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Q02FT9 (Q02FT9_PSEAB) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 49. 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:acsB EMBL ABJ14116.1
Synonyms:acsA HAMAP-Rule MF_01123
Ordered Locus Names:PA14_62630 EMBL ABJ14116.1
OrganismPseudomonas aeruginosa (strain UCBPP-PA14) [Complete proteome] [HAMAP] EMBL ABJ14116.1
Taxonomic identifier208963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length645 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 SAAS011904

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

Region408 – 4136Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5141 By similarity HAMAP-Rule MF_01123
Metal binding5341Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5361Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5391Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3081Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3321Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3841Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site4971Substrate By similarity HAMAP-Rule MF_01123
Binding site5121Substrate By similarity HAMAP-Rule MF_01123
Binding site5201Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5231Substrate By similarity HAMAP-Rule MF_01123
Binding site5811Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6061N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
Q02FT9 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: D3F63891F880B1EA

FASTA64571,640
        10         20         30         40         50         60 
MFEISVHPVP DAVRQRAYLN DDDYQRLYRQ SVENPDEFWS EQAKAFLDWF KPWHSVHHGD 

        70         80         90        100        110        120 
LRKGQATWFK GGQLNVAYNC IDRHLERRGE QIAIVWEGDN PSESAHITYR KLHHNVCRLA 

       130        140        150        160        170        180 
NVLKSRGVEK GDRVCIYMPM IPEAAYAMLA CARIGAVHSV VFGGFSPDSL RDRILDADCR 

       190        200        210        220        230        240 
TVITADEGVR GGKYIPLKQN VEKALKDCPD VSTVVVVERT QGDIPWVEGR DIWYHEALHA 

       250        260        270        280        290        300 
ASADCPAEAM DAEDPLFILY TSGSTGKPKG VLHTTGGYLL GAAMTHKYVF DYHDGDVYWC 

       310        320        330        340        350        360 
TADVGWVTGH SYIVYGPLAN GATTLMFEGV PNYPDASRFW QVIDKHQVNI FYTAPTAIRA 

       370        380        390        400        410        420 
LMREGDAPVR QTSRSSLRLL GSVGEPINPE AWEWYYQVVG EKRCPIVDTW WQTETGSILI 

       430        440        450        460        470        480 
TPLPGATALK PGSATRPFFG VQPVLLDEKG KEIDGAGSGV LAIKASWPSQ IRSVYGDHQR 

       490        500        510        520        530        540 
MIDTYFKPYP GYYFSGDGAR RDEDGYYWIT GRVDDVINVS GHRIGTAEVE SALVLHDAVA 

       550        560        570        580        590        600 
EAAVVGCPHD VKGQAIYAFV TLMAGSQPSE ALQQELLALV GKEIGSFAKP DHLQWAPSLP 

       610        620        630        640 
KTRSGKIMRR ILRKIACNEL DSLGDTSTLA DPGVVQGLID NRLNR 

« Hide

References

[1]"Genomic analysis reveals that Pseudomonas aeruginosa virulence is combinatorial."
Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.
Genome Biol. 7:R90.1-R90.14(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UCBPP-PA14 EMBL ABJ14116.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000438 Genomic DNA. Translation: ABJ14116.1.
RefSeqYP_793197.1. NC_008463.1.

3D structure databases

ProteinModelPortalQ02FT9.
SMRQ02FT9. Positions 7-642.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208963.PA14_62630.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ14116; ABJ14116; PA14_62630.
GeneID4383182.
KEGGpau:PA14_62630.
PATRIC19856442. VBIPseAer79785_5138.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMARRIFEPT.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycPAER208963:GI5K-5113-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 nameQ02FT9_PSEAB
AccessionPrimary (citable) accession number: Q02FT9
Entry history
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: June 11, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)