861Substrate; 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 site5831Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6081N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
D7A5Y5 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: 1A1A1258EB1694A6

FASTA65272,499
        10         20         30         40         50         60 
MSDKIYDVPA EWAKRAFLNE HAYRAKYEAS VRDTEGFWAE EGKRIEWFEP YTIVKNTSYD 

        70         80         90        100        110        120 
PGHVSIKWFE DGVTNVAWNC IDRHLPRLAD QTAIIWEGDD PSQSRHITYQ ELHDEVCRFA 

       130        140        150        160        170        180 
NVLRNRNVEK GDRVTIYMPM IPEAAYAMLA CARLGAIHSV VFGGFSPDSL AGRIRDCGSK 

       190        200        210        220        230        240 
VIITADEGLR GGRKVPLKAN VDAAIAKVSD VEIDHVIVVK RTGGEVDMKP GRDVWYHQAA 

       250        260        270        280        290        300 
DLVTSECPAV PMNAEDPLFI LYTSGSTGLP KGVLHTTGGY LVYASMTHQY VFDYHDGDVY 

       310        320        330        340        350        360 
WCTADIGWVT GHSYIVYGPL ANGATTLMFE GVPNYPSNSR FWEVIDKHKV NIFYTAPTAI 

       370        380        390        400        410        420 
RALMQAGDEP VKKTSRASLR LLGSVGEPIN PEAWEWYHRV VGEDRCPIVD TWWQTETGGI 

       430        440        450        460        470        480 
LITPLPGATR LKPGSATQPF FGVIPQVVDA EGRVLEGACE GNLVIADSWP GQMRTVYGDH 

       490        500        510        520        530        540 
ERFMQTYFAT YPGKYFTGDG CRRDSDGYYW ITGRVDDVIN VSGHRMGTAE VESALVAHPK 

       550        560        570        580        590        600 
VSEAAVVGYP HDIKGQGIYA YVTLMAGAEP TEELRKELVA WVRREIGPIA SPDLIQFAPS 

       610        620        630        640        650 
LPKTRSGKIM RRILRKIAED EFGNLGDTST LADPTVVQDL ISQRQNKKHA AA 

« Hide

References

[1]"Complete sequence of Starkeya novella DSM 506."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U., Woyke T.
Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB 9113.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002026 Genomic DNA. Translation: ADH90100.1.
RefSeqYP_003694719.1. NC_014217.1.

3D structure databases

ProteinModelPortalD7A5Y5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADH90100; ADH90100; Snov_2812.
GeneID9333895.
KEGGsno:Snov_2812.
PATRIC38258209. VBIStaNov45716_2813.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000229981.
KOK01895.
OMAWVMGRVD.

Enzyme and pathway databases

BioCycSNOV639283:GCS4-2845-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 nameD7A5Y5_STAND
AccessionPrimary (citable) accession number: D7A5Y5
Entry history
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: February 19, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)