ID   CDTS_MYCTO              Reviewed;         289 AA.
AC   P9WPF8; Q50688; Q7D7C6;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Cyclo(L-tyrosyl-L-tyrosyl) synthase;
DE            EC=2.3.2.21;
DE   AltName: Full=Cyclodipeptide synthase;
DE            Short=CDPS;
DE   AltName: Full=Cyclodityrosine synthase;
GN   OrderedLocusNames=MT2335;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Involved in the biosynthesis of mycocyclosin. It uses
CC       activated amino acids in the form of aminoacyl-tRNAs (aa-tRNAs) as
CC       substrates to catalyze the ATP-independent formation of cyclodipeptides
CC       which are intermediates in diketopiperazine (DKP) biosynthetic
CC       pathways. Catalyzes the formation of cyclo(L-Tyr-L-Tyr) (cYY) from L-
CC       tyrosyl-tRNA(Tyr) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-tyrosyl-tRNA(Tyr) = cyclo(L-tyrosyl-L-tyrosyl) + 2
CC         tRNA(Tyr); Xref=Rhea:RHEA:46448, Rhea:RHEA-COMP:9706, Rhea:RHEA-
CC         COMP:9707, ChEBI:CHEBI:65063, ChEBI:CHEBI:78442, ChEBI:CHEBI:78536;
CC         EC=2.3.2.21;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CDPS family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46619.1; -; Genomic_DNA.
DR   PIR; G70730; G70730.
DR   RefSeq; WP_003411681.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPF8; -.
DR   SMR; P9WPF8; -.
DR   EnsemblBacteria; AAK46619; AAK46619; MT2335.
DR   KEGG; mtc:MT2335; -.
DR   PATRIC; fig|83331.31.peg.2512; -.
DR   HOGENOM; CLU_084186_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Transferase.
FT   CHAIN           1..289
FT                   /note="Cyclo(L-tyrosyl-L-tyrosyl) synthase"
FT                   /id="PRO_0000426959"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        88
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         229..233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            91
FT                   /note="Could have a critical role in the catalytic
FT                   mechanism"
FT                   /evidence="ECO:0000250"
FT   SITE            139
FT                   /note="Could be involved in aa-tRNA binding"
FT                   /evidence="ECO:0000250"
FT   SITE            229
FT                   /note="Could be involved in aa-tRNA binding"
FT                   /evidence="ECO:0000250"
FT   SITE            233
FT                   /note="Could have a critical role in the catalytic
FT                   mechanism"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   289 AA;  31612 MW;  D0B98859EE8CEF38 CRC64;
     MSYVAAEPGV LISPTDDLQS PRSAPAAHDE NADGITGGTR DDSAPNSRFQ LGRRIPEATA
     QEGFLVRPFT QQCQIIHTEG DHAVIGVSPG NSYFSRQRLR DLGLWGLTNF DRVDFVYTDV
     HVAESYEALG DSAIEARRKA VKNIRGVRAK ITTTVNELDP AGARLCVRPM SEFQSNEAYR
     ELHADLLTRL KDDEDLRAVC QDLVRRFLST KVGPRQGATA TQEQVCMDYI CAEAPLFLDT
     PAILGVPSSL NCYHQSLPLA EMLYARGSGL RASRNQGHAI VTPDGSPAE