Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B0KHW7 (B0KHW7_PSEPG) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:PputGB1_4701 EMBL ABZ00588.1
OrganismPseudomonas putida (strain GB-1) [Complete proteome] [HAMAP] EMBL ABZ00588.1
Taxonomic identifier76869 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length644 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

Region407 – 4126Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5131 By similarity HAMAP-Rule MF_01123
Metal binding5331Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5351Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5381Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3071Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3311Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3831Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site4961Substrate By similarity HAMAP-Rule MF_01123
Binding site5111Substrate By similarity HAMAP-Rule MF_01123
Binding site5191Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5221Substrate By similarity HAMAP-Rule MF_01123
Binding site5801Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6051N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
B0KHW7 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 6DA55322F09A7A93

FASTA64471,051
        10         20         30         40         50         60 
MFDIRNYPQA LAVSQSATPT PDEYHRLYRQ SVDDPDTFWA EQAKRLDWIK PWSSVQQCDL 

        70         80         90        100        110        120 
NTGKARWFDG AQLNVSYNCI DRHLAQRGEQ TALLWEGDDP KDSKAITYRE LHRQVCRLAN 

       130        140        150        160        170        180 
AMKARGVKKG DRVCIYMPMI PEAAFAMLAC TRIGAIHSVV FGGFSPDALR DRILDADCRT 

       190        200        210        220        230        240 
VITADEGVRG GKRVPLKQNV DKALASCPAV SSVLVVRRTG GDVAWAEGRD LWYHEVTEKA 

       250        260        270        280        290        300 
GDDCPPEPMA AEDPLFILYT SGSTGKPKGV LHTTGGYLLQ ATMTFKVVFD YRDGEVFWCT 

       310        320        330        340        350        360 
ADVGWVTGHS YIVYGPLANG AISLMFEGVP NYPDTSRFWQ VVDKHQVNIF YTAPTALRAL 

       370        380        390        400        410        420 
MREGSAPLQG TSRKSLRLLG SVGEPINPEA WEWYFEAVGQ KRCPIVDTWW QTETGGIMLT 

       430        440        450        460        470        480 
PLPGSQALKP GCATQPMFGV QPALLDEKGK LIEGPGAGLL VIKASWPGQI RSVYGDHQRM 

       490        500        510        520        530        540 
VDTYFKPMPG YYFTGDGARR DADGDYWITG RIDDVINVSG HRIGTAEVES ALVLHDSVAE 

       550        560        570        580        590        600 
AAVVGYPHDL KGQGVYAFVT TMNGVTPDDT LKAELLALVS KEIGSFAKPE LIQWAPALPK 

       610        620        630        640 
TRSGKIMRRI LRKIACNELD NLGDTSTLAD PSVVQGLIDK RLNQ 

« Hide

References

[1]"Complete sequence of Pseudomonas putida GB-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-1 EMBL ABZ00588.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000926 Genomic DNA. Translation: ABZ00588.1.
RefSeqYP_001670923.1. NC_010322.1.

3D structure databases

ProteinModelPortalB0KHW7.
SMRB0KHW7. Positions 21-641.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING76869.PputGB1_4701.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ00588; ABZ00588; PputGB1_4701.
GeneID5872512.
KEGGppg:PputGB1_4701.
PATRIC19936495. VBIPsePut76638_4709.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAYGDHQRM.
OrthoDBEOG68WR2H.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycPPUT76869:GIXB-4782-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 nameB0KHW7_PSEPG
AccessionPrimary (citable) accession number: B0KHW7
Entry history
Integrated into UniProtKB/TrEMBL: March 18, 2008
Last sequence update: March 18, 2008
Last modified: February 19, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)