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

Q01NE9 (Q01NE9_SOLUE) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 51. 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:Acid_7927 EMBL ABJ88821.1
OrganismSolibacter usitatus (strain Ellin6076) [Complete proteome] [HAMAP] EMBL ABJ88821.1
Taxonomic identifier234267 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaSolibacteresSolibacteralesSolibacteraceaeCandidatus Solibacter

Protein attributes

Sequence length643 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

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 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
Q01NE9 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 207212BA2B0D0D0E

FASTA64372,281
        10         20         30         40         50         60 
MADANVYPPS AEFVSTANVK GMAGYRALYQ RAAEKPEEFW GELADQELHW FRKWTHVFEW 

        70         80         90        100        110        120 
DPPFAKWFAG GKINASYNCI DRHLSTPRKN KVAILWEGEP GDQRMITYQE LHRLVCRFAN 

       130        140        150        160        170        180 
VLKARGLKAG DRAIIYMGMV PELPVAVLAC ARLGIIHSVV FGGFSAEALK ARIQDLEAQV 

       190        200        210        220        230        240 
VITCDGAWRR GKEVRLKDAV DESLAGCDTV KDVIVYRRTG GSIPMQEGRD HWWHDLDTEA 

       250        260        270        280        290        300 
SEVCPAEELD SEHPLYVLYT SGTTGKPKGI VHTTGGYLLQ AHMTMKWVFD LHEEDTYWCT 

       310        320        330        340        350        360 
ADIGWVTGHS YIVYGPLSAG ATSVMYEGAP DFPQPDRFWR LIEKYKVNIF YTSPTAIRSF 

       370        380        390        400        410        420 
VRQGDQWPNA HDMSSLRLLG SVGEPINPAA WEWYYKVIGK ERCPIVDTWW QTETGAIMIA 

       430        440        450        460        470        480 
PMPGAVPLKP GSGTLPLPGV IADIVDLQGN PVEANREGFL IVRRPWPSIA RTLWREPDRY 

       490        500        510        520        530        540 
KQAYWERVPG VYLAGDAARR DEDGYFWILG RVDDVMNVSG HRLSTMELES ALVRHPAVAE 

       550        560        570        580        590        600 
AAVVGKPHEI TGQAVACFVT LKKGTWDHTA LAEELRKWVA HEIGSFAKPE QIRFTDSLPK 

       610        620        630        640 
TRSGKIMRRL LREIVTSNSV TGDVTTLEDL SVVTRLSAQH DED 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000473 Genomic DNA. Translation: ABJ88821.1.
RefSeqYP_829106.1. NC_008536.1.

3D structure databases

ProteinModelPortalQ01NE9.
SMRQ01NE9. Positions 10-617.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234267.Acid_7927.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ88821; ABJ88821; Acid_7927.
GeneID4424186.
KEGGsus:Acid_7927.
PATRIC32018658. VBICanSol30224_8273.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAAWIWYRD.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycSUSI234267:GHSK-7980-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 nameQ01NE9_SOLUE
AccessionPrimary (citable) accession number: Q01NE9
Entry history
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: June 11, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)