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B1Z3L5 (B1Z3L5_BURA4) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 41. 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:BamMC406_5891 EMBL ACB68328.1
OrganismBurkholderia ambifaria (strain MC40-6) [Complete proteome] [HAMAP] EMBL ACB68328.1
Taxonomic identifier398577 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length664 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

Regions

Region425 – 4306Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5341 By similarity HAMAP-Rule MF_01123
Metal binding5541Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5561Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5591Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3211Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site4011Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5161Substrate By similarity HAMAP-Rule MF_01123
Binding site5321Substrate By similarity HAMAP-Rule MF_01123
Binding site5401Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5431Substrate By similarity HAMAP-Rule MF_01123
Binding site6041Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6291N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
B1Z3L5 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 208A8B2F4243E6FD

FASTA66472,777
        10         20         30         40         50         60 
MENTLTAIVS ILQERRIFEP TADTRERATI SGMPAYQALA AEAERDYEGF WARLAREGLS 

        70         80         90        100        110        120 
WHKPFTKVLD ESDAPFYKWF DDGELNASYN CLDRHVEAGN GERVAVIFEA DDGTVTRVTY 

       130        140        150        160        170        180 
ADLLARVSRF ANALKKRGIA KGDRVVIYMP MSIEGIVAMQ ACARIGATHS VVFGGFSAKS 

       190        200        210        220        230        240 
LNERLVDVGA VALITADEQA RGGKTLPLKS IADEAIAMGG CEAVKSVIVY RRTGGKVDWH 

       250        260        270        280        290        300 
AGRDLWMHEL AHAESDTCAP EWVGAEHPLF ILYTSGSTGK PKGVQHSTGG YLLWAAQTMK 

       310        320        330        340        350        360 
WTFDWKPTDV FWCTADIGWV TGHTYITYGP LACGGTQVVF EGVPTYPDAG RFWKMIADHK 

       370        380        390        400        410        420 
VTVFYTAPTA IRSLIKAAEA DDKVHPKSYD LSSLRIIGTV GEPINPEAWM WYHKHVGQER 

       430        440        450        460        470        480 
CPIVDTWWQT ETGGHMITPL PGATPTVPGS CTLPLPGIMA AVVDETGQDV PNGQGGILVV 

       490        500        510        520        530        540 
KRPWPAMIRT IWGDPERFKK SYYPEELGGR LYLAGDGTVR DKDTGYFTIM GRIDDVLNVS 

       550        560        570        580        590        600 
GHRLGTMEIE SALVSHELVA EAAVVGRPDD TTGEAVVAFV VLKRSRPEGE EAAALAKTLR 

       610        620        630        640        650        660 
DWVGKQIGPI AKPKDIRFGD NLPKTRSGKI MRRLLRSLAK GEAITQDTST LENPAILDQL 


GQSL 

« Hide

References

[1]"Complete sequence of chromosome 3 of Burkholderia ambifaria MC40-6."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A. expand/collapse author list , Ramette A., Konstantinidis K., Tiedje J., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC40-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001027 Genomic DNA. Translation: ACB68328.1.
RefSeqYP_001815881.1. NC_010557.1.

3D structure databases

ProteinModelPortalB1Z3L5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398577.BamMC406_5891.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB68328; ACB68328; BamMC406_5891.
GeneID6182474.
KEGGbac:BamMC406_5891.
PATRIC19042153. VBIBurAmb82852_6352.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMARRIFEPT.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycBAMB398577:GH38-5979-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 nameB1Z3L5_BURA4
AccessionPrimary (citable) accession number: B1Z3L5
Entry history
Integrated into UniProtKB/TrEMBL: May 20, 2008
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)