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Protein

Carboxyethyl-arginine beta-lactam-synthase

Gene

bls

Organism
Streptomyces clavuligerus
Status
Reviewed-Annotation score: 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 Mg2+ ion per subunit.

Pathwayi: clavulanate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes clavulanate from D-glyceraldehyde 3-phosphate and L-arginine.
Proteins known to be involved in the 8 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Carboxyethyl-arginine beta-lactam-synthase (bls)
  3. no protein annotated in this organism
  4. Proclavaminate amidinohydrolase (pah)
  5. no protein annotated in this organism
  6. no protein annotated in this organism
  7. no protein annotated in this organism
  8. no protein annotated in this organism
This subpathway is part of the pathway clavulanate biosynthesis, which is itself part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes clavulanate from D-glyceraldehyde 3-phosphate and L-arginine, the pathway clavulanate biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi253Magnesium1
Metal bindingi351Magnesium1

GO - Molecular functioni

GO - Biological processi

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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000569391 – 513Carboxyethyl-arginine beta-lactam-synthaseAdd BLAST513

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi443255.SclaA2_010100020123.

Structurei

Secondary structure

1513
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 18Combined sources9
Beta strandi32 – 36Combined sources5
Helixi42 – 44Combined sources3
Beta strandi47 – 52Combined sources6
Helixi58 – 61Combined sources4
Beta strandi62 – 65Combined sources4
Beta strandi67 – 80Combined sources14
Helixi82 – 87Combined sources6
Beta strandi89 – 92Combined sources4
Helixi98 – 109Combined sources12
Helixi110 – 115Combined sources6
Beta strandi119 – 127Combined sources9
Beta strandi130 – 135Combined sources6
Beta strandi144 – 148Combined sources5
Beta strandi151 – 156Combined sources6
Helixi158 – 162Combined sources5
Beta strandi164 – 166Combined sources3
Beta strandi175 – 177Combined sources3
Beta strandi191 – 196Combined sources6
Turni197 – 200Combined sources4
Beta strandi201 – 206Combined sources6
Helixi219 – 237Combined sources19
Beta strandi240 – 242Combined sources3
Beta strandi245 – 247Combined sources3
Helixi252 – 265Combined sources14
Beta strandi269 – 274Combined sources6
Helixi281 – 291Combined sources11
Beta strandi294 – 299Combined sources6
Helixi302 – 306Combined sources5
Helixi309 – 316Combined sources8
Helixi321 – 336Combined sources16
Beta strandi343 – 345Combined sources3
Turni348 – 350Combined sources3
Helixi351 – 354Combined sources4
Turni355 – 357Combined sources3
Helixi364 – 376Combined sources13
Helixi386 – 389Combined sources4
Turni390 – 392Combined sources3
Beta strandi394 – 396Combined sources3
Helixi398 – 400Combined sources3
Helixi402 – 410Combined sources9
Helixi413 – 416Combined sources4
Beta strandi421 – 423Combined sources3
Helixi424 – 430Combined sources7
Turni431 – 433Combined sources3
Helixi436 – 440Combined sources5
Helixi446 – 449Combined sources4
Helixi455 – 463Combined sources9
Turni467 – 469Combined sources3
Helixi470 – 485Combined sources16
Turni486 – 488Combined sources3
Helixi492 – 494Combined sources3
Helixi497 – 505Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the asparagine synthetase family.Curated

Phylogenomic databases

eggNOGiENOG4105TCH. Bacteria.
COG0367. LUCA.
KOiK12674.

Family and domain databases

CDDicd01991. Asn_Synthase_B_C. 1 hit.
Gene3Di3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProiIPR001962. Asn_synthase.
IPR017932. GATase_2_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.
RefSeqiWP_003952510.1. NZ_CP016559.1.

Genome annotation databases

KEGGiag:AAC31901.

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.
PIRiS57668.
RefSeqiWP_003952510.1. NZ_CP016559.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi443255.SclaA2_010100020123.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC31901.

Phylogenomic databases

eggNOGiENOG4105TCH. Bacteria.
COG0367. LUCA.
KOiK12674.

Enzyme and pathway databases

UniPathwayiUPA00112; UER00243.
BioCyciMetaCyc:MONOMER-13483.

Family and domain databases

CDDicd01991. Asn_Synthase_B_C. 1 hit.
Gene3Di3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProiIPR001962. Asn_synthase.
IPR017932. GATase_2_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.
ProtoNetiSearch...

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 2, 2016
This is version 22 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.