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P0DJQ7

- BLS_STRCL

UniProt

P0DJQ7 - BLS_STRCL

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Protein

Carboxyethyl-arginine beta-lactam-synthase

Gene
bls
Organism
Streptomyces clavuligerus
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 1 magnesium ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi253 – 2531Magnesium
Metal bindingi351 – 3511Magnesium

GO - Molecular functioni

  1. (carboxyethyl)arginine beta-lactam-synthase activity Source: UniProtKB-EC
  2. asparagine synthase (glutamine-hydrolyzing) activity Source: InterPro
  3. ATP binding Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. asparagine biosynthetic process Source: InterPro
  2. clavulanic acid biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13483.
UniPathwayiUPA00112; UER00243.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxyethyl-arginine beta-lactam-synthase (EC:6.3.3.4)
Alternative name(s):
Beta-lactam synthetase
Gene namesi
Name:bls
OrganismiStreptomyces clavuligerus
Taxonomic identifieri1901 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513Carboxyethyl-arginine beta-lactam-synthasePRO_0000056939Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
513
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 189
Beta strandi32 – 365
Helixi42 – 443
Beta strandi47 – 526
Helixi58 – 614
Beta strandi62 – 654
Beta strandi67 – 8014
Helixi82 – 876
Beta strandi89 – 924
Helixi98 – 10912
Helixi110 – 1156
Beta strandi119 – 1279
Beta strandi130 – 1356
Beta strandi144 – 1485
Beta strandi151 – 1566
Helixi158 – 1625
Beta strandi175 – 1773
Beta strandi191 – 1966
Turni197 – 2004
Beta strandi201 – 2066
Helixi219 – 23719
Beta strandi240 – 2423
Beta strandi245 – 2473
Helixi252 – 26514
Beta strandi269 – 2746
Helixi281 – 29111
Beta strandi294 – 2996
Helixi302 – 3065
Helixi309 – 3168
Helixi321 – 33616
Beta strandi343 – 3453
Turni348 – 3503
Helixi351 – 3544
Turni355 – 3573
Helixi364 – 37613
Helixi386 – 3894
Turni390 – 3923
Beta strandi394 – 3963
Helixi398 – 4003
Helixi402 – 4109
Helixi413 – 4164
Beta strandi421 – 4233
Helixi424 – 4307
Turni431 – 4333
Helixi436 – 4405
Helixi446 – 4494
Helixi455 – 4639
Turni467 – 4693
Helixi470 – 48516
Turni486 – 4883
Helixi492 – 4943
Helixi497 – 5059

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0DJQ7.
SMRiP0DJQ7. Positions 2-508.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProiIPR001962. Asn_synthase.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00733. Asn_synthase. 2 hits.
PF13537. GATase_7. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.

Sequencei

Sequence statusi: Complete.

P0DJQ7-1 [UniParc]FASTAAdd to Basket

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MGAPVLPAAF GFLASARTGG GRAPGPVFAT RGSHTDIDTP QGERSLAATL    50
VHAPSVAPDR AVARSLTGAP TTAVLAGEIY NRDELLSVLP AGPAPEGDAE 100
LVLRLLERYD LHAFRLVNGR FATVVRTGDR VLLATDHAGS VPLYTCVAPG 150
EVRASTEAKA LAAHRDPKGF PLADARRVAG LTGVYQVPAG AVMDIDLGSG 200
TAVTHRTWTP GLSRRILPEG EAVAAVRAAL EKAVAQRVTP GDTPLVVLSG 250
GIDSSGVAAC AHRAAGELDT VSMGTDTSNE FREARAVVDH LRTRHREITI 300
PTTELLAQLP YAVWASESVD PDIIEYLLPL TALYRALDGP ERRILTGYGA 350
DIPLGGMHRE DRLPALDTVL AHDMATFDGL NEMSPVLSTL AGHWTTHPYW 400
DREVLDLLVS LEAGLKRRHG RDKWVLRAAM ADALPAETVN RPKLGVHEGS 450
GTTSSFSRLL LDHGVAEDRV HEAKRQVVRE LFDLTVGGGR HPSEVDTDDV 500
VRSVADRTAR GAA 513
Length:513
Mass (Da):54,530
Last modified:September 5, 2012 - v1
Checksum:iEC2F460A77EB65CE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF071051 Genomic DNA. Translation: AAC31901.1.
X84101 Genomic DNA. Translation: CAA58903.1.
PIRiS57668.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF071051 Genomic DNA. Translation: AAC31901.1 .
X84101 Genomic DNA. Translation: CAA58903.1 .
PIRi S57668.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JGT X-ray 1.95 A/B 1-513 [» ]
1M1Z X-ray 1.95 A/B 1-513 [» ]
1MB9 X-ray 2.11 A/B 1-513 [» ]
1MBZ X-ray 2.47 A/B 1-513 [» ]
1MC1 X-ray 2.16 A/B 1-513 [» ]
ProteinModelPortali P0DJQ7.
SMRi P0DJQ7. Positions 2-508.
ModBasei Search...
MobiDBi Search...

Chemistry

DrugBanki DB00131. Adenosine monophosphate.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00112 ; UER00243 .
BioCyci MetaCyc:MONOMER-13483.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProi IPR001962. Asn_synthase.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
Pfami PF00733. Asn_synthase. 2 hits.
PF13537. GATase_7. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
ProtoNeti Search...

Publicationsi

  1. 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.

Entry informationi

Entry nameiBLS_STRCL
AccessioniPrimary (citable) accession number: P0DJQ7
Secondary accession number(s): Q53938, Q9R8E3
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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