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Q9R8E3 (BLS_STRCL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. 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
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 lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

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

1 ..................................................................................... 513
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9R8E3 [UniParc].

Last modified May 1, 2000. 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: 9689037] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Enzymes catalyzing the early steps of clavulanic acid biosynthesis are encoded by two sets of paralogous genes in Streptomyces clavuligerus."
Jensen S.E., Elder K.J., Aidoo K.A., Paradkar A.S.
Antimicrob. Agents Chemother. 44:720-726(2000) [PubMed: 10681345] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602.
[3]"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: 8529893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-513.
[4]"Kinetic mechanism of the beta-lactam synthetase of Streptomyces clavuligerus."
Bachmann B.O., Townsend C.A.
Biochemistry 39:11187-11193(2000) [PubMed: 10985764] [Abstract]
Cited for: CHARACTERIZATION.
[5]"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: 11473258] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 4-507.
[6]"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: 12409610] [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.
U87786 Genomic DNA. Translation: AAF86620.1.
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[»]
ProteinModelPortalQ9R8E3.
SMRQ9R8E3. Positions 2-508.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC29741627. VBIStrCla15562_0196.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13483.

Family and domain databases

InterProIPR001962. Asn_synthase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PfamPF00733. Asn_synthase. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00131. Adenosine monophosphate.

Entry information

Entry nameBLS_STRCL
AccessionPrimary (citable) accession number: Q9R8E3
Secondary accession number(s): Q53938
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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