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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

Mg2+Note: Binds 1 Mg(2+) 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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MGAPVLPAAF GFLASARTGG GRAPGPVFAT RGSHTDIDTP QGERSLAATL
60 70 80 90 100
VHAPSVAPDR AVARSLTGAP TTAVLAGEIY NRDELLSVLP AGPAPEGDAE
110 120 130 140 150
LVLRLLERYD LHAFRLVNGR FATVVRTGDR VLLATDHAGS VPLYTCVAPG
160 170 180 190 200
EVRASTEAKA LAAHRDPKGF PLADARRVAG LTGVYQVPAG AVMDIDLGSG
210 220 230 240 250
TAVTHRTWTP GLSRRILPEG EAVAAVRAAL EKAVAQRVTP GDTPLVVLSG
260 270 280 290 300
GIDSSGVAAC AHRAAGELDT VSMGTDTSNE FREARAVVDH LRTRHREITI
310 320 330 340 350
PTTELLAQLP YAVWASESVD PDIIEYLLPL TALYRALDGP ERRILTGYGA
360 370 380 390 400
DIPLGGMHRE DRLPALDTVL AHDMATFDGL NEMSPVLSTL AGHWTTHPYW
410 420 430 440 450
DREVLDLLVS LEAGLKRRHG RDKWVLRAAM ADALPAETVN RPKLGVHEGS
460 470 480 490 500
GTTSSFSRLL LDHGVAEDRV HEAKRQVVRE LFDLTVGGGR HPSEVDTDDV
510
VRSVADRTAR GAA
Length:513
Mass (Da):54,530
Last modified:September 5, 2012 - v1
Checksum:iEC2F460A77EB65CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071051 Genomic DNA. Translation: AAC31901.1.
X84101 Genomic DNA. Translation: CAA58903.1.
PIRiS57668.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071051 Genomic DNA. Translation: AAC31901.1 .
X84101 Genomic DNA. Translation: CAA58903.1 .
PIRi S57668.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

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: November 26, 2014
This is version 14 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