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A4F6L2 (A4F6L2_SACEN) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 43. 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 CAL99686.1
Ordered Locus Names:SACE_0337 EMBL CAL99686.1
OrganismSaccharopolyspora erythraea (strain NRRL 23338) [Complete proteome] [HAMAP] EMBL CAL99686.1
Taxonomic identifier405948 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Saccharopolyspora ›

Protein attributes

Sequence length660 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

Region417 – 4226Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5251 By similarity HAMAP-Rule MF_01123
Metal binding5451Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5471Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5501Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3171Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3411Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3931Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5081Substrate By similarity HAMAP-Rule MF_01123
Binding site5231Substrate By similarity HAMAP-Rule MF_01123
Binding site5311Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5341Substrate 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
A4F6L2 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: F986E6A54DAD71C8

FASTA66072,043
        10         20         30         40         50         60 
MSEPDGQSNT LDNLLTESRT FPPSGEFAAQ ANATSELYAQ ADADREAFWA DQARHLHWDT 

        70         80         90        100        110        120 
EWEQVLDWSG APFAKWFVGG KLNVAYNCVD RHVEAGNGDR VAIHWEGEPG DSRAITYAEL 

       130        140        150        160        170        180 
AREVSRTANA LASLGVGAGD RVAIYLPMLP EAVYSMLACA RLGALHSVVF GGFSSEALRT 

       190        200        210        220        230        240 
RINDAQAKVV ITADGQYRRG KAMPLKTNVD EAVAATPSVE HVLVVQRTKT DVEWNDGRDQ 

       250        260        270        280        290        300 
WWHDVVEGRP ASHTPEFFDS EHPLFILYTS GTTGRPKGIL HTSGGYLTQA AYTHRTVFDL 

       310        320        330        340        350        360 
KPETDVYWCT ADIGWVTGHT YIVYGPLANG ATQVIYEGTP NTPHEGRHWD IVQKYGVTLY 

       370        380        390        400        410        420 
YTAPTTIRTF MKWGAEIPAR YDLSTLRVLG SVGEPINPEA WMWYREHIGG NRAPIVDTWW 

       430        440        450        460        470        480 
QTETGAIMIS PLPGVTATKP GSAQVPLPGI AAKVVDESGE QVGHGGGGLL VLDQPWPAML 

       490        500        510        520        530        540 
RGIWGDDDRY RETYWSKFAD KGYYFAGDGA KYDDDGDIWL LGRVDDVMNV SGHRISTTEV 

       550        560        570        580        590        600 
ESALVSHPTV AEAAVVGASD PTTGQGIVAF VILRGGADDQ ASGEAAIKAL RDHVAHEIGP 

       610        620        630        640        650        660 
IAKPRQIMVV PELPKTRSGK IMRRLLRDVA ENREIGDVST LADSSVMDLI SAGLGKSTED

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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: CAL99686.1.
RefSeqYP_001102612.1. NC_009142.1.

3D structure databases

ProteinModelPortalA4F6L2.
ModBaseSearch...

Protein-protein interaction databases

STRING405948.SACE_0337.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL99686; CAL99686; SACE_0337.
GeneID4940204.
KEGGsen:SACE_0337.
PATRIC23408036. VBISacEry28377_0340.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAPEAMEST.
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 nameA4F6L2_SACEN
AccessionPrimary (citable) accession number: A4F6L2
Entry history
Integrated into UniProtKB/TrEMBL: April 17, 2007
Last sequence update: April 17, 2007
Last modified: May 1, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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