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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei37 – 371Nucleophile1 Publication
Binding sitei40 – 401SubstrateBy similarity
Sitei40 – 401Could have a critical role in the catalytic mechanismBy similarity
Sitei98 – 981Could be involved in aa-tRNA bindingBy similarity
Sitei178 – 1781Could be involved in aa-tRNA bindingBy similarity
Sitei182 – 1821Could have a critical role in the catalytic mechanismBy similarity
Sitei200 – 2001Essential for the cyclodipeptide synthase specificity
Binding sitei202 – 2021SubstrateBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 351G → A: Poorly active. 1 Publication
Mutagenesisi37 – 371S → A: Inactive. 1 Publication
Mutagenesisi37 – 371S → C: Does not completely abolish the enzymatic activity. 1 Publication
Mutagenesisi178 – 1781Y → A: Almost inactive. 1 Publication
Mutagenesisi178 – 1781Y → F: Poorly active. 1 Publication
Mutagenesisi182 – 1821E → A: Inactive. 1 Publication
Mutagenesisi182 – 1821E → Q: Inactive. 1 Publication
Mutagenesisi200 – 2001L → N: It synthesizes mainly cyclo(L-Tyr-L-Leu) (cYL) instead of cFL. 1 Publication
Mutagenesisi202 – 2021Y → F: It retains 11% of the enzymatic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 239239Cyclo(L-leucyl-L-phenylalanyl) synthasePRO_0000423355Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
239
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 175Combined sources
Helixi20 – 223Combined sources
Helixi23 – 286Combined sources
Beta strandi29 – 3911Combined sources
Helixi41 – 433Combined sources
Helixi45 – 5814Combined sources
Beta strandi59 – 679Combined sources
Helixi71 – 788Combined sources
Helixi82 – 10726Combined sources
Helixi111 – 1133Combined sources
Beta strandi114 – 1185Combined sources
Helixi119 – 1224Combined sources
Helixi126 – 14116Combined sources
Helixi143 – 15816Combined sources
Beta strandi161 – 1633Combined sources
Helixi169 – 19325Combined sources
Beta strandi198 – 2025Combined sources
Helixi207 – 2126Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi225 – 2295Combined sources
Helixi232 – 2387Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ8GED7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni178 – 1825Substrate bindingBy similarity

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3OQVX-ray1.90A2-239[»]
4Q24X-ray2.90A1-239[»]
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...

Publicationsi

  1. "The albonoursin gene cluster of S noursei biosynthesis of diketopiperazine metabolites independent of nonribosomal peptide synthetases."
    Lautru S., Gondry M., Genet R., Pernodet J.L.
    Chem. Biol. 9:1355-1364(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, NOMENCLATURE.
    Strain: ATCC 11455 / DSM 40635 / JCM 4922 / NBRC 15452 / NCIMB 8593 / NRRL B-1714.
  2. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  3. "Cyclodipeptide synthases, a family of class-I aminoacyl-tRNA synthetase-like enzymes involved in non-ribosomal peptide synthesis."
    Sauguet L., Moutiez M., Li Y., Belin P., Seguin J., Le Du M.H., Thai R., Masson C., Fonvielle M., Pernodet J.L., Charbonnier J.B., Gondry M.
    Nucleic Acids Res. 39:4475-4489(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-239, MUTAGENESIS OF GLY-35; SER-37; TYR-178; GLU-182; LEU-200 AND TYR-202, ACTIVE SITE, REACTION MECHANISM, SUBUNIT.

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: April 13, 2016
This is version 31 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.