ID   TUBAT_MYCTO             Reviewed;         296 AA.
AC   P9WJ60; F2GEC4; L0TCL2; O50407; Q7D5L5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Tuberculosinyl adenosine transferase {ECO:0000250|UniProtKB:P9WJ61};
DE            EC=2.5.1.153 {ECO:0000250|UniProtKB:P9WJ61};
DE   AltName: Full=Diterpene synthase {ECO:0000250|UniProtKB:P9WJ61};
DE   AltName: Full=Isotuberculosinol synthase {ECO:0000250|UniProtKB:P9WJ61};
DE   AltName: Full=Nosyberkol synthase {ECO:0000250|UniProtKB:P9WJ61};
DE   AltName: Full=Tuberculosinol synthase {ECO:0000250|UniProtKB:P9WJ61};
GN   OrderedLocusNames=MT3488;
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: Tuberculosinyl transferase that catalyzes the condensation of
CC       adenosine and tuberculosinyl diphosphate (TbPP) to generate 1-
CC       tuberculosinyladenosine (1-TbAd), which acts as an antiacid that
CC       directly protects M.tuberculosis from acid pH and physically remodels
CC       M.tuberculosis phagolysosomes. In addition, acts as a phosphatase that
CC       catalyzes the diphosphate-removal from TbPP to produce both
CC       tuberculosinol (TOH) and isotuberculosinol (iso-TOH).
CC       {ECO:0000250|UniProtKB:P9WJ61}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine + H(+) + tuberculosinyl diphosphate = 1-
CC         tuberculosinyladenosine + diphosphate; Xref=Rhea:RHEA:46000,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58822, ChEBI:CHEBI:85603; EC=2.5.1.153;
CC         Evidence={ECO:0000250|UniProtKB:P9WJ61};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + tuberculosinyl diphosphate = diphosphate +
CC         tuberculosinol; Xref=Rhea:RHEA:31783, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:50387, ChEBI:CHEBI:58822;
CC         Evidence={ECO:0000250|UniProtKB:P9WJ61};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + tuberculosinyl diphosphate = (13R)-edaxadiene +
CC         diphosphate; Xref=Rhea:RHEA:31787, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58822, ChEBI:CHEBI:63178;
CC         Evidence={ECO:0000250|UniProtKB:P9WJ61};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + tuberculosinyl diphosphate = (13S)-edaxadiene +
CC         diphosphate; Xref=Rhea:RHEA:31791, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58822, ChEBI:CHEBI:63180;
CC         Evidence={ECO:0000250|UniProtKB:P9WJ61};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WJ61};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WJ61}.
CC   -!- SIMILARITY: Belongs to the diterpene synthase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47824.1; -; Genomic_DNA.
DR   PIR; A70973; A70973.
DR   RefSeq; WP_003417908.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJ60; -.
DR   SMR; P9WJ60; -.
DR   BindingDB; P9WJ60; -.
DR   EnsemblBacteria; AAK47824; AAK47824; MT3488.
DR   KEGG; mtc:MT3488; -.
DR   HOGENOM; CLU_1100473_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   Gene3D; 3.40.1180.10; -; 1.
DR   InterPro; IPR036424; UPP_synth-like_sf.
PE   3: Inferred from homology;
KW   Transferase.
FT   CHAIN           1..296
FT                   /note="Tuberculosinyl adenosine transferase"
FT                   /id="PRO_0000427886"
SQ   SEQUENCE   296 AA;  34031 MW;  D79E55CFDE338E07 CRC64;
     MNLVSEKEFL DLPLVSVAEI VRCRGPKVSV FPFDGTRRWF HLECNPQYDD YQQAALRQSI
     RILKMLFEHG IETVISPIFS DDLLDRGDRY IVQALEGMAL LANDEEILSF YKEHEVHVLF
     YGDYKKRLPS TAQGAAVVKS FDDLTISTSS NTEHRLCFGV FGNDAAESVA QFSISWNETH
     GKPPTRREII EGYYGEYVDK ADMFIGFGRF STFDFPLLSS GKTSLYFTVA PSYYMTETTL
     RRILYDHIYL RHFRPKPDYS AMSADQLNVL RNRYRAQPDR VFGVGCVHDG IWFAEG