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Protein

Cyclo(L-leucyl-L-phenylalanyl) synthase

Gene

albC

Organism
Streptomyces noursei
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of albonoursin (cyclo[(alpha,beta-dehydro-Phe)-(alpha,beta-dehydro-Leu)]), an antibacterial peptide. It uses activated amino acids in the form of aminoacyl-tRNAs (aa-tRNAs) as substrates to catalyze the ATP-independent formation of cyclodipeptides which are intermediates in diketopiperazine (DKP) biosynthetic pathways. Catalyzes the formation of cyclo(L-Phe-L-Leu) (cFL) as major products from L-L-phenylalanyl-tRNA(Phe) and L-leucyl-tRNA(Leu). AlbC can also incorporate various nonpolar residues, such as L-phenylalanine, L-leucine, L-tyrosine and L-methionine, and to a much lesser extent L-alanine and L-valine, into cyclodipeptides. Indeed, ten possible cyclodipeptides composed of L-phenylalanine, L-leucine, L-tyrosine and L-methionine are all synthesized to detectable amounts by AlbC.2 Publications

Catalytic activityi

L-leucyl-tRNA(Leu) + L-phenylalanyl-tRNA(Phe) = tRNA(Leu) + tRNA(Phe) + cyclo(L-leucyl-L-phenylalanyl).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei37Nucleophile1 Publication1
Binding sitei40SubstrateBy similarity1
Sitei40Could have a critical role in the catalytic mechanismBy similarity1
Sitei98Could be involved in aa-tRNA bindingBy similarity1
Sitei178Could be involved in aa-tRNA bindingBy similarity1
Sitei182Could have a critical role in the catalytic mechanismBy similarity1
Sitei200Essential for the cyclodipeptide synthase specificity1
Binding sitei202SubstrateBy similarity1

GO - Molecular functioni

  • transferase activity, transferring amino-acyl groups Source: UniProtKB

GO - Biological processi

  • antibacterial peptide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.3.2.20. 11755.
2.3.2.22. 11755.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclo(L-leucyl-L-phenylalanyl) synthase (EC:2.3.2.20)
Alternative name(s):
Cyclodipeptide synthase
Short name:
CDPS
Gene namesi
Name:albC
OrganismiStreptomyces noursei
Taxonomic identifieri1971 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi35G → A: Poorly active. 1 Publication1
Mutagenesisi37S → A: Inactive. 1 Publication1
Mutagenesisi37S → C: Does not completely abolish the enzymatic activity. 1 Publication1
Mutagenesisi178Y → A: Almost inactive. 1 Publication1
Mutagenesisi178Y → F: Poorly active. 1 Publication1
Mutagenesisi182E → A: Inactive. 1 Publication1
Mutagenesisi182E → Q: Inactive. 1 Publication1
Mutagenesisi200L → N: It synthesizes mainly cyclo(L-Tyr-L-Leu) (cYL) instead of cFL. 1 Publication1
Mutagenesisi202Y → F: It retains 11% of the enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004233551 – 239Cyclo(L-leucyl-L-phenylalanyl) synthaseAdd BLAST239

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1239
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 17Combined sources5
Helixi20 – 22Combined sources3
Helixi23 – 28Combined sources6
Beta strandi29 – 39Combined sources11
Helixi41 – 43Combined sources3
Helixi45 – 58Combined sources14
Beta strandi59 – 67Combined sources9
Helixi71 – 78Combined sources8
Helixi82 – 107Combined sources26
Helixi111 – 113Combined sources3
Beta strandi114 – 118Combined sources5
Helixi119 – 122Combined sources4
Helixi126 – 141Combined sources16
Helixi143 – 158Combined sources16
Beta strandi161 – 163Combined sources3
Helixi169 – 193Combined sources25
Beta strandi198 – 202Combined sources5
Helixi207 – 212Combined sources6
Beta strandi217 – 219Combined sources3
Beta strandi225 – 229Combined sources5
Helixi232 – 238Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OQVX-ray1.90A2-239[»]
4Q24X-ray2.90A1-239[»]
SMRiQ8GED7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GED7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni178 – 182Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the CDPS family.Curated

Family and domain databases

InterProiIPR030903. CDPS.
[Graphical view]
PfamiPF16715. CDPS. 1 hit.
[Graphical view]
TIGRFAMsiTIGR04539. tRNA_cyclodipep. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8GED7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAGLVPAPD HGMREEILGD RSRLIRQRGE HALIGISAGN SYFSQKNTVM
60 70 80 90 100
LLQWAGQRFE RTDVVYVDTH IDEMLIADGR SAQEAERSVK RTLKDLRRRL
110 120 130 140 150
RRSLESVGDH AERFRVRSLS ELQETPEYRA VRERTDRAFE EDAEFATACE
160 170 180 190 200
DMVRAVVMNR PGDGVGISAE HLRAGLNYVL AEAPLFADSP GVFSVPSSVL
210 220 230
CYHIDTPITA FLSRRETGFR AAEGQAYVVV RPQELADAA
Length:239
Mass (Da):26,774
Last modified:March 1, 2003 - v1
Checksum:iCD368019F6EF87F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY129235 Genomic DNA. Translation: AAN07909.1.

Genome annotation databases

KEGGiag:AAN07909.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY129235 Genomic DNA. Translation: AAN07909.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OQVX-ray1.90A2-239[»]
4Q24X-ray2.90A1-239[»]
SMRiQ8GED7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAN07909.

Enzyme and pathway databases

BRENDAi2.3.2.20. 11755.
2.3.2.22. 11755.

Miscellaneous databases

EvolutionaryTraceiQ8GED7.

Family and domain databases

InterProiIPR030903. CDPS.
[Graphical view]
PfamiPF16715. CDPS. 1 hit.
[Graphical view]
TIGRFAMsiTIGR04539. tRNA_cyclodipep. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCLPS_STRNR
AccessioniPrimary (citable) accession number: Q8GED7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 18, 2013
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The reaction proceeds following a ping-pong mechanism forming a covalent intermediate between an active site Ser-37 and the L-phenylalanine residue.1 Publication

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.