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A4FCA0 (A4FCA0_SACEN) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 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:acsA HAMAP-Rule MF_01123 EMBL CAM01675.1
Ordered Locus Names:SACE_2375 EMBL CAM01675.1
OrganismSaccharopolyspora erythraea (strain NRRL 23338) [Complete proteome] [HAMAP] EMBL CAM01675.1
Taxonomic identifier405948 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora

Protein attributes

Sequence length668 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

Region425 – 4306Substrate 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 site3251Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3491Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site4011Substrate; 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 site6031Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6281N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
A4FCA0 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: C7663AB223D18862

FASTA66873,110
        10         20         30         40         50         60 
MSSKRVERLE VGKHSQNTLD NLLHEERIHA PSGEFAAQAN ATSELYAQAD ADREAFWADQ 

        70         80         90        100        110        120 
ARHLHWDTEW EQVLDWSGAP FAKWFVGGKL NVAYNCVDRH VEAGNGDRVA IHWEGEPGDS 

       130        140        150        160        170        180 
RAITYAELAR EVSRTANALA SLGVGAGDRV AIYLPMLPEA VYSMLACARL GALHSVVFGG 

       190        200        210        220        230        240 
FSSEALRTRI NDAQAKVVIT ADGQYRRGKA MPLKTNVDEA VAATPSVEHV LVVQRTKTDV 

       250        260        270        280        290        300 
EWNDGRDQWW HDVVEGRPAS HTPEFFDSEH PLFILYTSGT TGRPKGILHT SGGYLTQAAY 

       310        320        330        340        350        360 
THRTVFDLKP ETDVYWCTAD IGWVTGHTYI VYGPLANGAT QVIYEGTPNT PHEGRHWDIV 

       370        380        390        400        410        420 
QKYGVTLYYT APTTIRTFMK WGAEIPARYD LSTLRVLGSV GEPINPEAWM WYREHIGGNR 

       430        440        450        460        470        480 
APIVDTWWQT ETGAIMISPL PGVTATKPGS AQVPLPGIAA KVVDESGEQV GHGGGGLLVL 

       490        500        510        520        530        540 
DQPWPAMLRG IWGDDDRYRE TYWSKFADKG YYFAGDGAKY DDDGDIWLLG RVDDVMNVSG 

       550        560        570        580        590        600 
HRISTTEVES ALVSHPTVAE AAVVGASDPT TGQGIVAFVI LRGGADDQAS GEAAIKALRD 

       610        620        630        640        650        660 
HVAHEIGPIA KPRQIMVVPE LPKTRSGKIM RRLLRDVAEN REIGDVSTLA DSSVMNLISA 


GFATSSDD 

« Hide

References

[1]"Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338."
Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F.
Nat. Biotechnol. 25:447-453(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NRRL 23338.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM420293 Genomic DNA. Translation: CAM01675.1.
RefSeqYP_001104600.1. NC_009142.1.

3D structure databases

ProteinModelPortalA4FCA0.
SMRA4FCA0. Positions 29-641.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405948.SACE_2375.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM01675; CAM01675; SACE_2375.
GeneID4942224.
KEGGsen:SACE_2375.
PATRIC23412162. VBISacEry28377_2375.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAHVYKGYY.
OrthoDBEOG68WR2H.
ProtClustDBPRK00174.

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 nameA4FCA0_SACEN
AccessionPrimary (citable) accession number: A4FCA0
Entry history
Integrated into UniProtKB/TrEMBL: April 17, 2007
Last sequence update: April 17, 2007
Last modified: February 19, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)