CDLS_PHOLL
ID CDLS_PHOLL Reviewed; 234 AA.
AC Q7N9M5;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Cyclo(L-leucyl-L-leucyl) synthase;
DE EC=2.3.2.22;
DE AltName: Full=Cyclodileucine synthase;
DE AltName: Full=Cyclodipeptide synthase;
DE Short=CDPS;
GN OrderedLocusNames=plu0297;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=19430487; DOI=10.1038/nchembio.175;
RA Gondry M., Sauguet L., Belin P., Thai R., Amouroux R., Tellier C.,
RA Tuphile K., Jacquet M., Braud S., Courcon M., Masson C., Dubois S.,
RA Lautru S., Lecoq A., Hashimoto S., Genet R., Pernodet J.L.;
RT "Cyclodipeptide synthases arec a family of tRNA-dependent peptide bond-
RT forming enzymes.";
RL Nat. Chem. Biol. 5:414-420(2009).
CC -!- FUNCTION: It uses activated amino acids in the form of aminoacyl-tRNAs
CC (aa-tRNAs) as substrates to catalyze the ATP-independent formation of
CC cyclodipeptides which are intermediates in diketopiperazine (DKP)
CC biosynthetic pathways. Catalyzes the formation of cyclo(L-Leu-L-Leu)
CC (cLL) from L-leucyl-tRNA(Leu). Can incorporate various nonpolar
CC residues, such as L-phenylalanine, L-leucine and L-methionine, into
CC cyclodipeptides. {ECO:0000269|PubMed:19430487}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-leucyl-tRNA(Leu) = cyclo(L-leucyl-L-leucyl) + 2 H(+) + 2
CC tRNA(Leu); Xref=Rhea:RHEA:46452, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:15378, ChEBI:CHEBI:67269, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78494; EC=2.3.2.22;
CC Evidence={ECO:0000269|PubMed:19430487};
CC -!- SIMILARITY: Belongs to the CDPS family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571859; CAE12592.1; -; Genomic_DNA.
DR RefSeq; WP_011144694.1; NC_005126.1.
DR AlphaFoldDB; Q7N9M5; -.
DR SMR; Q7N9M5; -.
DR STRING; 243265.plu0297; -.
DR EnsemblBacteria; CAE12592; CAE12592; plu0297.
DR GeneID; 24168354; -.
DR KEGG; plu:plu0297; -.
DR eggNOG; ENOG50332PQ; Bacteria.
DR HOGENOM; CLU_084186_1_0_6; -.
DR OMA; LAYHRPW; -.
DR OrthoDB; 1802439at2; -.
DR BioCyc; PLUM243265:PLU_RS01450-MON; -.
DR Proteomes; UP000002514; Chromosome.
DR GO; GO:0016755; F:aminoacyltransferase activity; IDA:UniProtKB.
DR Gene3D; 3.40.50.11710; -; 1.
DR InterPro; IPR030903; CDPS.
DR InterPro; IPR038622; CDPS_sf.
DR Pfam; PF16715; CDPS; 1.
DR TIGRFAMs; TIGR04539; tRNA_cyclodipep; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..234
FT /note="Cyclo(L-leucyl-L-leucyl) synthase"
FT /id="PRO_0000423353"
FT ACT_SITE 33
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179..183
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 208..209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 36
FT /note="Could have a critical role in the catalytic
FT mechanism"
FT /evidence="ECO:0000250"
FT SITE 85
FT /note="Could be involved in aa-tRNA binding"
FT /evidence="ECO:0000250"
FT SITE 95
FT /note="Could be involved in aa-tRNA binding"
FT /evidence="ECO:0000250"
FT SITE 179
FT /note="Could be involved in aa-tRNA binding"
FT /evidence="ECO:0000250"
FT SITE 183
FT /note="Could have a critical role in the catalytic
FT mechanism"
FT /evidence="ECO:0000250"
SQ SEQUENCE 234 AA; 26893 MW; B9291248C7B7E8B6 CRC64;
MLHENSPSFT VQGETSRCDQ IIQKGDHALI GISPFNSRFS KDYVVDLIQW SSHYFRQVDI
LLPCEREASR LLVASGIDNV KAIKKTHREI RRHLRNLDYV ISTATLKSKQ IRVIQFSDFS
LNHDYQSLKT QVENAFNESE SFKKSCLDMS FQAIKGRLKG TGQYFGQIDL QLVYKALPYI
FAEIPFYLNT PRLLGVKYST LLYHRPWSIG KGLFNGSYPI QVADKQSYGI VTQL
