ID   TSAD_MYCPN              Reviewed;         319 AA.
AC   P75055;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01445};
DE            EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_01445};
DE   AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_01445};
DE            Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_01445};
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445};
GN   Name=tsaD {ECO:0000255|HAMAP-Rule:MF_01445}; Synonyms=gcp;
GN   OrderedLocusNames=MPN_059; ORFNames=MP095;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasmoides pneumoniae).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC       adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC       with adenine. Is involved in the transfer of the threonylcarbamoyl
CC       moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37,
CC       together with TsaE and TsaB. TsaD likely plays a direct catalytic role
CC       in this reaction. {ECO:0000255|HAMAP-Rule:MF_01445}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC         H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC         Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01445};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01445};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01445};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445}.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01445}.
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DR   EMBL; U00089; AAB95743.1; -; Genomic_DNA.
DR   PIR; S73421; S73421.
DR   RefSeq; NP_109747.1; NC_000912.1.
DR   RefSeq; WP_010874416.1; NZ_OU342337.1.
DR   AlphaFoldDB; P75055; -.
DR   SMR; P75055; -.
DR   IntAct; P75055; 2.
DR   STRING; 272634.MPN_059; -.
DR   EnsemblBacteria; AAB95743; AAB95743; MPN_059.
DR   GeneID; 66609300; -.
DR   KEGG; mpn:MPN_059; -.
DR   PATRIC; fig|272634.6.peg.59; -.
DR   HOGENOM; CLU_023208_0_1_14; -.
DR   OrthoDB; 9806197at2; -.
DR   BioCyc; MPNE272634:G1GJ3-94-MONOMER; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_01445; TsaD; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR017861; KAE1/TsaD.
DR   InterPro; IPR017860; Peptidase_M22_CS.
DR   InterPro; IPR022450; TsaD.
DR   NCBIfam; TIGR00329; gcp_kae1; 1.
DR   NCBIfam; TIGR03723; T6A_TsaD_YgjD; 1.
DR   PANTHER; PTHR11735; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1.
DR   PANTHER; PTHR11735:SF6; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00814; TsaD; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   PROSITE; PS01016; GLYCOPROTEASE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Iron; Metal-binding; Reference proteome;
KW   Transferase; tRNA processing.
FT   CHAIN           1..319
FT                   /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT                   /id="PRO_0000096968"
FT   BINDING         110
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         114
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         135..139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         301
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
SQ   SEQUENCE   319 AA;  35210 MW;  39021A8BBC6A95CE CRC64;
     MEQPLCILGI ETTCDDTSIG VITESKVQAH IVLSSAKLHA QTGGVVPEVA ARSHEQNLLK
     ALQQSGVVLE QITHIAYAAN PGLPGCLHVG ATFARSLSFL LDKPLLPINH LYAHIFSALI
     DQDINQLKLP ALGLVVSGGH TAIYLIKSLF DLELIAETSD DAIGEVYDKV GRAMGFPYPA
     GPQLDSLFQP ELVKSHYFFR PSTKWTKFSY SGLKSQCFTK IKQLRERKGF NPQTHDWNEF
     ASNFQATIID HYINHVKDAI QQHQPQMLLL GGGVSANKYL REQVTQLQLP YLIAPLKYTS
     DNGAMIGFYA NLLINGKNN
//