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

Q88EH6 (ACSA1_PSEPK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase 1

Short name=AcCoA synthetase 1
Short name=Acs 1
EC=6.2.1.1
Alternative name(s):
Acetate--CoA ligase 1
Acyl-activating enzyme 1
Gene names
Name:acsA1
Ordered Locus Names:PP_4487
OrganismPseudomonas putida (strain KT2440) [Complete proteome] [HAMAP]
Taxonomic identifier160488 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 653653Acetyl-coenzyme A synthetase 1 HAMAP-Rule MF_01123
PRO_0000208376

Regions

Region411 – 4166Substrate binding By similarity

Sites

Active site5171 By similarity
Metal binding5371Magnesium; via carbonyl oxygen By similarity
Metal binding5391Magnesium; via carbonyl oxygen By similarity
Metal binding5421Magnesium; via carbonyl oxygen By similarity
Binding site3111Coenzyme A By similarity
Binding site3351Coenzyme A By similarity
Binding site3871Substrate; via amide nitrogen By similarity
Binding site5001Substrate By similarity
Binding site5151Substrate By similarity
Binding site5231Coenzyme A By similarity
Binding site5261Substrate By similarity
Binding site5841Coenzyme A

Amino acid modifications

Modified residue6091N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q88EH6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: CE626C86C922E8F4

FASTA65371,797
        10         20         30         40         50         60 
MSAAPLYPVR PEVAATTLTD EATYKAMYQQ SVINPDGFWR EQAQRIDWIK PFTKVKQTSF 

        70         80         90        100        110        120 
DDHHVDIKWF ADGTLNVSSN CLDRHLEERG DQLAIIWEGD DPSEHRNITY RELHEQVCKF 

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

       190        200        210        220        230        240 
KVVITADEGV RGGRRTPLKA NVDLALTNPE TSSVQKIIVC KRTGGDIAWH QHRDIWYEDL 

       250        260        270        280        290        300 
MKVASSHCAP KEMGAEEALF ILYTSGSTGK PKGVLHTTGG YLVYAALTHE RVFDYRPGEV 

       310        320        330        340        350        360 
YWCTADVGWV TGHSYIVYGP LANGATTLLF EGVPNYPDIT RVSKIVDKHK VNILYTAPTA 

       370        380        390        400        410        420 
IRAMMAEGQA AVEGADGSSL RLLGSVGEPI NPEAWNWYYK TVGKERCPIV DTWWQTETGG 

       430        440        450        460        470        480 
ILISPLPGAT GLKPGSATRP FFGVVPALVD NLGNLIDGAA EGNLVILDSW PGQSRSLYGD 

       490        500        510        520        530        540 
HDRFVDTYFK TFRGMYFTGD GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESAMVAHS 

       550        560        570        580        590        600 
KVAEAAVVGV PHDIKGQGIY VYVTLNAGIE ASEQLRLELK NWVRKEIGPI ASPDVIQWAP 

       610        620        630        640        650 
GLPKTRSGKI MRRILRKIAT GEYDALGDIS TLADPGVVQH LIDTHKAMNL ASA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015451 Genomic DNA. Translation: AAN70062.1.
RefSeqNP_746598.1. NC_002947.3.

3D structure databases

ProteinModelPortalQ88EH6.
SMRQ88EH6. Positions 7-647.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING160488.PP_4487.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN70062; AAN70062; PP_4487.
GeneID1042436.
KEGGppu:PP_4487.
PATRIC19947676. VBIPsePut30601_4775.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAGGCEAVT.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycPPUT160488:GIXO-4574-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 nameACSA1_PSEPK
AccessionPrimary (citable) accession number: Q88EH6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families