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F4DQJ9 (F4DQJ9_PSEMN) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 13. 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:MDS_3395 EMBL AEB59426.1
OrganismPseudomonas mendocina (strain NK-01) [Complete proteome] [HAMAP] EMBL AEB59426.1
Taxonomic identifier1001585 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length653 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

Region411 – 4166Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5171 By similarity HAMAP-Rule MF_01123
Metal binding5371Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5391Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5421Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3111Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3351Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3871Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5001Substrate By similarity HAMAP-Rule MF_01123
Binding site5151Substrate By similarity HAMAP-Rule MF_01123
Binding site5231Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5261Substrate 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
F4DQJ9 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: FAD6AE26483A4D3D

FASTA65372,265
        10         20         30         40         50         60 
MSAASLYPVR PEVAARTLTD EATYKAMYQQ SVVNPEGFWR EQGKRIDWIK PYTKVKQTTF 

        70         80         90        100        110        120 
DDHHVDIKWY ADGTLNVSYN CLDRHLEERG DQVAIIWEGD DPSEHREITY RQLHEEVSKF 

       130        140        150        160        170        180 
ANALRGQDVH RGDVVTIYMP MIPEAVVAML ACARIGAIHS VVFGGFSPEA LAGRIIDCES 

       190        200        210        220        230        240 
KVVITADEGL RGGRKVPLKA NVDDALTNPE TASVQKIIVV KRTGSDIKWN QHRDIWYEDL 

       250        260        270        280        290        300 
MKVAGSVCAP KEMGAEEALF ILYTSGSTGK PKGVLHTTGG YLTYASLTHE RVFDYRPGEV 

       310        320        330        340        350        360 
FWCTADIGWV TGHTYLVYGP LSNGATTLMF EGVPNYPDVR RVAQIVDKHK VNILYTAPTA 

       370        380        390        400        410        420 
IRAMMAEGKA AVEGADGSSL RLLGSVGEPI NPEAWQWYYE NVGQSRCPIV DTWWQTETGA 

       430        440        450        460        470        480 
CLMTPLPGAH GLKPGSAARP FFGVQPALVD NLGNIIEGPA EGNLVIIDSW PGQARTLYGD 

       490        500        510        520        530        540 
HDRFVDTYFK TFRGMYFTGD GARRDEDGYW WITGRVDDVL NVSGHRMGTA EVESAMVAHP 

       550        560        570        580        590        600 
KVAEAAVVGV PHDIKGQGIY VYVTLNAGEE SSEQLRQELK NWVRKEIGPI ATPDVIQWAP 

       610        620        630        640        650 
GLPKTRSGKI MRRILRKIAT AEYDSLGDIS TLADPGVVQH LIDTHRQMQA ACA

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References

[1]"Complete genome of Pseudomonas mendocina NK-01, which synthesizes medium-chain-length polyhydroxyalkanoates and alginate oligosaccharides."
Guo W., Wang Y., Song C., Yang C., Li Q., Li B., Su W., Sun X., Song D., Yang X., Wang S.
J. Bacteriol. 193:3413-3414(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NK-01 EMBL AEB59426.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002620 Genomic DNA. Translation: AEB59426.1.
RefSeqYP_004381178.1. NC_015410.1.

3D structure databases

ProteinModelPortalF4DQJ9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEB59426; AEB59426; MDS_3395.
GeneID10458177.
KEGGpmk:MDS_3395.
PATRIC54487546. VBIPseMen187712_3448.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01895.

Enzyme and pathway databases

BioCycPMEN1001585:GIWS-3446-MONOMER.

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 nameF4DQJ9_PSEMN
AccessionPrimary (citable) accession number: F4DQJ9
Entry history
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: April 3, 2013
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info