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P0DJQ7

- BLS_STRCL

UniProt

P0DJQ7 - BLS_STRCL

Protein

Carboxyethyl-arginine beta-lactam-synthase

Gene

bls

Organism
Streptomyces clavuligerus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 12 (01 Oct 2014)
      Sequence version 1 (05 Sep 2012)
      Previous versions | rss
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    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the asparagine synthetase family.Curated

    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

    « Hide

    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: October 1, 2014
    This is version 12 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