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C5AA24 (C5AA24_BURGB) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 33. 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:acsA HAMAP-Rule MF_01123
Ordered Locus Names:bglu_1g25360 EMBL ACR29612.1
OrganismBurkholderia glumae (strain BGR1) [Complete proteome] [HAMAP] EMBL ACR29612.1
Taxonomic identifier626418 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length660 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. HAMAP-Rule MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site5301 By similarity HAMAP-Rule MF_01123
Metal binding5501Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5521Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5551Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3171Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3971Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5121Substrate By similarity HAMAP-Rule MF_01123
Binding site5281Substrate By similarity HAMAP-Rule MF_01123
Binding site5361Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5391Substrate By similarity HAMAP-Rule MF_01123
Binding site6001Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6251N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
C5AA24 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 2C43F2FA5C9CF54C

FASTA66072,189
        10         20         30         40         50         60 
MSAIESVLHE RRQFAPPASV EQAANISGMD AYRALVDEAG RDYEGFWARL ARESLDWHKP 

        70         80         90        100        110        120 
FSSVLDESNA PFYKWFEDGE LNASYNCLDR HVAAGRGERV AVIFEADDGT VTRVTYAELL 

       130        140        150        160        170        180 
ARVCRLANAL KARGIGRGDR VIIYIPMSIE GIVAMQACAR IGATHSVVFG GFSAKSLNER 

       190        200        210        220        230        240 
LVDVGACALI TADEQVRGGK TLPIKSIADD AIAMGGCEAV KSVIVYRRTG GEVAWHEGRD 

       250        260        270        280        290        300 
LWLDEITANQ PDTCEPEWVG AEHPLFILYT SGSTGKPKGL QHSTGGYLLW AALTMDWTFD 

       310        320        330        340        350        360 
RKPDDVFWCT ADIGWITGHT YITYGPLATC STQVVFEGVP TYPNAGRFWK MVADHKVTVF 

       370        380        390        400        410        420 
YTAPTAIRSL IKASGADEAA HPSRYDLSSL RIIGTVGEPI NPESWMWYHK NVGGERCPIV 

       430        440        450        460        470        480 
DTWFQTETGG HMITPLPGAT PTVPGSCTLG LPGIMAAVVD ETGQDVPNGQ GGILVIKRPW 

       490        500        510        520        530        540 
PAMARTIWGD PDRFRKSYFP DELGGRLYLA GDGTVRDKDT GYFTIMGRID DVLNVSGHRL 

       550        560        570        580        590        600 
GTMEIESALV SHELVAEAAV VGRPDDMTGE AVVAFVVLKR TRPEGEEAQQ IAKMLRDWVG 

       610        620        630        640        650        660 
KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEAV TQDTSTLENP AILEQLAEAR 

« Hide

References

[1]"Complete genome sequence of Burkholderia glumae BGR1."
Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.
J. Bacteriol. 191:3758-3759(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BGR1 EMBL ACR29612.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001503 Genomic DNA. Translation: ACR29612.1.
RefSeqYP_002912316.1. NC_012724.2.

3D structure databases

ProteinModelPortalC5AA24.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING626418.bglu_1g25360.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR29612; ACR29612; bglu_1g25360.
GeneID7906710.
KEGGbgl:bglu_1g25360.
PATRIC19112782. VBIBurGlu130723_5450.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAWVMGRVD.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycBGLU626418:GJI5-2579-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 nameC5AA24_BURGB
AccessionPrimary (citable) accession number: C5AA24
Entry history
Integrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: April 16, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)