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Q02I47 (Q02I47_PSEAB) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 32. 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 1 HAMAP MF_01123

EC=6.2.1.1 HAMAP MF_01123
Alternative name(s):
Acetate--CoA ligase 1 HAMAP MF_01123
Acyl-activating enzyme 1 HAMAP MF_01123
Gene names
Name:acsA EMBL ABJ10047.1
Synonyms:acsA1 HAMAP MF_01123
Ordered Locus Names:PA14_52800
OrganismPseudomonas aeruginosa (strain UCBPP-PA14) [Complete proteome] [HAMAP]
Taxonomic identifier208963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP MF_01123

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP MF_01123

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family. HAMAP MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site5171 By similarity HAMAP MF_01123

Amino acid modifications

Modified residue6091N6-acetyllysine By similarity HAMAP MF_01123

Sequences

Sequence LengthMass (Da)Tools
Q02I47 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 991802723539AD23

FASTA65171,763
        10         20         30         40         50         60 
MSAASLYPVH PEAVARTFTD EATYKTMYQQ SVVNPDGFWR EQAQRIDWIK PFEKVKQTSF 

        70         80         90        100        110        120 
DDHHVDIKWF ADGTLNVSHN CLDRHLAERG DQVAIIWEGD DPADHQEITY RQLHEQVCKF 

       130        140        150        160        170        180 
ANALRGQDVH RGDVVTIYMP MIPEAVVAML ACTRIGAIHS VVFGGFSPEA LAGRIIDCKS 

       190        200        210        220        230        240 
KVVITADEGV RGGKRTPLKA NVDDALTNPE TSSVQKIIVC KRTGAEIKWN QHRDVWYDDL 

       250        260        270        280        290        300 
MKVAGSTCAP KEMGAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASLTHE RVFDYRPGEV 

       310        320        330        340        350        360 
YWCTADIGWV TGHTYIVYGP LANGATTILF EGVPNYPDVT RVAKIIDKHK VNILYTAPTA 

       370        380        390        400        410        420 
IRAMMAEGKA AVAGADGSSL RLLGSVGEPI NPEAWQWYYE TVGQSRCPIV DTWWQTETGA 

       430        440        450        460        470        480 
CLMTPLPGAH AMKPGSAAKP FFGVVPALVD NLGNLIEGAA EGNLVILDSW PGQARTLFGD 

       490        500        510        520        530        540 
HDRFVDTYFK TFKGMYFTGD GARRDEDGYY WITGRVDDVL NVSGHRMGTA EVESAMVAHP 

       550        560        570        580        590        600 
KVAEAAVVGM QHDIKGQGIY VYVTLNSGVE PSEALRQELK QWVRREIGPI ATPDVIQWAP 

       610        620        630        640        650 
GLPKTRSGKI MRRILRKIAA AEYDTLGDIS TLADPGVVQH LIETHRSMQA A 

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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: 17038190] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000438 Genomic DNA. Translation: ABJ10047.1.
RefSeqYP_792389.1. NC_008463.1.

3D structure databases

ProteinModelPortalQ02I47.
SMRQ02I47. Positions 16-647.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ02I47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4385591.
GenomeReviewsGene locus PA14_52800 in contig CP000438_GR.
KEGGpau:PA14_52800.
PATRIC19854812. VBIPseAer79785_4343.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHBG547964.
OMADYWWHEE.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycPAER208963:PA14_52800-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
[Tree]
InterProIPR011904. Ac_CoA_lig.
IPR024597. Acyl-CoA_synth_DUF3448.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
KOK01895.
PANTHERPTHR24095:SF42. PTHR24095:SF42. 1 hit.
PfamPF00501. AMP-binding. 1 hit.
PF11930. DUF3448. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ02I47_PSEAB
AccessionPrimary (citable) accession number: Q02I47
Entry history
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: December 14, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)