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P0DJQ7 (BLS_STRCL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Carboxyethyl-arginine beta-lactam-synthase

EC=6.3.3.4
Alternative name(s):
Beta-lactam synthetase
Gene names
Name:bls
OrganismStreptomyces clavuligerus
Taxonomic identifier1901 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-N(2)-(2-carboxyethyl)arginine = AMP + diphosphate + deoxyamidinoproclavaminate.

Cofactor

Binds 1 magnesium ion per subunit.

Pathway

Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate from D-glyceraldehyde 3-phosphate and L-arginine: step 2/8.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the asparagine synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 513513Carboxyethyl-arginine beta-lactam-synthase
PRO_0000056939

Sites

Metal binding2531Magnesium
Metal binding3511Magnesium

Secondary structure

.............................................................................................. 513
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0DJQ7 [UniParc].

Last modified September 5, 2012. Version 1.
Checksum: EC2F460A77EB65CE

FASTA51354,530
        10         20         30         40         50         60 
MGAPVLPAAF GFLASARTGG GRAPGPVFAT RGSHTDIDTP QGERSLAATL VHAPSVAPDR 

        70         80         90        100        110        120 
AVARSLTGAP TTAVLAGEIY NRDELLSVLP AGPAPEGDAE LVLRLLERYD LHAFRLVNGR 

       130        140        150        160        170        180 
FATVVRTGDR VLLATDHAGS VPLYTCVAPG EVRASTEAKA LAAHRDPKGF PLADARRVAG 

       190        200        210        220        230        240 
LTGVYQVPAG AVMDIDLGSG TAVTHRTWTP GLSRRILPEG EAVAAVRAAL EKAVAQRVTP 

       250        260        270        280        290        300 
GDTPLVVLSG GIDSSGVAAC AHRAAGELDT VSMGTDTSNE FREARAVVDH LRTRHREITI 

       310        320        330        340        350        360 
PTTELLAQLP YAVWASESVD PDIIEYLLPL TALYRALDGP ERRILTGYGA DIPLGGMHRE 

       370        380        390        400        410        420 
DRLPALDTVL AHDMATFDGL NEMSPVLSTL AGHWTTHPYW DREVLDLLVS LEAGLKRRHG 

       430        440        450        460        470        480 
RDKWVLRAAM ADALPAETVN RPKLGVHEGS GTTSSFSRLL LDHGVAEDRV HEAKRQVVRE 

       490        500        510 
LFDLTVGGGR HPSEVDTDDV VRSVADRTAR GAA 

« Hide

References

[1]"Beta-lactam synthetase: a new biosynthetic enzyme."
Bachmann B.O., Li R., Townsend C.A.
Proc. Natl. Acad. Sci. U.S.A. 95:9082-9086(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Clavulanic acid biosynthesis in Streptomyces clavuligerus: gene cloning and characterization."
Hodgson J.E., Fosberry A.P., Rawlinson N.S., Ross H.N.M., Neal R.J., Arnell J.C., Earl A.J., Lawlor E.J.
Gene 166:49-55(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-513.
[3]"Kinetic mechanism of the beta-lactam synthetase of Streptomyces clavuligerus."
Bachmann B.O., Townsend C.A.
Biochemistry 39:11187-11193(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[4]"Structure of beta-lactam synthetase reveals how to synthesize antibiotics instead of asparagine."
Miller M.T., Bachmann B.O., Townsend C.A., Rosenzweig A.C.
Nat. Struct. Biol. 8:684-689(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 4-507.
[5]"The catalytic cycle of beta -lactam synthetase observed by X-ray crystallographic snapshots."
Miller M.T., Bachmann B.O., Townsend C.A., Rosenzweig A.C.
Proc. Natl. Acad. Sci. U.S.A. 99:14752-14757(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 4-507.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF071051 Genomic DNA. Translation: AAC31901.1.
X84101 Genomic DNA. Translation: CAA58903.1.
PIRS57668.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JGTX-ray1.95A/B1-513[»]
1M1ZX-ray1.95A/B1-513[»]
1MB9X-ray2.11A/B1-513[»]
1MBZX-ray2.47A/B1-513[»]
1MC1X-ray2.16A/B1-513[»]
ProteinModelPortalP0DJQ7.
SMRP0DJQ7. Positions 2-508.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB00131. Adenosine monophosphate.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13483.
UniPathwayUPA00112; UER00243.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProIPR001962. Asn_synthase.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00733. Asn_synthase. 2 hits.
PF13537. GATase_7. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBLS_STRCL
AccessionPrimary (citable) accession number: P0DJQ7
Secondary accession number(s): Q53938, Q9R8E3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: September 5, 2012
Last modified: June 11, 2014
This is version 11 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways